Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase
about
Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor XaSpecificity of binding of the low density lipoprotein receptor-related protein to different conformational states of the clade E serpins plasminogen activator inhibitor-1 and proteinase nexin-1Neuroserpin Differentiates Between Forms of Tissue Type Plasminogen Activator via pH Dependent Deacylation.Structure of native protein C inhibitor provides insight into its multiple functionsC1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational diseaseMechanistic characterization and crystal structure of a small molecule inactivator bound to plasminogen activator inhibitor-1Rezymogenation of active urokinase induced by an inhibitory antibodyCytokine response modifier a inhibition of initiator caspases results in covalent complex formation and dissociation of the caspase tetramerAnalysis of substructural variation in families of enzymatic proteins with applications to protein function prediction.Inhibition of plasminogen activator inhibitor-1 binding to endocytosis receptors of the low-density-lipoprotein receptor family by a peptide isolated from a phage display library.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Analysis of mutually exclusive alternatively spliced serpin-1 isoforms and identification of serpin-1 proteinase complexes in Manduca sexta hemolymph.Characterization of a novel serine protease inhibitor gene from a marine metagenome.Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases.Serpin protease inhibitors in plant biology.Thrombin inhibition by serpins disrupts exosite IISerpins in rice: protein sequence analysis, phylogeny and gene expression during development.The complete N-terminal extension of heparin cofactor II is required for maximal effectiveness as a thrombin exosite 1 ligand.Protein misfolding and the serpinopathies.Fusion of the C-terminal triskaidecapeptide of hirudin variant 3 to alpha1-proteinase inhibitor M358R increases the serpin-mediated rate of thrombin inhibition.Energy landscapes of functional proteins are inherently risky.SerpinB1 in cystic fibrosis airway fluids: quantity, molecular form and mechanism of elastase inhibition.Determining serpin conformational distributions with single molecule fluorescenceThe High Affinity Binding Site on Plasminogen Activator Inhibitor-1 (PAI-1) for the Low Density Lipoprotein Receptor-related Protein (LRP1) Is Composed of Four Basic Residues.A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism.Cellular folding pathway of a metastable serpin.Serpins in T cell immunity.Kinetic intermediates en route to the final serpin-protease complex: studies of complexes of α1-protease inhibitor with trypsinExosite determinants of serpin specificity.The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Phage display of the serpin alpha-1 proteinase inhibitor randomized at consecutive residues in the reactive centre loop and biopanned with or without thrombin.Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.Antithrombin deficiency and its laboratory diagnosis.Unravelling the twists and turns of the serpinopathies.Vaspin (serpinA12) in obesity, insulin resistance, and inflammation.Characterization of the conformational alterations, reduced anticoagulant activity, and enhanced antiangiogenic activity of prelatent antithrombinInhibitors and Antibody Fragments as Potential Anti-Inflammatory Therapeutics Targeting Neutrophil Proteinase 3 in Human Disease.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Structural differences between active forms of plasminogen activator inhibitor type 1 revealed by conformationally sensitive ligands.A hydrophobic patch on proteinase 3, the target of autoantibodies in Wegener granulomatosis, mediates membrane binding via NB1 receptors.
P2860
Q24632861-2EB78192-B311-4D42-8BDE-265059390CD3Q24650291-CA7F0BA1-0943-49A9-9D8F-7C0005A58C29Q27319705-D13FECDA-6618-4E7F-AEB4-EA6A8011DACFQ27643980-32643300-ACCF-49A1-BF2F-9354D569C897Q27644724-AF820D6A-B687-4B6B-986D-BD8EF00DECEDQ27680739-1EABBD1D-9862-40C2-A837-6CFCAE7D3C20Q27682519-683B9DF7-E708-4564-8878-3B3EDCE4E6E8Q28269534-6D851F37-D4A2-47C8-A2DB-6D6D3E15703BQ30389018-9EF6A3E6-8E2E-4D1E-BCA4-015EB23511F9Q33248476-CB6767F5-DE03-490D-AF2F-F73ACB52A572Q33609148-08785762-5441-4659-BA61-2F37CFA84F85Q33631026-8C1BCFC0-8714-4B20-971C-B17DA0DB0C83Q34087530-452DB656-FA87-4BCC-9D59-57317E504089Q34149948-1758C68C-6518-471B-B35D-62EC8D0FCEE7Q34232828-557B642E-A761-49EE-9378-5A19B969FDE7Q34352365-5AC611CC-ABFA-4E46-B83F-7175429DBBE0Q34402652-B8B7E6C1-8893-4FEA-BB7F-6D977632B738Q34621763-71078E34-8CD0-4339-9C58-F5E31C03884CQ34928474-EB6E7D88-E5F0-4C1B-94E4-D0C3AE67AEFFQ35038471-B02C269C-D52C-4C2E-9F66-F1CDE15E86D3Q35558791-30AC59AC-C874-4F6A-B740-AB979FFE1854Q35776816-158523FE-A614-4EFC-8307-70661B0824BBQ36058093-D5211705-FC8D-4952-A1BD-3B75D2EDCADAQ36442395-57FC9BF0-C0F2-4FDD-BDC7-5CDDF0711204Q37168402-4DBC4294-BF15-4397-87F6-CBD45A3E8DB7Q37183716-FB67673E-5079-4831-AA82-94AF3DACAB9BQ37222018-F8A83D06-6DB2-4D3F-9EEB-09C4F12E268CQ37272213-D7B12F82-A3BC-475A-916E-500B5271A410Q37343928-3A0AACEE-EA7B-4B4D-9488-B40F8AF2A7E2Q37447881-403C37EE-FE56-4A9C-BAD5-67608EF2279DQ37464698-02F06A0E-A2A7-41D1-9656-DB9B4165DDF5Q37777806-C111A656-9653-4822-811A-C6544F5529E3Q37808223-89AE1958-C5A4-497A-A859-CD930C2C7940Q37882046-4107CE0A-3EB0-4E59-A475-31FDE8F6796EQ38193391-75064DD6-E0CB-47E2-A9D9-822E5A49A94DQ38531516-56961DFA-8B00-4A3D-95AB-ACC31684758EQ38850115-FDF374C1-BDF2-4CF2-B927-0A6100D97EEEQ38912052-EBE39353-4915-4E5A-92DF-99B36364061EQ39599940-805EB1CA-108E-4F4B-973C-9CF3A9073004Q39929455-94F92159-DAA7-47FB-B0EE-F814DDF46E9D
P2860
Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Active site distortion is suff ...... th porcine pancreatic elastase
@ast
Active site distortion is suff ...... th porcine pancreatic elastase
@en
Active site distortion is suff ...... th porcine pancreatic elastase
@nl
type
label
Active site distortion is suff ...... th porcine pancreatic elastase
@ast
Active site distortion is suff ...... th porcine pancreatic elastase
@en
Active site distortion is suff ...... th porcine pancreatic elastase
@nl
prefLabel
Active site distortion is suff ...... th porcine pancreatic elastase
@ast
Active site distortion is suff ...... th porcine pancreatic elastase
@en
Active site distortion is suff ...... th porcine pancreatic elastase
@nl
P2093
P2860
P3181
P356
P1476
Active site distortion is suff ...... th porcine pancreatic elastase
@en
P2093
Alexey Dementiev
József Dobó
Peter G W Gettins
P2860
P304
P3181
P356
10.1074/JBC.M510564200
P407
P577
2006-02-10T00:00:00Z