Glu332 in the nicastrin ectodomain is essential for γ-secretase complex maturation but not for its activity

Journal of Biological Chemistry

Volumn 283, Issue 29, 2008, Pages 20096-20105

  Chávez Gutiérrez, Lucía ^a,b   Tolia, Alexandra ^a,b   Maes, Elke ^a,b   Li, Tong ^c   Wong, Philip C ^c   De Strooper, Bart ^a,b  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b VIB4 ^*  (Belgium)

^c JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINES; ANIMAL CELL CULTURE; BINDING ENERGY; BINDING SITES; PORT TERMINALS; PROTEINS;

ACTIVE SITES; AMINO PEPTIDASES; BINDING POCKETS; DO-MAINS; ECTODOMAIN; ENZYMATIC ACTIVITIES; IN VITRO; IN-VIVO; INTEGRAL MEMBRANE PROTEINS; NICASTRIN; PUTATIVE BINDING SITES; SECRETASE; SECRETASE COMPLEXES; SUBSTRATE RECOGNITIONS; TERMINAL GROUPS;

SUBSTRATES;

ALPHA AMINO ACID; AMINOPEPTIDASE; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; GLUTAMIC ACID; NICASTRIN; NOTCH RECEPTOR; MEMBRANE PROTEIN; NICASTRIN PROTEIN; SECRETASE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; IN VITRO STUDY; IN VIVO STUDY; MOUSE; MUTAGENESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PROCESSING; WILD TYPE; ANIMAL; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; GENE EXPRESSION; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; MOUSE MUTANT; NUCLEOTIDE SEQUENCE; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; BINDING SITES; CELL LINE; CONSERVED SEQUENCE; GENE EXPRESSION; GLUTAMIC ACID; HUMANS; MEMBRANE GLYCOPROTEINS; MICE; MICE, KNOCKOUT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 50649119079     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M803040200     Document Type: Article

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