Structure of an XRCC1 BRCT domain: a new protein-protein interaction module-Reference-Cited by-同舟云学术

Structure of an XRCC1 BRCT domain: a new protein-protein interaction module

Published:1998-11-02 Issue:21 Volume:17 Page:6404-6411
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:

Author:

Zhang Xiaodong¹,Moréra Solange¹²,Bates Paul A.³,Whitehead Philip C.⁴,Coffer Arnold I.⁴,Hainbucher Karl¹⁵,Nash Rachel A.⁶,Sternberg Michael J.E.³,Lindahl Tomas⁶,Freemont Paul S.¹

Affiliation:

1. Molecular Structure and Function, Imperial Cancer Research Fund; 44 Lincoln's Inn Fields London WC2A 3PX GB

2. Present address: Laboratoire d'Enzymologie et de Biochimie Structurales, UPR9063 CNRS-Université Paris-Sud, Bât. 34; 1 Avenue de la Terrasse 91198 Gif-sur-Yvette France

3. Biomolecular Modelling, Imperial Cancer Research Fund; 44 Lincoln's Inn Fields London WC2A 3PX GB

4. Protein Isolation and Cloning Laboratories, Imperial Cancer Research Fund; 44 Lincoln's Inn Fields London WC2A 3PX GB

5. Present address: Institut für Physikalische Chemie, Universität Graz, Heinrichstraße 28; 8010 Graz Austria

6. ICRF Clare Hall Laboratories; South Mimms Herts EN6 3LD GB

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference39 articles.

1. BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A;Anderson;Nature Genet,1998

2. Model building by comparison: a combination of expert knowledge and computer automation;Bates,1997

3. Functions of the BRCA1 and BRCA2 genes;Bertwistle;Curr Opin Genet Dev,1998

4. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins;Bork;FASEB J,1997

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