Snake Venom Metalloproteinases

Snake Venom Metalloproteinases

Paperback | June 8, 2017

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This special edition of Toxins will cover recent developments in snake venom metalloproteinase structure, function and clinical implications. It will include a historical retrospective of the discovery of Snake Venom Metalloproteinases (SVMPs) and early insights into their biochemical mechanisms and how they function in envenomation. The individual articles will review
• SVMP Structure
• Pathologies associated with SVMPs activities
• Mechanism of action; evolution and orthologs
• SVMP processing and disintegrins
• Potential clinical applications of SVMP scaffolds

Title:Snake Venom MetalloproteinasesFormat:PaperbackProduct dimensions:276 pages, 9.61 X 6.69 X 0.75 inShipping dimensions:276 pages, 9.61 X 6.69 X 0.75 inPublished:June 8, 2017Publisher:MDPI AGLanguage:English

The following ISBNs are associated with this title:

ISBN - 10:3038424269

ISBN - 13:9783038424260

Appropriate for ages: All ages

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Table of Contents

1) Understanding the Snake Venom Metalloproteinases: An Interview with Jay Fox and José María Gutiérrez
2) A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions
3) ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview
4) Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation
5) A Comprehensive View of the Structural and Functional Alterations of Extracellular Matrix by Snake Venom Metalloproteinases (SVMPs): Novel Perspectives on the Pathophysiology of Envenoming
6) Hemorrhage Caused by Snake Venom Metalloproteinases: A Journey of Discovery and Understanding
7) Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites
8) Natural Inhibitors of Snake Venom Metalloendopeptidases: History and Current Challenges
9) Snake Genome Sequencing: Results and Future Prospects
10) Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif
11) Viperid Envenomation Wound Exudate Contributes to Increased Vascular Permeability via a DAMPs/TLR-4 Mediated Pathway
12) Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom
13) Insights into the Evolution of a Snake Venom Multi-Gene Family from the Genomic Organization of Echis ocellatus SVMP Genes