Results 91 to 100 of about 28,143 (190)

Drosophila IAP1-mediated ubiquitylation controls activation of the initiator caspase DRONC independent of protein degradation.

open access: yesPLoS Genetics, 2011
Ubiquitylation targets proteins for proteasome-mediated degradation and plays important roles in many biological processes including apoptosis. However, non-proteolytic functions of ubiquitylation are also known. In Drosophila, the inhibitor of apoptosis
Tom V Lee   +6 more
doaj   +1 more source

Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast Cells.: Probing interactions of ubiquitylation enzymes in living cells

open access: yes, 2016
International audienceUbiquitylation is a versatile posttranslational protein modification catalyzed through the concerted action of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s).
Ewa Blaszczak   +5 more
core   +1 more source

NUP85 Mediates Endoplasmic Reticulum Stress through the USP47/ASK1 Signaling Pathway to Regulate the Progression of Liver Fibrosis

open access: yesAdvanced Science, Volume 13, Issue 33, 15 June 2026.
In the present study, we have demonstrated that the NUP85‐USP47‐ASK1 signaling pathway may have regulated the progression of liver fibrosis through modulating ERS. Additionally, we have developed a CREKA‐coupled liposome to target delivery of MV, a pharmacological inhibitor of NUP85, to activated HSCs, thereby attenuating liver fibrosis. ABSTRACT Liver
Dashuai Yang   +11 more
wiley   +1 more source

Localization-Dependent and -Independent Roles of SLX4 in Regulating Telomeres

open access: yesCell Reports, 2013
SLX4, a scaffold for structure-specific DNA repair nucleases, is important for several types of DNA repair. Many repair proteins bind to sites of DNA damage, resulting in subnuclear “foci,” but SLX4 forms foci in human cells even without DNA damage ...
Jamie S.J. Wilson   +5 more
doaj   +1 more source

Auto-ubiquitylation of LsRING.

open access: yes
E3 ubiquitin ligase activity of purified recombinant LsRING by auto-ubiquitylation. (TIF)
Yao Li (154923)   +5 more
core   +1 more source

Prediction of Lysine Ubiquitylation with Ensemble Classifier and Feature Selection

open access: yes, 2011
Ubiquitylation is an important process of post-translational modification. Correct identification of protein lysine ubiquitylation sites is of fundamental importance to understand the molecular mechanism of lysine ubiquitylation in biological systems ...
Xiaowei Zhao   +3 more
core   +1 more source

PRMT5/Sohlh2/Sirt1 Signaling Pathway in Vascular Endothelial Cells Modulates Lung Metastasis of Triple‐Negative Breast Cancer

open access: yesAdvanced Science, Volume 13, Issue 31, 4 June 2026.
The cover image shows that vascular endothelial cells play an important role in lung metastasis of TNBC. Endothelial Sohlh2 acts as a gatekeeper against TNBC lung metastasis by limiting endothelial activation and tumor cell passage. PRMT5 reduces Sohlh2 stability, weakening this protective barrier.
Ruihong Zhang   +8 more
wiley   +1 more source

UCHL3 Regulates Topoisomerase-Induced Chromosomal Break Repair by Controlling TDP1 Proteostasis

open access: yesCell Reports, 2018
Summary: Genomic damage can feature DNA-protein crosslinks whereby their acute accumulation is utilized to treat cancer and progressive accumulation causes neurodegeneration.
Chunyan Liao   +9 more
doaj   +1 more source

The Polymers of Life: Exploring Cellular Function Through Polymer Concepts

open access: yesAdvanced Science, Volume 13, Issue 33, 15 June 2026.
Biomolecular phase separation reveals that a hidden layer of cellular organization is governed by the principles of polymer science. This review bridges polymer physics and cell biology, offering a primer on fundamental concepts, proposing a framework for interrogating cellular function, and synthesizing biophysical methods for decoding macromolecular ...
Mark Chen, Ashutosh Chilkoti
wiley   +1 more source

Proteomic analyses reveal divergent ubiquitylation site patterns in murinetissues

open access: yes, 2012
Posttranslational modifications of proteins increase the complexity of the cellular proteome andenable rapid regulation of protein functions in response to environmental changes.
Olsen, Jesper V   +9 more
core   +1 more source

Home - About - Disclaimer - Privacy