Glutamate carboxypeptidase II does not process amyloid-beta peptide
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10189921" target="_blank" >RIV/00216208:11310/13:10189921 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/13:00424007
Result on the web
<a href="http://dx.doi.org/10.1096/fj.12-225094" target="_blank" >http://dx.doi.org/10.1096/fj.12-225094</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1096/fj.12-225094" target="_blank" >10.1096/fj.12-225094</a>
Alternative languages
Result language
angličtina
Original language name
Glutamate carboxypeptidase II does not process amyloid-beta peptide
Original language description
The accumulation of amyloid- (A) peptide is thought to be a major causative mechanism of Alzheimer's disease. A accumulation could be caused by dysregulated processing of amyloid precursor protein, yielding excessive amounts of A, and/or by inefficient proteolytic degradation of the peptide itself. Several proteases have been described as A degradation enzymes, most notably metalloendopeptidases, aspartic endopeptidases, and some exopeptidases. Recently a report suggested that another metallopeptidase,glutamate carboxypeptidase II (GCPII), can also cleave A. GCPII is a zinc exopeptidase that cleaves glutamate from N-acetyl-l-aspartyl-l-glutamate in the central nervous system and from pteroylpoly--glutamate in the jejunum. GCPII has been proposed as apromising therapeutic target for disorders caused by glutamate neurotoxicity. However, an A-degrading activity of GCPII would compromise potential pharmaceutical use of GCPII inhibitors, because the enzyme inhibition might lead to increas
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP304%2F12%2F0847" target="_blank" >GAP304/12/0847: Glutamate Carboxypeptidase II and its role in cancer development</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FASEB Journal
ISSN
0892-6638
e-ISSN
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Volume of the periodical
27
Issue of the periodical within the volume
7
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
2626-2632
UT code for WoS article
000328841000012
EID of the result in the Scopus database
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