Structure of astacin with a transition-state analogue inhibitor
about
Meprins, membrane-bound and secreted astacin metalloproteinasesStructure of neurolysin reveals a deep channel that limits substrate accessACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysisSwapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseProenzyme Structure and Activation of Astacin MetallopeptidaseStructural basis for the autoprocessing of zinc metalloproteases in the thermolysin familyStructural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1Structural and Functional Analyses Reveal That Staphylococcus aureus Antibiotic Resistance Factor HmrA Is a Zinc-dependent EndopeptidaseStructural basis for the sheddase function of human meprin metalloproteinase at the plasma membraneStructure and mechanism of a type III secretion protease, NleCStructural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP12 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding modeMutational analysis of the proteolytic domain of pregnancy-associated plasma protein-A (PAPP-A): classification as a metzincinHeterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitroMarked differences between metalloproteases meprin A and B in substrate and peptide bond specificityIdentification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activityCrystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localizationRXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage.Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases.Allosteric inhibition of the neuropeptidase neurolysin.Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substratesIdentification and activity of inhibitors of the essential nematode-specific metalloprotease DPY-31Catalytic domain architecture of metzincin metalloproteases.Architecture and function of metallopeptidase catalytic domains.Shaping BMP morphogen gradients through enzyme-substrate interactionsHuman meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.Phosphinic peptides, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors.Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor alpha convertase inhibitors.A tyrosine residue essential for catalytic activity in aminopeptidase A.cDNA cloning, bacterial expression, in vitro renaturation and affinity purification of the zinc endopeptidase astacin.Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A.pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15).Comparative analysis of binding sites of human meprins with hydroxamic acid derivative by molecular dynamics simulation study.A novel secreted metzincin metalloproteinase from Bacillus intermedius.Domain-selective ligand-binding modes and atomic level pharmacophore refinement in angiotensin I converting enzyme (ACE) inhibitors.Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities.Overexpression and mechanistic characterization of blastula protease 10, a metalloprotease involved in sea urchin embryogenesis and development.Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism.Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family
P2860
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P2860
Structure of astacin with a transition-state analogue inhibitor
description
1996 nî lūn-bûn
@nan
1996 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Structure of astacin with a transition-state analogue inhibitor
@ast
Structure of astacin with a transition-state analogue inhibitor
@en
Structure of astacin with a transition-state analogue inhibitor
@nl
type
label
Structure of astacin with a transition-state analogue inhibitor
@ast
Structure of astacin with a transition-state analogue inhibitor
@en
Structure of astacin with a transition-state analogue inhibitor
@nl
prefLabel
Structure of astacin with a transition-state analogue inhibitor
@ast
Structure of astacin with a transition-state analogue inhibitor
@en
Structure of astacin with a transition-state analogue inhibitor
@nl
P2093
P2860
P356
P1476
Structure of astacin with a transition-state analogue inhibitor
@en
P2093
Yiallouros I
Yiotakis A
Zwilling R
P2860
P304
P356
10.1038/NSB0896-671
P577
1996-08-01T00:00:00Z