Next Article in Journal
Transcript Abundance of Photorhabdus Insect-Related (Pir) Toxin in Manduca sexta and Galleria mellonella Infections
Next Article in Special Issue
Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif
Previous Article in Journal
Effects of Citric and Lactic Acid on the Reduction of Deoxynivalenol and Its Derivatives in Feeds
Previous Article in Special Issue
Natural Inhibitors of Snake Venom Metalloendopeptidases: History and Current Challenges
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessReview
Toxins 2016, 8(10), 284; doi:10.3390/toxins8100284

Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Protein Science Laboratory, Department of Biological Sciences, Faculty of Science, 14 Science Drive 4, National University of Singapore, Singapore 117543, Singapore
*
Author to whom correspondence should be addressed.
Academic Editors: Jay Fox and José María Gutiérrez
Received: 8 September 2016 / Revised: 21 September 2016 / Accepted: 22 September 2016 / Published: 29 September 2016
(This article belongs to the Special Issue Snake Venom Metalloproteinases)
View Full-Text   |   Download PDF [4501 KB, uploaded 29 September 2016]   |  

Abstract

Snake venom metalloproteases, in addition to their contribution to the digestion of the prey, affect various physiological functions by cleaving specific proteins. They exhibit their activities through activation of zymogens of coagulation factors, and precursors of integrins or receptors. Based on their structure–function relationships and mechanism of action, we have defined classification and nomenclature of functional sites of proteases. These metalloproteases are useful as research tools and in diagnosis and treatment of various thrombotic and hemostatic conditions. They also contribute to our understanding of molecular details in the activation of specific factors involved in coagulation, platelet aggregation and matrix biology. This review provides a ready reference for metalloproteases that interfere in blood coagulation, fibrinolysis and platelet aggregation. View Full-Text
Keywords: procoagulant; anticoagulant; factor X activator; prothrombin activator; platelet aggregation; fibrinolytic; exosites in enzymes; allosteric sites procoagulant; anticoagulant; factor X activator; prothrombin activator; platelet aggregation; fibrinolytic; exosites in enzymes; allosteric sites
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Kini, R.M.; Koh, C.Y. Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites. Toxins 2016, 8, 284.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top