I spent my time in high school editing newspaper columns and conjugating Latin verbs.
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Conjugating the Latin verb desero (in the above phrases), Reines delicately balance her own identity against the word's imbricated meanings.
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Those mind-numbing exercises in high school—factoring polynomials, conjugating verbs, memorizing the periodic table—were possibly the opposite: mind-sensitizing.
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You may recall, as I do, countless hours in third grade poring over multiplication tables or, in ninth grade, endlessly conjugating French (or Spanish) verbs, or in 11th grade, incessantly reciting Macbeth's "Tomorrow, and tomorrow, and tomorrow" soliloquy in the attempt to firmly place them in long-term memory.
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The school offers yoga and a play space designed by the architect Bjarke Ingels, and children get to spend one day a week at a farm upstate and then sell produce at a student-run WeWork farm stand, because isn't it better that they are nudged into becoming Danny Meyer rather than task-mastered into conjugating verbs??
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But they're best taken with the historical context in mind, and what the characters are experiencing from their secluded vantage point: the dismay of knowing their social order is disappearing, and the dreariness of living from day to day with nothing to do but keep at the embroidery, practice conjugating French verbs, maybe practice the violin.
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The causative passive form is obtained by first conjugating in the causative form and then conjugating the result in the passive form.
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Ubiquitin-conjugating enzyme E2 variant 2 is a protein that in humans is encoded by the UBE2V2 gene. Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family.
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Ubiquitin/ISG15-conjugating enzyme E2 L6 is a protein that in humans is encoded by the UBE2L6 gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1S), ubiquitin-conjugating enzymes (E2S) and ubiquitin-protein ligases (E3s). This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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SUMO-conjugating enzyme UBC9 is an enzyme that in humans is encoded by the UBE2I gene. It is also sometimes referred to as "ubiquitin conjugating enzyme E2I" or "ubiquitin carrier protein 9", even though these names do not accurately describe its function.
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Ubiquitin-conjugating enzyme E2 J1 is a protein that in humans is encoded by the UBE2J1 gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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Ubiquitin-conjugating enzyme E2 variant 1, also known as Kua-UEV, is a human gene. The Kua-UEV mRNA is an infrequent but naturally occurring co-transcribed product of the neighboring Kua and UBE2V1 genes. Ubiquitin-conjugating E2 enzyme variant proteins constitute a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s.
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Ubiquitin-conjugating enzyme E2 C is a protein that in humans is encoded by the UBE2C gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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Ubiquitin-conjugating enzyme E2 H is a protein that in humans is encoded by the UBE2H gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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NEDD8-conjugating enzyme Ubc12 is a protein that in humans is encoded by the UBE2M gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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Ubiquitin-conjugating enzyme E2 G2 is a protein that in humans is encoded by the UBE2G2 gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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Ubiquitin-conjugating enzyme E2 E3 is a protein that in humans is encoded by the UBE2E3 gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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Ubiquitin-conjugating enzyme E2 A is a protein that in humans is encoded by the UBE2A gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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Ubiquitin-conjugating enzyme E2 B is a protein that in humans is encoded by the UBE2B gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family.
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UBE2V2 has sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene also shares homology with ubiquitin- conjugating enzyme E2 variant 1 and yeast MMS2 gene product.
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Ubiquitin-conjugating enzyme E2 R2 is a protein that in humans is encoded by the UBE2R2 gene. Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase involved in cell growth and transformation. This gene encodes a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. Studies suggest that CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP, enhancing beta-catenin degradation.
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Ubiquitin-conjugating enzyme E2 E2 is a protein that in humans is encoded by the UBE2E2 gene.
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Ubiquitin-conjugating enzyme E2 E1 is a protein that in humans is encoded by the UBE2E1 gene.
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Ubiquitin conjugating enzyme E2 Q2 is a protein that in humans is encoded by the UBE2Q2 gene.
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Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene.
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Ubiquitin-conjugating enzyme E2 D1 is a protein that in humans is encoded by the UBE2D1 gene.
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Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 gene.
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Ubiquitin-conjugating enzyme E2 D3 is a protein that in humans is encoded by the UBE2D3 gene.
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Ubiquitin-conjugating enzyme E2 G1 is a protein that in humans is encoded by the UBE2G1 gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to other proteins.
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Ubiquitin-fold modifier conjugating enzyme 1 is a protein that in humans is encoded by the UFC1 gene.
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Ubiquitin conjugating enzyme E2 F (putative) is a protein that in humans is encoded by the UBE2F gene.
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Ubiquitin-conjugating enzyme E2 variant 1 is a protein that in humans is encoded by the UBE2V1 gene.
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A.Shirokov); symmetric spaces with uncertain metrics (P.A.Shirokov); tensor analysis (P.A.Shirokov); conjugating in zero-systems (V. A. Yablokov); Finsler spaces (B.
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The conjugating process is substantially aberrant. Spirotaenia may actually be more than one distinct lineage which may not be closely related.
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Ubiquitin-conjugating enzyme E2 K is a protein that in humans is encoded by the UBE2K gene. The protein encoded by this gene belongs to the ubiquitin- conjugating enzyme family. It binds selectively to a large region at the N terminus of huntingtin. This interaction is not influenced by the length of the huntingtin polyglutamine tract.
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The protein encoded by this gene is a member of the ubiquitin- conjugating enzyme family. Ubiquitin-conjugating enzyme catalyzes the covalent attachment of ubiquitin to other proteins. This protein is a part of the large multiprotein complex, which is required for ubiquitin-mediated degradation of cell cycle G1 regulators, and for the initiation of DNA replication.
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For the example of the general linear group GL(n, R), this corresponds to the fact that any inner product on Rn defines a (compact) orthogonal group (its isometry group) – and that it admits an orthonormal basis: the change of basis defines the conjugating element conjugating the isometry group to the classical orthogonal group O(n, R).
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The verbs can now and then be totally foreign for other Norwegians, and it is hard to find a pattern in conjugating them.
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CDC34 is a gene encoding a protein product that has ubiquitin conjugating activity. CDC34 was originally discovered by work in baker's yeast as a gene that has a role in the cell division cycle. Cdc34 in yeast targets numerous substrates (Sic1, Far1, Cln1, Cln2) for ubiquitin mediated degradation. Ubiquitin-conjugating enzyme E2 R1 is a protein that in humans is encoded by the CDC34 gene.
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This protein belongs to the ubiquitin conjugating enzyme family and is one of the E2 enzymes. UBE2Z spans 246 amino acids, 150 of which encode a conserved 16–18 kDa ubiquitin conjugating enzyme E2 domain (UBC domain) that is located at the enzyme’s N-terminal and responsible for the enzyme’s catalytic function. This UBC domain has a relatively inflexible β-sheet structure with flanking helices and contains a highly conserved cysteine residue, Cys80, which functions as an active site for the thiol ester formation with ubiquitin. UBE2Z also contains a C-terminal extension, suggested to participate in substrate binding, which is characteristic of a class II E2 ubiquitin conjugating enzyme.
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UBE2V2 has been shown to interact with HLTF. Although UBE2V2 itself lacks ubiquitin-conjugating activity, it can interact with different Ubiquitin- conjugating enzymes to facilitate their catalytic activities. For instance, UBE2V2 can complex with UBE2N to form a heterodimer capable of synthesizing Lys-63 linked polyubiquitin chains. UBE2V2 may facilitate UBE2N activity by coordinating UBE2N's positioning to promote ubiquitin chain formation specifically at Lys-63, as the ubiquitin molecule has multiple potential Lysine binding sites. Similarly, it has been shown that UBE2V2 interact with the ubiquitin-conjugating enzyme, Ubc13, to induce Ubc13 to adopt an active conformation that can create Lys-63 polyubituitin chains on various substrates.
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UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1 (UFM1; MIM 610553) (Komatsu et al., 2004 [PubMed 15071506]).[supplied by OMIM, Mar 2008].
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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Studies in mouse suggest that this protein plays a role in DNA postreplication repair.
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If ƒ is a C2 map, then the hypothesis on the derivative holds; however, for any irrational rotation number Denjoy constructed an example showing that this condition cannot be relaxed to C1, continuous differentiability of ƒ. Vladimir Arnold showed that the conjugating map need not be smooth, even for an analytic diffeomorphism of the circle. Later Michel Herman proved that nonetheless, the conjugating map of an analytic diffeomorphism is itself analytic for "most" rotation numbers, forming a set of full Lebesgue measure, namely, for those that are badly approximable by rational numbers. His results are even more general and specify differentiability class of the conjugating map for Cr diffeomorphisms with any r ≥ 3\.
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Ubiquitin conjugating enzyme E2 Z (UBE2Z), also known as UBA6-specific E2 enzyme 1 (USE1), is an enzyme that in humans is encoded by the UBE2Z gene on chromosome 17. It is ubiquitously expressed in many tissues and cell types. UBE2Z is an E2 ubiquitin conjugating enzyme and participates in the second step of protein ubiquitination during proteolysis. A genome-wide association study (GWAS) revealed the UBE2Z gene to be associated with chronic kidney disease.
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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is closely related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis.
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This is a stereoselective situation based on the relative orientation of the two separate components when they react with each other. In the context of the Diels–Alder reaction, the transition state in which the most significant substituent (an electron-withdrawing and/or conjugating group) on the dienophile is oriented towards the diene π system and slips under it as the reaction takes place is known as the endo transition state. In the alternative exo transition state, it is oriented away from it. (There is a more general usage of the terms endo and exo in stereochemical nomenclature.) In cases where the dienophile has a single electron-withdrawing / conjugating substituent, or two electron-withdrawing / conjugating substituents cis to each other, the outcome can often be predicted.
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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase.
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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase.
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Ubiquitin-conjugating E2 enzyme variant proteins constitute a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene is located in the nucleus and can cause transcriptional activation of the human FOS proto-oncogene. It is thought to be involved in the control of differentiation by altering cell cycle behavior.
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Most verbs (not all verbs have causative forms) can be made causative by adding the suffix -ন/নো to it. For example: "to do" is করা, which takes the -নো suffix to become করানো, or "to cause to do". The stem of such a causative verb - to be used when conjugating it - is thus the verbal noun form of the base verb (করা in the case of করানো). However, such stems do not undergo any vowel transformations when conjugating for tenses.
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Prefixes in Hebrew serve multiple purposes. A prefix can serve as a conjunction, preposition, definite article, or interrogative. Prefixes are also used when conjugating verbs in the future tense and for various other purposes.
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Ubiquitin-conjugating enzyme E2 O is a protein that in humans is encoded by the UBE2O gene. UBE2O functions during terminal erythroid differentiation to eliminate generic cellular components in parallel with abundant synthesis of hemoglobin.
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Mansi conjugation has three persons, three numbers, two tenses, and four moods. Active and passive voices exist. Intransitive and transitive conjugations are distinguished. This means that there are two possible ways of conjugating a verb.
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This gene encodes a protein with a BIR (baculoviral inhibition of apoptosis protein repeat) domain and a UBCc (ubiquitin-conjugating enzyme E2, catalytic) domain. This protein inhibits apoptosis by facilitating the degradation of apoptotic proteins by ubiquitination.
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Smith GP, and Scott JK. Libraries of peptides and proteins displayed on filamentous phage. Methods in Enzymology. 1993. 217:228-257 The next step is the capturing step. It involves conjugating the phage library to the desired target.
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A phase- conjugating mirror uses nonlinear optics to reverse the phase difference between incident beams. Such mirrors may be used, for example, for combination and self-guiding of laser beams and correction of atmospheric distortions in imaging systems.
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In many ciliates, such as Paramecium, conjugating partners (gamonts) are similar or indistinguishable in size and shape. This is referred to as "isogamontic" conjugation. In some groups, partners are different in size and shape. This is referred to as "anisogamontic" conjugation.
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FulvalenesA fulvalene is a hydrocarbon obtained by formally cross-conjugating two rings through a common exocyclic double bond.The Fulvalenes, Brian Halton, Eur. J. Org. Chem. 2005, 3391–3414 The name is derived from the similarly structured fulvenes which lack one ring.
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Although used less frequently, a subtle shift takes place in conjugating a masculine noun from indefinitive to definitive, e.g., from bekk to bekkjen (, [beçːen] or ). This is found in rural dialects along the coast from Farsund to the border between Troms and Finnmark.
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When NEDD8 binds to the ubiquitin E2 Ubc4, the interaction stimulates cullin-based ubiquitin ligases, although the exact mechanism is unclear.Sakata E, Yamaguchi Y, Miyauchi Y, et al. Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.
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Chemical structure of fulvene Fulvenes are the class of hydrocarbon obtained by formally cross-conjugating one ring and methylidene through a common exocyclic double bond. The name is derived from fulvene, which has one pentagonal ring. Other examples include methylenecyclopropene (triafulvene) and heptafulvene.
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The phase- conjugating Michelson interferometry is a promising technology for coherent summation of laser amplifiers . Constructive interference in an array containing N/2 beamsplitters of N laser beams synchronized by phase conjugation may increase the brightness of amplified beams as N^2.
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May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. This protein is a part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2. It also interacts with RNF7. Part of a complex with TIP120A/CAND1 and RBX1.
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Grammatically, one of its most notable features is the use of , instead of , with the verb conjugating differently: e.g. and instead of and . However, use of the standard você is also not rare. The same feature also occurs in other dialects of Brazilian Portuguese.
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Electrostatic interactions were also investigated by Rotello et al by conjugating AuNPs with anionic and cationic functional groups. Their results showed that toxicity was more established in AuNPs conjugated with cationic functional groups as a consequence of electrostatic interactions with the anionic cell membrane.
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The ER membrane anchored RING finger containing ubiquitin ligases Hrd1 and Doa10 are the major mediators of substrate ubiquitination during ERAD. The tail anchored membrane protein Ubc6 as well as Ubc1 and the Cue1 dependent membrane bound Ubc7 are the ubiquitin conjugating enzymes involved in ERAD.
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Conjugating each subdomain to a different protein allows protein-protein interactions to be studied, because cAMP production indicates close interaction of the proteins. Similarly, the two subdomains can be linked by a studied protein, which is then digested by proteases. Loss of cAMP production indicates cleavage by protease.
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Nanoparticle delivery through the BBB can be increased by introducing peptide conjugates to improve permeability to the central nervous system. For instance, recent studies have shown an improvement in gold nanoparticle delivery efficiency by conjugating a peptide that binds to the transferrin receptors expressed in brain endothelial cells.
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Studies of the mouse counterpart suggested the involvement of this gene in the specification of anterior-posterior axis, as well as in cell proliferation in early development. This protein was also found to interact with huntingtin interacting protein 2 (HIP2), an ubiquitin-conjugating enzyme, and possess ubiquitin ligase activity.
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They can store them in cells, inactivate them, or cannibalise already-formed hormones by conjugating them with carbohydrates, amino acids, or peptides. Plants can also break down hormones chemically, effectively destroying them. Plant hormones frequently regulate the concentrations of other plant hormones. Plants also move hormones around the plant diluting their concentrations.
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Ubiquitin-fold modifier 1, also known as UFM1, is a protein which in humans is encoded by the UFM1 gene. UFM1 is a ubiquitin-like protein that is conjugated to target proteins by E1-like activating enzyme UBA5 and E2-like conjugating enzyme UFC1. This process is often referred to as UFMylation.
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Ubiquitin residues are usually added to the lysine at position 120 on histone H2B. Ubiquitinating this lysine residue activates transcription. Scientists have discovered other ubiquitination sites in recent years, but they are not well studied or understood at this time. Ubiquitin- conjugating enzymes and ubiquitin ligases regulate the ubiquitination of histone H2B.
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Spirotaenia is a genus of basal green algae that may be sister to the Chlorokybophyceae. It was previously considered to be part of the Zygnemataceae. It is sexually conjugating, a mode of reproduction that was previously only known in the Zygnemataceae/Mesotaeniaceae, the sister groups to the land plants. This is surprising, as Spirotaenia is much more basal.
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A p orbital has a more suitable shape and orientation to overlap with the neighboring π system, resulting in more effective charge delocalization. As a consequence, alkyl carbanions with neighboring conjugating groups (e.g., allylic anions, enolates, nitronates, etc.) are generally planar rather than pyramidized. Likewise, delocalized alkenyl carbanions sometimes favor a linear instead of bent geometry.
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The protein encoded by this gene contains a RING finger motif. The mouse counterpart of this protein has been shown to interact with Rela, the p65 subunit of NF-kappaB (NF-κB), and modulate NF-κB- mediated transcription activity. The mouse protein also binds ubiquitin- conjugating enzymes (E2s) and is a substrate for E2-dependent ubiquitination.
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In abstract algebra an inner automorphism is an automorphism of a group, ring, or algebra given by the conjugation action of a fixed element, called the conjugating element. These inner automorphisms form a subgroup of the automorphism group, and the quotient of the automorphism group by this subgroup gives rise to the concept of the outer automorphism group.
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It has been shown that by using a parasitic array, the transmitted modulation in different directions could be controlled independently. Secrecy could be realized by making the modulations in undesired directions difficult to decode. Directional modulation data transmission was experimentally demonstrated using a phased array. Others have demonstrated directional modulation with switched arrays and phase-conjugating lenses.
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It has been shown that the integrin ITGB3 and the ubiquitin conjugating E2 enzyme UBC9 are downregulated by miR-30. It has also been suggested that the TP53 protein may be a target of miR-30c and miR-30e. An immunoblot analysis revealed that p53 expression levels were elevated upon knockdown of miR-30c and miR-30e.
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In S. cerevisiae, Pds1p (also known as securin) regulates sister chromatids cohesion, because it binds and inhibits the protease Esp1p (separin or separase). When anaphase onset is triggered, the anaphase- promoting complex (APC/C or Cyclosome) degrades securin. APC/C is a ring E3 ubiquitin ligase that recruits an E2 ubiquitin-conjugating enzyme loaded with ubiquitin.
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A general schematic of an artificial antigen presenting cell (aAPC). aAPCs are made by conjugating both T cell stimulatory Signals to material platforms. Modeled after APCs, aAPCs need to have at least two signals to stimulate antigen specific T cells. The first signal is the major histocompatibility complex (MHC), which in humans is also called the human leukocyte antigen (HLA).
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At St Jude's Children's Research Hospital, Helen Walden developed her interest in the mechanisms of ubiquitination, solving the structure of the E1 for Nedd8. In London, Walden studied the specificity and regulation of E3 ubiquitin ligases. In recent years Walden has studied the mechanism and disease association of E2-conjugating enzymes. Walden has investigated the role of Parkin in Parkinson's disease.
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Finally, Atg8 is detached from Atg3 and coupled to the amine head group of PE via an amide bond. This final step was found to be facilitated and stimulated by the ATG5-ATG12 complex. Both proteins, Atg5 and Atg12 were originally identified as part of another Ubl conjugating system that promotes conjugation of ATG12 to ATG5 via ATG7 and Atg10.
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This gene encodes the largest subunit of TFIID. This subunit binds to core promoter sequences encompassing the transcription start site. It also binds to activators and other transcriptional regulators, and these interactions affect the rate of transcription initiation. This subunit contains two independent protein kinase domains at the N and C-terminals, but also possesses acetyltransferase activity and can act as a ubiquitin-activating/conjugating enzyme.
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Nonlinear interactions of light waves are used widely to synchronize the laser beams in multichannel optical systems. Self-adjusting of phases may be robustly achievable in binary-tree array of beam-splitters and degenerate four-wave mixing Kerr Phase conjugation in Chirped pulse amplification extreme light facilities. This phase-conjugating Michelson interferometer increases the brightness as N^2, where N is the number of phase-locked channels.
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The E3 ubiquitin-protein ligases SMURF1 and SMURF2 regulate the levels of SMADs. They accept ubiquitin from an E2 conjugating enzyme where they transfer ubiquitin to the RSMADs which causes their ubiquitination and subsequent proteosomal degradation. SMURF1 binds to SMAD1 and SMAD5 while SMURF2 binds SMAD1, SMAD2, SMAD3, SMAD6 and SMAD7. It enhances the inhibitory action of SMAD7 while reducing the transcriptional activities of SMAD2.
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Harold Holcroft devised a different method for conjugating valve gear by linking the middle cylinder to the combination lever assembly of an outside cylinder, creating the Holcroft valve gear derivative. On a 4-cylinder locomotive the arrangement is simpler. The valve gear may be inside or outside and only short rocking-shafts are needed to link the valves on the inside and outside cylinders.
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Ubiquitin-conjugating enzyme E2 L3 (UBE2L3), also called UBCH7, is a protein that in humans is encoded by the UBE2L3 gene. As an E2 enzyme, UBE2L3 participates in ubiquitination to target proteins for degradation. The role of UBE2L3 in the ubiquitination of the NF-κB precursor implicated it in various major autoimmune diseases, including rheumatoid arthritis (RA), celiac disease, Crohn's disease(CD), and systemic lupus erythematosus.
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In molecular biology, the HECT domain is a protein domain found in ubiquitin- protein ligases. The name HECT comes from 'Homologous to the E6-AP Carboxyl Terminus'. Proteins containing this domain at the C terminus include ubiquitin-protein ligase, which regulates ubiquitination of CDC25. Ubiquitin- protein ligase accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester, and then directly transfers the ubiquitin to targeted substrates.
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QCD is an SU(3) gauge theory involving gluons and quarks. The left-handed quarks belong to a triplet representation, the right-handed to an antitriplet representation (after charge-conjugating them) and the gluons to a real adjoint representation. A quark edge is assigned a color and orientation and a gluon edge is assigned a color pair. In the large N limit, we only consider the dominant term.
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It can be used as a marker of proteins, with which it easily forms conjugates via the sulfonyl chloride (SO2Cl) group. In water, the sulfonyl chloride group of unreacted Texas Red molecules hydrolyses to sulfonate and the molecule becomes the very water-soluble sulforhodamine 101 which is easy to wash out selectively. This is one of the advantages of conjugating with Texas Red vs. using a rhodamine-isothiocyanate for conjugation.
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Secondly, CuAAC outperforms SPAAC in click reactions where proteins with a high cytosine content, such as 4RepCT, are present. The SPAAC process, in the presence of proteins like 4RepCT, will often create ‘clicks’ in off-target sites resulting in the ligand conjugating to the wrong part of the protein and rendering the protein essentially useless. In order to maximize the number of functional sites along the fiber, CuAAC is preferred.
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Store sign showing usage of manual keigotr. "You kindly allow [us] to be closed" or "[We] receive the favor of [your] allowing [us] to be closed." This form is created by conjugating verbs with the saseru ("to force/to allow/let") + itadaku ("to accept/to receive the favor of.") It is called sasete itadakimasu because suru ("to do") is often attached to nouns which can function as verbs with suru.
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Ober, bezañ and eus can all be used as auxiliary verbs. In the present, Breton (like Cornish and Irish but unlike the other Celtic language) distinguishes between the simple and progressive present. The simple present is formed by either conjugating the verb or using the verbal noun with the present of ober. The progressive present, on the other hand, is formed with the present situative of bezañ combined with present participle.
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The traJ 5' UTR is a cis acting RNA element which is involved in regulating plasmid transfer in bacteria. In conjugating bacteria the FinOP system regulates the transfer of F-like plasmids. The FinP gene encodes an antisense RNA product that is complementary to part of the 5' UTR of the traJ mRNA. The traJ gene encodes a protein required for transcription from the major transfer promoter, pY.
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TRIM25 has an N-terminal RING domain, followed by a B-box type 1 domain, a B-box type 2 domain, a coiled-coil domain (CCD) and a C-terminal SPRY domain. The RING domain coordinates two zinc atoms and is essential for recruiting ubiquitin- conjugating enzymes. The function of the B-box domains is unknown. The CCD domain has been implicated in multimerization and other protein-protein interactions.
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Research begun in the 1970s led to clinical trials in humans of a hCG birth control vaccine. A phase I (safety) clinical trial examined 15 women from clinics in Helsinki, Finland, Uppsala, Sweden, Bahia, Brazil, and Santiago, Chile with a vaccine formed by conjugating the beta subunit of hCG with a tetanus toxoid. The women had previously had tubal ligations. In the trial the immune response was reversible and no significant health issues were found.
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In order to increase the effectiveness of AMO delivery, a 2011 paper proposed using functionalized gold nanoparticles. The gold nanoparticles increase delivery efficiency by conjugating with a cargo DNA that anneals to the AMO using complementarity. The cargo DNA is attached to the surface of the nanoparticle. Because many variations of DNA and RNA are unstable in in vivo conditions, carriers, such as nanoparticles, are necessary to protect from degeneration by nucleases.
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F-box proteins are an expanding family of eukaryotic proteins characterized by an approximately 40 amino acid motif, the F box. Some F-box proteins have been shown to be critical for the ubiquitin- mediated degradation of cellular regulatory proteins. In fact, F-box proteins are one of the four subunits of ubiquitin protein ligases, called SCFs. SCF ligases bring ubiquitin conjugating enzymes to substrates that are specifically recruited by the different F-box proteins.
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Ubiquitin-like modifier-activating enzyme 7 is a protein that in humans is encoded by the UBA7 gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family.
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E3 ubiquitin-protein ligase RNF19A is an enzyme that in humans is encoded by the RNF19A gene. The protein encoded by this gene contains two RING-finger motifs and an IBR (in between RING fingers) motif. This protein is an E3 ubiquitin ligase that is localized in Lewy bodies (LBs), neuronal inclusions characteristic of Parkinson's disease (PD). This protein interacts with UBE2L3/UBCH7 and UBE2E2/UBCH8, but not other ubiquitin-conjugating enzymes.
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The body removes xenobiotics by xenobiotic metabolism. This consists of the deactivation and the excretion of xenobiotics, and happens mostly in the liver. Excretion routes are urine, feces, breath, and sweat. Hepatic enzymes are responsible for the metabolism of xenobiotics by first activating them (oxidation, reduction, hydrolysis and/or hydration of the xenobiotic), and then conjugating the active secondary metabolite with glucuronic acid, sulfuric acid, or glutathione, followed by excretion in bile or urine.
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Schematic diagram of the ubiquitylation system. The ubiquitin ligase is referred to as an E3, and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. There is one major E1 enzyme, shared by all ubiquitin ligases, that uses ATP to activate ubiquitin for conjugation and transfers it to an E2 enzyme. The E2 enzyme interacts with a specific E3 partner and transfers the ubiquitin to the target protein.
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Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations.
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NEDD4L is a ubiquitin-protein ligase (E3) that accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then transfers it to specific substrates. In vivo NEDD4-2 regulates ENaC in the lung and kidney, the renal NCC and several Navs. It has also been shown to regulate EGFR, TGFβ receptor and WNT signalling. NEDD4L has been implicated in viral budding and viral latency processes via ubiquitination of viral proteins.
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In a ubiquitin-like fashion, ISG15 is covalently linked by its C-terminal LRLRGG motif to lysine residues on newly synthesized proteins. This process, termed ISGylation, is catalyzed by a series of conjugating enzymes. The activating E1 enzyme (UBE1L) charges ISG15 by forming a high-energy thiolester intermediate and transfers it to the UbcH8 E2 enzyme. UbcH8 has been identified as the major E2 for ISGylation, although it also functions in ubiquitination.
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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short- lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). E2s play a key role in the whole ubiquitin (Ub) transfer pathway and are responsible for Ub cellular signaling. Unlike many E2s that transfer Ub with RINGs, UBE2L3 has E3-independent reactivity with lysine.
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NEDD8-activating enzyme E1 catalytic subunit is a protein that in humans is encoded by the UBA3 gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family.
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Vaccines evoke an immune response to an antigen, and the immune system reacts by producing T cells and antibodies. The T cells remember the antigen so that if the body encounters it later, antibodies can be produced by B cells to break down the antigen. For bacteria with a polysaccharide coating, the immune response creates B cells independent of T cell stimulation. By conjugating the polysaccharide to a protein carrier, a T cell response can be induced.
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Placon Therapeutics is developing platinum-based cancer therapies. These include BTP-114, the first clinical candidate to use an albumin- conjugating, platinum-prodrug platform, based on Lippard's work. BTP-114 has been cleared for Phase 1 cancer-treatment clinical trials by the Food and Drug Administration (FDA). Tarveda Therapeutics is developing BTP-277 (renamed PEN-221) and other Pentarins, a proprietary class of therapeutics which use peptide ligands to carry a target drug to tumor cells.
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APC/C substrates have recognition amino acid sequences that enable the APC/C to identify them. The most common sequence is known as the destruction box or D-box. APC/C brings together an E2 ubiquitin- conjugating enzyme and the D-box rather than being an intermediate covalent carrier. The D-box should have a version of the following amino acid sequence: RXXLXXXXN, where R is arginine, X is any amino acid, L is Leucine, and N is asparagine.
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As an E3 ubiquitin ligases, enzyme MARCH 5 catalyzes the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to an identified protein substrate. MARCH5 was firstly identified as a mitofusin 2- and Drp1-binding protein. MARCH5 promotes ubiquitination of Drp1 and a knockdown of MARCH5 is by RNAi led to abnormal mitochondrial fusion. Further evidences show that MARCH 5 specifically interacts with mitofusin 1, by reducing the levels of it during certain phases of the cell cycle.
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Ubiquitin conjugation factor E4 B is a protein that in humans is encoded by the UBE4B gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes an additional conjugation factor, E4, which is involved in multiubiquitin chain assembly.
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Ubiquitin conjugation factor E4 A is a protein that in humans is encoded by the UBE4A gene. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes an additional conjugation factor, E4, which is involved in multiubiquitin chain assembly.
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Phenylbutyrate, which is the product of phenylacetate, conjugates with glutamine to form phenylacetylglutamine, which is excreted by the kidneys. Similarly, sodium benzoate reduces ammonia content in the blood by conjugating with glycine to form hippuric acid, which is rapidly excreted by the kidneys. A preparation containing sodium phenylacetate and sodium benzoate is available under the trade name Ammonul. Acidification of the intestinal lumen using lactulose can decrease ammonia levels by protonating ammonia and trapping it in the stool.
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Proteins are targeted for degradation by the proteasome with covalent modification of a lysine residue that requires the coordinated reactions of three enzymes. In the first step, a ubiquitin- activating enzyme (known as E1) hydrolyzes ATP and adenylylates a ubiquitin molecule. This is then transferred to E1's active-site cysteine residue in concert with the adenylylation of a second ubiquitin. This adenylylated ubiquitin is then transferred to a cysteine of a second enzyme, ubiquitin- conjugating enzyme (E2).
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The protein encoded by this gene belongs to a group of apparently inactive homologs of ubiquitin-conjugating enzymes. The gene product contains a coiled-coil domain that interacts with stathmin, a cytosolic phosphoprotein implicated in tumorigenesis. The protein may play a role in cell growth and differentiation and act as a negative growth regulator. In vitro steady-state expression of this tumor susceptibility gene appears to be important for maintenance of genomic stability and cell cycle regulation.
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At the C-terminal end, CUL4B interacts with the RBX1/ROC1 protein via its RING domain. RBX1 is a core component of Cullin-RING ubiquitin ligase (CRL) complexes and functions to recruit E2 ubiquitin conjugating enzymes. Therefore, the C-terminus of CUL4B - along with RBX1 and activated E2 enzymes - compose the catalytic core of CRL4B complexes. CUL4B is also modified by covalent attachment of a NEDD8 molecule at a highly conserved lysine residue in the C-terminal region.
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The enedial intermediate is toxic, as it can bind to proteins. However, it can be detoxified in phase II metabolism, in which the enedial can be conjugated with either N-acetyl lysine (NAL) or N-acetyl cysteine (NAC). This results in a NAL/NAC-IPO adduct, which can be excreted. Furthermore, 4-IPO can directly undergo phase II metabolism, by conjugating glucuronosyl to the hydroxyl group of 4-IPO by uridine 5’-diphospho-glucuronosyltransferase (UGT), forming 4-IPO glucuronide.
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The ubiquitination of terminally misfolded proteins is caused by a cascade of enzymatic reactions. The first of these reactions takes place when the ubiquitin-activating enzyme E1 hydrolyses ATP and forms a high-energy thioester linkage between a cysteine residue in its active site and the C-terminus of ubiquitin. The resulting activated ubiquitin is then passed to E2, which is a ubiquitin-conjugating enzyme. Another group of enzymes, more specifically ubiquitin protein ligases called E3, bind to the misfolded protein.
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That works particularly well on cancer tumors, because tumors naturally absorb more ICG than other tissue. When ICG is injected near tumors, tumors react to the laser 2.5 times as much as the surrounding tissue does. It is also possible to target specific cells by conjugating the ICG to antibodies such as daclizumab (Dac), trastuzumab (Tra), or panitumumab (Pan). ICG and laser therapy has been shown to kill human pancreatic cancer cells (MIA PaCa-2, PANC-1, and BxPC-3) in vitro.
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The protein encoded by this gene is highly similar to S. cerevisiae DNA damage repair protein Rad18. Yeast Rad18 functions through interaction with Rad6, which is a ubiquitin-conjugating enzyme required for post-replication repair of damaged DNA. Similar to its yeast counterpart, this protein is able to interact with the human homolog of yeast Rad6 protein through a conserved ring finger motif. Mutation of this motif results in defective replication of UV-damaged DNA and hypersensitivity to multiple mutagens.
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The protein encoded by this gene contains a RING finger motif and an FHA domain. This protein has been shown to interact with several class II ubiquitin-conjugating enzymes (E2), including UBE2E1/UBCH6, UBE2E2, and UBE2E3, and may act as a ubiquitin ligase (E3) in the ubiquitination of certain nuclear proteins. Alternatively spliced transcript variants encoding distinct isoforms have been reported. RNF8 promotes repair of DNA damage through three DNA repair pathways: homologous recombinational repair (HRR), non-homologous end joining (NHEJ), and nucleotide excision repair (NER).
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The protein encoded by this gene contains a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein interacts with androgen receptor (AR) and may function as a coactivator that induces AR target gene expression in prostate. A dominant negative mutant of this gene has been demonstrated to inhibit the AR-mediated growth of prostate cancer. This protein also interacts with class III ubiquitin-conjugating enzymes (E2s) and may act as a ubiquitin-ligase (E3) in the ubiquitination of certain nuclear proteins.
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The Klingon language does not have a T-V distinction, with the second-person pronouns SoH (singular) and tlhIH (plural) and their appropriate conjugating verb prefixes covering all forms of address. However, Klingon does employ a number of honorifics, such as qaH (Sir or Madam) or joHwI' (my lord or my lady) to express formality. A honorific verb suffix -neS exists, used to express extreme politeness or deference towards a superior in a social or military hierarchy. It is rarely employed and never required.
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RBX1 is a core component of Cullin-RING ubiquitin ligase (CRL) complexes and functions to recruit E2 ubiquitin conjugating enzymes. Therefore, the C-terminus of CUL4A - along with RBX1 and activated E2 enzymes - compose the catalytic core of CRL4 complexes. CUL4A is also modified by covalent attachment of a NEDD8 molecule at a highly conserved lysine residue in the C-terminal region. This modification appears to induce conformational changes which promotes flexibility in the RING domain of cullin proteins and enhanced ubiquitin ligase activity.
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Schematic representation DUBs function DUBs play several roles in the ubiquitin pathway. One of the best characterised functions of DUBs is the removal of monoubiqutin and polyubiquitin chains from proteins. These modifications are a post translational modification (addition to a protein after it has been made) where single ubiquitin proteins or chains of ubiquitin are added to lysines of a substrate protein. These ubiquitin modifications are added to proteins by the ubiquitination machinery; ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s).
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Green algae conjugating Green algae are a group of photosynthetic, eukaryotic organisms that include species with haplobiontic and diplobiontic life cycles. The diplobiontic species, such as Ulva, follow a reproductive cycle called alternation of generations in which two multicellular forms, haploid and diploid, alternate, and these may or may not be isomorphic (having the same morphology). In haplobiontic species only the haploid generation, the gametophyte is multicellular. The fertilized egg cell, the diploid zygote, undergoes meiosis, giving rise to haploid cells which will become new gametophytes.
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The end result of this process is the addition of one ubiquitin molecule (monoubiquitylation) or a chain of ubiquitin molecules (polyubiquitination) to the substrate protein. Ubiquitination requires three types of enzyme: ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin ligases, known as E1s, E2s, and E3s, respectively. The process consists of three main steps: # Activation: Ubiquitin is activated in a two- step reaction by an E1 ubiquitin-activating enzyme, which is dependent on ATP. The initial step involves production of a ubiquitin-adenylate intermediate.
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Her fourth volume of poems, Geografija bližine (Geography of Closeness), appeared in 2000. In 2003, she published Spregatev milosti (Conjugating Mercy). This was followed by Obleganje sreče (Siege of Happiness, 2008), Pojdimo vezat kosti (Let's Go Tie Up Some Bones, 2010), and Kaj smo, ko smo (What We Are When We Are, 2015)of which the English translation was nominated for the Canadian Robert Kroetsch Award for Poetry 2019. Lipuš has received numerous prizes, and her poems have been translated into several other languages, including English, German, and Bulgarian.
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Parkin is a 465-residue E3 ubiquitin ligase that plays a critical role in ubiquitination- the process whereby molecules are covalently labelled with ubiquitin (Ub) and directed towards degradation in proteasomes or lysosomes. Ubiquitination involves the sequential action of three enzymes. First, an E1 ubiquitin-activating enzyme binds to inactive Ub in eukaryotic cells via a thioester bond and mobilises it in an ATP-dependent process. Ub is then transferred to an E2 ubiquitin-conjugating enzyme before being conjugated to the target protein via an E3 ubiquitin ligase.
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AKT-interacting protein is a protein that in humans is encoded by the AKTIP gene. The mouse homolog of this gene produces fused toes and thymic hyperplasia in heterozygous mutant animals while homozygous mutants die in early development. This gene may play a role in apoptosis as these morphological abnormalities are caused by altered patterns of programmed cell death. The protein encoded by this gene is similar to the ubiquitin ligase domain of other ubiquitin-conjugating enzymes but lacks the conserved cysteine residue that enables those enzymes to conjugate ubiquitin to the target protein.
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The folding reporter, a model protein for aggregation, was a Ubc9 (SUMO- conjugating enzyme) mutant (UBC9ts), harboring a missense mutation (Y68L) with a temperature- sensitive (ts) phenotype. The marginally stable Ubc9ts is fully functional under physiological permissive conditions (25 °C) due to active cellular chaperones. The GFP–Ubc9ts was transformed into yeast and visualized using a fluorescence microscope. Monitoring the folding sensor GFP–Ubc9ts was thought to indicate the cellular proteostasis, and to assay the ability of the cellular protein quality control system to deal with various kinds of stress.
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Conjugating TNP to ATP renders this nucleotide triphosphate fluorescent and colored whilst allowing it to retain its biological activity. TNP-ATP is thus a fluorescent analog of ATP. This conjugation is very useful in providing information about interactions between ATP and an ATP-binding protein because TNP-ATP interacts with proteins and enzymes as a substitute for its parent nucleotide, and has a strong binding affinity for most systems that require ATP. TNP is excited at a wavelength of 408 and 470 nm, and fluoresces in the 530–560 nm range.
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Under replication stress, for example a DNA polymerase mismatch error, USP20 disassociates from HERC2 and deubiquitinates claspin, stabilising it to then bind and activate Chk1. This allows for DNA replication to be paused and the error corrected. At the site of doubles stranded breaks, HERC2 facilitates the binding of RNF8, a RING finger ubiquitin ligase to the E2 ubiquitin-conjugating enzyme UBC13. This association is required for RNF8 mediated Lys-63 poly-ubiquitination signalling, which both recruits and retains repair factors at the site of DNA damage to commence homologous recombination repair.
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There is an important division of verbs into two main classes: volitional and non-volitional. The former concerns controllable actions, and the latter non-controllable actions. This difference is comparable to that in English between look and see, and between listen and hear: listen and look are volitional because one can choose to do them or not, while see and hear are non-volitional because they do not denote deliberate actions. These two classes are important when conjugating any Tibetan verb because each class can only use a particular set of suffixes.
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This protein also interacts with various protein kinases including IRAK1/IRAK, SRC and PKCzeta, which provides a link between distinct signaling pathways. This protein functions as a signal transducer in the NF-kappaB pathway that activates IkappaB kinase (IKK) in response to proinflammatory cytokines. The interaction of this protein with UBE2N/UBC13, and UBE2V1/UEV1A, which are ubiquitin conjugating enzymes catalyzing the formation of polyubiquitin chains, has been found to be required for IKK activation by this protein. Two alternatively spliced transcript variants encoding identical proteins have been reported.
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The future tense is formed by taking the present tense form of 'خواستن' (xāstan), to want, and conjugating it to the correct person; this verb in third person singular is 'خواهد' (xāhad). Next, it is put in front of the shortened infinitive of the verb, e.g. خورد (xord), thus خواهد خورد (xāhad xord) 'he/she/it will eat'. For compound verbs, such as تمیز کردن (tamiz kardan) 'to clean', خواهد goes in between both words, and کردن is reduced to its stem, thus تمیز خواهد کرد (tamiz xāhad kard) 'he/she/it will clean'.
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If is a finite group, then for any group element , the elements in the conjugacy class of are in one-to-one correspondence with cosets of the centralizer . This can be seen by observing that any two elements and belonging to the same coset (and hence, for some in the centralizer ) give rise to the same element when conjugating : . That can also be seen from the orbit-stabilizer theorem, when considering the group as acting on itself through conjugation, so that orbits are conjugacy classes and stabilizer subgroups are centralizers. The converse holds as well.
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Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin- homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s).
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Like other type II nuclear receptors, when activated, it forms a heterodimer with the retinoid X receptor, and binds to hormone response elements on DNA which elicits expression of gene products. One of the primary targets of PXR activation is the induction of CYP3A4, an important phase I oxidative enzyme that is responsible for the metabolism of many drugs. In addition, PXR up regulates the expression of phase II conjugating enzymes such as glutathione S-transferase and phase III transport uptake and efflux proteins such as OATP2 and MDR1.
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Affinity therapy, or immunotoxins is a biorecognition-based approach to selectively deliver a cytotoxic drug or toxin to a specific target cell. The field of affinity therapy was pioneered by Wilchek, together with Michael Sela, Ester Hurwitz, and Ruth Arnon. In 1975, they applied drug-conjugated antibodies for the targeted delivery of cytotoxic compounds to cancer cells. They also demonstrated the advantage of having a polymeric spacer between the antibody and the drug and showed the effectiveness of conjugating simple polymers such as dextran for drug delivery and targeting.
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E3 ubiquitin-protein ligase RNF216 is an enzyme that in humans is encoded by the RNF216 gene. This gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor- interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates.
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The interplay between ubiquitination and phosphorylation has been an ongoing research interest since phosphorylation often serves as a marker where ubiquitination leads to degradation. Moreover, ubiquitination can also act to turn on/off the kinase activity of a protein. The critical role of phosphorylation is largely underscored in the activation and removal of autoinhibition in Cbl protein. Cbl is an E3 ubiquitin ligase with a RING finger domain that interacts with its tyrosine kinase binding (TKB) domain, preventing interaction of the RING domain with an E2 ubiquitin-conjugating enzyme.
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Attachment of UBLs might, alter substrate conformation, affect the affinity for ligands or other interacting molecules, alter substrate localization, and influence protein stability. UBLs are structurally similar to ubiquitin and are processed, activated, conjugated, and released from conjugates by enzymatic steps that are similar to the corresponding mechanisms for ubiquitin. UBLs are also translated with C-terminal extensions that are processed to expose the invariant C-terminal LRGG. These modifiers have their own specific E1 (activating), E2 (conjugating) and E3 (ligating) enzymes that conjugate the UBLs to intracellular targets.
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In very rare cases, the F factor will be completely transferred and the F- cell will become an Hfr cell. If the F-plasmid that is transferred has previously been integrated into the donor's genome (producing an Hfr strain ["High Frequency of Recombination"]) some of the donor's chromosomal DNA may also be transferred with the plasmid DNA. The amount of chromosomal DNA that is transferred depends on how long the two conjugating bacteria remain in contact. In common laboratory strains of E. coli the transfer of the entire bacterial chromosome takes about 100 minutes.
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This gene encodes a protein that contains a domain with homology to the ancient conserved region of the archain 1 gene and a domain that may be involved in binding ubiquitin-conjugating enzymes. The protein encoded by this gene has been shown to bind to the conserved membrane- proximal sequence of the cytoplasmic tail of integrin alpha (IIb) subunits. These subunits play a crucial role in the integrin alpha (IIb) beta (3) inside-out signalling in platelets and megakaryocytes that leads to platelet aggregation and thrombus formation. This gene overlaps the gene for mitochondrial serine protease 25.
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In this process (which is also known as phase conjugation), light bounces exactly back in the direction from which it came due to a nonlinear optical process. Not only the direction of the light is reversed, but the actual wavefronts are reversed as well. A conjugate reflector can be used to remove aberrations from a beam by reflecting it and then passing the reflection through the aberrating optics a second time. If one were to look into a complex conjugating mirror, it would be black because only the photons which left the pupil would reach the pupil.
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A critical step in the pathway is the monoubiquitination of FANCD2 by the RING E3 ligase FANCL. FANCL comprises 3 domains, a RING domain that interacts with E2 conjugating enzymes, a central domain required for substrate interaction, and an N-terminal E2-like fold (ELF) domain that interacts with FANCB. The ELF domain of FANCL is also required to mediate a non-covalent interaction between FANCL and ubiquitin. The ELF domain is required to promote efficient DNA damage-induced FANCD2 monoubiquitination in vertebrate cells, suggesting an important function of FANCB and ubiquitin binding by FANCL in vivo.
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Dinocyst drawn by Ehrenberg in 1837 The first person to recognize fossil dinoflagellates was Christian Gottfried Ehrenberg, who reported his discovery in a paper presented to the Berlin Academy of Sciences in July 1836. He had observed clearly tabulate dinoflagellates in thin flakes of Cretaceous flint and considered those dinoflagellates to have been silicified. Along with them, and of comparable size, were spheroidal to ovoidal bodies bearing an array of spines or tubes of variable character. Ehrenberg interpreted these as being originally siliceous and thought them to be desmids (freshwater conjugating algae), placing them within his own Recent desmid genus Xanthidium.
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In some charophyte groups, such as the Zygnematophyceae or conjugating green algae, flagella are absent and sexual reproduction does not involve free-swimming flagellate sperm. Flagellate sperm, however, are found in stoneworts (Charales) and Coleochaetales, orders of parenchymatous charophytes that are the closest relatives of the land plants, where flagellate sperm are also present in all except the conifers and flowering plants. Fossil stoneworts of early Devonian age that are similar to those of the present day have been described from the Rhynie chert of Scotland.Somewhat different charophytes have also been collected from the Late Devonian (Famennian) Waterloo Farm lagerstätte of South Africa.
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A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that recruits an E2 ubiquitin-conjugating enzyme that has been loaded with ubiquitin, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. The ubiquitin is attached to a lysine on the target protein by an isopeptide bond. E3 ligases interact with both the target protein and the E2 enzyme, and so impart substrate specificity to the E2. Commonly, E3s polyubiquitinate their substrate with Lys48-linked chains of ubiquitin, targeting the substrate for destruction by the proteasome.
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Dog Latin, also known as Cod Latin, macaronic Latin, mock Latin, or Canis Latinicus,Canis Latinicus - Television Tropes and Idioms refers to the creation of a phrase or jargon in imitation of Latin,Dog-Latin, Bartleby.com often by "translating" English words (or those of other languages) into Latin by conjugating or declining them as if they were Latin words. Unlike the similarly named language game of Pig Latin (a form of playful spoken code), Dog Latin is more of a humorous device for invoking scholarly seriousness. Sometimes "dog Latin" can mean a poor-quality attempt at writing genuine Latin.
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Neonates are deficient in this conjugating system, making them particularly vulnerable to drugs such as chloramphenicol, which is inactivated by the addition of glucuronic acid, resulting in gray baby syndrome. Bilirubin is excreted in the bile as bilirubin diglucuronide (80%), bilirubin glucuronide (20%), and unconjugated bilirubin (< 1%). In the Crigler–Najjar syndrome and the Gilbert syndrome, UDPGT activity is reduced or nearly absent due to mutations, resulting in jaundice. It is possible to exhaust the bodies supply of glucuronic acid by combining multiple drugs/substances whose metabolism and excretion are primarily or entirely dependent on glucuronidation.
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If one allows taking the set of relators to any Nielsen equivalent set, and one allows conjugating the relators, then one gets an equivalence relation on ordered subsets of a relators of a finitely presented group. The Andrews–Curtis conjecture is that the relators of any balanced presentation of the trivial group are equivalent to a set of trivial relators, stating that each generator is the identity element. In the textbook , an application of Nielsen transformations is given to solve the generalized word problem for free groups, also known as the membership problem for subgroups given by finite generating sets in free groups.
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PML phosphorylation triggers further modification through the attachment of SUMO proteins to the RING domain by UBC9 SUMO- conjugating enzyme, which occurs in a cell cycle dependent way. PML contains a SUMO-binding domain necessary for its interaction with other SUMOylated proteins such as itself and many others. Both ubiquitination and SUMOylation of PML protein can trigger its degradation in the proteasome, thus providing a means of modulating PML protein lability within the cell. PML is translated in the cytoplasm of the cell, but its N-terminus contains a nuclear localization signal which causes its import to the nucleus.
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The NEDD4 protein has a modular structure that is shared among the NEDD4 family, consisting of an amino-terminal C2 calcium-dependent phospholipid binding domain, 3-4 WW protein-protein interaction domains, and a carboxyl-terminal catalytic HECT ubiquitin ligase domain. The C2 domain targets proteins to the phospholipid membrane, and can also be involved in targeting substrates. The WW domains interact with proline rich PPxY motifs in target proteins to mediate interactions with substrates and adaptors. The catalytic HECT domain forms a thioester bond with activated ubiquitin transferred from an E2 ubiquitin conjugating enzyme, before transferring ubiquitin directly to a specific substrate.
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Cullin 3-RING complex consists of Cullin 3 protein, RING-box protein 1 (RBX1), which recruits the ubiquitin-conjugating enzyme (E2), and a Bric-a- brac/Tramtrack/Broad (BTB) protein, a substrate recognition subunit. Cullin 3 protein is a core scaffold protein coordinating other components of the CRL complex. Cullin 3-RING complexes can also dimerise via their BTB domains which lead to creation of two substrate receptors and two catalytic RING domains. Activation of the complex is regulated by the attachment of the ubiquitin-like protein NEDD8 to a conserved Lys residue in the cullin-homology domain, the process called neddylation.
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The UBE2Z gene is ubiquitously expressed in human tissues, and its expression is relatively high in placenta, pancreas, spleen and testis. Notably, its expression in cancer tissues is much higher than in relevant normal tissues, especially in kidney, lymph node, colon and ovary cancer. As an E2 member of the ubiquitin-conjugating enzyme family, UBE2Z mainly participates in the second step of protein ubiquitination, which is a major component of protein degradation machinery. Specifically, UBE2Z receives ubiquitin (Ub) from ubiquitin-activating enzyme (E1), mediates the transfer of Ub from E2 to substrate, directly or indirectly with the help of ligase enzyme (E3), which interacts with the substrate and E2-Ub complex.
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The process of ubiquitination is a tightly regulated three- step sequence: activation, performed by ubiquitin-activating enzymes (E1); conjugation, performed by ubiquitin-conjugating enzymes (E2); and ligation, performed by ubiquitin ligases (E3). The result of this process is the formation of a covalent bond between the C-terminus of ubiquitin and a residue (typically a lysine) on the target protein. Many UBL families have a similar three-step process catalyzed by a distinct set of enzymes specific to that family. Deubiquitination or deconjugation - that is, removal of ubiquitin from a protein substrate - is performed by deubiquitinating enzymes (DUBs); UBLs can also be degraded through the action of ubiquitin-specific proteases (ULPs).
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Additionally, there are irregular verbs, such as ꠎꠣꠅꠀ (zaoa, to go) that change the first consonant in their stem in certain conjugations. Like many other Indo-Aryan languages (such as Bengali or Assamese), nouns can be turned into verbs by combining them with select auxiliary verbs. In Sylheti, the most common such auxiliary verb is ꠇꠞꠣ (xôra, to do); thus, verbs such as joke are formed by combining the noun form of joke (ꠓꠋ) with to do (ꠇꠞꠣ) to create ꠓꠋ ꠇꠞꠣ. When conjugating such verbs the noun part of such a verb is left untouched, so in the previous example, only ꠇꠞꠣ would be inflected or conjugated (e.g.
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Progression through the cell cycle is tightly regulated by cyclin-dependent kinases (CDKs), and their interactions with cyclins and CDK inhibitors (CKIs). Relative amounts of these signals oscillate during each stage of the cell cycle due to periodic proteolysis; the ubiquitin-proteasome system mediates the degradation of these mitotic regulatory proteins, controlling their intracellular concentrations. These and other proteins are recognized and degraded by the proteasome from the sequential action of three enzymes: E1 (ubiquitin-activating enzyme), one of many E2s (ubiquitin-conjugating enzyme), and one of many E3 ubiquitin ligase. The specificity of ubiquitination is provided by the E3 ligases; these ligases physically interact with the target substrates.
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Prior to secreting any of the bile acids (primary or secondary, see below), liver cells conjugate them with either glycine or taurine, to form a total of 8 possible conjugated bile acids. These conjugated bile acids are often referred to as bile salts. The pKa of the unconjugated bile acids are between 5 and 6.5, and the pH of the duodenum ranges between 3 and 5, so when unconjugated bile acids are in the duodenum, they are almost always protonated (HA form), which makes them relatively insoluble in water. Conjugating bile acids with amino acids lowers the pKa of the bile-acid/amino-acid conjugate to between 1 and 4.
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FePt NPs also provide a non-toxic, more persistent alternative to iodinated molecules that are harmful to the kidney and survive in the body for only a short time. The superparamagnetic properties of the nanoparticles and the systematic method for conjugating ligands to the FePt surface makes them viable vehicles for detection of pathogens such as gram-positive bacteria. Antibodies for the bacteria conjugated to the FePt NP bind to the bacteria and magnetic dipoles are used to detect the FePt NP-bacteria conjugate. By attaching peptides to the surface of the face-centered cubic FePt NPs, cytotoxic iron can be delivered to specific locations and taken up with high selectivity.
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Polymer streptavidin systems can also be empowered to cross the cellular membrane by conjugating with cell penetrating molecules such as peptides and membrane disturbing polymers. Polymer streptavidin systems can also be modulated to respond to certain environmental changes such as pH. By incorporating pH responsive poly(propylacrylic acid) (PPAAc) into the system, tumor cell suppressor p53 and cytochrome C can be delivered into cancer cells efficiently. For biomolecules that are not hampered by the biotin-streptavidin interaction, iminobiotin, an analogue of biotin, has been applied as a pH-sensitive linker that allows the controlled and reversible assembly and intracellular release of cargo molecules in acidic intracellular compartments.
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One of the primary roles of bacterial glutathione transferases is to reduce the toxic effects of xenobiotics from the cell using the phase II system of detoxification metabolism. Xenobiotics are compounds foreign to the bacterium’s natural biochemistry, and phase II of their detoxification involves conjugating them to polar, soluble compounds that can be safely excreted from the cell. GSTs are essential in this process because they catalyze the nucleophilic attack of glutathione on various electrophilic residues of xenobiotic substrates, thereby preventing their disruption of vital cellular proteins and nucleic acids. Similar to the mechanism GSTs use for catalyzation of redox reactions, the mechanism for detoxification first involves the binding of two substrates to the enzyme.
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By conjugating with cullin-3 ubiquitin ligase complex, KCTD7 may modulate the expression level of a negative regulator of potassium channel. Therefore, the overexpression of KCTD7 in neurons would increase the degradation of that regulatory molecule leading to the increase of potassium current through the cell membrane as observed in patch clamp experiments. In cultured mouse hippocampal cells, expression is found in the cell soma, in neuritic varicosities along the developing neuronal extensions, and in neurite growth cones, but not in the nucleus. Kctd7 is widely expressed in neurons throughout the intact mouse brain, including in cortical neurons, in granular and pyramidal cell layers of the hippocampus, and in cerebellar Purkinje cells.
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Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.
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From the political right, traditionalist conservative philosopher Russell Kirk criticized libertarianism by quoting T. S. Eliot's expression "chirping sectaries" to describe them. Kirk had questioned fusionism between libertarian and traditionalist conservatives that marked much of the post-war conservatism in the United States. Kirk stated that "although conservatives and libertarians share opposition to collectivism, the totalist state and bureaucracy, they have otherwise nothing in common" and called the libertarian movement "an ideological clique forever splitting into sects still smaller and odder, but rarely conjugating". Believing that a line of division exists between believers in "some sort of transcendent moral order" and "utilitarians admitting no transcendent sanctions for conduct", he included the libertarians in the latter category.
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Tirrell realized that the majority of the ways that such molecules were being presented was very haphazard and uncontrolled. His research group began to explore the idea of conjugating peptides to lipids in order to use the self- assembly character of lipids to direct a controlled presentation of peptides. This has led to current work in peptide amphiphile micelles, which are versatile, modular, biofunctional nanoparticles that can be injected into the circulation to target, image and, in some cases, treat pathological conditions. The Tirrell group has active work now in using such particles to diagnose and treat atherosclerosis, and also to stimulate the adaptive immune system to generate desired B-cell and T-cell responses.
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Through a multi-step process, free ubiquitin is first attached to an activating enzyme (E1) and then transferred to a conjugating enzyme (E2) which partners with a ligase (E3) which functions as an adaptor to selectively transfer the ubiquitin to specific protein substrates. Numb expression was found to selectively tag the membrane Notch1 receptor for ubiquitination through the interaction of its Phosphotyrosine- binding domain with the E3 ubiquitin ligase Itch. Numb and Itch work in concert to promote the ubiquitination of the full-length membrane-tethered Notch receptor prior to activation. However, Numb only appears to promote the degradation of the NICD cleavage product following receptor activation, targeting it for proteasome degradation and preventing its translocation to the nucleus.
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In Bengali, the most common such auxiliary verb is করা (kôra, to do); thus, verbs such as joke are formed by combining the noun form of joke (রসিকতা) with to do (করা) to create রসিকতা করা. When conjugating such verbs the noun part of such a verb is left untouched, so in the previous example, only করা would be inflected or conjugated (e.g.: "I will make a joke" becomes আমি রসিকতা করব; see more on tenses below). Other auxiliary verbs include দেওয়া and নেওয়া, but the verb করা enjoys significant usage because it can be combined with foreign verbs to form a native version of the verb, even if a direct translation exists.
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The addition of ubiquitin to a substrate protein is called ubiquitylation (or, alternatively, ubiquitination or ubiquitinylation). Ubiquitylation affects proteins in many ways: it can mark them for degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions. Ubiquitylation involves three main steps: activation, conjugation, and ligation, performed by ubiquitin- activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s), respectively. The result of this sequential cascade is to bind ubiquitin to lysine residues on the protein substrate via an isopeptide bond, cysteine residues through a thioester bond, serine and threonine residues through an ester bond, or the amino group of the protein's N-terminus via a peptide bond.
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Acetaminophen (3D structure) overdose is the most common cause of drug-induced liver disease Acetaminophen (in the US and Japan), paracetamol (INN), also known by the brand name Tylenol and Panadol, is usually well tolerated in prescribed dose, but overdose is the most common cause of drug-induced liver disease and acute liver failure worldwide. Damage to the liver is not due to the drug itself but to a toxic metabolite (N-acetyl-p-benzoquinone imine (NAPQI)) produced by cytochrome P-450 enzymes in the liver. In normal circumstances, this metabolite is detoxified by conjugating with glutathione in phase 2 reaction. In an overdose, a large amount of NAPQI is generated, which overwhelms the detoxification process and leads to liver cell damage.
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140 The result would be a reduction in weight and the amount of mechanical equipment in this inaccessible part of the locomotive. Holcroft’s valve gear design was also an attempt to address the problems associated with Gresley’s conjugated valve gear, which was prone to variations in valve events caused by heat expansion of the valve spindles within the pistons.Holcroft, (1946), pp. 145-147 The design utilised the motion of the outside valve rods (the rods transmitting the motion of the driving axles to the valves, such as the combination lever) instead, although the restricted space between the back of the outside cylinders and the front driving wheels made it impossible to locate the rocking arms controlling the conjugating mechanism in the vicinity.
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The chemistries of isopeptide bond formation are divided in the same manner as their biological roles. In the case of isopeptides used for conjugating one protein to another for the purpose of signal transduction, the literature is generally dominated by the very well-studied Ubiquitin protein and related proteins. While there are many related proteins to Ubiquitin, such as SUMO, Atg8, Atg12, and so on, they all tend to follow relatively the same protein ligation pathway. Therefore, the best example is to look at Ubiquitin, as while there can be certain differences, Ubiquitin is essentially the model followed in all these cases. The process essentially has three tiers, in the initial step, the activating protein generally denominated as E1 activates the Ubiquitin protein by adenylating it with ATP.
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"The Last Steam Locomotives of British Railways", Ransome-Wallis, P., Ian Allan, Shepperton, 1966 The main difficulty with this valve gear was that at high speeds, inertial forces caused the long conjugating lever to bend or "whip".Bill Harvey's 60 years in steam, Harvey, D.W. David & Charles. Newton Abbot, 1986 This had the effect of causing the middle cylinder to operate at a longer cutoff than the outer cylinders, therefore producing a disproportionate share of the total power output, leading to increased wear of the middle big end. Sustained high speed running could sometimes cause the big end to wear rapidly enough that the increased travel afforded to the middle piston by the increased play in the bearing was enough to knock the ends off the middle cylinder.
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Hyperconjugation is less important for species in which all atoms satisfy the octet rule, but a recent computational study supports hyperconjugation as the origin of the increased stability of alkenes with a higher degree of substitution (Zaitsev's rule). Homoconjugation is an overlap of two π-systems separated by a non-conjugating group, such as CH2. Unambiguous examples are comparatively rare in neutral systems, due to a comparatively minor energetic benefit that is easily overridden by a variety of other factors; however, they are common in cationic systems in which a large energetic benefit can be derived from delocalization of positive charge (see the article on homoaromaticity for details.).Some orbital overlap is possible even between bonds separated by one (or more) CH2 because the bonding electrons occupy orbitals which are quantum-mechanical functions and extend indefinitely in space.
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Like other members of the RING-between-RING (RBR) family of E3 ligases, parkin possesses two RING finger domains and an in-between-RING (IBR) region. RING1 forms the binding site for E2 Ub-conjugating enzyme while RING2 contains the catalytic cysteine residue (Cys431) that cleaves Ub off E2 and transiently binds it to E3 via a thioester bond. Ub transfer is aided by neighbouring residues histidine His433, which accepts a proton from Cys431 to activate it, and glutamate Glu444, which is involved in autoubiquitination. Together these form the catalytic triad, whose assembly is required for parkin activation. Parkin also contains an N-terminal Ub-like domain (Ubl) for specific substrate recognition, a unique RING0 domain and a repressor (REP) region that tonically suppresses ligase activity. Under resting conditions, the tightly coiled conformation of parkin renders it inactive, as access to the catalytic RING2 residue is sterically blocked by RING0, while the E2 binding domain on RING1 is occluded by Ubl and REP.
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Another aspect that distinguishes sortases in general is that they have a very specific targeting for their substrate, as sortases have generally two functions, the first is the fusing of proteins to the cell wall of the bacteria and the second is the polymerization of pilin. For the process of localization of proteins to the cell wall there is three-fold requirement that the protein contain a hydrophobic domain, a positively charged tail region, and final specific sequence used for recognition. The best studied of these signals is the LPXTG, which acts as the point of cleavage, where the sortase attacks in between Thr and Gly, conjugating to the Thr carboxyl group. Then the thioester is resolved by the transfer of the peptide to a primary amine, and this generally has a very high specificity, which is seen in the example of B. cereus where the sortase D enzyme helps to polymerize the BcpA protein via two recognition signals, the LPXTG as the cleavage and thioester forming point, and the YPKN site which acts as the recognition signal as where the isopeptide will form.
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A linear fractional transformation defined by a matrix from PSL(2,C) will preserve the Riemann sphere P1(C) = C ∪ ∞, but will send the upper-half plane H to some open disk Δ. Conjugating by such a transformation will send a discrete subgroup of PSL(2,R) to a discrete subgroup of PSL(2,C) preserving Δ. This motivates the following definition of a Fuchsian group. Let Γ ⊂ PSL(2,C) act invariantly on a proper, open disk Δ ⊂ C ∪ ∞, that is, Γ(Δ) = Δ. Then Γ is Fuchsian if and only if any of the following three equivalent properties hold: # Γ is a discrete group (with respect to the standard topology on PSL(2,C)). # Γ acts properly discontinuously at each point z ∈ Δ. # The set Δ is a subset of the region of discontinuity Ω(Γ) of Γ. That is, any one of these three can serve as a definition of a Fuchsian group, the others following as theorems. The notion of an invariant proper subset Δ is important; the so-called Picard group PSL(2,Z[i]) is discrete but does not preserve any disk in the Riemann sphere.
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SUMO attachment to its target is similar to that of ubiquitin (as it is for the other ubiquitin-like proteins such as NEDD 8). The SUMO precursor has some extra amino acids that need to be removed, therefore a C-terminal peptide is cleaved from the SUMO precursor by a protease (in human these are the SENP proteases or Ulp1 in yeast) to reveal a di-glycine motif. The obtained SUMO then becomes bound to an E1 enzyme (SUMO Activating Enzyme (SAE)) which is a heterodimer. It is then passed to an E2, which is a conjugating enzyme (Ubc9). Finally, one of a small number of E3 ligating proteins attaches it to the protein. In yeast, there are four SUMO E3 proteins, Cst9, Mms21, Siz1 and Siz2. While in ubiquitination an E3 is essential to add ubiquitin to its target, evidence suggests that the E2 is sufficient in SUMOylation as long as the consensus sequence is present. It is thought that the E3 ligase promotes the efficiency of SUMOylation and in some cases has been shown to direct SUMO conjugation onto non-consensus motifs.
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