Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin
about
An overview of the serpin superfamilyMechanisms of protein-folding diseases at a glanceThe conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regionsCrystal structure of the complex of plasminogen activator inhibitor 2 with a peptide mimicking the reactive center loopSerpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerolMechanistic characterization and crystal structure of a small molecule inactivator bound to plasminogen activator inhibitor-1The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesisNeuroserpin binds Abeta and is a neuroprotective component of amyloid plaques in Alzheimer diseaseMolecular and cell biology of porcine HSP47 during wound healing: complete cDNA sequence and regulation of gene expression.A redox-sensitive loop regulates plasminogen activator inhibitor type 2 (PAI-2) polymerizationPolymerization of plasminogen activator inhibitor-1.Nondenaturing two-dimensional electrophoretic analysis of loop-sheet polymerization of serpin, squamous cell carcinoma antigen-2.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.Hydration effects of heparin on antithrombin probed by osmotic stress.The shapes of Z-α1-antitrypsin polymers in solution support the C-terminal domain-swap mechanism of polymerization.Cell surface heparan sulfate and its roles in assisting viral infections.Small Molecule Probes That Perturb A Protein-protein Interface In AntithrombinBlocking formation of large protein aggregates by small peptides.Mixture-based combinatorial libraries from small individual peptide libraries: a case study on α1-antitrypsin deficiency.Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiologyFluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides.Molecular Mechanism of Z α1-Antitrypsin Deficiencyalpha1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies.Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency.The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity.Characterization of the conformational alterations, reduced anticoagulant activity, and enhanced antiangiogenic activity of prelatent antithrombinStructural differences between active forms of plasminogen activator inhibitor type 1 revealed by conformationally sensitive ligands.Small-molecule peptides inhibit Z alpha1-antitrypsin polymerization.Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition.An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.The heparin-binding site of antithrombin is crucial for antiangiogenic activityAntiangiogenic forms of antithrombin specifically bind to the anticoagulant heparin sequence.Serpins (serine protease inhibitors).Molecular contortionism - on the physical limits of serpin 'loop-sheet' polymers.Probing the local conformational change of alpha1-antitrypsin.Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway.Interaction between the P14 residue and strand 2 of beta-sheet B is critical for reactive center loop insertion in plasminogen activator inhibitor-2.Regulation of glycosaminoglycan function by osmotic potentials. Measurement of water transfer during antithrombin activation by heparin.Helix D elongation and allosteric activation of antithrombin.
P2860
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P2860
Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin
description
1998 nî lūn-bûn
@nan
1998 թուականին հրատարակուած գիտական յօդուած
@hyw
1998 թվականին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Implications for function and ...... binary-complexed antithrombin
@ast
Implications for function and ...... binary-complexed antithrombin
@en
Implications for function and ...... binary-complexed antithrombin
@nl
type
label
Implications for function and ...... binary-complexed antithrombin
@ast
Implications for function and ...... binary-complexed antithrombin
@en
Implications for function and ...... binary-complexed antithrombin
@nl
prefLabel
Implications for function and ...... binary-complexed antithrombin
@ast
Implications for function and ...... binary-complexed antithrombin
@en
Implications for function and ...... binary-complexed antithrombin
@nl
P2093
P3181
P356
P1476
Implications for function and ...... binary-complexed antithrombin
@en
P2093
Carrell RW
Huntington JA
P3181
P356
10.1006/JMBI.1998.2083
P407
P577
1998-01-01T00:00:00Z