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Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved.
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- Author(s): Serrano SM;Serrano SM; Maroun RC
- Source:
Toxicon : official journal of the International Society on Toxinology [Toxicon] 2005 Jun 15; Vol. 45 (8), pp. 1115-32. Date of Electronic Publication: 2005 Apr 19.
- Publication Type:
Journal Article; Review
- Language:
English
- Additional Information
- Source:
Publisher: Pergamon Press Country of Publication: England NLM ID: 1307333 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0041-0101 (Print) Linking ISSN: 00410101 NLM ISO Abbreviation: Toxicon Subsets: MEDLINE
- Publication Information:
Original Publication: Oxford ; New York : Pergamon Press, c1962-
- Subject Terms:
- Abstract:
Snake venom glands synthesize a variety of serine proteinases capable of affecting the haemostatic system. They act on macromolecular substrates of the coagulation, fibrinolytic, and kallikrein-kinin systems, and on platelets to cause an imbalance of the haemostatic system of the prey. In this review we describe their biochemical/biophysical characteristics, biological activities as well as aspects of their evolution and structure-activity relationship.
- Number of References:
116
- Accession Number:
0 (Serine Proteinase Inhibitors)
0 (Snake Venoms)
EC 3.4.21.- (Serine Endopeptidases)
- Publication Date:
Date Created: 20050601 Date Completed: 20050811 Latest Revision: 20220408
- Publication Date:
20240829
- Accession Number:
10.1016/j.toxicon.2005.02.020
- Accession Number:
15922778
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