RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
about
Structure of Mre11–Nbs1 complex yields insights into ataxia-telangiectasia–like disease mutations and DNA damage signalingEffect of the BRCA2 CTRD domain on RAD51 filaments analyzed by an ensemble of single molecule techniques.RecN is a cohesin-like protein that stimulates intermolecular DNA interactions in vitro.Productive replication of human papillomavirus 31 requires DNA repair factor Nbs1.The MRN complex in double-strand break repair and telomere maintenance.Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.Mre11-Rad50 complex crystals suggest molecular calisthenics.The Rad50 coiled-coil domain is indispensable for Mre11 complex functionsSFMetrics: an analysis tool for scanning force microscopy images of biomolecules.Interdependence of the rad50 hook and globular domain functionsArchitectural plasticity of human BRCA2-RAD51 complexes in DNA break repair.Human RAD50 deficiency in a Nijmegen breakage syndrome-like disorder.The Mre11-Nbs1 Interface Is Essential for Viability and Tumor Suppression.Preparation of DNA and nucleoprotein samples for AFM imaging.ATM protein kinase: the linchpin of cellular defenses to stress.Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair.Eukaryotic Rad50 functions as a rod-shaped dimer.Caffeine suppresses homologous recombination through interference with RAD51-mediated joint molecule formation.Impact of the MRN Complex on Adeno-Associated Virus Integration and Replication during Coinfection with Herpes Simplex Virus 1.Modification in the expression of Mre11/Rad50/Nbs1 complex in low dose irradiated human lymphocytes.Molecular recognition of DNA-protein complexes: a straightforward method combining scanning force and fluorescence microscopy.Imaging of DNA and Protein by SFM and Combined SFM-TIRF Microscopy.Protein-DNA interactions in high speed AFM: single molecule diffusion analysis of human RAD54.Interdependent and separable functions of Caenorhabditis elegans MRN-C complex members couple formation and repair of meiotic DSBs.Mitotic and Meiotic Functions for the SUMOylation Pathway in the Caenorhabditis elegans Germline.
P2860
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P2860
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@ast
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@en
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@en-gb
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@nl
type
label
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@ast
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@en
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@en-gb
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@nl
prefLabel
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@ast
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@en
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@en-gb
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@nl
P2093
P2860
P921
P356
P1476
RAD50 and NBS1 form a stable complex functional in DNA binding and tethering
@en
P2093
Claire Wyman
Eddy van der Linden
Eri Kinoshita
Humberto Sanchez
Roland Kanaar
P2860
P304
P356
10.1093/NAR/GKN1072
P407
P577
2009-04-01T00:00:00Z