Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

Journal of Biological Chemistry

Volumn 281, Issue 36, 2006, Pages 26569-26577

  Spasic, Dragana ^a   Tolia, Alexandra ^a   Dillen, Katleen ^a   Baert, Veerle ^a   De Strooper, Bart ^a   Vrijens, Stefan ^a   Annaert, Wim ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTINYLATION; INTRAMEMBRANE PROTEOLYSIS; MUTANTS; TRANSMEMBRANE PROTEINS;

BIOLOGICAL MEMBRANES; CELLS; ENZYMES; MUTAGENESIS; PHYSIOLOGY; SURFACE PHENOMENA;

BIOCHEMISTRY;

CYSTEINE; MEMBRANE PROTEIN; PRESENILIN 1;

ARTICLE; BIOTINYLATION; CARBOXY TERMINAL SEQUENCE; CELL SURFACE; CONFORMATIONAL TRANSITION; CONSENSUS; ENDOPLASMIC RETICULUM; GLYCOSYLATION; GOLGI COMPLEX; HUMAN; HUMAN CELL; HYPOTHESIS; MEMBRANE STRUCTURE; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN SECRETION; PROTEIN TRANSPORT;

AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; GLYCOSYLATION; HELA CELLS; HUMANS; MICE; MICE, KNOCKOUT; MODELS, MOLECULAR; PRESENILIN-1; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 33748746861     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M600592200     Document Type: Article

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