Unexpected crucial role of residue 225 in serine proteases
about
Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handleThermodynamic linkage between the S1 site, the Na+ site, and the Ca2+ site in the protease domain of human activated protein C (APC). Sodium ion in the APC crystal structure is coordinated to four carbonyl groups from two separate loopsCrystal structure of the anticoagulant slow form of thrombinStructural basis of Na+ activation mimicry in murine thrombinEngineering Protein Allostery: 1.05 Å Resolution Structure and Enzymatic Properties of a Na+-activated TrypsinMutant N143P Reveals How Na+ Activates ThrombinDifferent active-site loop orientation in serine hydrolases versus acyltransferasesCrystallographic and Kinetic Evidence of Allostery in a Trypsin-like ProteaseProtein sectors: evolutionary units of three-dimensional structureMolecular markers of serine protease evolutionMurine serine proteases MASP-1 and MASP-3, components of the lectin pathway activation complex of complement, are encoded by a single structural geneStructure-based predictive models for allosteric hot spots.Redesigning the monovalent cation specificity of an enzymeEngineering thrombin for selective specificity toward protein C and PAR1.Bi-factor analysis based on noise-reduction (BIFANR): a new algorithm for detecting coevolving amino acid sites in proteins.WEDGE: an anticoagulant thrombin mutant produced by autoactivation.Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.A structural perspective on enzymes activated by monovalent cations.Role of Na+ and K+ in enzyme function.Factor Va alters the conformation of the Na+-binding loop of factor Xa in the prothrombinase complexThrombin.Mutagenesis studies toward understanding allostery in thrombin.Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site.A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases.Prostate-specific antigen is a "chymotrypsin-like" serine protease with unique P1 substrate specificity.Serine protease variants encoded by Echis ocellatus venom gland cDNA: cloning and sequencing analysis.Ser(214) is crucial for substrate binding to serine proteases.Three-dimensional models of proteases involved in patterning of the Drosophila Embryo. Crucial role of predicted cation binding sites.Residue Asp-189 controls both substrate binding and the monovalent cation specificity of thrombin.Computationally-driven identification of antibody epitopes.Molecular dissection of Na+ binding to thrombin.Molecular cloning and characterization of glucanase inhibitor proteins: coevolution of a counterdefense mechanism by plant pathogens.Murine thrombin lacks Na+ activation but retains high catalytic activity.Co-evolution networks of HIV/HCV are modular with direct association to structure and function
P2860
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P2860
Unexpected crucial role of residue 225 in serine proteases
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Unexpected crucial role of residue 225 in serine proteases
@ast
Unexpected crucial role of residue 225 in serine proteases
@en
Unexpected crucial role of residue 225 in serine proteases
@nl
type
label
Unexpected crucial role of residue 225 in serine proteases
@ast
Unexpected crucial role of residue 225 in serine proteases
@en
Unexpected crucial role of residue 225 in serine proteases
@nl
prefLabel
Unexpected crucial role of residue 225 in serine proteases
@ast
Unexpected crucial role of residue 225 in serine proteases
@en
Unexpected crucial role of residue 225 in serine proteases
@nl
P2093
P2860
P356
P1476
Unexpected crucial role of residue 225 in serine proteases
@en
P2093
P2860
P304
P356
10.1073/PNAS.96.5.1852
P407
P577
1999-03-02T00:00:00Z