A 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.
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Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastaseCrystal structure of the complex of plasminogen activator inhibitor 2 with a peptide mimicking the reactive center loopCytokine 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)-antitrypsinEpitope mapping for four monoclonal antibodies against human plasminogen activator inhibitor type-1: implications for antibody-mediated PAI-1-neutralization and vitronectin-binding.A urokinase-type plasminogen activator-inhibiting cyclic peptide with an unusual P2 residue and an extended protease binding surface demonstrates new modalities for enzyme inhibition.Thrombin inhibition by serpins disrupts exosite IISerum-stable RNA aptamers to urokinase-type plasminogen activator blocking receptor binding.Targeting tumor cell invasion and dissemination in vivo by an aptamer that inhibits urokinase-type plasminogen activator through a novel multifunctional mechanism.The 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.Mechanisms of glycosaminoglycan activation of the serpins in hemostasis.Protein-binding RNA aptamers affect molecular interactions distantly from their binding sitesTargeting the autolysis loop of urokinase-type plasminogen activator with conformation-specific monoclonal antibodiesA novel mode of intervention with serine protease activity: targeting zymogen activation.The mosaic receptor sorLA/LR11 binds components of the plasminogen-activating system and platelet-derived growth factor-BB similarly to LRP1 (low-density lipoprotein receptor-related protein), but mediates slow internalization of bound ligand.Biochemical mechanism of action of a diketopiperazine inactivator of plasminogen activator inhibitor-1.Plasminogen activator inhibitor-1 polymers, induced by inactivating amphipathic organochemical ligands.Molecular contortionism - on the physical limits of serpin 'loop-sheet' polymers.A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands. Ligand-induced serpin polymerization.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.Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator: relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme.Importance of the amino-acid composition of the shutter region of plasminogen activator inhibitor-1 for its transitions to latent and substrate forms.Mapping of the epitope of a monoclonal antibody protecting plasminogen activator inhibitor-1 against inactivating agents.Elucidation of a novel epitope of a substrate-inducing monoclonal antibody against the serpin PAI-1.Distortion of the catalytic domain of tissue-type plasminogen activator by plasminogen activator inhibitor-1 coincides with the formation of stable serpin-proteinase complexes.Protonation state of a single histidine residue contributes significantly to the kinetics of the reaction of plasminogen activator inhibitor-1 with tissue-type plasminogen activator.Binding areas of urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex for endocytosis receptors of the low-density lipoprotein receptor family, determined by site-directed mutagenesis.
P2860
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P2860
A 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.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
A serpin-induced extensive pro ...... e serpin inhibitory mechanism.
@ast
A serpin-induced extensive pro ...... e serpin inhibitory mechanism.
@en
type
label
A serpin-induced extensive pro ...... e serpin inhibitory mechanism.
@ast
A serpin-induced extensive pro ...... e serpin inhibitory mechanism.
@en
prefLabel
A serpin-induced extensive pro ...... e serpin inhibitory mechanism.
@ast
A serpin-induced extensive pro ...... e serpin inhibitory mechanism.
@en
P2093
P2860
P1433
P1476
A serpin-induced extensive pro ...... e serpin inhibitory mechanism.
@en
P2093
P A Andreasen
T E Petersen
P2860
P304
P356
10.1046/J.1432-1327.2001.01921.X
P407
P577
2001-02-01T00:00:00Z