The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding.
about
Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicaseStructure and function of the regulatory C-terminal HRDC domain from Deinococcus radiodurans RecQStructural and Mechanistic Studies of a Stabilized Subunit Dimer Variant of Escherichia coli Bacterioferritin Identify Residues Required for Core FormationSolution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein.Characterization of biochemical properties of Bacillus subtilis RecQ helicaseSit down, relax and unwind: structural insights into RecQ helicase mechanisms.Mutations in RECQL Gene Are Associated with Predisposition to Breast CancerThe HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling.Recognition Code of ZNF191(243-368) and Its Interaction with DNAThe arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling.Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stabilityMechanistic insight into cadmium-induced inactivation of the Bloom protein.A nucleotide-dependent and HRDC domain-dependent structural transition in DNA-bound RecQ helicase.RecQ helicases: multiple structures for multiple functions?RecQ helicases; at the crossroad of genome replication, repair, and recombination.Probing Genome Maintenance Functions of human RECQ1.The Human RecQ4 Helicase Contains a Functional RecQ C-terminal Region (RQC) That Is Essential for Activity.A novel DNA helicase with strand-annealing activity from the crenarchaeon Sulfolobus solfataricusModulation of Werner syndrome protein function by a single mutation in the conserved RecQ domain.Site-directed mutants of human RECQ1 reveal functional importance of the zinc binding domainOn BLM helicase in recombination-mediated telomere maintenance.
P2860
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P2860
The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
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2004年學術文章
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2004年學術文章
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name
The zinc finger motif of Esche ...... A binding and protein folding.
@en
The zinc finger motif of Esche ...... A binding and protein folding.
@nl
type
label
The zinc finger motif of Esche ...... A binding and protein folding.
@en
The zinc finger motif of Esche ...... A binding and protein folding.
@nl
prefLabel
The zinc finger motif of Esche ...... A binding and protein folding.
@en
The zinc finger motif of Esche ...... A binding and protein folding.
@nl
P2093
P2860
P356
P1476
The zinc finger motif of Esche ...... NA binding and protein folding
@en
P2093
Jie Lin Liu
Peng-Ye Wang
Shuo-Xing Dou
Xu Guang Xi
P2860
P304
42794-42802
P356
10.1074/JBC.M405008200
P407
P577
2004-07-29T00:00:00Z