Results 71 to 80 of about 226,967 (304)

ATPase-dependent control of the Mms21 SUMO ligase during DNA repair.

open access: yesPLoS Biology, 2015
Modification of proteins by SUMO is essential for the maintenance of genome integrity. During DNA replication, the Mms21-branch of the SUMO pathway counteracts recombination intermediates at damaged replication forks, thus facilitating sister chromatid ...
Marcelino Bermúdez-López   +11 more
doaj   +1 more source

Mammalian DNA ligase II [PDF]

open access: yes, 1994
DNA ligases are essential for DNA replication, repair and recombination. Two DNA ligases have been described previously in mammalian cells and other eukaryotes. DNA ligase I has been purified and the cDNA encoding the enzyme has been cloned.
Roberts, Emma
core  

Single Cell Analysis of Human RAD18-Dependent DNA Post-Replication Repair by Alkaline Bromodeoxyuridine Comet Assay

open access: yes, 2013
Damage to DNA can block replication progression resulting in gaps in the newly synthesized DNA. Cells utilize a number of post-replication repair (PRR) mechanisms such as the RAD18 controlled translesion synthesis or template switching to overcome the ...
Himabindu Gali   +14 more
core   +1 more source

A multidimensional strategy to detect polypharmacological targets in the absence of structural and sequence homology [PDF]

open access: yes, 2010
Conventional drug design embraces the "one gene, one drug, one disease" philosophy. Polypharmacology, which focuses on multi-target drugs, has emerged as a new paradigm in drug discovery.
Chen Zhijun   +39 more
core   +1 more source

DNA Ligases: Progress and Prospects [PDF]

open access: yesJournal of Biological Chemistry, 2009
DNA ligases seal 5'-PO4 and 3'-OH polynucleotide ends via three nucleotidyl transfer steps involving ligase-adenylate and DNA-adenylate intermediates. DNA ligases are essential guardians of genomic integrity, and ligase dysfunction underlies human genetic disease syndromes.
openaire   +2 more sources

Heterozygous loss‐of‐function alleles associate the conserved 3′‐5′ exoribonuclease EXOSC10 with hypersensitivity to the anticancer drug 5‐fluorouracil

open access: yesMolecular Oncology, EarlyView.
EXOSC10, an essential nuclear RNA exosome‐associated 3′‐5′ exoribonuclease, is inhibited by the anticancer drug 5‐fluorouracil (5‐FU), and EXOSC10 depletion increases 5‐FU sensitivity. The colon‐cancer variant EXOSC10S402T, located in a proteolysis motif, is stable and nuclear but nonfunctional in vivo.
Radhika Sain   +10 more
wiley   +1 more source

In vitro Assay to Measure DNA Polymerase β Nucleotide Insertion Coupled with the DNA Ligation Reaction during Base Excision Repair

open access: yesBio-Protocol, 2017
We previously reported that oxidized nucleotide insertion by DNA polymerase β (pol β) can confound the DNA ligation step during base excision repair (BER) (Çağlayan et al., 2017).
Melike Çağlayan, Samuel Wilson
doaj   +1 more source

USP29‐regulated noncanonical stabilization of the hypoxia‐inducible factor‐α in aggressive prostate cancer

open access: yesMolecular Oncology, EarlyView.
We identify USP29 as the only DUB mirroring CA9 expression, a marker of hypoxia and HIF pathway activation associated with PCA aggressiveness. USP29 stabilizes HIF‐1α and HIF‐2α via a noncanonical mechanism that is independent of PHD/pVHL activity yet relies on proteasomal regulation, establishing USP29 as a previously unrecognized regulator of hypoxic
Amelie S Schober   +16 more
wiley   +1 more source

Finding novel vulnerabilities of hypomorphic BRCA1 alleles

open access: yesMolecular Oncology, EarlyView.
Synthetic lethality screens performed to identify novel vulnerabilities often model complete gene loss, thereby overlooking patient‐derived hypomorphic mutations. In this study, we have performed genome‐wide CRISPR screens on BRCA1 hypomorphic mutations, showing BRCA1I26A behaves like wild‐type, while BRCA1R1699Q mimics deficiency. Furthermore, we have
Anne Schreuder   +10 more
wiley   +1 more source

Closing the gap on DNA ligase [PDF]

open access: yesStructure, 1996
The crystal structure of T7 DNA ligase complexed with ATP illuminates the mechanism of covalent catalysis by a superfamily of nucleotidyl transferases that includes the ATP-dependent polynucleotide ligases and the GTP-dependent mRNA capping enzymes.
openaire   +2 more sources

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