The histone-fold complex MHF is remodeled by FANCM to recognize branched DNA and protect genome stability

Cell Research

Volumn 24, Issue 5, 2014, Pages 560-575

  Fox, David ^a   Yan, Zhijiang ^a   Ling, Chen ^a   Zhao, Ye ^b   Lee, Duck Yeon ^c   Fukagawa, Tatsuo ^d   Yang, Wei ^b   Wang, Weidong ^a  

^a NATIONAL INSTITUTE ON AGING   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^d GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

Author keywords

branched DNA; FANCM; Fanconi anemia; genome stability; histone fold; MHF

Indexed keywords

APITD1 PROTEIN, HUMAN; APOPTOSIS REGULATORY PROTEIN; CRUCIFORM DNA; DNA; DNA BINDING PROTEIN; DNA HELICASE; FANCM PROTEIN, HUMAN; HISTONE; MULTIPROTEIN COMPLEX; NUCLEAR PROTEIN; STRA13 PROTEIN, HUMAN; TUMOR SUPPRESSOR PROTEIN;

CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; DNA DAMAGE; DNA REPAIR; FANCONI ANEMIA; GENETICS; GENOMIC INSTABILITY; HEK293 CELL LINE; HELA CELL LINE; HUMAN; METABOLISM; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION;

APOPTOSIS REGULATORY PROTEINS; DNA; DNA DAMAGE; DNA HELICASES; DNA REPAIR; DNA, CRUCIFORM; DNA-BINDING PROTEINS; FANCONI ANEMIA; GENOMIC INSTABILITY; HEK293 CELLS; HELA CELLS; HISTONES; HUMANS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; NUCLEAR PROTEINS; NUCLEIC ACID CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; TUMOR SUPPRESSOR PROTEINS;

EID: 84899948111     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2014.42     Document Type: Article

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