Results 41 to 50 of about 28,838 (280)

Homologous Recombination: To Fork and Beyond [PDF]

open access: yes, 2018
Accurate completion of genome duplication is threatened by multiple factors that hamper the advance and stability of the replication forks. Cells need to tolerate many of these blocking lesions to timely complete DNA replication, postponing their repair ...
Prado Velasco, José Félix
core   +1 more source

SUMO: regulating the regulator

open access: yesCell Division, 2006
Post-translational modifiers of the SUMO (Small Ubiquitin-related Modifier) family have emerged as key regulators of protein function and fate. While the past few years have seen an enormous increase in knowledge on SUMO enzymes, substrates, and ...
Bossis Guillaume, Melchior Frauke
doaj   +1 more source

Site-specific identification and quantitation of endogenous SUMO modifications under native conditions. [PDF]

open access: yes, 2017
Small ubiquitin-like modifier (SUMO) modification regulates numerous cellular processes. Unlike ubiquitin, detection of endogenous SUMOylated proteins is limited by the lack of naturally occurring protease sites in the C-terminal tail of SUMO proteins ...
Ahmad, Alla S   +8 more
core   +2 more sources

RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]

open access: yes, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S.   +2 more
core   +1 more source

Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9 [PDF]

open access: yesAngewandte Chemie International Edition, 2016
AbstractConjugation of the small ubiquitin‐like modifier (SUMO) to protein substrates is an important disease‐associated posttranslational modification, although few inhibitors of this process are known. Herein, we report the discovery of an allosteric small‐molecule binding site on Ubc9, the sole SUMO E2 enzyme.
William M. Hewitt   +12 more
openaire   +3 more sources

Molecular Characterization and Functional Localization of a Novel SUMOylation Gene in Oryza sativa

open access: yesBiology, 2021
Small ubiquitin-related modifier (SUMO) regulates the cellular function of diverse proteins through post-translational modifications. The current study defined a new homolog of SUMO genes in the rice genome and named it OsSUMO7. Putative protein analysis
Eid I. Ibrahim   +5 more
doaj   +1 more source

SUMOylation regulates LKB1 localization and its oncogenic activity in liver cancer [PDF]

open access: yes, 2019
BACKGROUND: Even though liver kinase B1 (LKB1) is usually described as a tumor suppressor in a wide variety of tissues, it has been shown that LKB1 aberrant expression is associated with bad prognosis in Hepatocellular Carcinoma (HCC).
Díaz Moreno, Irene   +4 more
core   +1 more source

Site-specific inhibition of the small ubiquitin-like modifier (SUMO)-conjugating enzyme Ubc9 selectively impairs SUMO chain formation [PDF]

open access: yesJournal of Biological Chemistry, 2017
Posttranslational modifications by small ubiquitin-like modifiers (SUMOs) regulate many cellular processes, including genome integrity, gene expression, and ribosome biogenesis. The E2-conjugating enzyme Ubc9 catalyzes the conjugation of SUMOs to ϵ-amino groups of lysine residues in target proteins.
Svenja, Wiechmann   +9 more
openaire   +2 more sources

Global SUMO proteome responses guide gene regulation, mRNA biogenesis, and plant stress responses

open access: yesFrontiers in Plant Science, 2012
Small-ubiquitin-like MOdifier (SUMO) is a key regulator of abiotic stress, disease resistance and development in plants. The identification of >350 plant SUMO targets has revealed many processes modulated by SUMO and potential consequences of SUMO on ...
Magdalena eMazur   +1 more
doaj   +1 more source

Structural modeling and functional analysis of the essential ribosomal processing protease Prp from Staphylococcus aureus [PDF]

open access: yes, 2017
In Firmicutes and related bacteria, ribosomal large subunit protein L27 is encoded with a conserved N-terminal extension that is removed to expose residues critical for ribosome function. Bacteria encoding L27 with this N-terminal extension also encode a
Christie, Gail E.   +3 more
core   +2 more sources

Home - About - Disclaimer - Privacy