Results 171 to 180 of about 133,567 (215)

GRAIL1 Stabilizes Misfolded Mutant p53 through a Ubiquitin Ligase-Independent, Chaperone Regulatory Function. [PDF]

open access: yesMol Cancer Res
Ray P   +16 more
europepmc   +1 more source

The Nedd4L ubiquitin ligase is activated by FCHO2-generated membrane curvature. [PDF]

open access: yesEMBO J
Sakamoto Y   +7 more
europepmc   +1 more source

E3 ubiquitin ligase CHIP facilitates cAMP and cGMP signalling cross-talk by polyubiquitinating PDE9A. [PDF]

open access: yesEMBO J
Hao X   +24 more
europepmc   +1 more source

A giant ubiquitin ligase [PDF]

open access: possibleNature Chemical Biology, 2021
The structure of a giant ubiquitin E3 ligase sheds light on its activation in a substrate-dependent manner and shows how a single E3 enzyme uses distinct recognition modules to confer substrate specificity.
openaire   +2 more sources
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On ubiquitin ligases and cancer

Human Mutation, 2005
Protein kinase genes account for almost 10% of all currently known cancer genes, highlighting the role of signal transduction in oncogenesis. A reexamination of the literature and available databases shows that E3 ubiquitin ligases are also key mediators of tumorigenesis. Altogether kinase and E3 genes represent more than 15% of the known cancer genes,
Laurent Falquet   +3 more
openaire   +3 more sources

E3 ubiquitin ligases

Essays in Biochemistry, 2005
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C. Ardley, Philip A. Robinson
openaire   +3 more sources

Ubiquitin ligases: guardians of mammalian development

Nature Reviews Molecular Cell Biology, 2022
Mammalian development demands precision. Millions of molecules must be properly located in temporal order, and their function regulated, to orchestrate important steps in cell cycle progression, apoptosis, migration and differentiation, to shape developing embryos.
David A. Cruz Walma   +3 more
openaire   +2 more sources

Ubiquitin Ligases in Malignant Lymphoma

Leukemia & Lymphoma, 2004
The highly controlled degradation of proteins via the ubiquitin-proteasome pathway represents a key mechanism for cell regulation and homeostasis. Ubiquitin-dependent proteolysis, carried out in large part by the E3 ubiquitin ligases, is a critical mode of post-translational modification that is important in regulation of cell cycle progression, signal
Megan S. Lim   +1 more
openaire   +3 more sources

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