The arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling.
about
Structure of human Bloom's syndrome helicase in complex with ADP and duplex DNACrystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changesComputational and experimental approaches to reveal the effects of single nucleotide polymorphisms with respect to disease diagnosticsThe HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling.Multimeric BLM is dissociated upon ATP hydrolysis and functions as monomers in resolving DNA structuresA nucleotide-dependent and HRDC domain-dependent structural transition in DNA-bound RecQ helicase.
P2860
The arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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name
The arginine finger of the Blo ...... d its role in energy coupling.
@ast
The arginine finger of the Blo ...... d its role in energy coupling.
@en
type
label
The arginine finger of the Blo ...... d its role in energy coupling.
@ast
The arginine finger of the Blo ...... d its role in energy coupling.
@en
prefLabel
The arginine finger of the Blo ...... d its role in energy coupling.
@ast
The arginine finger of the Blo ...... d its role in energy coupling.
@en
P2093
P2860
P356
P1476
The arginine finger of the Blo ...... nd its role in energy coupling
@en
P2093
Mounira Amor-Gueret
Peng-Ye Wang
Shuo-Xing Dou
Xu Guang Xi
P2860
P304
P356
10.1093/NAR/GKM544
P407
P577
2007-08-30T00:00:00Z