Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis

Journal of Biological Chemistry

Volumn 289, Issue 52, 2014, Pages 36059-36069

  Ham, Hyeilin ^a   Woolery, Andrew R ^a   Tracy, Charles ^b   Stenesen, Drew ^b   Krämer, Helmut ^b   Orth, Kim ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; PHYSIOLOGY; SUBSTRATES;

ADENOSINE MONOPHOSPHATE; COVALENT ATTACHMENT; DROSOPHILA S2 CELLS; ENDOPLASMIC RETICULUM; HYDROXYL SIDES; MISFOLDED PROTEINS; PROTEIN SUBSTRATE; UNFOLDED PROTEIN RESPONSE;

PROTEINS;

CYCLIC AMP; FILAMENTATION INDUCED BY CYCLIC AMP PROTEIN; GLUCOSE REGULATED PROTEIN 78; UNCLASSIFIED DRUG; ADENOSINE PHOSPHATE; DROSOPHILA PROTEIN; FIC PROTEIN, DROSOPHILA; HEAT SHOCK COGNATE PROTEIN 70; HSC70-3 PROTEIN, DROSOPHILA; NUCLEOTIDYLTRANSFERASE;

AMPYLATION; ARTICLE; BIOACCUMULATION; CANCER THERAPY; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVATION; HOMEOSTASIS; HUMAN; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; UNFOLDED PROTEIN RESPONSE; AMINO ACID SEQUENCE; ANIMAL; CELL LINE; CHEMISTRY; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETIC TRANSCRIPTION; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; UPREGULATION;

ADENOSINE MONOPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CELL LINE; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; HOMEOSTASIS; HSC70 HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; NUCLEOTIDYLTRANSFERASES; PROTEIN PROCESSING, POST-TRANSLATIONAL; TRANSCRIPTION, GENETIC; UNFOLDED PROTEIN RESPONSE; UP-REGULATION;

EID: 84984801564     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.612515     Document Type: Article

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