A further examination of the active form of crotalus adamanteus phospholipase A2
Author:
Publisher
Elsevier BV
Subject
Endocrinology,Biochemistry,Biophysics
Reference18 articles.
1. Evidence that the phospholipases A2 of Crotalus adamanteus venom are dimers
2. Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus adamanteus. A new classification of phospholipases A2 based upon structural determinants.
3. Kinetic study of the hydrolysis of lecithin monolayers by Crotalus adamanteus .alpha.-phospholipase A2. Monomer-Dimer equilibrium
4. Phospholipase A2 of Crotalus atrox. Molecular weight and other properties
5. Isolation and characterization of two phospholipase as from the venom of Agkistrodon halys blomhoffii
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1. Carbon monoxide inhibits the anticoagulant activity of phospholipase A2 purified from Crotalus adamanteus venom;Journal of Thrombosis and Thrombolysis;2018-10-29
2. Molecular modeling and inhibition of phospholipase A2 by polyhydroxy phenolic compounds;European Journal of Medicinal Chemistry;2009-01
3. Molecular modeling of the inhibition of enzyme PLA2from snake venom by dipyrone and 1-phenyl-3-methyl-5-pyrazolone;International Journal of Quantum Chemistry;2008
4. A pH-Induced Dissociation of the Dimeric Form of a Lysine 49-Phospholipase A2 Abolishes Ca2+-Independent Membrane Damaging Activity;Biochemistry;2001-05-18
5. Solution and Interface Aggregation States of Crotalus atrox Venom Phospholipase A2 by Two-Photon Excitation Fluorescence Correlation Spectroscopy;Biochemistry;2001-05-18
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