Single-molecule sorting reveals how ubiquitylation affects substrate recognition and activities of FBH1 helicase

Nucleic Acids Research

Volumn 41, Issue 6, 2013, Pages 3576-3587

  Masuda Ozawa, Tokiha ^a,b   Hoang, Trish ^a   Seo, Yeon Soo ^c   Chen, Lin Feng ^a   Spies, Maria ^a,b,d  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^d UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; F BOX CONTAINING DNA HELICASE 1; HELICASE; RAD51 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DNA REPLICATION FORK; DNA STRUCTURE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE MICROSCOPY; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DNA INTERACTION; PROTEIN ISOLATION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SINGLE MOLECULE SORTING; TOTAL INTERNAL REFLECTION FLUORESCENCE MICROSCOPY; UBIQUITINATION;

BINDING SITES; DNA; DNA HELICASES; DNA REPLICATION; DNA-BINDING PROTEINS; HEK293 CELLS; HUMANS; PROTEIN STRUCTURE, TERTIARY; RAD51 RECOMBINASE; UBIQUITINATION;

EID: 84876021636     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt056     Document Type: Article

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