Isoaspartate residues dramatically influence substrate recognition and turnover by proteases

Biological Chemistry

Volumn 389, Issue 8, 2008, Pages 1043-1053

  Böhme, Livia ^a   Bär, Joachim Wolfgang ^b   Hoffmann, Torsten ^a   Manhart, Susanne ^a   Ludwig, Hans Henning ^a   Rosche, Fred ^a   Demuth, Hans Ulrich ^a  

^a PROBIODRUG AG   (Germany)

^b BOEHRINGER INGELHEIM PHARMA GMBH AND CO KG   (Germany)

Author keywords

Alzheimer's disease; Amyloid ; Isoaspartate; Peptidase; Substrate specificity

Indexed keywords

ACYLAMINO ACID RELEASING ENZYME; ASPARTIC ACID; CASPASE; CASPASE 6; DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE I; DIPEPTIDYL PEPTIDASE IV; ENTEROPEPTIDASE; EXOPEPTIDASE; ISOASPARTIC ACID; MICROSOMAL AMINOPEPTIDASE; PROLINE; PROLYL ENDOPEPTIDASE; PROTEINASE; SERUM AMYLOID A; STROMELYSIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; MOLECULAR RECOGNITION; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN HYDROLYSIS; PROTEIN METABOLISM; PROTEIN PROCESSING;

CELL LINE, TUMOR; ENZYME ACTIVATION; HUMANS; HYDROLYSIS; ISOASPARTIC ACID; KINETICS; MOLECULAR STRUCTURE; PEPTIDE HYDROLASES; SUBSTRATE SPECIFICITY;

EID: 50849124783     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2008.123     Document Type: Conference Paper

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