The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair-Reference-Cited by-同舟云学术

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The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair

Published:2009-11 Issue:11 Volume:8 Page:1300-1310
ISSN:1568-7864
Container-title:DNA Repair
language:en
Short-container-title:DNA Repair

Author:

Manelyte Laura,Guy Colin P.,Smith Rachel M.,Dillingham Mark S.,McGlynn Peter,Savery Nigel J.

Funder

BBSRC grant

MRC grant

Royal Society and by Wellcome Trust

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. Prokaryotic nucleotide excision repair: the UvrABC system;Truglio;Chem. Rev.,2006

2. DNA mismatch repair;Kunkel;Annu. Rev. Biochem.,2005

3. The UvrD helicase and its modulation by the mismatch repair protein MutL;Matson;Nucl. Acids Res.,2006

4. Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrD;Hall;EMBO J.,1998

5. Stimulation of UvrD Helicase by UvrAB;Atkinson;J. Biol. Chem.,2009

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1. Translation selectively destroys non-functional transcription complexes;Nature;2024-02-07

2. Tetrameric UvrD Helicase Is Located at the E. Coli Replisome due to Frequent Replication Blocks;Journal of Molecular Biology;2024-01

3. Advances in the joint profiling technologies of 5mC and 5hmC;RSC Chemical Biology;2024

4. Transcription-coupled global genomic repair in E. coli;Trends in Biochemical Sciences;2023-10

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