Results 31 to 40 of about 59,068 (260)
Nature Communications, 2023 UBA1 is the primary E1 ubiquitin-activating enzyme responsible for generation of activated ubiquitin required for ubiquitination, a process that regulates stability and function of numerous proteins.
Wenjing Yan +17 more
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An Essential Yeast Gene Encoding a Homolog of Ubiquitin-activating Enzyme [PDF]
Journal of Biological Chemistry, 1995 Ubiquitin (Ub) activation by the Ub-activating (E1) enzyme is the initial and essential step common to all of the known processes that involve post-translational conjugation of Ub to itself or other proteins. The "activated" Ub, linked via a thioester bond to a specific cysteine residue in one of several Ub-conjugating (E2) enzymes, which catalyze the ...
Dohmen, R. Jürgen +6 more
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In vitro Di-ubiquitin Formation Assay and E3 Cooperation Assay
Bio-Protocol, 2022 Ubiquitination is a post-translational modification conserved across eukaryotic species. It contributes to a variety of regulatory pathways, including proteasomal degradation, DNA repair, and cellular differentiation.
Rebecca Burge +3 more
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Proteasome inhibitors: new class of antitumor agents
Biomolecules & Biomedicine, 2003 The ubiquitin-proteasome pathway is the principal pathway for intracellular protein degradation1,2 (Fig 1). This pathway selectively degrades an extensive number of short-lived regulatory proteins involved in the control of normal cellular processes. In
Gordan Srkalović
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Pleiotropic Effects of ATP·Mg2+ Binding in the Catalytic Cycle of Ubiquitin-activating Enzyme [PDF]
Journal of Biological Chemistry, 2006 Conjugation of ubiquitin and other Class 1 ubiquitin-like polypeptides to specific protein targets serves diverse regulatory functions in eukaryotes. The obligatory first step of conjugation requires ATP-coupled activation of the ubiquitin-like protein by members of a superfamily of evolutionarily related enzymes. Kinetic and equilibrium studies of the
Zeynep, Tokgöz +2 more
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Incorporating distant sequence features and radial basis function networks to identify ubiquitin conjugation sites. [PDF]
PLoS ONE, 2011 Ubiquitin (Ub) is a small protein that consists of 76 amino acids about 8.5 kDa. In ubiquitin conjugation, the ubiquitin is majorly conjugated on the lysine residue of protein by Ub-ligating (E3) enzymes.
Tzong-Yi Lee +3 more
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Life Science Alliance, 2021 This study shows that ubiquitin conjugates associate with various types of stress granules and that an active ubiquitin system is required for the efficient clearance of some types of stress granules.
Nazife Tolay, Alexander Buchberger
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Isoforms of mammalian ubiquitin-activating enzyme.
Journal of Biological Chemistry, 1992 Ubiquitin-activating enzyme, "E1," is the first enzyme in the pathway leading to formation of ubiquitin-protein conjugates and represents a potential target for regulation in the metabolic control of the conjugation reaction. Antiserum raised against human E1 recognizes two immunoreactive proteins in extracts from several human cell lines and animal ...
J C, Cook, P B, Chock
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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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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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