GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1823, Issue 3, 2012, Pages 774-787

  Marzec, Michal ^a   Eletto, Davide ^a   Argon, Yair ^a  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

Author keywords

Endoplasmic reticulum; ER stress response; Glucose regulated protein 94; Protein folding; Secretory proteins pathway

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; GLUCOSE REGULATED PROTEIN 94;

ACETYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; CELL ACTIVITY; CELLULAR DISTRIBUTION; CONFORMATIONAL TRANSITION; CYTOSOL; DIMERIZATION; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVITY; GLYCOSYLATION; HUMAN; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN SECRETION; QUALITY CONTROL; TRANSCRIPTION REGULATION;

AMINO ACID SEQUENCE; ANIMALS; ENDOPLASMIC RETICULUM; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING;

EID: 84857053996     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.10.013     Document Type: Article

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