Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
about
The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division siteATP hydrolysis catalyzed by human replication factor C requires participation of multiple subunitsCrystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexesEscherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay.UvrAB activity at a damaged DNA site: is unpaired DNA present?Distinct properties of hexameric but functionally conserved Mycobacterium tuberculosis transcription-repair coupling factor.Nucleotide excision repair: Dick Setlow: how he influenced my scientific life.RecA K72R filament formation defects reveal an oligomeric RecA species involved in filament extensionSequence and complementation analysis of recF genes from Escherichia coli, Salmonella typhimurium, Pseudomonas putida and Bacillus subtilis: evidence for an essential phosphate binding loop.Agrobacterium tumefaciens VirB11 protein requires a consensus nucleotide-binding site for function in virulence.Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities.Structure of the gene complementing uvr-402 in Streptococcus pneumoniae: homology with Escherichia coli uvrB and the homologous gene in Micrococcus luteus.Nucleotide excision repair in Escherichia coliFunctions of the gene products of Escherichia coli.ATP-dependent partitioning of the DNA template into supercoiled domains by Escherichia coli UvrAB.Mutational analysis of ERCC3, which is involved in DNA repair and transcription initiation: identification of domains essential for the DNA repair function.Identification of the VirB4-VirB8-VirB5-VirB2 pilus assembly sequence of type IV secretion systems.Damage recognition by UvrABC. A study of vectorial movement.Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicase-primase.Regulation and rate enhancement during transcription-coupled DNA repair.Stimulation of UvrD helicase by UvrAB.Bacterial ApbC protein has two biochemical activities that are required for in vivo function.The binding of UvrAB proteins to bubble and loop regions in duplex DNA.Structural and functional characterization of the human DNA repair helicase XPD by comparative molecular modeling and site-directed mutagenesis of the bacterial repair protein UvrB.Mutation accumulation under UV radiation in Escherichia coli.Base flipping in nucleotide excision repair.Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp.Domain structure of Thermus thermophilus UvrB protein. Similarity in domain structure to a helicase.
P2860
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P2860
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
description
1989 nî lūn-bûn
@nan
1989 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@ast
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@en
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@nl
type
label
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@ast
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@en
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@nl
prefLabel
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@ast
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@en
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@nl
P2860
P356
P1476
Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.
@en
P2093
L Grossman
T W Seeley
P2860
P304
P356
10.1073/PNAS.86.17.6577
P407
P577
1989-09-01T00:00:00Z