Polar transmembrane-based amino acids in presenilin 1 are involved in endoplasmic reticulum localization, Pen2 protein binding, and γ-secretase complex stabilization

Journal of Biological Chemistry

Volumn 286, Issue 44, 2011, Pages 38390-38396

  Fassler, Matthias ^a   Li, Xiaolin ^a   Kaether, Christoph ^a  

^a FRITZ LIPMANN INSTITUTE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATES; ENDOPLASMIC RETICULUM; HIGH MOLECULAR WEIGHT; MEMBRANE PROTEINS; NICASTRIN; POLAR AMINO ACIDS; POLAR INTERFACE; PRESENILINS; PROTEIN BINDING; PROTEIN-PROTEIN INTERACTIONS; SECRETASE COMPLEX; SECRETASES; TRANSMEMBRANE DOMAIN;

ACTIVATION ANALYSIS; AMINO ACIDS; BIOCHEMISTRY; BIOLOGICAL MEMBRANES; CATALYST ACTIVITY; COORDINATION REACTIONS;

PROTEINS;

AMINO ACID; ASPARAGINE; ASPARTIC ACID; GAMMA SECRETASE; PEN2 PROTEIN; POLAR AMINO ACID; PRESENILIN 1; PROTEIN SUBUNIT; THREONINE; TMD4 PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBUNIT; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

ALZHEIMER DISEASE; AMINO ACIDS; ANIMALS; ASPARAGINE; BINDING SITES; GLYCOSYLATION; HEK293 CELLS; HUMANS; MICE; MICE, KNOCKOUT; MUTATION; PRESENILIN-1; PRESENILIN-2; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 80055086480     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.252429     Document Type: Article

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