Results 41 to 50 of about 381,302 (291)
Structural Insights into E1-Catalyzed Ubiquitin Activation and Transfer to Conjugating Enzymes [PDF]
Cell, 2008 Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific cascades involving three classes of enzymes, E1, E2, and E3. Each E1 adenylates the C terminus of its cognate Ubl, forms a E1 approximately Ubl thioester intermediate, and ultimately generates a thioester-linked E2 approximately Ubl product. We have determined
Lee, Imsang, Schindelin, Hermann
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VEXAS Syndrome: A Call for Diagnostic Awareness Based on a Case Series of Seven Patients
Acta Médica Portuguesa, 2023 N/a.
Filipe R. Pinto +4 more
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Journal of Medicinal Chemistry, 2021 SUMOylation is a reversible post-translational modification that regulates protein function through covalent attachment of small ubiquitin-like modifier (SUMO) proteins. The process of SUMOylating proteins involves an enzymatic cascade, the first step of
S. Langston +52 more
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In vitro Ubiquitin Dimer Formation Assay
Bio-Protocol, 2017 The process of protein ubiquitination typically consists of three sequential steps to add an ubiquitin (Ub) or Ub chain to a substrate protein, requiring three different enzymes, ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ...
Sheng Wang, Ling Cao, Hong Wang
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Ubiquitin enzymes in the regulation of immune responses
Critical reviews in biochemistry and molecular biology, 2017 Ubiquitination plays a central role in the regulation of various biological functions including immune responses. Ubiquitination is induced by a cascade of enzymatic reactions by E1 ubiquitin activating enzyme, E2 ubiquitin conjugating enzyme, and E3 ...
P. Ebner, Gijs A. Versteeg, Fumiyo Ikeda
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"Covalent affinity" purification of ubiquitin-activating enzyme.
Journal of Biological Chemistry, 1982 We have previously described an enzyme that activates ubiquitin, the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes (Ciechanover, A., Heller, H., Katz-Etzion, R., and Hershko, A. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 761-765). It carries out ubiquitin-dependent PPi-ATP and AMP-ATP exchange reactions and binds to
A, Ciechanover +3 more
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Frontiers in Endocrinology, 2023 Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like molecule (UBL) discovered almost two decades ago, but our knowledge about the cellular and molecular mechanisms of this novel protein post-translational modification is still very fragmentary.
Yun Cheng +3 more
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Insights in Post-Translational Modifications: Ubiquitin and SUMO
International Journal of Molecular Sciences, 2022 Both ubiquitination and SUMOylation are dynamic post-translational modifications that regulate thousands of target proteins to control virtually every cellular process.
D. Salas-Lloret, R. González-Prieto
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Mathematical model for the ubiquitin activating enzyme E1
Journal of Biomedical Science and Engineering, 2010 The ubiquitin-activating enzyme E1 (EC 6.3.2.19) represents the first step in the degradation of proteins by the ubiquitin proteasome pathway. E1 transfers ubiquitin from the ubiquitinated E1 to the ubiquitin carrier proteins (E2), ubiquitin-protein ligases (E3) and proteins. This process is rather complex, and known from the work of Haas, Ciechanover,
Francisco Javier López-Cánovas +3 more
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HyperISGylation of Old World monkey ISG15 in human cells. [PDF]
PLoS ONE, 2008 BACKGROUND: ISG15 is an Ubiquitin-like protein, highly induced by Type I Interferons. Upon the cooperative activity of specific Ubiquitinating enzymes, ISG15 can be conjugated to its substrates. Increasing evidence points to a role for protein ISGylation
Els Pattyn +8 more
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