Post-translational modification of the 26S proteasome subunits.
نویسندگان
چکیده
منابع مشابه
Impaired assembly and post-translational regulation of 26S proteasome in human end-stage heart failure.
BACKGROUND This study examined the hypothesis that 26S proteasome dysfunction in human end-stage heart failure is associated with decreased docking of the 19S regulatory particle to the 20S proteasome. Previous studies have demonstrated that 26S proteasome activity is diminished in human end-stage heart failure associated with oxidation of the 19S regulatory particle Rpt5 subunit. Docking of th...
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The proteasome is an essential proteolytic machine in eukaryotic cells, where it removes damaged proteins and regulates many cellular activities by degrading ubiquitinated proteins. Its heterohexameric AAA+ ATPase Rpt subunits play a central role in proteasome activity by the engagement of substrate unfolding and translocation for degradation; however, its detailed mechanism remains poorly unde...
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Post-translational modifications (PTMs) have been recognized to impact protein function in two ways: (i) orthosterically, via direct recognition by protein domains or through interference with binding; and (ii) allosterically, via conformational changes induced at the functional sites. Because different chemical types of PTMs elicit different structural alterations, the effects of combinatorial...
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Post-translational modifications (PTMs) are chemical alterations to a protein following translation, regulating stability and function. Reversible phosphorylation is an example of an important and well studied PTM involved in a number of cellular processes. SUMOylation is another PTM known to modify a large number of proteins and plays a role in various cellular processes including: cell cycle ...
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A new global post-translational modification (PTM) discovery strategy, G-PTM-D, is described. A proteomics database containing UniProt-curated PTM information is supplemented with potential new modification types and sites discovered from a first-round search of mass spectrometry data with ultrawide precursor mass tolerance. A second-round search employing the supplemented database conducted wi...
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ژورنال
عنوان ژورنال: SEIBUTSU BUTSURI KAGAKU
سال: 2003
ISSN: 0031-9082,1349-9785
DOI: 10.2198/sbk.47.143