Results 21 to 30 of about 291,935 (374)

TRIM5α is a SUMO substrate [PDF]

open access: yesRetrovirology, 2015
The TRIM5α restriction factor interferes with retroviral infections by inhibiting an early step of viral replication. TRIM5α activity was recently proposed to be regulated by the SUMO machinery and one SUMO consensus conjugation site as well as three putative SUMO interacting motifs (SIMs) were identified within TRIM5α sequence. Whereas mutation of the
Dutrieux, Jacques   +4 more
openaire   +3 more sources

Traffic Simulation with Open-Source and Commercial Traffic Microsimulators: A Case Study

open access: yesCommunications, 2022
The analysis of traffic problems in large urban centers often requires the use of computational tools, which give the possibility to make a more detailed analysis of the issue, suggest solutions, predict behaviors and, above all, support efficient ...
Nelson Baza-Solares   +4 more
doaj   +1 more source

SUMO Wrestling with Specificity [PDF]

open access: bronzeStructure, 2002
A new structure reveals how substrates are recognized for conjugation to the ubiquitin-like protein SUMO, a posttranslational modification that functions in activation of transcription factors, nuclear import, and cell division.
Andrew P. VanDemark, Christopher P. Hill
openalex   +4 more sources

SUMO enables substrate selectivity by mitogen-activated protein kinases to regulate immunity in plants

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2021
Significance The functional diversity of MAPKs is dependent on differential selection of substrates for phosphorylation. Nevertheless, the mechanisms assisting MAPKs to maintain substrate specificity in plants are not known.
Vivek Verma   +10 more
semanticscholar   +1 more source

A conserved SUMO pathway repairs topoisomerase DNA-protein cross-links by engaging ubiquitin-mediated proteasomal degradation

open access: yesScience Advances, 2020
A conserved SUMO-ubiquitin-proteasome pathway protects cells from DNA damage induced by topoisomerases. Topoisomerases form transient covalent DNA cleavage complexes to perform their reactions.
Yilun Sun   +5 more
semanticscholar   +1 more source

SUMO is Growing Senescent [PDF]

open access: yesCell Cycle, 2007
Cellular senescence is an irreversible cell cycle arrest that curbs unrestrained, aberrant proliferation of mammalian cells and is now recognized as a prominent tumor suppressive mechanism. We have shown recently that the E3 SUMO ligase PIASy actively contributes to execution of the senescence program, thus, providing the first evidence for a direct ...
Bischof, Oliver, Dejean, Anne
openaire   +4 more sources

An adaptive real-time grey-box model for advanced control and operations in WRRFs

open access: yesWater Science and Technology, 2021
Grey-box models, which combine the explanatory power of first-principle models with the ability to detect subtle patterns from data, are gaining increasing attention in wastewater sectors.
Cheng Yang   +3 more
doaj   +1 more source

SUMO Signaling by Hypoxic Inactivation of SUMO-Specific Isopeptidases [PDF]

open access: yesCell Reports, 2016
Post-translational modification of proteins with ubiquitin-like SUMO modifiers is a tightly regulated and highly dynamic process. The SENP family of SUMO-specific isopeptidases comprises six cysteine proteases. They are instrumental in counterbalancing SUMO conjugation, but their regulation is not well understood.
Kunz Kathrin   +5 more
openaire   +6 more sources

Sumo-dependent substrate targeting of the SUMO protease Ulp1 [PDF]

open access: yesBMC Biology, 2011
AbstractBackgroundIn the yeastSaccharomyces cerevisiae, the essential small ubiquitin-like modifier (SUMO) protease Ulp1 is responsible for both removing SUMO/Smt3 from specific target proteins and for processing precursor SUMO into its conjugation-competent form.
Helen A. Murphy   +5 more
openaire   +4 more sources

Protein SUMOylation and Its Research Progress in Maize

open access: yesGuangdong nongye kexue, 2023
Small ubiquitin-like modification (SUMOylation) is a crucial post-translational modification of proteins that plays a vital role in various biological processes in plants.
Ruiqiang LAI   +5 more
doaj   +1 more source

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