Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
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The Alzheimer's amyloid-degrading peptidase, neprilysin: can we control it?The Kell protein of the common K2 phenotype is a catalytically active metalloprotease, whereas the rare Kell K1 antigen is inactive. Identification of novel substrates for the Kell proteinNeprilysin is identical to skin fibroblast elastase: its role in skin aging and UV responsesHuman recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoproteinStructure of neurolysin reveals a deep channel that limits substrate accessSwapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseThe first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate bindingCrystal Structure of Mycobacterium tuberculosis Zinc-dependent Metalloprotease-1 (Zmp1), a Metalloprotease Involved in PathogenicityStructure of Gentlyase, the neutral metalloprotease ofPaenibacillus polymyxaCrystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzymeEngineering Neprilysin Activity and Specificity to Create a Novel Therapeutic for Alzheimer’s DiseaseRole of B Cell Development Marker CD10 in Cancer Progression and PrognosisBiological mechanisms underlying the ultraviolet radiation-induced formation of skin wrinkling and sagging II: over-expression of neprilysin plays an essential roleFGF23, PHEX, and MEPE regulation of phosphate homeostasis and skeletal mineralizationProteolytic processing of osteopontin by PHEX and accumulation of osteopontin fragments in Hyp mouse bone, the murine model of X-linked hypophosphatemiaCharacterization of PHEX endopeptidase catalytic activity: identification of parathyroid-hormone-related peptide107-139 as a substrate and osteocalcin, PPi and phosphate as inhibitorsProteolysis controls endogenous substance P levelsPrivate selective sweeps identified from next-generation pool-sequencing reveal convergent pathways under selection in two inbred Schistosoma mansoni strainsMatrix metalloproteinase (MMP) system in brain: identification and characterization of brain-specific MMP highly expressed in cerebellumThe catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid beta peptide: implications for Alzheimer disease pathogenesisA three-dimensional model of the neprilysin 2 active site based on the X-ray structure of neprilysin. Identification of residues involved in substrate hydrolysis and inhibitor binding of neprilysin 2Sialorphin, a natural inhibitor of rat membrane-bound neutral endopeptidase that displays analgesic activityDynamic changes in the secondary structure of ECE-1 and XCE account for their different substrate specificities.Angiotensin I-converting enzyme transition state stabilization by HIS1089: evidence for a catalytic mechanism distinct from other gluzincin metalloproteinases.The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function.Bioinformatic analysis of the neprilysin (M13) family of peptidases reveals complex evolutionary and functional relationshipsHomology modeling and site-directed mutagenesis to identify selective inhibitors of endothelin-converting enzyme-2Proposed Bioactive Conformations of Opiorphin, an Endogenous Dual APN/NEP Inhibitor.Urinary neprilysin in the critically ill patient.Active site mutations change the cleavage specificity of neprilysin.The discovery of small molecule inhibitors of neutral endopeptidase. Structure-activity studies on functionalized glutaramides.Amyloid beta-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin.Human neprilysin-2 (NEP2) and NEP display distinct subcellular localisations and substrate preferences.A peptidomics strategy to elucidate the proteolytic pathways that inactivate peptide hormones.Natriuretic peptide pharmacogenetics: membrane metallo-endopeptidase (MME): common gene sequence variation, functional characterization and degradation.The wrickkened pathways of FGF23, MEPE and PHEX.CD10-Equipped Melanoma Cells Acquire Highly Potent Tumorigenic Activity: A Plausible Explanation of Their Significance for a Poor PrognosisCharacterization of a New M13 Metallopeptidase from Deep-Sea Shewanella sp. E525-6 and Mechanistic Insight into Its Catalysis.Presenilin-1 280Glu-->Ala mutation alters C-terminal APP processing yielding longer abeta peptides: implications for Alzheimer's diseaseImpact of clinically tested NEP/ACE inhibitors on tumor uptake of [(111)In-DOTA]MG11-first estimates for clinical translation.
P2860
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P2860
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
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2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2000 թվականի փետրվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@ast
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@en
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@nl
type
label
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@ast
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@en
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@nl
prefLabel
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@ast
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@en
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@nl
P2093
P3181
P356
P1476
Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon
@en
P2093
P3181
P356
10.1006/JMBI.1999.3492
P407
P577
2000-02-18T00:00:00Z