Analyzing the handoff of DNA from UvrA to UvrB utilizing DNA-protein photoaffinity labeling. - Wikidata - wikimedia - TriplyDB

Analyzing the handoff of DNA from UvrA to UvrB utilizing DNA-protein photoaffinity labeling.

Analyzing the handoff of DNA from UvrA to UvrB utilizing DNA-protein photoaffinity labeling.

http://www.wikidata.org/entity/Q38337796

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Investigation of bacterial nucleotide excision repair using single-molecule techniques.A Structural Model for the Damage-sensing Complex in Bacterial Nucleotide Excision Repair Structure of UvrA nucleotide excision repair protein in complex with modified DNA Structural insights into the first incision reaction during nucleotide excision repair Exploring damage recognition models in prokaryotic nucleotide excision repair with a benzo[a]pyrene-derived lesion in UvrB Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins.DNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway.Repair of the major lesion resulting from C5'-oxidation of DNA.The C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific DNA binding.Real-time single-molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes.Robust incision of Benoz[a]pyrene-7,8-dihyrodiol-9,10-epoxide-DNA adducts by a recombinant thermoresistant interspecies combination UvrABC endonuclease system New synthetic substrates of mammalian nucleotide excision repair system Efficient processing of TFO-directed psoralen DNA interstrand crosslinks by the UvrABC nuclease NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution 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 Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot.A new photoactive building block for investigation of DNA backbone interactions: photoaffinity labeling of human DNA polymerase beta.Identification of residues within UvrB that are important for efficient DNA binding and damage processing.Deciphering the biosynthesis pathway of the antitumor thiocoraline from a marine actinomycete and its expression in two streptomyces species.Recruitment of UvrBC complexes to UV-induced damage in the absence of UvrA increases cell survival.UvrB domain 4, an autoinhibitory gate for regulation of DNA binding and ATPase activity.

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P2860

Analyzing the handoff of DNA from UvrA to UvrB utilizing DNA-protein photoaffinity labeling.

http://www.wikidata.org/entity/Q38337796

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

@zh-my

2004年学术文章

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2004年學術文章

@yue

2004年學術文章

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2004年學術文章

@zh-hant

name

Analyzing the handoff of DNA f ...... rotein photoaffinity labeling.

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Analyzing the handoff of DNA f ...... rotein photoaffinity labeling.

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Analyzing the handoff of DNA f ...... rotein photoaffinity labeling.

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P1433

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Journal of Biological Chemistry

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Analyzing the handoff of DNA f ...... rotein photoaffinity labeling.

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Bennett Van Houten

http://www.w3.org/2001/XMLSchema#string

Deborah L Croteau

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Matthew J DellaVecchia

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Milan Skorvaga

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Olga I Lavrik

http://www.w3.org/2001/XMLSchema#string

Sergey V Dezhurov

http://www.w3.org/2001/XMLSchema#string

P2860

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

Catalytic sites for 3' and 5' incision of Escherichia coli nucleotide excision repair are both located in UvrC

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

Expression of human DNA polymerase beta in Escherichia coli and characterization of the recombinant enzyme

The UvrABC endonuclease system of Escherichia coli--a view from Baltimore

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

DNA excision repair

Molecular anatomy of the human excision nuclease assembled at sites of DNA damage.

Alternative conformations of human replication protein A are detected by crosslinks with primers carrying a photoreactive group at the 3'-end.

Spatial organization of the core region of yeast TFIIIB-DNA complexes

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45245-45256

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10.1074/JBC.M408659200

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43

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279

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15308661

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