Results 161 to 170 of about 23,719 (175)

Ubiquitylation in the ERAD Pathway

2010
Ubiquitylation is a protein modification mechanism, which is found in a multitude of cellular processes like DNA repair and replication, cell signaling, intracellular trafficking and also, very prominently, in selective protein degradation. One specific protein degradation event in the cell concerns the elimination of misfolded proteins to prevent ...
Frederik, Eisele, Antje, Schäfer, Dieter H, Wolf   +2 more
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Analysis of Chaperone-Assisted Ubiquitylation

2012
Molecular chaperones are traditionally viewed as cellular protein folding and assembly factors. However, in recent years it became more and more evident that certain chaperones, i.e., members of the 70-kDa heat shock protein family (Hsp70s), participate very actively in protein degradation and in this way significantly contribute to protein homeostasis.
Michael, Dreiseidler, Niko, Dick, Jörg, Höhfeld   +2 more
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Nonenzymatic Ubiquitylation

ChemBioChem, 2010
Tomasz, Fekner, Xin, Li, Michael K, Chan
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Themes and variations on ubiquitylation

Nature Reviews Molecular Cell Biology, 2001
Ubiquitylation--the conjugation of proteins with a small protein called ubiquitin--touches upon all aspects of eukaryotic biology, and its defective regulation is manifest in diseases that range from developmental abnormalities and autoimmunity to neurodegenerative diseases and cancer.
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Histone Ubiquitylation by Mdm2

Science's STKE, 2004
The Mdm2 oncoprotein is a critical inhibitor of the p53 tumor suppressor protein and apparently does so through multiple mechanisms. Mdm2 is an E3 ubiquitin ligase that ubiquitylates p53, thus targeting p53 for degradation by the proteasome. Mdm2 also directly binds the transactivation domain of p53 and interacts with the histone deactylase HDAC1 and ...
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Semisynthesis of ubiquitylated proteins.

Methods in enzymology, 2009
Most, if not all, proteins are at one point or another posttranslationally modified so as to regulate their biological function. One of the most common protein modifications is ubiquitylation, in which the small protein ubiquitin is attached to a target protein in a multistep process involving dedicated ubiquitin ligases.
Robert K, McGinty, Champak, Chatterjee, Tom W, Muir   +2 more
openaire   +1 more source

Ubiquitylation block

Nature Reviews Cancer, 2013
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Ubiquitylation

2013
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Ubiquitylation

2011
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Regulatory ribosomal ubiquitylation

Nature Reviews Molecular Cell Biology, 2015
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