LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplamic reticulum

EMBO Journal

Volumn 19, Issue 23, 2000, Pages 6440-6452

  Tyson, J R ^a   Stirling, C J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Endoplasmic reticulum; IRE1; LHS1; SIL1,PER100,YOL031c; Translocation; UPR

Indexed keywords

CHAPERONE; SIGNAL RECOGNITION PARTICLE;

AMINO ACID SEQUENCE; ARTICLE; DROSOPHILA; ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; INTRACELLULAR TRANSPORT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN TRANSPORT; SEQUENCE HOMOLOGY; TRANSPORT KINETICS; YARROWIA LIPOLYTICA;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; ANIMALS; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; BETA-GALACTOSIDASE; CARRIER PROTEINS; CELL DIVISION; DROSOPHILA; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPLASMIC RETICULUM; GENES, REPORTER; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GUANINE NUCLEOTIDE EXCHANGE FACTORS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; IMMUNOBLOTTING; MEMBRANE TRANSPORT PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTATION; PLASMIDS; PRECIPITIN TESTS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SEPHAROSE; SEQUENCE HOMOLOGY, AMINO ACID; SUPPRESSION, GENETIC; TIME FACTORS; TUNICAMYCIN;

ESCHERICHIA COLI; EUKARYOTA; MAMMALIA; YARROWIA LIPOLYTICA;

EID: 0034388026     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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