Results 81 to 90 of about 54,326 (298)

Using dot blot with immunochemical detection to evaluate global changes in SUMO-2/3 conjugation

open access: yesBioTechniques, 2012
Small ubiquitin-related modifier-2/3 (SUMO-2/3) is a member of the ubiquitin-like (Ubl) protein family. Conjugation of SUMO-2/3 to target proteins is influenced by various stress conditions and chemical inhibitors.
Markéta Častorálová   +2 more
doaj   +1 more source

SUMOylation of Rad52-Rad59 synergistically change the outcome of mitotic recombination [PDF]

open access: yes, 2016
Homologous recombination (HR) is essential for maintenance of genome stability through double-strand break (DSB) repair, but at the same time HR can lead to loss of heterozygosity and uncontrolled recombination can be genotoxic.
Lisby, Michael, Silva, Sonia
core   +1 more source

Modification of CCAAT/Enhancer-binding Protein-β by the Small Ubiquitin-like Modifier (SUMO) Family Members, SUMO-2 and SUMO-3 [PDF]

open access: yesJournal of Biological Chemistry, 2003
CCAAT/enhancer-binding protein-beta (C/EBP beta) activator isoforms, C/EBP beta-1 and C/EBP beta-2, differ by only 23 amino acids in the human; however, evidence is accumulating that these transcription factors are functionally distinct. Here we demonstrate that C/EBP beta-1, but not C/EBP beta-2, is conjugated to the small ubiquitin-like modifier ...
Erin M, Eaton, Linda, Sealy
openaire   +2 more sources

Aberrant SUMOylation Restricts the Targetable Cancer Immunopeptidome

open access: yesAdvanced Science, EarlyView.
Pharmacological SUMOylation inhibition (SUMOi) counteracts tumor immune evasion by unmasking an immunogenic HLA‐I peptide and neoepitope repertoire. By restoring HLA‐I ligand availability through increased antigen processing and presentation, enhanced proteasomal cleavage, and modulated TAP1 peptide affinity, SUMOi boosts tumor immunogenicity ...
Uta M. Demel   +19 more
wiley   +1 more source

Structure‐Based Development of Ultra‐Broad‐Spectrum 3C‐Like Protease Inhibitors

open access: yesAdvanced Science, EarlyView.
This study provides an in‐depth analysis of the substrate binding pocket of 3CLpros across all coronavirus species using bioinformatics and structural insights, revealing the critical impact of S2/S4 subsite diversity on the broad‐spectrum activity of approved therapeutics.
Haixia Su   +15 more
wiley   +1 more source

Smc5/6: a link between DNA repair and unidirectional replication? [PDF]

open access: yes, 2008
Of the three structural maintenance of chromosome (SMC) complexes, two directly regulate chromosome dynamics. The third, Smc5/6, functions mainly in homologous recombination and in completing DNA replication.
A Losada   +46 more
core   +1 more source

SUMO defeats protein aggregates

open access: yesJournal of Cell Biology, 2011
![Figure][1] Unsumoylated α-synuclein aggregates into fibrils (right), whereas sumoylated α-synuclein doesn't (left). Sumoylation might prevent the protein aggregations that typify Parkinson's disease (PD), [Krumova et al.][2] report.
openaire   +2 more sources

PDIA3 Inhibition Facilitates Sensitivity of IKE‐Induced Ferroptosis via STAT3/LCN2 Axis to Improve Glioblastoma Therapy

open access: yesAdvanced Science, EarlyView.
In this manuscript, protein disulfide isomerase A3 (PDIA3) is identified as a key factor mediating the susceptibility of ferroptosis in GBM. Inhibition of PDIA3 enhances IKE or cystine starvation‐induced ferroptosis in GBM cells by resulting in the accumulation of lipid peroxidation and a reduction in GSH level.
Jie Zhang   +19 more
wiley   +1 more source

A global S. cerevisiae small ubiquitin‐related modifier (SUMO) system interactome

open access: yesMolecular Systems Biology, 2013
The small ubiquitin‐related modifier (SUMO) system has been implicated in a number of biological functions, yet the individual components of the SUMO machinery involved in each of these activities were largely unknown.
Tharan Srikumar   +2 more
doaj   +1 more source

Regulation of SUMO Modification [PDF]

open access: yes, 2007
The small ubiquitin related modifier SUMO is a posttranslational modifier that functions in a wide range of cellular processes like intracellular transport, cell cycle regulation, DNA repair and regulation of transcription.
Knipscheer, P.M. (Puck Maria)
core   +1 more source

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