Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer. - Wikidata - wikimedia - TriplyDB

Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer.

Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer.

http://www.wikidata.org/entity/Q37149796

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Structure of UvrA nucleotide excision repair protein in complex with modified DNA The biological and structural characterization of Mycobacterium tuberculosis UvrA provides novel insights into its mechanism of action Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins.Single molecule techniques in DNA repair: a primer Lesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging.Single-molecule imaging of UvrA and UvrB recruitment to DNA lesions in living Escherichia coli.Dynamics of lesion processing by bacterial nucleotide excision repair proteins DNA substrate preparation for atomic force microscopy studies of protein-DNA interactions.Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair.Single-walled carbon nanotubes as scaffolds to concentrate DNA for the study of DNA-protein interactions.Capture of unstable protein complex on the streptavidin-coated single-walled carbon nanotubes

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Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer.

http://www.wikidata.org/entity/Q37149796

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 10 February 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Single-molecule analysis revea ...... e Escherichia coli UvrA dimer.

@en

Single-molecule analysis revea ...... e Escherichia coli UvrA dimer.

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label

Single-molecule analysis revea ...... e Escherichia coli UvrA dimer.

@en

Single-molecule analysis revea ...... e Escherichia coli UvrA dimer.

@nl

prefLabel

Single-molecule analysis revea ...... e Escherichia coli UvrA dimer.

@en

Single-molecule analysis revea ...... e Escherichia coli UvrA dimer.

@nl

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Nucleic Acids Research

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Single-molecule analysis revea ...... e Escherichia coli UvrA dimer.

@en

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Geri Moolenaar

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John van Noort

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Koen Wagner

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Nora Goosen

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P2860

Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions

Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair.

Crystal Structure of Bacillus stearothermophilus UvrA Provides Insight into ATP-Modulated Dimerization, UvrB Interaction, and DNA Binding

The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands.

Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition.

The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex.

Prokaryotic nucleotide excision repair: the UvrABC system.

Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures.

ATPase activity of the UvrA and UvrAB protein complexes of the Escherichia coli UvrABC endonuclease

'Close-fitting sleeves': DNA damage recognition by the UvrABC nuclease system.

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1962-1972

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scholarly article

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10.1093/NAR/GKP071

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6

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37

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2009-02-10T00:00:00Z

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23999053

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19208636

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Escherichia coli

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2665241

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