The Q motif of fanconi anemia group J protein (FANCJ) DNA helicase regulates its dimerization, DNA binding, and DNA repair function

Journal of Biological Chemistry

Volumn 287, Issue 26, 2012, Pages 21699-21716

  Wu, Yuliang ^a,d   Sommers, Joshua A ^a   Loiland, Jason A ^a   Kitao, Hiroyuki ^b   Kuper, Jochen ^c   Kisker, Caroline ^c   Brosh, Robert M ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b KYUSHU UNIVERSITY   (Japan)

^c UNIVERSITY OF WÜRZBURG   (Germany)

^d UNIVERSITY OF SASKATCHEWAN   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL CULTURE; DIMERS; DNA; RECOMBINANT PROTEINS; REPAIR; SIZE EXCLUSION CHROMATOGRAPHY;

ATP-BINDING; DIMERIZATIONS; DNA HELICASES; DNA-BINDING; DNA-REPAIR; FANCONI ANEMIAS; HELICASE ACTIVITIES; REPAIR FUNCTIONS; RNA HELICASES; STRUCTURAL DATA;

MONOMERS;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; DIMER; DNA; FANCONI ANEMIA GROUP J PROTEIN; FANCONI ANEMIA PROTEIN; GLUTAMINE; HELICASE; MONOMER; MUTANT PROTEIN; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DIMERIZATION; DNA REPAIR; ENZYME ACTIVITY; ENZYME DEFECT; FANCJ GENE; GEL PERMEATION CHROMATOGRAPHY; GENE; GENE FUNCTION; GENE MUTATION; GENETIC CODE; GENETIC CONSERVATION; HYDROLYSIS; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MOTIF; SEDIMENTATION RATE; STRUCTURE ACTIVITY RELATION; WILD TYPE;

EID: 84862663683     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.351338     Document Type: Article

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