Literature DB >> 16480903

Structure and interaction modes of thrombin.

Wolfram Bode1.   

Abstract

Any vascular injury triggers the burst-like release of the trypsin-like serine proteinase alpha-thrombin. Thrombin, the main executioner of the coagulation cascade, exhibits procoagulant as well as anticoagulant and antifibrinolytic properties, very specifically interacting with a number of protein substrates, receptors, cofactors, inhibitors, carbohydrates, and modulators. A large number of crystal structures of alpha-thrombin have shown that the thrombin surface can be subdivided into several functional regions, which recognize different substrates, inhibitors, and mediators with high specificity.

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Year:  2006        PMID: 16480903     DOI: 10.1016/j.bcmd.2005.12.027

Source DB:  PubMed          Journal:  Blood Cells Mol Dis        ISSN: 1079-9796            Impact factor:   3.039


  26 in total

1.  Crystal structure of thrombin bound to the uncleaved extracellular fragment of PAR1.

Authors:  Prafull S Gandhi; Zhiwei Chen; Enrico Di Cera
Journal:  J Biol Chem       Date:  2010-03-17       Impact factor: 5.157

2.  Effects of dabigatran in vitro on thrombin biomarkers by Calibrated Automated Thrombography in patients after ischemic stroke.

Authors:  Victor Serebruany; Yanti Sani; Donald Lynch; Alex Schevchuck; Stan Svetlov; Alan Fong; Lionel Thevathasan; Dan Hanley
Journal:  J Thromb Thrombolysis       Date:  2012-01       Impact factor: 2.300

3.  Structural identification of the pathway of long-range communication in an allosteric enzyme.

Authors:  Prafull S Gandhi; Zhiwei Chen; F Scott Mathews; Enrico Di Cera
Journal:  Proc Natl Acad Sci U S A       Date:  2008-02-04       Impact factor: 11.205

4.  Impact of moderate blast exposures on thrombin biomarkers assessed by calibrated automated thrombography in rats.

Authors:  Victor Prima; Victor L Serebruany; Artem Svetlov; Ronald L Hayes; Stanislav I Svetlov
Journal:  J Neurotrauma       Date:  2013-10-04       Impact factor: 5.269

5.  Thrombomodulin Binding Selects the Catalytically Active Form of Thrombin.

Authors:  Lindsey D Handley; Nicholas A Treuheit; Varun J Venkatesh; Elizabeth A Komives
Journal:  Biochemistry       Date:  2015-10-26       Impact factor: 3.162

6.  Molecular dynamics simulations of aptamer-binding reveal generalized allostery in thrombin.

Authors:  Jiajie Xiao; Freddie R Salsbury
Journal:  J Biomol Struct Dyn       Date:  2016-11-29

7.  Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation.

Authors:  Yan G Fulcher; Steven R Van Doren
Journal:  Biochemistry       Date:  2011-10-11       Impact factor: 3.162

8.  Rigidification of the autolysis loop enhances Na(+) binding to thrombin.

Authors:  Nicola Pozzi; Raymond Chen; Zhiwei Chen; Alaji Bah; Enrico Di Cera
Journal:  Biophys Chem       Date:  2011-04-12       Impact factor: 2.352

9.  Expression of allosteric linkage between the sodium ion binding site and exosite I of thrombin during prothrombin activation.

Authors:  Heather K Kroh; Guido Tans; Gerry A F Nicolaes; Jan Rosing; Paul E Bock
Journal:  J Biol Chem       Date:  2007-04-12       Impact factor: 5.157

10.  Apolipoprotein-E forms dimers in human frontal cortex and hippocampus.

Authors:  David A Elliott; Glenda M Halliday; Brett Garner
Journal:  BMC Neurosci       Date:  2010-02-20       Impact factor: 3.288

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