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A novel heparin-dependent inhibitor of activated protein C that potentiates consumptive coagulopathy in Russell's viper envenomation. J Biol Chem. 2012 May 4;287(19):15739-48. doi: 10.1074/jbc.M111.323063. Epub 2012 Mar 13.
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Cloning and nucleotide sequence of a cDNA encoding ammodytoxin A, the most toxic phospholipase A2 from the venom of long-nosed viper (Vipera ammodytes). Toxicon. 1991;29(2):269-73. doi: 10.1016/0041-0101(91)90112-5.
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Ammodytoxin A, a highly lethal phospholipase A2 from Vipera ammodytes ammodytes venom. Biochim Biophys Acta. 1985 Apr 29;828(3):306-12. doi: 10.1016/0167-4838(85)90312-7.
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| Ref 4 |
An aromatic, but not a basic, residue is involved in the toxicity of group-II phospholipase A2 neurotoxins. Biochem J. 1999 Jul 1;341 ( Pt 1)(Pt 1):139-45.
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| Ref 5 |
The amino acid region 115-119 of ammodytoxins plays an important role in neurotoxicity. Biochem Biophys Res Commun. 2000 Oct 5;276(3):1229-34. doi: 10.1006/bbrc.2000.3605.
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Charge reversal of ammodytoxin A, a phospholipase A2-toxin, does not abolish its neurotoxicity. Biochem J. 2000 Dec 1;352 Pt 2(Pt 2):251-5. doi: 10.1042/0264-6021:3520251.
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The facilitatory actions of snake venom phospholipase A(2) neurotoxins at the neuromuscular junction are not mediated through voltage-gated K(+) channels. Toxicon. 2001 Dec;39(12):1871-82. doi: 10.1016/s0041-0101(01)00170-2.
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Phenylalanine-24 in the N-terminal region of ammodytoxins is important for both enzymic activity and presynaptic toxicity. Biochem J. 2002 Apr 15;363(Pt 2):353-8. doi: 10.1042/0264-6021:3630353.
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The C-terminal region of ammodytoxins is important but not sufficient for neurotoxicity. Eur J Biochem. 2002 Dec;269(23):5759-64. doi: 10.1046/j.1432-1033.2002.03301.x.
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Identification of a novel binding site for calmodulin in ammodytoxin A, a neurotoxic group IIA phospholipase A2. Eur J Biochem. 2003 Jul;270(14):3018-25. doi: 10.1046/j.1432-1033.2003.03679.x.
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Ammodytoxin, a neurotoxic secreted phospholipase A(2), can act in the cytosol of the nerve cell. Biochem Biophys Res Commun. 2004 Nov 19;324(3):981-5. doi: 10.1016/j.bbrc.2004.09.144.
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| Ref 12 |
Basic amino acid residues in the beta-structure region contribute, but not critically, to presynaptic neurotoxicity of ammodytoxin A. Biochim Biophys Acta. 2004 Nov 1;1702(2):217-25. doi: 10.1016/j.bbapap.2004.09.002.
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Ammodytoxins, potent presynaptic neurotoxins, are also highly efficient phospholipase A2 enzymes. Biochemistry. 2005 Sep 20;44(37):12535-45. doi: 10.1021/bi051024r.
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| Ref 14 |
The C-terminal and beta-wing regions of ammodytoxin A, a neurotoxic phospholipase A2 from Vipera ammodytes ammodytes, are critical for binding to factor Xa and for anticoagulant effect. Biochimie. 2006 Jan;88(1):69-76. doi: 10.1016/j.biochi.2005.06.015. Epub 2005 Jul 7.
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Binding to the high-affinity M-type receptor for secreted phospholipases A(2) is not obligatory for the presynaptic neurotoxicity of ammodytoxin A. Biochimie. 2006 Oct;88(10):1425-33. doi: 10.1016/j.biochi.2006.06.008. Epub 2006 Jun 21.
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| Ref 16 |
A presynaptically toxic secreted phospholipase A2 is internalized into motoneuron-like cells where it is rapidly translocated into the cytosol. Biochim Biophys Acta. 2008 Jun;1783(6):1129-39. doi: 10.1016/j.bbamcr.2008.01.011. Epub 2008 Jan 26.
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Ammodytoxin: a window into understanding presynaptic toxicity of secreted phospholipases A(2) and more. Toxicon. 2011 Sep 1;58(3):219-29. doi: 10.1016/j.toxicon.2011.06.009. Epub 2011 Jun 26.
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Comparative structural studies of two natural isoforms of ammodytoxin, phospholipases A2 from Vipera ammodytes ammodytes which differ in neurotoxicity and anticoagulant activity. J Struct Biol. 2010 Mar;169(3):360-9. doi: 10.1016/j.jsb.2009.10.010. Epub 2009 Oct 24.
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