Results 71 to 80 of about 29,730 (229)

Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes

open access: yes
Chromatin regulation relies on “writer” enzymes that add posttranslational modifications to histone proteins. Variant polycomb repressive complex 1 (PRC1) exists as several subtypes, which are “writers” of ubiquitylation on histone H2A K118 and K119 ...
Fierz, Beat, Teslenko, Alexandra
core   +1 more source

Efficient monitoring of protein ubiquitylation levels using TUBEs-based microarrays

open access: yes, 2016
International audienceAnalyzing protein ubiquitylation changes during physiological or pathological processes is challenging due to its high reversibility and dynamic turnover of modified targets.
Reichardt, Niels   +6 more
core   +1 more source

An Ensemble Deep Learning based Predictor for Simultaneously Identifying Protein Ubiquitylation and SUMOylation Sites

open access: yesBMC Bioinformatics, 2021
Background Several computational tools for predicting protein Ubiquitylation and SUMOylation sites have been proposed to study their regulatory roles in gene location, gene expression, and genome replication.
Fei He   +4 more
doaj   +1 more source

Metabolic Dysfunction‐Associated Steatotic Liver Disease and Obesity: Pathogenesis, Diagnostics, Risk Stratification, and Therapeutic Approach

open access: yesThe Kaohsiung Journal of Medical Sciences, EarlyView.
ABSTRACT Metabolic dysfunction‐associated steatotic liver disease (MASLD) has emerged as the most prevalent chronic liver disease worldwide, closely linked to the global rising incidence of obesity and metabolic syndrome. This review synthesizes current evidence on the pathogenesis, gut–liver axis, and multidisciplinary management of MASLD within the ...
Beom Kyung Kim
wiley   +1 more source

Oligomerization-driven MLKL ubiquitylation antagonizes necroptosis

open access: yes, 2021
Mixed lineage kinase domain-like (MLKL) is the executioner in the caspase-independent form of programmed cell death called necroptosis. Receptor-interacting serine/threonine protein kinase 3 (RIPK3) phosphorylates MLKL, triggering MLKL oligomerization ...
Wang, X   +16 more
core   +1 more source

Mitofusins: ubiquitylation promotes fusion [PDF]

open access: yesCell Research, 2014
Mitochondrial genes including Mfn2 are at the center of many diseases, underscoring their potential as a therapeutical target. The Chen group now identified 15-oxospiramilactone as a chemical inhibitor of the mammalian deubiquitylase USP30, acting on Mfn1 and Mfn2.
openaire   +2 more sources

Macromolecular juggling by ubiquitylation enzymes [PDF]

open access: yesBMC Biology, 2013
Abstract The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes. Members of the E1 and E3 enzyme families can undergo particularly large conformational changes during their catalytic cycles, involving the remodeling of domain ...
Lorenz, Sonja   +3 more
openaire   +5 more sources

The EF-hand domain of MINDY3 is a ubiquitin and RAD23 UBL-binding domain

open access: yesEMBO Reports
The MINDY family of deubiquitinases (DUBs) are exemplified by their preference for cleaving K48-linked polyubiquitin. MINDY3 is architecturally distinct from other MINDY DUBs as its catalytic domain spans the entire length of the protein except for an ...
Lee A Armstrong   +7 more
doaj   +1 more source

Regulation of DNA repair by ubiquitylation

open access: yesBiochemistry (Moscow), 2011
Cellular DNA repair is a frontline system that is responsible for maintaining genome integrity and thus preventing premature aging and cancer by repairing DNA lesions and strand breaks caused by endogenous and exogenous mutagens. However, it is also the principal cellular system in cancer cells that counteracts the killing effect of the major cancer ...
Dianov, G, Meisenberg, C, Parsons, J
openaire   +2 more sources

Elmo1 inhibits ubiquitylation of Dock180 [PDF]

open access: yesJournal of Cell Science, 2006
Dock180, a member of the CDM family of proteins, plays roles in biological processes such as phagocytosis and motility through its association with the signalling adaptor protein Crk. Recently, the complex formation between Dock180 and Elmo1 was reported to function as a bipartite guanine nucleotide exchange factor for Rac.
Yoshinori, Makino   +8 more
openaire   +2 more sources

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