Molecular diversity of spider venom

@article{Vassilevski2009MolecularDO,
  title={Molecular diversity of spider venom},
  author={Alexander A. Vassilevski and Sergey A Kozlov and Eugene V. Grishin},
  journal={Biochemistry (Moscow)},
  year={2009},
  volume={74},
  pages={1505-1534}
}
Spider venom, a factor that has played a decisive role in the evolution of one of the most successful groups of living organisms, is reviewed. Unique molecular diversity of venom components including substances of variable structure (from simple low molecular weight compounds to large multidomain proteins) with different functions is considered. Special attention is given to the structure, properties, and biosynthesis of toxins of polypeptide nature. 

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References

SHOWING 1-10 OF 409 REFERENCES
Polypeptide neurotoxins from spider venoms.
  • E. Grishin
  • Medicine, Biology
  • European journal of biochemistry
  • 1999
TLDR
The structural and functional properties of spider polypeptide toxins are reviewed and high molecular mass toxic proteins was found in the venom of the spider genus Latrodectus, causing a massive transmitter release from a diversity of nerve endings. Expand
Molecular diversification in spider venoms: A web of combinatorial peptide libraries
TLDR
Gene duplication and focal hypermutation appear to be common mechanisms to venomous mollusks and spiders, leading to the pharmacologically complex cocktails used for predation and defense. Expand
Pharmacology and biochemistry of spider venoms.
  • L. Rash, W. Hodgson
  • Biology, Medicine
  • Toxicon : official journal of the International Society on Toxinology
  • 2002
TLDR
This review covers the pharmacological and biochemical activities of spider venoms and the nature of the active components, and focuses on the wide variety of ion channel toxins, novel non-neurotoxic peptide toxins, enzymes and low molecular weight compounds that have been isolated. Expand
Structure and pharmacology of spider venom neurotoxins.
TLDR
Following diverse molecular evolution mechanisms, and in particular selective hypermutation, short spider peptides appear to have functionally diversified while retaining a conserved molecular scaffold. Expand
Therapeutic potential of venom peptides
TLDR
The pharmacology of venom peptides is surveyed and their therapeutic prospects are assessed for the treatment of pain, diabetes, multiple sclerosis and cardiovascular diseases are assessed. Expand
A rational nomenclature for naming peptide toxins from spiders and other venomous animals.
TLDR
A rational nomenclature is introduced that can be applied to the naming of peptide toxins from spiders and other venomous animals to enable these toxins to be rationally classified, catalogued, and compared. Expand
Spider and wasp neurotoxins: pharmacological and biochemical aspects.
TLDR
In this work, several biochemical and pharmacological aspects related to spider and wasp neurotoxins are summarized and compiled. Expand
The anticoagulant action of phospholipase A from Eresus niger spider venom.
  • P. Usmanov, F. Nuritova
  • Biology, Medicine
  • Toxicon : official journal of the International Society on Toxinology
  • 1994
TLDR
Phospholipase A, named component EnPA, was isolated from Eresus niger spider venom and it was concluded that anticoagulant action of compound EnPA is due to inactivation of the procoagulate activity of phospholipids because of its high binding with them. Expand
A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies.
TLDR
This article describes the classification of K+-channel-blocking peptides belonging to family 2 peptides and comprising 30-40 amino acids linked by three or four disulfide bridges, and provides evidence for the existence of 12 molecular subfamilies, named alpha-KTx1-12, containing 49 different peptides. Expand
Genetic mechanisms of scorpion venom peptide diversification.
TLDR
Toxinomics (genomics and proteomics of scorpion toxins and toxin-like peptides) are expected to greatly advance in the near future in order to completely clarify the diversity of scorpions' venom peptides. Expand
...
1
2
3
4
5
...