Mutant N143P Reveals How Na+ Activates Thrombin - Test2 - elhamkhani - TriplyDB

Mutant N143P Reveals How Na+ Activates Thrombin

Mutant N143P Reveals How Na+ Activates Thrombin

http://www.wikidata.org/entity/Q27657884

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Biomolecular electrostatics and solvation: a computational perspective Crystal Structure of Thrombin Bound to the Uncleaved Extracellular Fragment of PAR1 Crystal structure of prethrombin-1 Rigidification of the autolysis loop enhances Na+ binding to thrombin Crystallographic and Kinetic Evidence of Allostery in a Trypsin-like Protease Loop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in Thrombin A revisit to the one form kinetic model of prothrombinase Engineering thrombin for selective specificity toward protein C and PAR1.Evidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa.Redesigning allosteric activation in an enzyme.Why Ser and not Thr brokers catalysis in the trypsin fold Allostery in trypsin-like proteases suggests new therapeutic strategies.Conformational selection in trypsin-like proteases.Looking at the proteases from a simple perspective.Proteases as therapeutics.Structural basis of thrombin-protease-activated receptor interactions.Molecular Mechanisms of Enzyme Activation by Monovalent Cations.

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P2860

Mutant N143P Reveals How Na+ Activates Thrombin

http://www.wikidata.org/entity/Q27657884

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Mutant N143P Reveals How Na+ Activates Thrombin

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Mutant N143P Reveals How Na+ Activates Thrombin

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Mutant N143P Reveals How Na+ Activates Thrombin

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type

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Mutant N143P Reveals How Na+ Activates Thrombin

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Mutant N143P Reveals How Na+ Activates Thrombin

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Mutant N143P Reveals How Na+ Activates Thrombin

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Mutant N143P Reveals How Na+ Activates Thrombin

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Mutant N143P Reveals How Na+ Activates Thrombin

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Mutant N143P Reveals How Na+ Activates Thrombin

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JBC.M109.069500

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Journal of Biological Chemistry

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Mutant N143P Reveals How Na+ Activates Thrombin

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P2093

Alaji Bah

http://www.w3.org/2001/XMLSchema#string

Enrico Di Cera

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Leslie A Bush-Pelc

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Prafull S Gandhi

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Weiling Niu

http://www.w3.org/2001/XMLSchema#string

Zhiwei Chen

http://www.w3.org/2001/XMLSchema#string

P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Unexpected crucial role of residue 225 in serine proteases

Crystal structure reveals basis for the inhibitor resistance of human brain trypsin

Thermodynamic 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 loops

Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole

High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop

Structure of human pro-chymase: a model for the activating transition of granule-associated proteases

The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

Mechanism of the Anticoagulant Activity of Thrombin Mutant W215A/E217A

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36175-85

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scholarly article

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10.1074/JBC.M109.069500

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52

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284

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2009-12-25T00:00:00Z

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19846563

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2794733

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