Results 61 to 70 of about 37,758 (275)
NF-κB repression by PIAS3 mediated RelA SUMOylation. [PDF]
PLoS ONE, 2012 Negative regulation of the NF-κB transcription factor is essential for tissue homeostasis in response to stress and inflammation. NF-κB activity is regulated by a variety of biochemical mechanisms including phosphorylation, acetylation, and ...
Yuangang Liu +3 more
doaj +1 more source
SUMOylation and bacterial pathogens [PDF]
Virulence, 2010 During infection, bacterial pathogens interfere with many different post-translational modifications of the host cell to promote their own survival and replication. By stimulating or counteracting host post-translational modifications, these pathogens may control locally and specifically the fate and function of host factors critical for the infection ...
David Ribet, Pascale Cossart
openaire +3 more sources
iSUMOK-PseAAC: prediction of lysine sumoylation sites using statistical moments and Chou’s PseAAC
PeerJ, 2021 Sumoylation is the post-translational modification that is involved in the adaption of the cells and the functional properties of a large number of proteins.
Y. Khan +3 more
semanticscholar +1 more source
Forkhead box protein A2 (FOXA2) protein stability and activity are regulated by sumoylation. [PDF]
PLoS ONE, 2012 The forkhead box protein A2 (FOXA2) is an important regulator of glucose and lipid metabolism and organismal energy balance. Little is known about how FOXA2 protein expression and activity are regulated by post-translational modifications.
Narasimhaswamy S Belaguli +3 more
doaj +1 more source
Cells, 2023 Diabetic peripheral neuropathy (DPN) is the prevalent type of peripheral neuropathy; it primarily impacts extremity nerves. Its multifaceted nature makes the molecular mechanisms of diabetic neuropathy intricate and incompletely elucidated. Several types
Nicolas Mandel +4 more
doaj +1 more source
Detection of Sumoylated Proteins [PDF]
, 2005 Small ubiquitin-related modifier (SUMO) is an ubiquitin-like protein that is covalently attached to a variety of target proteins. Unlike ubiquitination, sumoylation does not target proteins for proteolytic breakdown, but is involved in regulation of protein function, nuclear targeting, and the formation of subcellular structures.
Kevin D. Sarge, Ok Kyong Park-Sarge
openaire +4 more sources
Extranuclear SUMOylation in Neurons [PDF]
Trends in Neurosciences, 2018 Post-translational modification of substrate proteins by SUMO conjugation regulates a diverse array of cellular processes. While predominantly a nuclear protein modification, there is a growing appreciation that SUMOylation of proteins outside the nucleus plays direct roles in controlling synaptic transmission, neuronal excitability, and adaptive ...
Jeremy M. Henley +2 more
openaire +5 more sources
Mechanisms and functions of SUMOylation in health and disease: a review focusing on immune cells
Journal of Biomedical SciencesSUMOylation, which is a type of post-translational modification that involves covalent conjugation of small ubiquitin-like modifier (SUMO) proteins to target substrates, regulates various important molecular and cellular processes, including ...
Chien-Hsin Huang +2 more
semanticscholar +1 more source
bioRxiv, 2020 Cytoplasmic stress granules (SG) form in response to a variety of cellular stresses by phase-separation of proteins associated with non-translating mRNAs.
Hagai Marmor-Kollet +17 more
semanticscholar +1 more source
SUMOylation and cell signalling
Biotechnology Journal, 2009 AbstractSUMOylation is a highly transient post‐translational protein modification. Attachment of SUMO to target proteins occurs via a number of specific activating and ligating enzymes that form the SUMO‐substrate complex, and other SUMO‐specific proteases that cleave the covalent bond, thus leaving both SUMO and target protein free for the next round ...
Nektarios Tavernarakis +1 more
openaire +4 more sources