MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes. - Wikidata - awgldk - TriplyDB

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

http://www.wikidata.org/entity/Q34165707

about

The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea Crystal structure of the NurA-dAMP-Mn2+ complex Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex End-resection at DNA double-strand breaks in the three domains of life Efficient 5'-3' DNA end resection by HerA and NurA is essential for cell viability in the crenarchaeon Sulfolobus islandicus Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging Nanobiomotors of archaeal DNA repair machineries: current research status and application potential Linked domain architectures allow for specialization of function in the FtsK/SpoIIIE ATPases of ESX secretion systems Biochemical and Functional Characterization of the NurA-HerA Complex from Deinococcus radiodurans.Development of a simvastatin selection marker for a hyperthermophilic acidophile, Sulfolobus islandicus.NurA Is Endowed with Endo- and Exonuclease Activities that Are Modulated by HerA: New Insight into Their Role in DNA-End Processing A Novel C-Terminal Domain of RecJ is Critical for Interaction with HerA in Deinococcus radiodurans Rad50 is not essential for the Mre11-dependent repair of DNA double-strand breaks in Halobacterium sp. strain NRC-1.Archaeal genome guardians give insights into eukaryotic DNA replication and damage response proteins.Structural studies of DNA end detection and resection in homologous recombination.Redox stress proteins are involved in adaptation response of the hyperthermoacidophilic archaeon Sulfolobus solfataricus to nickel challenge.Molecular architecture of the HerA-NurA DNA double-strand break resection complex.Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA double-strand break.The carboxyl terminal of the archaeal nuclease NurA is involved in the interaction with single-stranded DNA-binding protein and dimer formation.Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex.Resistance to UV Irradiation Caused by Inactivation of and Genes in Thermus thermophilus

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P2860

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

http://www.wikidata.org/entity/Q34165707

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@ast

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@en

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@nl

type

label

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@ast

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@en

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@nl

prefLabel

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@ast

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@en

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@nl

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SJ.EMBOR.7400037

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P1476

MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.

@en

P2093

Angelo Manzan

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

Cara E Lang

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

Günter Pfeiffer

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

James P Carney

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

Melissa L Hefferin

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

P2860

RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G(2)/M checkpoint control

Mre11 complex and DNA replication: linkage to E2F and sites of DNA synthesis

MDC1 is a mediator of the mammalian DNA damage checkpoint

The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response

BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures

Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair

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

Distinct roles of two separable in vitro activities of yeast Mre11 in mitotic and meiotic recombination.

DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50*Mre11 complex.

Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response

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54-59

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scholarly article

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10.1038/SJ.EMBOR.7400037

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1

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5

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Karl-Peter Hopfner

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2004-01-01T00:00:00Z

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8930482

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14710187

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P932

1298954

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