Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
about
Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulationThe metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidasesSwapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseThe neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylationCrystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localizationMolecular cloning and expression of rat liver aminopeptidase BCharacterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidaseMolecular cloning and expression of rat brain endopeptidase 3.4.24.16Thimet oligopeptidase: similarity to 'soluble angiotensin II-binding protein' and some corrections to the published amino acid sequence of the rat testis enzymeThe role of Tyr605 and Ala607 of thimet oligopeptidase and Tyr606 and Gly608 of neurolysin in substrate hydrolysis and inhibitor bindingExocytosis and protein secretion in Trypanosoma.Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin releasing hormone.Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme.Sequence analysis of rat mitochondrial intermediate peptidase: similarity to zinc metallopeptidases and to a putative yeast homologue.N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes.dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product.Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain.Rat thimet oligopeptidase: large-scale expression in Escherichia coli and characterization of the recombinant enzyme.Structural features that make oligopeptides susceptible substrates for hydrolysis by recombinant thimet oligopeptidaseFamilies of metalloendopeptidases and their relationships.Phosphorus-containing peptides as mixed inhibitors of endopeptidase 3.4.24.15 and 3.4.24.16: effect on neurotensin degradation in vitro and in vivo.Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimuriumDevelopment of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24-15 using combinatorial chemistry.Luteinizing hormone-releasing hormone I (LHRH-I) and its metabolite in peripheral tissues.Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selectionThe Trypanosoma brucei gambiense secretome impairs lipopolysaccharide-induced maturation, cytokine production, and allostimulatory capacity of dendritic cellsThe A alpha mating locus of Schizophyllum commune encodes two dissimilar multiallelic homeodomain proteins.Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4.24.15. Identification of active site histidine and glutamate residues.Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells.Intracellular peptides as natural regulators of cell signaling.Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15.Endopeptidase 3.4.24.11 converts N-1-(R,S)carboxy-3-phenylpropyl-Ala-Ala-Phe-p-carboxyanilide into a potent inhibitor of angiotensin-converting enzyme.Regulation of cell-surface major histocompatibility complex class I expression by the endopeptidase EC3.4.24.15 (thimet oligopeptidase).Thimet oligopeptidase (EC 3.4.24.15): the same by any name?Thimet oligopeptidase expression is differentially regulated in neuroendocrine and spermatid cell lines by transcription factor binding to SRY (sex-determining region Y), CAAT and CREB (cAMP-response-element-binding protein) promoter consensus sequeA higher plant mitochondrial homologue of the yeast m-AAA protease. Molecular cloning, localization, and putative function.A structure-based site-directed mutagenesis study on the neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) catalysis.Targeting of endopeptidase 24.16 to different subcellular compartments by alternative promoter usage.Tissue distribution and subcellular localization of rabbit liver metalloendopeptidase.THOP1 cleaves oligopeptide fragment (8-16aa)
P2860
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P2860
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
description
1990 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1990
@ast
im November 1990 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1990/11/13)
@sk
vědecký článek publikovaný v roce 1990
@cs
wetenschappelijk artikel (gepubliceerd op 1990/11/13)
@nl
наукова стаття, опублікована в листопаді 1990
@uk
مقالة علمية (نشرت في 13-11-1990)
@ar
name
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@ast
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@en
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@nl
type
label
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@ast
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@en
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@nl
prefLabel
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@ast
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@en
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@nl
P2093
P356
P1433
P1476
Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
@en
P2093
A. Pierotti
J. L. Roberts
K. W. Dong
M. J. Glucksman
M. Orlowski
P304
10323–10329
P356
10.1021/BI00497A006
P407
P577
1990-11-13T00:00:00Z