Results 41 to 50 of about 540 (119)
Ubiquitin proteomics identifies RNA polymerase I as a target of the Smc5/6 complex
Cell Reports, 2023 Summary: Ubiquitination controls numerous cellular processes, and its deregulation is associated with many pathologies. The Nse1 subunit in the Smc5/6 complex contains a RING domain with ubiquitin E3 ligase activity and essential functions in genome ...
Eva Ibars +10 more
doaj +1 more source
Mass Spectrometry Reviews, Volume 42, Issue 6, Page 2324-2348, November/December 2023., 2023 Abstract The data‐independent acquisition mass spectrometry (DIA‐MS) has rapidly evolved as a powerful alternative for highly reproducible proteome profiling with a unique strength of generating permanent digital maps for retrospective analysis of biological systems.
Reta Birhanu Kitata +2 more
wiley +1 more source
Engineering, 2020 Primary hepatocytes (PHCs) are widely used in various fields, but the progressive deterioration of liver-specific features in vitro significantly limits their application.
Zhengyi Jiang +9 more
doaj +1 more source
MedComm, Volume 4, Issue 3, June 2023., 2023 The reversible and irreversible protein posttranslational modifications, such as acetylation, methylation, phosphorylation, ubiquitination, glycosylation, SUMOylation, and redox modifications, are essential regulators in organisms and cells. This work systematically summarizes the features, regulatory mechanisms, substrates, functions, and related ...
Qian Zhong +10 more
wiley +1 more source
Cells, 2020 Ubiquitination regulates several biological processes, however the role of specific members of the ubiquitinome on intracellular membrane trafficking is not yet fully understood.
Hianara A Bustamante +16 more
doaj +1 more source
Ubiquitous Ubiquitin: The K63 Ubiquitinome [PDF]
The Plant Cell, 2019 Polyubiquitination, the sequential attachment of the small 8 kDa globular protein ubiquitin (Ub) to target proteins, represents a major posttranslational modification that ultimately determines the substrate’s cellular fate. Ub conjugation is an extremely versatile form of protein regulation,
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Detection of the Ubiquitinome in Cells Undergoing Oncogene-Induced Senescence [PDF]
, 2016 Senescent cells exhibit dramatic changes in protein post-translational modifications. Here, we describe a method, stable isotope labeling with amino acids in cell culture (SILAC) coupled to liquid chromatography tandem mass spectrometry (LC-MS/MS), to identify changes in the ubiquitinome in cells that have undergone oncogene-induced senescence.
Hengrui, Zhu +4 more
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The FASEB Journal, Volume 35, Issue 9, September 2021., 2021 Abstract Ubiquitination is an essential post‐translational modification that regulates protein stability or function. Its substrate specificity is dictated by various E3 ligases. The human C‐terminal to LisH (CTLH) complex is a newly discovered multi‐subunit really interesting new gene (RING) E3 ligase with only a few known ubiquitination targets. Here,
Matthew E. R. Maitland +4 more
wiley +1 more source
Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress [PDF]
Journal of Proteome Research, 2018 During oxidative stress, K63-linked polyubiquitin chains modify a variety of proteins including ribosomes. Knowledge of the precise sites of K63 ubiquitin is key to understand its function during the response to stress. To identify the sites of K63 ubiquitin, we developed a new mass spectrometry based method that quantified >1100 K63 ubiquitination ...
Songhee Back +3 more
openaire +2 more sources
Molecular & Cellular Proteomics, 2023 Ubiquitination has crucial roles in many cellular processes, and dysregulation of ubiquitin machinery enzymes can result in various forms of pathogenesis. Cells only have a limited set of ubiquitin-conjugating (E2) enzymes to support the ubiquitination of many cellular targets.
Zeliha Yalçin +10 more
openaire +7 more sources