A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides.
about
Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulationHuman thimet oligopeptidaseSwapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseThe neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylationMajor histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidaseCrystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localizationMolecular cloning and expression of rat liver aminopeptidase BRole of angiotensin converting enzyme in the vascular effects of an endopeptidase 24.15 inhibitorMolecular 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 enzymeHormonal regulation of female reproduction.Specificity of the dynorphin-processing endoprotease: comparison with prohormone convertases.The role of Tyr605 and Ala607 of thimet oligopeptidase and Tyr606 and Gly608 of neurolysin in substrate hydrolysis and inhibitor bindingPrologue: kinins and related systems. New life for old discoveries.Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin releasing hormone.Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase.Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme.Metalloendopeptidases EC 3.4.24.15/16 regulate bradykinin activity in the cerebral microvasculature.Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit.Purification and characterization of a dynorphin-processing endopeptidase.Overexpression of the PepF oligopeptidase inhibits sporulation initiation in Bacillus subtilis.The cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for S-glutathiolation and oxidative oligomerization.Modulation of bradykinin signaling by EP24.15 and EP24.16 in cultured trigeminal ganglia.Metalloendopeptidase EC 3.4.24.15 is necessary for Alzheimer's amyloid-beta peptide degradation.Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain.Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides.Recycling of the high valence States of heme proteins by cysteine residues of THIMET-oligopeptidase.Metallopeptidase inhibition potentiates bradykinin-induced hyperalgesia.Kinin receptors of the central nervous system of spontaneously hypertensive rats related to the pressor response to bradykininPhosphorus-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.Synthetic inhibitors of endopeptidase EC 3.4.24.15: potency and stability in vitro and in vivoRole of bradykinin receptors in the renal effects of inhibition of angiotensin converting enzyme and endopeptidases 24.11 and 24.15 in conscious rabbits.EP24.15 as a Potential Regulator of Kisspeptin Within the Neuroendocrine Hypothalamus.The role of neurotensin in central nervous system pathophysiology: what is the evidence?Development 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.Degradation of thyrotropin-releasing hormone and luteinising hormone-releasing hormone by enzymes of brain tissue.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.
P2860
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P2860
A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides.
description
1983 nî lūn-bûn
@nan
1983 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1983 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1983年の論文
@ja
1983年論文
@yue
1983年論文
@zh-hant
1983年論文
@zh-hk
1983年論文
@zh-mo
1983年論文
@zh-tw
1983年论文
@wuu
name
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@ast
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@en
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@nl
type
label
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@ast
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@en
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@nl
prefLabel
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@ast
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@en
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@nl
P2093
P2860
P1433
P1476
A soluble metalloendopeptidase ...... ynthetic and natural peptides.
@en
P2093
P2860
P356
10.1111/J.1432-1033.1983.TB07620.X
P407
P577
1983-09-01T00:00:00Z