Results 221 to 230 of about 39,029 (256)
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Annual Review of Biochemistry, 2012
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds.
David, Komander, Michael, Rape
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The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds.
David, Komander, Michael, Rape
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Proteomic insights into ubiquitin and ubiquitin-like proteins
Current Opinion in Chemical Biology, 2005The dynamic and specific modification of cellular proteins by members of the ubiquitin protein family is a vital regulatory mechanism that lies at the heart of almost all biological processes. Because of both their pervasive and complex nature, these regulatory pathways have been the target of many recent proteomic studies.
Carilee, Denison +2 more
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The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
Trends in Biochemical Sciences, 2017The conjugation of the 76 amino acid protein ubiquitin to other proteins can alter the metabolic stability or non-proteolytic functions of the substrate. Once attached to a substrate (monoubiquitination), ubiquitin can itself be ubiquitinated on any of its seven lysine (Lys) residues or its N-terminal methionine (Met1).
Yong Tae, Kwon, Aaron, Ciechanover
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Trends in Biochemical Sciences, 1997
Eukaryotes contain a highly conserved multi-enzyme system that covalently links ubiquitin to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, a large ATP-dependent protease.
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Eukaryotes contain a highly conserved multi-enzyme system that covalently links ubiquitin to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, a large ATP-dependent protease.
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Ubiquitin and ubiquitin-like proteins as multifunctional signals
Nature Reviews Molecular Cell Biology, 2005Protein ubiquitylation is a recognized signal for protein degradation. However, it is increasingly realized that ubiquitin conjugation to proteins can be used for many other purposes. Furthermore, there are many ubiquitin-like proteins that control the activities of proteins.
Rebecca L, Welchman +2 more
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Trends in Biochemical Sciences, 2000
The ubiquitin-proteasome system fulfills an essential function in eukaryotes by controlling the levels of crucial intracellular regulatory proteins. In this system, a specific type of polyubiquitin chain acts as the proximal signal for targeting substrates to 26S proteasomes for degradation.
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The ubiquitin-proteasome system fulfills an essential function in eukaryotes by controlling the levels of crucial intracellular regulatory proteins. In this system, a specific type of polyubiquitin chain acts as the proximal signal for targeting substrates to 26S proteasomes for degradation.
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Ubiquitin adenylate: structure and role in ubiquitin activation
Biochemistry, 1983The acid precipitate of the ubiquitin activating enzyme after reaction with ATP and ubiquitin contains one enzyme equivalent of ubiquitin adenylate in which the carboxyl-terminal glycine of ubiquitin and AMP are in an acyl-phosphate linkage. The recovered ubiquitin adenylate has the catalytic properties proposed for it as a reaction intermediate. Thus,
A L, Haas, J V, Warms, I A, Rose
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Emerging Role of Ubiquitination in the Regulation of PD-1/PD-L1 in Cancer Immunotherapy
Molecular Therapy, 2021Zhi-Wei Wang, Xueqiong Zhu
exaly
K63 Ubiquitination in Immune Signaling
Trends in Immunology, 2022Charitha Madiraju, Shu-Ichi Matsuzawa
exaly