Comparison of enzymatic and pharmacological activities of lysine-49 and aspartate-49 phospholipases A2 from Agkistrodon piscivorus piscivorus snake venom. A reconsideration
Author:
Publisher
Elsevier BV
Subject
Toxicology
Reference5 articles.
1. Comparison of enzymatic and pharmacological activities of lysine-49 and aspartate-49 phospholipases A2 from Agkistrodon piscivorus piscivorus snake venom;Dhillon;Biochem. Pharmac.,1987
2. The lysine-49 phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus;Maraganore;J. biol. Chem.,1986
3. A new class of phospholipases A2 with lysine in place of aspartate 49;Maraganore;J. biol. Chem.,1984
4. Phospholipases A2;Maraganore;J. prot. Chem.,1987
5. The role of aspartic acid-49 in the active site of phospholipase A2;Van den Bergh;Eur. J. Biochem.,1988
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1. Lys49 myotoxins, secreted phospholipase A2-like proteins of viperid venoms: A comprehensive review;Toxicon;2023-03
2. A predominant role for hydrogen bonding in the stability of the homodimer of bothropstoxin-I, A lysine 49-phospholipase A2;Biochimie;2005-11
3. Topology of the substrate-binding site of a Lys49-phospholipase A2 influences Ca2+-independent membrane-damaging activity;Biochemical Journal;2004-08-10
4. Chemical denaturation of a homodimeric lysine-49 phospholipase A2: a stable dimer interface and a native monomeric intermediate;Archives of Biochemistry and Biophysics;2003-03
5. Structural Basis for Low Catalytic Activity in Lys49 Phospholipases A2A Hypothesis: The Crystal Structure of Piratoxin II Complexed to Fatty Acid,;Biochemistry;2000-12-12
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