Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
about
Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseDeregulation of gluconeogenic structural genes by variants of the transcriptional activator Cat8p of the yeast Saccharomyces cerevisiae.Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localizationNeurolysin knockout mice generation and initial phenotype characterizationIdentification of membrane-bound variant of metalloendopeptidase neurolysin (EC 3.4.24.16) as the non-angiotensin type 1 (non-AT1), non-AT2 angiotensin binding siteThe role of Tyr605 and Ala607 of thimet oligopeptidase and Tyr606 and Gly608 of neurolysin in substrate hydrolysis and inhibitor bindingThe effects of para-chloromercuribenzoic acid and different oxidative and sulfhydryl agents on a novel, non-AT1, non-AT2 angiotensin binding site identified as neurolysin.Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme.Functional up-regulation of endopeptidase neurolysin during post-acute and early recovery phases of experimental stroke in mouse brain.Characterization and localization of mitochondrial oligopeptidase (MOP) (EC 3.4.24.16) activity in the human cervical adenocarcinoma cell line HeLa.Modulation of bradykinin signaling by EP24.15 and EP24.16 in cultured trigeminal ganglia.Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain.MHC class I alleles and their exploration of the antigen-processing machinery.Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selectionRecent insights and therapeutic perspectives of angiotensin-(1-9) in the cardiovascular system.Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4.24.15. Identification of active site histidine and glutamate residues.A structure-based site-directed mutagenesis study on the neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) catalysis.pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15).Targeting of endopeptidase 24.16 to different subcellular compartments by alternative promoter usage.
P2860
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P2860
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
description
1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1995
@ast
im November 1995 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/11/10)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/11/10)
@nl
наукова стаття, опублікована в листопаді 1995
@uk
name
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@ast
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@en
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@nl
type
label
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@ast
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@en
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@nl
prefLabel
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@ast
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@en
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@nl
P2093
P2860
P356
P1476
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
@en
P2093
F. Checler
J. P. Vincent
P2860
P304
27266–27271
P356
10.1074/JBC.270.45.27266
P407
P577
1995-11-10T00:00:00Z