Results 201 to 210 of about 29,730 (229)
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H2B ubiquitylation and de-ubiquitylation in gene activation.
Novartis Foundation symposium, 2004Previous models for the role of histone modifications suggest that adding and removing modifications, such as acetylation/deacetylation in gene regulation, are functionally antagonistic. We have investigated a transcriptional role of H2B C-terminal ubiquitylation and de-ubiquitylation in Saccharomyces cerevisiae.
Anastasia, Wyce +2 more
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Regulation of DNA repair by ubiquitylation
Nature Reviews Molecular Cell Biology, 2006The process of ubiquitylation is best known for its role in targeting proteins for degradation by the proteasome. However, recent studies of DNA-repair and DNA-damage-response pathways have significantly broadened the scope of the role of ubiquitylation to include non-proteolytic functions of ubiquitin.
Tony T, Huang, Alan D, D'Andrea
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Ubiquitylation in innate and adaptive immunity
Nature, 2009Protein ubiquitylation has emerged as a key mechanism that regulates immune responses. Much like phosphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, activity and localization of target proteins. As such, ubiquitylation regulates the development of the immune system and many phases of the immune response ...
Vijay G, Bhoj, Zhijian J, Chen
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Proteasomal recognition of ubiquitylated substrates
Trends in Plant Science, 2010Ubiquitin/26S proteasome-mediated proteolysis controls the half-life of numerous critical regulatory proteins and is an intimate regulatory component for nearly all aspects of cellular processes. In addition to ubiquitin conjugation, an additional level of substrate specificity is regulated at the step of proteasomal recognition of ubiquitylated ...
Hongyong, Fu +2 more
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Analysis of Chaperone-Assisted Ubiquitylation
2012Molecular 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 +2 more
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Histone Ubiquitylation and the Regulation of Transcription
2006The small (76 amino acids) and highly conserved ubiquitin protein plays key roles in the physiology of eukaryotic cells. Protein ubiquitylation has emerged as one of the most important intracellular signaling mechanisms, and in 2004 the Nobel Prize was awarded to Aaron Ciechanower, Avram Hersko, and Irwin Rose for their pioneering studies of the ...
Mary Ann, Osley +2 more
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H2B ubiquitylation: the end is in sight
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2004Historically, the first eukaryotic protein found to be modified by ubiquitin was H2A, originally isolated from HeLa cells in 1975 by Harrison Busch and coworkers as a histone-like, nonhistone chromosomal protein called A24. Ubiquitylated histones have subsequently been found in many eukaryotic species, and to date, the core histones H2A, H2B, H3, the ...
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Detection of Ubiquitylated Proteins in Yeast
Cold Spring Harbor Protocols, 2006INTRODUCTIONThis assay is performed to detect ubiquitylated proteins in yeast. Yeast that have been transformed with a vector expressing polyhistidine-tagged ubiquitin (Ub) under the control of a copper-inducible promoter are grown, induced with copper, and harvested.
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Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection
Nature, 2021Balaji Santhanam +2 more
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