Eggert et al., 2004 - Google Patents

The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves α-, β-, γ-, and ϵ-like cleavages: modulation of APLP-1 …

Eggert et al., 2004

View HTML @Full View
Document ID
3246637319216622042
Author
Eggert S
Paliga K
Soba P
Evin G
Masters C
Weidemann A
Beyreuther K
Publication year
Publication venue
Journal of Biological Chemistry

External Links

Snippet

Amyloid precursor protein (APP) processing is of major interest in Alzheimer's disease research, since sequential cleavages by β-and γ-secretase lead to the formation of the 4- kDa amyloid Aβ protein peptide that accumulates in Alzheimer's disease brain. The …
Continue reading at www.jbc.org (HTML) (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90—Enzymes; Proenzymes
    • G01N2333/914—Hydrolases (3)
    • G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
    • G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
    • G01N2333/964—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
    • G01N2333/96425—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals
    • G01N2333/96427—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing

Similar Documents

Publication Publication Date Title
Eggert et al. The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves α-, β-, γ-, and ϵ-like cleavages: modulation of APLP-1 processing by N-glycosylation
Benjannet et al. Post-translational processing of β-secretase (β-amyloid-converting enzyme) and its ectodomain shedding: the pro-and transmembrane/cytosolic domains affect its cellular activity and amyloid-β production
Fluhrer et al. A non‐amyloidogenic function of BACE‐2 in the secretory pathway
Bennett et al. A furin-like convertase mediates propeptide cleavage of BACE, the Alzheimer's β-secretase
Vassar The β-secretase, BACE: a prime drug target for Alzheimer’s disease
Nunan et al. The C‐terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome‐dependent mechanism distinct from γ‐secretase
Vassar Bace 1: The β-secretase enzyme in alzheimer’s disease
Kitazume et al. Characterization of α2, 6-sialyltransferase cleavage by Alzheimer's β-secretase (BACE1)
Mathews et al. Calpain activity regulates the cell surface distribution of amyloid precursor protein: inhibition of calpains enhances endosomal generation of β-cleaved C-terminal APP fragments
Qi-Takahara et al. Longer forms of amyloid β protein: implications for the mechanism of intramembrane cleavage by γ-secretase
Sato et al. The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the γ-secretase
Schulz et al. Syndecan 3 intramembrane proteolysis is presenilin/γ-secretase-dependent and modulates cytosolic signaling
Wolfe Secretase targets for Alzheimer's disease: identification and therapeutic potential
Lichtenthaler et al. The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1
Roßner et al. Neuronal and glial β‐secretase (BACE) protein expression in transgenic Tg2576 mice with amyloid plaque pathology
Evin et al. Proteolytic processing of the Alzheimer's disease amyloid precursor protein in brain and platelets
Farmery et al. Partial purification and characterization of γ-secretase from post-mortem human brain
Sevalle et al. Aminopeptidase A contributes to the N‐terminal truncation of amyloid β‐peptide
Liu et al. Glu11 site cleavage and N-terminally truncated Aβ production upon BACE overexpression
Westmeyer et al. Dimerization of β-site β-amyloid precursor protein-cleaving enzyme
Zhou et al. Inhibition of β-secretase in vivo via antibody binding to unique loops (D and F) of BACE1
Wolfe Toward the structure of presenilin/γ-secretase and presenilin homologs
US20020159991A1 (en) Modulation of Abeta levels by beta-secretase BACE2
Nunan et al. Proteasome‐mediated degradation of the C‐terminus of the Alzheimer's disease β‐amyloid protein precursor: Effect of C‐terminal truncation on production of β‐amyloid protein
Wiley et al. Familial Alzheimer's disease mutations inhibit γ‐secretase‐mediated liberation of β‐amyloid precursor protein carboxy‐terminal fragment