Mre11-Rad50 complex crystals suggest molecular calisthenics. - Wikidata - thesis-toulmin - TriplyDB

Mre11-Rad50 complex crystals suggest molecular calisthenics.

Mre11-Rad50 complex crystals suggest molecular calisthenics.

http://www.wikidata.org/entity/Q35256261

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Autoinhibition of bacteriophage T4 Mre11 by its C-terminal domain.Interdependence of the rad50 hook and globular domain functions Functional Analysis of the Bacteriophage T4 Rad50 Homolog (gp46) Coiled-coil Domain Disruption of the bacteriophage T4 Mre11 dimer interface reveals a two-state mechanism for exonuclease activity Processing of DNA double-stranded breaks and intermediates of recombination and repair by Saccharomyces cerevisiae Mre11 and its stimulation by Rad50, Xrs2, and Sae2 proteins.The Mre11-Nbs1 Interface Is Essential for Viability and Tumor Suppression.Targeting homologous recombination-mediated DNA repair in cancer.Eukaryotic Rad50 functions as a rod-shaped dimer.A network of allosterically coupled residues in the bacteriophage T4 Mre11-Rad50 complex Synthetic lethality in ATM-deficient RAD50-mutant tumors underlies outlier response to cancer therapy

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Mre11-Rad50 complex crystals suggest molecular calisthenics.

http://www.wikidata.org/entity/Q35256261

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Mre11-Rad50 complex crystals suggest molecular calisthenics.

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Mre11-Rad50 complex crystals suggest molecular calisthenics.

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Mre11-Rad50 complex crystals suggest molecular calisthenics.

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Mre11-Rad50 complex crystals suggest molecular calisthenics.

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Mre11-Rad50 complex crystals suggest molecular calisthenics.

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Mre11-Rad50 complex crystals suggest molecular calisthenics.

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J.DNAREP.2011.07.008

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Mre11-Rad50 complex crystals suggest molecular calisthenics.

@en

P2093

Claire Wyman

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Joyce Lebbink

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Roland Kanaar

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P2860

The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair

RAD50 and NBS1 form a stable complex functional in DNA binding and tethering

Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95

Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex

DNA end resection: many nucleases make light work

Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase

The alternating ATPase domains of MutS control DNA mismatch repair

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1066-1070

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scholarly article

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10.1016/J.DNAREP.2011.07.008

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10

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51619785

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