Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast

Autophagy

Volumn 10, Issue 6, 2014, Pages 1093-1104

  Popelka, Hana ^a   Uversky, Vladimir N ^b,c   Klionsky, Daniel J ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF SOUTH FLORIDA   (United States)

^c INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

Author keywords

Atg3; Autophagy; Intrinsically disordered protein; Stress; Vacuole; Yeast

Indexed keywords

ATG3 PROTEIN; ATG3DELTAFR PROTEIN; ATG3FR PROTEIN; FUNGAL PROTEIN; HYBRID PROTEIN; INTRINSICALLY DISORDERED PROTEIN; PROTEIN VARIANT; UNCLASSIFIED DRUG; ATG3 PROTEIN, HUMAN; ATG3 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN CONJUGATING ENZYME;

AMINO ACID SEQUENCE; ARTICLE; AUTOPHAGY; BIOINFORMATICS; CONFORMATIONAL TRANSITION; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SACCHAROMYCES CEREVISIAE; CHEMICAL STRUCTURE; CHEMISTRY; CYTOLOGY; GENETICS; PHYSIOLOGY;

AUTOPHAGY; HUMANS; INTRINSICALLY DISORDERED PROTEINS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN-CONJUGATING ENZYMES;

EID: 84903585372     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.28616     Document Type: Article

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