Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 50, 2005, Pages 17999-18004

  Sato, Takehiro ^a   Esaki, Masatoshi ^a,c   Fernandez, Julio M ^b   Endo, Toshiya ^a  

^a NAGOYA UNIVERSITY   (Japan)

^b Och Spine at New York Presbyterian Hospitals   (United States)

^c UNIVERSITY OF CHICAGO   (United States)

Author keywords

Hsp70; Mechanical stability; Mitochondria; Titin

Indexed keywords

CONNECTIN; DIHYDROFOLATE REDUCTASE; DNA FRAGMENT; HEAT SHOCK PROTEIN 70; HYBRID PROTEIN; LACTATE DEHYDROGENASE (CYTOCHROME); MITOCHONDRIAL PROTEIN; PEPTIDASE; PROTEIN PRECURSOR; VALINOMYCIN;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HYDROGEN BOND; MEMBRANE TRANSPORT; MITOCHONDRIAL MEMBRANE; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TRANSPORT; PROTEIN UNFOLDING; SACCHAROMYCES CEREVISIAE;

MICROSCOPY, ATOMIC FORCE; MITOCHONDRIA; MODELS, MOLECULAR; MUSCLE PROTEINS; MUTAGENESIS; PROTEIN FOLDING; PROTEIN KINASES; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 29144439725     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0504495102     Document Type: Article

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