Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis.
about
Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastaseCytokine response modifier a inhibition of initiator caspases results in covalent complex formation and dissociation of the caspase tetramerThe role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsinA serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism.The effects of reactive site location on the inhibitory properties of the serpin alpha(1)-antichymotrypsin.Formation of the covalent chymotrypsin.antichymotrypsin complex involves no large-scale movement of the enzyme.Thrombin inhibition by serpins disrupts exosite IIThe molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1: roles of the reactive centre loop, the shutter region, the flexible joint region and the small serpin fragment.SERPINB11 is a new noninhibitory intracellular serpin. Common single nucleotide polymorphisms in the scaffold impair conformational change.Mechanisms of glycosaminoglycan activation of the serpins in hemostasis.Structural insights into the unique inhibitory mechanism of the silkworm protease inhibitor serpin18.Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant.Pivotal role for alpha1-antichymotrypsin in skin repair.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Stability of mutant serpin/furin complexes: dependence on pH and regulation at the deacylation step.Inactivation of papain by antithrombin due to autolytic digestion: a model of serpin inactivation of cysteine proteinases.Molecular contortionism - on the physical limits of serpin 'loop-sheet' polymers.Conformational change in elastase following complexation with alpha1-proteinase inhibitor: a CD investigation.Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition.The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop.The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium.Conformational changes in thrombin when complexed by serpins.Mapping of the epitope of a monoclonal antibody protecting plasminogen activator inhibitor-1 against inactivating agents.Influence of the P5 residue on alpha1-proteinase inhibitor mechanism.Characterization of a human alpha1-antitrypsin variant that is as stable as ovalbumin.
P2860
Q24297624-067DDE25-72D7-420F-BE41-ABA263F03825Q28269534-6C950E17-E260-4261-8408-5E74396891A1Q28364511-BAC9B073-C383-4C1D-B0ED-B537107FE17DQ30168478-07A22723-92BF-45F5-B9AC-AD1889432CB8Q31072774-4F37437A-D9BE-4D4F-B639-E351076ADFF7Q31454902-C361C6CD-347D-42FB-94D8-8E2C7314F259Q34352365-57C2A34B-7B7B-464F-AB2B-B2AFB07D7EA3Q34584787-9E353E3D-31F0-4751-B808-D659C3DD60A9Q34636554-EAB72316-E8C9-4192-BB4F-86C24FA2E7B9Q35181635-3B725F2F-C90B-472B-B12A-6B1617BCE6D4Q35824673-59A7EA37-C284-40E8-89BC-FED98DBD5F21Q36331710-C16B7EE5-85EE-43D9-85F3-D5E5214D7CB8Q38354158-0FCEB554-6DF5-4D15-810F-ADDCC0B47157Q38672932-68E6C30F-6F6C-463A-9ADD-CFE2AE2C1DB1Q38912052-2A0D8C67-AAB0-4126-A307-4FA6AE1CE105Q40469066-07F6C359-79CE-49AD-8525-E21F3CC2AF54Q42159081-4D3C557F-94EF-4002-84AF-5D5097722AC6Q42929194-180033B0-0C69-4FD7-B203-9643DBEEE235Q43002650-FC1BF707-5A7E-4A0C-A062-DAA79494943FQ43571718-67665223-9273-4747-B626-2289FC2E607BQ43590670-E25AECEF-A2E4-44CF-B54C-D87CC068F168Q43638841-740AAD87-4A1D-4992-81F4-BA18238C9374Q43754806-602E1927-B8FB-4CE2-9F62-B81403C9EA2CQ44402629-D9134B64-5ACE-47D7-A310-20883DE4286CQ52529169-A2002BD1-2375-4AB0-9AE5-DB1CBE61F4A2Q53959131-E597101D-A2DE-4FE8-92E6-2125386662A1
P2860
Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis.
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
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@ast
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@en
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@nl
type
label
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@ast
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@en
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@nl
prefLabel
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@ast
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@en
Structural change in alpha-chy ...... ed sensitivity to proteolysis.
@nl
P2093
P356
P1433
P1476
Structural change in alpha-chy ...... ced sensitivity to proteolysis
@en
P2093
Christianson DW
Cooperman BS
O'Malley K
Stavridi ES
P304
10608-10615
P356
10.1021/BI9605806
P407
P577
1996-08-01T00:00:00Z