Results 181 to 190 of about 29,696 (227)
Some of the next articles are maybe not open access.
2010
Sumoylation, the covalent attachment of SUMO peptide to cellular proteins, is an essential regulator of protein function involved in a wide range of cellular events. Deregulation of the SUMO pathway is implicated in the pathogenesis of several diseases, so it is important to understand how this system is controlled.
Maderböck, K., Pichler, A.
openaire +3 more sources
Sumoylation, the covalent attachment of SUMO peptide to cellular proteins, is an essential regulator of protein function involved in a wide range of cellular events. Deregulation of the SUMO pathway is implicated in the pathogenesis of several diseases, so it is important to understand how this system is controlled.
Maderböck, K., Pichler, A.
openaire +3 more sources
SUMO Conjugation and SUMO Chain Formation by Plant Enzymes
2022SUMO conjugation is a conserved process of eukaryotes, and essential in metazoa. Similar to ubiquitylation, a SUMO-activating enzyme links to the SUMO carboxyl-terminal Gly in a thioester bond, and a SUMO-conjugating enzyme accepts activated SUMO and can transfer it to substrates.
Tomanov, Konstantin +3 more
openaire +3 more sources
Biochemical Society Transactions, 2008
During the last decade, SUMOylation has emerged as a central regulatory post-translational modification in the control of the fate and function of proteins. However, how SUMOylation is regulated itself has just started to be delineated. It appears now that SUMO (small ubiquitin-related modifier) conjugation/deconjugation equilibrium is affected by ...
Denis, Tempé +2 more
openaire +2 more sources
During the last decade, SUMOylation has emerged as a central regulatory post-translational modification in the control of the fate and function of proteins. However, how SUMOylation is regulated itself has just started to be delineated. It appears now that SUMO (small ubiquitin-related modifier) conjugation/deconjugation equilibrium is affected by ...
Denis, Tempé +2 more
openaire +2 more sources
Annual Review of Cell and Developmental Biology, 2000
▪ Abstract SUMO (small ubiquitin-related modifier) is the best-characterized member of a growing family of ubiquitin-related proteins. It resembles ubiquitin in its structure, its ability to be ligated to other proteins, as well as in the mechanism of ligation.
openaire +2 more sources
▪ Abstract SUMO (small ubiquitin-related modifier) is the best-characterized member of a growing family of ubiquitin-related proteins. It resembles ubiquitin in its structure, its ability to be ligated to other proteins, as well as in the mechanism of ligation.
openaire +2 more sources
Analysis of Cellular SUMO and SUMO–Ubiquitin Hybrid Conjugates
2012Posttranslational modification of proteins with the small ubiquitin-related modifier (SUMO) has been implicated in many important physiological functions, including the regulation of transcription and DNA repair. In most cases, only a small fraction of the total cellular amounts of a given protein is sumoylated at a certain point in time.
Marion, Schnellhardt +6 more
openaire +2 more sources
Biochemical Society Transactions, 2007
Post-translational modification of cellular proteins by the SUMO (small ubiquitin-related modifier) is involved in numerous modes of regulation in widely different biological processes. In contrast with ubiquitination, SUMO conjugation is highly specific in terms of target lysine residues, but many aspects of substrate and lysine selection by the SUMO ...
J, Anckar, L, Sistonen
openaire +2 more sources
Post-translational modification of cellular proteins by the SUMO (small ubiquitin-related modifier) is involved in numerous modes of regulation in widely different biological processes. In contrast with ubiquitination, SUMO conjugation is highly specific in terms of target lysine residues, but many aspects of substrate and lysine selection by the SUMO ...
J, Anckar, L, Sistonen
openaire +2 more sources
SUMO conjugation and deconjugation
Molecular and General Genetics MGG, 2000Ligation of the ubiquitin-like protein SUMO (Smt3p) to other proteins is essential for viability of the yeast Saccharomyces cerevisiae. Like ubiquitin (Ub), SUMO undergoes ATP-dependent activation by a specific activating enzyme. SUMO-activating enzyme is a heterodimer composed of Uba2p and Aos1p, polypeptides with sequence similarities, respectively ...
I, Schwienhorst +2 more
openaire +2 more sources
Signalling mechanisms and cellular functions of SUMO
Nature Reviews Molecular Cell Biology, 2022Alfred C O Vertegaal
exaly

