Lis1 regulates dynein by sterically blocking its mechanochemical cycle

eLife

Volumn 3, Issue , 2014, Pages

  Toropova, Katerina ^a   Zou, Sirui ^a   Roberts, Anthony J ^a   Redwine, William B ^a   Goodman, Brian S ^a   Reck Peterson, Samara L ^a   Leschziner, Andres E ^a  

^a HARVARD UNIVERSITY   (United States)

Author keywords

biochemistry; biophysics; dynein; electron microscopy; Lis1; microtubules; S. cerevisiae; structural biology; structure

Indexed keywords

ADENOSINE TRIPHOSPHATE; DYN1 PROTEIN, S CEREVISIAE; DYNEIN ADENOSINE TRIPHOSPHATASE; PAC1 PROTEIN, S CEREVISIAE; RECOMBINANT PROTEIN; RIBONUCLEASE; SACCHAROMYCES CEREVISIAE PROTEIN;

AMINO ACID SEQUENCE; BIOMECHANICS; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN ENGINEERING; SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BIOMECHANICAL PHENOMENA; DYNEINS; ENDORIBONUCLEASES; GENE EXPRESSION REGULATION, FUNGAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84963853379     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.03372     Document Type: Article

References (0)