Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway

Journal of Biological Chemistry

Volumn 288, Issue 41, 2013, Pages 29586-29594

  Kakihana, Taichi ^a,b   Araki, Kazutaka ^d   Vavassori, Stefano ^c   Iemura, Shun Ichiro ^e   Cortini, Margherita ^d   Fagioli, Claudio ^c   Natsume, Tohru ^d   Sitia, Roberto ^c   Nagata, Kazuhiro ^b  

^a KYOTO UNIVERSITY   (Japan)

^b KYOTO SANGYO UNIVERSITY   (Japan)

^c SAN RAFFAELE HOSPITAL   (Italy)

^d NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^e FUKUSHIMA MEDICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROPERTIES; DYNAMIC REGULATION; INTRACELLULAR LOCALIZATION; NASCENT PROTEIN; OXIDATIVE FOLDING; PROTEIN DISULFIDE ISOMERASES; SECRETORY PATHWAYS; SEQUENTIAL INTERACTIONS;

BINDING ENERGY; ENZYME ACTIVITY; PHYSIOLOGY; PROTEIN FOLDING;

PROTEINS;

ERO1 ALPHA PROTEIN; ERP44 PROTEIN; FLAVOPROTEIN; PEROXIREDOXIN 4; PROTEIN DISULFIDE ISOMERASE; UNCLASSIFIED DRUG;

ARTICLE; CELL LEVEL; CELL PH; CELLULAR DISTRIBUTION; CONTROLLED STUDY; DOWN REGULATION; EARLY SECRETORY COMPARTMENT; HUMAN; HUMAN CELL; INTRACELLULAR SIGNALING; INTRACELLULAR SPACE; MOLECULAR MECHANICS; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; REGULATORY MECHANISM; SECRETORY PATHWAY;

ENDOPLASMIC RETICULUM (ER); ERO1; OXIDASE; PEROXIREDOXIN; PRX4; RETENTION MECHANISM; THIOL; TRAFFICKING;

AMINO ACID SEQUENCE; BLOTTING, WESTERN; ENDOPLASMIC RETICULUM; HEK293 CELLS; HELA CELLS; HOMEOSTASIS; HUMANS; KINETICS; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; MICROSCOPY, CONFOCAL; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PEROXIREDOXINS; PROTEIN BINDING; PROTEIN DISULFIDE-ISOMERASES; RNA INTERFERENCE; SECRETORY PATHWAY; SURFACE PLASMON RESONANCE;

EID: 84885668419     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.467845     Document Type: Article

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