Major proteinase movement upon stable serpin-proteinase complex formation
about
Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environmentCanonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinasesNeuroserpin Differentiates Between Forms of Tissue Type Plasminogen Activator via pH Dependent Deacylation.Application of linear free energy relationships to the serpin-proteinase inhibition mechanismCharacterization of four murine homologs of the human ov-serpin monocyte neutrophil elastase inhibitor MNEI (SERPINB1)Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survivalStructure of a serpin-enzyme complex probed by cysteine substitutions and fluorescence spectroscopy.The 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.Predicting permanent and transient protein-protein interfaces.A redox-sensitive loop regulates plasminogen activator inhibitor type 2 (PAI-2) polymerizationFormation of the covalent chymotrypsin.antichymotrypsin complex involves no large-scale movement of the enzyme.Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A.Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins.Proteinase 3 and prognosis of patients with acute myocardial infarction.Strand 6B deformation and residues exposure towards N-terminal end of helix B during proteinase inhibition by Serpins.Protein misfolding and the serpinopathies.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiologyRole of Lys335 in the metastability and function of inhibitory serpins.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 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.So how do you know you have a macromolecular complex?Kinetic intermediates en route to the final serpin-protease complex: studies of complexes of α1-protease inhibitor with trypsinSmoothing a rugged protein folding landscape by sequence-based redesign.Oxidized {alpha}1-antitrypsin stimulates the release of monocyte chemotactic protein-1 from lung epithelial cells: potential role in emphysema.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.A deletion mutant of vitronectin lacking the somatomedin B domain exhibits residual plasminogen activator inhibitor-1-binding activitySmall-molecule peptides inhibit Z alpha1-antitrypsin polymerization.Donor-donor energy migration for determining intramolecular distances in proteins: I. Application of a model to the latent plasminogen activator inhibitor-1 (PAI-1).Engineering functional antithrombin exosites in alpha1-proteinase inhibitor that specifically promote the inhibition of factor Xa and factor IXa.Structural factors affecting the choice between latency transition and polymerization in inhibitory serpins.Determination and analysis of antigenic epitopes of prostate specific antigen (PSA) and human glandular kallikrein 2 (hK2) using synthetic peptides and computer modeling.A novel antithrombin domain dictates the journey's end of a proteinase.Retarded protein folding of deficient human alpha 1-antitrypsin D256V and L41P variants.A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands. Ligand-induced serpin polymerization.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.6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis.Kinetic dissection of alpha 1-antitrypsin inhibition mechanism.alpha1-Proteinase inhibitor forms initial non-covalent and final covalent complexes with elastase analogously to other serpin-proteinase pairs, suggesting a common mechanism of inhibition.The contribution of the exosite residues of plasminogen activator inhibitor-1 to proteinase inhibition.
P2860
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P2860
Major proteinase movement upon stable serpin-proteinase complex formation
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Major proteinase movement upon stable serpin-proteinase complex formation
@ast
Major proteinase movement upon stable serpin-proteinase complex formation
@en
type
label
Major proteinase movement upon stable serpin-proteinase complex formation
@ast
Major proteinase movement upon stable serpin-proteinase complex formation
@en
prefLabel
Major proteinase movement upon stable serpin-proteinase complex formation
@ast
Major proteinase movement upon stable serpin-proteinase complex formation
@en
P2860
P356
P1476
Major proteinase movement upon stable serpin-proteinase complex formation
@en
P2093
E Stratikos
P G Gettins
P2860
P304
P356
10.1073/PNAS.94.2.453
P407
P577
1997-01-01T00:00:00Z