The dynamic structure of thrombin in solution - Wikidata - awgldk - TriplyDB

The dynamic structure of thrombin in solution

The dynamic structure of thrombin in solution

http://www.wikidata.org/entity/Q30155268

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Exploring the role of receptor flexibility in structure-based drug discovery Essential role of conformational selection in ligand binding Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D Loop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in Thrombin Correlated motions and residual frustration in thrombin.Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator.Detecting Allosteric Networks Using Molecular Dynamics Simulation Allosteric networks in thrombin distinguish procoagulant vs. anticoagulant activities.Thrombomodulin Binding Selects the Catalytically Active Form of Thrombin Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.Ligand binding to anion-binding exosites regulates conformational properties of thrombin.Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.NMR reveals a dynamic allosteric pathway in thrombin.Focusing and alignment of erythrocytes in a viscoelastic medium.Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.Through-bond effects in the ternary complexes of thrombin sandwiched by two DNA aptamers.Capturing Invisible Motions in the Transition from Ground to Rare Excited States of T4 Lysozyme L99A.Trypsinogen activation as observed in accelerated molecular dynamics simulations.Structural glycobiology of heparin dynamics on the exosite 2 of coagulation cascade proteases: Implications for glycosaminoglycans antithrombotic activity.Deciphering Conformational Changes Associated with the Maturation of Thrombin Anion Binding Exosite I.Ligand binding modulates the structural dynamics and activity of urokinase-type plasminogen activator: A possible mechanism of plasminogen activation.Interplay between conformational selection and zymogen activation.Mechanistic insights into thrombin's switch between "slow" and "fast" forms.Peptidic Macrocycles - Conformational Sampling and Thermodynamic Characterization.Malaria

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The dynamic structure of thrombin in solution

http://www.wikidata.org/entity/Q30155268

description

2012 nî lūn-bûn

@nan

2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հուլիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

The dynamic structure of thrombin in solution

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The dynamic structure of thrombin in solution

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The dynamic structure of thrombin in solution

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The dynamic structure of thrombin in solution

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The dynamic structure of thrombin in solution

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The dynamic structure of thrombin in solution

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J.BPJ.2012.05.047

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Biophysical Journal

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The dynamic structure of thrombin in solution

@en

P2093

Brian Fuglestad

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

Elizabeth A Komives

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

Marco Tonelli

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

Paul M Gasper

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Phineus R L Markwick

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P2860

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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

Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution

Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold

Crystallographic and Kinetic Evidence of Allostery in a Trypsin-like Protease

NMR structures of biomolecules using field oriented media and residual dipolar couplings

A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy

Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

NMR evidence for slow collective motions in cyanometmyoglobin

Evolutionarily conserved networks of residues mediate allosteric communication in proteins

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10.1016/J.BPJ.2012.05.047

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J. Andrew McCammon

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2012-07-01T00:00:00Z

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22828334

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3388214

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