P130Cas substrate domain is intrinsically disordered as characterized by single-molecule force measurements

Biophysical Chemistry

Volumn 180-181, Issue , 2013, Pages 37-43

  Lu, Chen ^a,b,c   Wu, Fei ^a,b   Qiu, Wu ^b   Liu, Ruchuan ^a,b,c  

^a CHONGQING UNIVERSITY   (China)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^c NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

AFM; Intrinsically disordered protein; Magnetic tweezer; Mechano transduction; P130Cas; Tyrosine phosphorylation

Indexed keywords

CRK ASSOCIATED SUBSTRATE PROTEIN;

ARTICLE; ATOMIC FORCE MICROSCOPY; FORCE; MOLECULAR INTERACTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN UNFOLDING; SINGLE MOLECULE FORCE; STRENGTH; STRETCHING; STRUCTURE ANALYSIS;

AFM; INTRINSICALLY DISORDERED PROTEIN; MAGNETIC TWEEZER; MECHANO-TRANSDUCTION; P130CAS; TYROSINE PHOSPHORYLATION;

AMINO ACID MOTIFS; CRK-ASSOCIATED SUBSTRATE PROTEIN; HUMANS; MICROSCOPY, ATOMIC FORCE; PHOSPHORYLATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY;

EID: 84879830235     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.06.008     Document Type: Article

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