Results 191 to 200 of about 29,730 (229)

Structural basis of ubiquitylation

Current Opinion in Structural Biology, 2002
The attachment of the small protein ubiquitin to other proteins, a process known as ubiquitylation, is a widespread form of post-translational modification that regulates numerous cellular functions in eukaryotes. Ubiquitylation is performed by complexes of E2 and E3 enzymes that are assembled and select substrates via a series of protein-protein ...
Christopher P Hill, Andrew P. VanDemark
exaly   +3 more sources

Prediction of Lysine Ubiquitylation with Ensemble Classifier and Feature Selection

International Journal of Molecular Sciences, 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 ...
Xiangtao Li, Minghao Yin, Xiaowei Zhao
exaly   +2 more sources

Ubiquitylation at the crossroads of development and disease

Nature Reviews Molecular Cell Biology, 2017
Human development requires intricate cell specification and communication pathways that allow an embryo to generate and appropriately connect more than 200 different cell types. Key to the successful completion of this differentiation programme is the quantitative and reversible regulation of core signalling networks, and post-translational ...
Michael Rape
exaly   +3 more sources

IAPs, RINGs and ubiquitylation

Nature Reviews Molecular Cell Biology, 2005
The inhibitor of apoptosis (IAP) proteins all contain one or more baculoviral IAP repeat motifs, through which they interact with various other proteins. Many IAPs also have another zinc-binding motif, the RING domain, which can recruit E2 ubiquitin-conjugating enzymes and catalyse the transfer of ubiquitin onto target proteins.
Vaux, David L., Silke, John.
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Protein Ubiquitylation and Synaptic Function

Annals of the New York Academy of Sciences, 2003
Abstract: Conjugation of ubiquitin to proteins is a well‐established signal to regulate an ever expanding range of cellular processes. Here, we discuss recent findings that deeply link ubiquitin signaling to synaptic activity.
O. Cremona, COLLESI, CHIARA, E. Raiteri
openaire   +4 more sources

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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Balancing act: To be, or not to be ubiquitylated

Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis, 2017
DNA double-strand breaks (DSBs) are one of the most deleterious DNA lesions. Appropriate repair of DSB either by homologous recombination or non-homologous end-joining is critical for maintaining genome stability and fitness. DSB repair cooperates with cellular signalling networks, namely DSB response (DDR), which plays pivotal roles in the choice of ...
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Global, site-resolved analysis of ubiquitylation occupancy and turnover rate reveals systems properties

Cell
Ubiquitylation regulates most proteins and biological processes in a eukaryotic cell. However, the site-specific occupancy (stoichiometry) and turnover rate of ubiquitylation have not been quantified.
Shankha Satpathy, Chunaram Choudhary, Brian T Weinert   +2 more
exaly   +2 more sources

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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Serine ubiquitylation

Science Signaling, 2016
A bacterial effector protein ubiquitylates host proteins through a mechanism that is independent of and blocks the host ubiquitylation machinery.
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