Structure and Behavior of Human α-Thrombin upon Ligand Recognition: Thermodynamic and Molecular Dynamics Studies-Reference-Cited by-同舟云学术

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Structure and Behavior of Human α-Thrombin upon Ligand Recognition: Thermodynamic and Molecular Dynamics Studies

Published:2011-09-14 Issue:9 Volume:6 Page:e24735
ISSN:1932-6203
Container-title:PLoS ONE
language:en
Short-container-title:PLoS ONE

Author:

Silva Vivian de Almeira,Cargnelutti Maria Thereza,Giesel Guilherme M.,Palmieri Leonardo C.,Monteiro Robson Q.,Verli Hugo,Lima Luis Mauricio T. R.

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference61 articles.

1. The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.;W Bode;EMBO J,1989

2. The molecular basis of thrombin allostery revealed by a 1.8 A structure of the “slow” form.;JA Huntington;Structure,2003

3. Molecular dissection of Na+ binding to thrombin.;AO Pineda;J Biol Chem,2004

4. Crystal structure of wild-type human thrombin in the Na+-free state.;DJ Johnson;Biochem J,2005

5. Principles of enzyme-inhibitor design.;DW Banner,2003

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1. Exosite Binding in Thrombin: A Global Structural/Dynamic Overview of Complexes with Aptamers and Other Ligands;International Journal of Molecular Sciences;2021-10-06

2. Broadband SERS Enhancement by DNA Origami Assembled Bimetallic Nanoantennas with Label-Free Single Protein Sensing;The Journal of Physical Chemistry Letters;2021-08-19

3. Role of the I16-D194 ionic interaction in the trypsin fold;Scientific Reports;2019-12

4. The Translocation of Na+Ion Inside Human Thrombin Accounts for the Activation of the Enzyme;Israel Journal of Chemistry;2017-02-28

5. Aptamer based electrostatic-stimuli responsive surfaces for on-demand binding/unbinding of a specific ligand;Journal of Materials Chemistry B;2017

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