Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase - Wikidata - wikimedia - TriplyDB

Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase

Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase

http://www.wikidata.org/entity/Q24810234

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Structural and functional analyses of disease-causing missense mutations in Bloom syndrome protein Disease-causing missense mutations in human DNA helicase disorders Structure of human Bloom's syndrome helicase in complex with ADP and duplex DNA Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein.Characterization of biochemical properties of Bacillus subtilis RecQ helicase Sgs1 truncations induce genome rearrangements but suppress detrimental effects of BLM overexpression in Saccharomyces cerevisiae.Determination of the biochemical properties of full-length human PIF1 ATPase.Sit down, relax and unwind: structural insights into RecQ helicase mechanisms.Unwinding forward and sliding back: an intermittent unwinding mode of the BLM helicase.The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling.DNA helicases associated with genetic instability, cancer, and aging.The 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 stability Mechanistic insight into cadmium-induced inactivation of the Bloom protein.Domain requirements for DNA unwinding by mycobacterial UvrD2, an essential DNA 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.Complex activities of the human Bloom's syndrome helicase are encoded in a core region comprising the RecA and Zn-binding domains.Site-directed mutants of human RECQ1 reveal functional importance of the zinc binding domain Identification and characterization of cysteinyl exposure in proteins by selective mercury labeling and nano-electrospray ionization quadrupole time-of-flight mass spectrometry.On BLM helicase in recombination-mediated telomere maintenance.

P2860

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P2860

Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase

http://www.wikidata.org/entity/Q24810234

description

2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005 թվականի հունիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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name

Structural and functional char ...... n in Bloom's syndrome helicase

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Structural and functional char ...... n in Bloom's syndrome helicase

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Structural and functional char ...... n in Bloom's syndrome helicase

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Structural and functional char ...... n in Bloom's syndrome helicase

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Structural and functional char ...... n in Bloom's syndrome helicase

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Structural and functional char ...... n in Bloom's syndrome helicase

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Nucleic Acids Research

P1476

Structural and functional char ...... n in Bloom's syndrome helicase

@en

P2093

Loussiné Zargarian

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

Rong-bin Guo

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

Serge Fermandjian

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

Xu Guang Xi

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

P2860

Association of the Bloom syndrome protein with topoisomerase IIIalpha in somatic and meiotic cells

Replication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activity

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases

Stimulation of flap endonuclease-1 by the Bloom's syndrome protein

Characterization and mutational analysis of the RecQ core of the bloom syndrome protein

The Bloom's syndrome gene product is a 3'-5' DNA helicase

The Bloom's syndrome gene product is homologous to RecQ helicases

Bloom syndrome: an analysis of consanguineous families assigns the locus mutated to chromosome band 15q26.1

Environment affects amino acid preference for secondary structure

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scholarly article

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1509342

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10.1093/NAR/GKI619

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10

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33

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2005-06-01T00:00:00Z

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15930159

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1142346

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