Results 21 to 30 of about 50,255 (242)

The potential role of As-sumo-1 in the embryonic diapause process and early embryo development of Artemia sinica.

open access: yesPLoS ONE, 2014
During embryonic development of Artemia sinica, environmental stresses induce the embryo diapause phenomenon, required to resist apoptosis and regulate cell cycle activity.
Bing Chu   +9 more
doaj   +1 more source

SUMO-SIM interactions regulate the activity of RGSZ2 proteins. [PDF]

open access: yesPLoS ONE, 2011
The RGSZ2 gene, a regulator of G protein signaling, has been implicated in cognition, Alzheimer's disease, panic disorder, schizophrenia and several human cancers.
Javier Garzón   +6 more
doaj   +1 more source

Generation of specific inhibitors of SUMO-1– and SUMO-2/3–mediated protein-protein interactions using Affimer (Adhiron) technology [PDF]

open access: yes, 2017
Because protein-protein interactions underpin most biological processes, developing tools that target them to understand their function or to inform the development of therapeutics is an important task.
Adrian Whitehouse   +24 more
core   +2 more sources

SUMO-1 Modification of Bovine Papillomavirus E1 Protein Is Required for Intranuclear Accumulation [PDF]

open access: yesJournal of Biological Chemistry, 2000
The E1 protein is a multifunctional, origin-binding helicase that is essential for replication of papillomaviruses. Recently, bovine papillomavirus E1 was shown to be post-translationally modified by the addition of the SUMO-1 polypeptide. Here we show that the site of sumoylation maps to lysine residue 514.
D, Rangasamy   +3 more
openaire   +2 more sources

The SUMO Ligase Protein Inhibitor of Activated STAT 1 (PIAS1) is a constituent PML-NB protein that contributes to the intrinsic antiviral immune response to herpes simplex virus 1 (HSV-1) [PDF]

open access: yes, 2016
Aspects of intrinsic antiviral immunity are mediated by promyelocytic leukaemia (PML)-nuclear body (PML-NB) constituent proteins. During herpesvirus infection, these antiviral proteins are independently recruited to nuclear domains that contain infecting
Boutell, Chris   +7 more
core   +1 more source

Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif.

open access: yesThe Journal of biological chemistry, 2000
Two-hybrid screening in yeast with p73alpha isolated SUMO-1 (small ubiquitin-like modifier 1), the enzyme responsible for its conjugation, Ubc-9, and a number of novel SUMO-1-interacting proteins, including thymine DNA glycosylase, PM-Scl75, PIASx, PKY, and CHD3/ZFH.
A, Minty, X, Dumont, M, Kaghad, D, Caput
openaire   +2 more sources

SUMO-1 Gene Silencing Inhibits Proliferation and Promotes Apoptosis of Human Gastric Cancer SGC-7901 Cells

open access: yesCellular Physiology and Biochemistry, 2017
Background: It has been reported that blocking small ubiquitin-like modifier (SUMO) conjugation by silencing SUMO gene remarkably decreased tumor growth in vivo.
Lifang Jin   +4 more
doaj   +1 more source

Distinct Mechanisms of Pathogenic DJ-1 Mutations in Mitochondrial Quality Control [PDF]

open access: yes, 2018
The deglycase and chaperone protein DJ-1 is pivotal for cellular oxidative stress responses and mitochondrial quality control. Mutations in PARK7, encoding DJ-1, are associated with early-onset familial Parkinson’s disease and lead to pathological ...
Abeti   +66 more
core   +3 more sources

Tissue-specific inhibition of protein sumoylation uncovers diverse SUMO functions during C. elegans vulval development.

open access: yesPLoS Genetics, 2022
The sumoylation (SUMO) pathway is involved in a variety of processes during C. elegans development, such as gonadal and vulval fate specification, cell cycle progression and maintenance of chromosome structure.
Aleksandra Fergin   +4 more
doaj   +1 more source

The Protein Stability and Transcriptional Activity of p63α are Regulated by SUMO-1 Conjugation [PDF]

open access: yesCell Cycle, 2004
Post-translational modification of proteins by the ubiquitin-like molecule SUMO-1 regulates their stability and activity with crucial implications for many cellular processes. Here we show that p63alpha, but not p63beta and gamma, is sumoylated in vitro and in vivo at a single lysine residue, K637, in the post-SAM domain.
P. Ghioni   +6 more
openaire   +4 more sources

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