Nicastrin, a presenilin-interacting protein, contains an aminopeptidase/transferrin receptor superfamily domain

Trends in Biochemical Sciences

Volumn 26, Issue 4, 2001, Pages 213-214

  Fagan, Richard ^a   Swindells, Mark ^a   Overington, John ^a   Weir, Malcolm ^a  

^a Inpharmatica   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; AMYLOID BETA PROTEIN; NICASTRIN; PRESENILIN 1; PRESENILIN 2; PROTEIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; BINDING AFFINITY; BINDING SITE; CATALYSIS; ENZYME ACTIVITY; ENZYME BINDING; HUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN INTERACTION; SEQUENCE ANALYSIS; SHORT SURVEY;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; AMYLOID PRECURSOR PROTEIN SECRETASES; HUMANS; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PRESENILIN-1; PRESENILIN-2; PROTEIN BINDING; RECEPTORS, TRANSFERRIN; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0035312603     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(01)01789-3     Document Type: Short Survey

References (7)

1. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
2. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
3. GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
4. Crystal structure of the ectodomain of human transferrin receptor
5. Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75 Å resolution
6. The extracellular regions of PSMA and the transferrin receptor contain an aminopeptidase domain: Implications for drug design
7. Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin