The large hydrophilic loop of presenilin 1 is important for regulating γ-secretase complex assembly and dictating the amyloid β peptide (Aβ) profile without affecting notch processing

Journal of Biological Chemistry

Volumn 285, Issue 12, 2010, Pages 8527-8536

  Wanngren, Johanna ^a   Frånberg, Jenny ^a   Svensson, Annelie I ^a   Laudon, Hanna ^a   Olsson, Fredrik ^b   Winblad, Bengt ^a   Liu, Frank ^c   Näslund, Jan ^b   Lundkvist, Johan ^b   Karlström, Helena ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b ASTRAZENECA R AND D   (Sweden)

^c ASTRAZENECA   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID PRECURSOR PROTEINS; CATALYTIC SUBUNITS; CLEAVAGE ACTIVITIES; DIFFERENTIAL EFFECT; ENDOPROTEOLYSIS; ENZYME COMPLEXES; INTRACELLULAR DOMAIN; NOTCH SIGNALING; PEPTIDE PRODUCTION; PRESENILINS; SECRETASE COMPLEX; SECRETASES; TWO PARAMETER;

AMINO ACIDS; ENZYME ACTIVITY; GLYCOPROTEINS; HYDROPHILICITY; ORGANIC ACIDS; PUMPING PLANTS;

PEPTIDES;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-38]; AMYLOID BETA PROTEIN[1-39]; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; GAMMA SECRETASE; NOTCH RECEPTOR; PRESENILIN 1; PRESENILIN 2; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); COMPLEMENTARY DNA; GLYCOSIDASE; PEPTIDE FRAGMENT; SECRETASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYTOPLASM; EMBRYO; ENZYME ACTIVITY; EXON; GENE DELETION; GLYCOSYLATION; HUMAN; HUMAN CELL; HYDROPHILICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN PROCESSING; BLASTOCYST; CELL LINE; CHEMISTRY; ENZYME ACTIVE SITE; GENETIC TRANSFECTION; METABOLISM; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE;

AMYLOID BETA-PROTEIN; AMYLOID PRECURSOR PROTEIN SECRETASES; BLASTOCYST; CATALYTIC DOMAIN; CELL LINE; DNA, COMPLEMENTARY; EXONS; GLYCOSIDE HYDROLASES; HUMANS; PEPTIDE FRAGMENTS; PRESENILIN-1; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, NOTCH; TRANSFECTION;

EID: 77950551338     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.055590     Document Type: Article

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