Structural Basis for Octameric Ring Formation and DNA Interaction of the Human Homologous-Pairing Protein Dmc1-Reference-Cited by-同舟云学术

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Structural Basis for Octameric Ring Formation and DNA Interaction of the Human Homologous-Pairing Protein Dmc1

Published:2004-05 Issue:3 Volume:14 Page:363-374
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Kinebuchi Takashi,Kagawa Wataru,Enomoto Rima,Tanaka Kozo,Miyagawa Kiyoshi,Shibata Takehiko,Kurumizaka Hitoshi,Yokoyama Shigeyuki

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference47 articles.

1. The N-terminal domain of the human Rad51 protein binds DNA;Aihara;J. Mol. Biol.,1998

2. Electrostatic calculations of the pKa values of ionizable groups in Bacteriorhodopsin;Bashford;J. Mol. Biol.,1992

3. Purification of human Rad51 protein by selective spermidine precipitation;Baumann;Mutat. Res.,1997

4. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA;Benson;EMBO J.,1994

5. Gromacs;Berendsen;Comp. Phys. Comm.,1995

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1. DMC1 and RAD51 bind FxxA and FxPP motifs of BRCA2 via two separate interfaces;Nucleic Acids Research;2024-06-03

2. BRCA2-HSF2BP oligomeric ring disassembly by BRME1 promotes homologous recombination;Science Advances;2023-10-27

3. DMC1 and RAD51 bind FxxA and FxPP motifs of BRCA2 via two separate interfaces;2023-10-05

4. Mechanisms of distinctive mismatch tolerance between Rad51 and Dmc1 in homologous recombination;Nucleic Acids Research;2021-12-06

5. Identification of fidelity-governing factors in human recombinases DMC1 and RAD51 from cryo-EM structures;Nature Communications;2021-01-14

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