Pro-domain removal in ASP-2 and the cleavage of the amyloid precursor areinfluenced by pH

BMC Biochemistry

Volumn 3, Issue , 2002, Pages 1-12

  Sidera, Christina ^a   Liu, Chibuu ^a   Austen, Brian ^a  

^a ST GEORGE'S UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ASPARTIC PROTEINASE; ASPARTIC PROTEINASE 1; ASPARTIC PROTEINASE 2; BETA SECRETASE; BETA SECRETASE INHIBITOR; NICKEL; PROTEIN PRECURSOR; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; SECRETASE;

ACIDITY; ALKALINITY; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; ELECTROPHORESIS; ENZYME ACTIVITY; ENZYME GLYCOSYLATION; ENZYME PURIFICATION; HUMAN; HUMAN CELL; IN VITRO STUDY; MASS SPECTROMETRY; MOLECULAR SIZE; PH; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROCESSING; AMINO ACID SEQUENCE; CELL LINE; COMPARATIVE STUDY; GENETICS; HYDROLYSIS; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; ASPARTIC ACID ENDOPEPTIDASES; CELL LINE; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY;

EID: 34248353880     PISSN: 14712091     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2091-3-25     Document Type: Article

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