Unraveling the Processing and Activation of Snake Venom Metalloproteinases
Author:
Affiliation:
1. Unidade de Proteômica, Departamento de Bioquímica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Rio de Janeiro 21941-909, Brazil
Funder
São Paulo Research Foundation
Coordenação de Aperfeiçoamento de Pessoal de NÃvel Superior
Consejo Nacional de Investigaciones CientÃficas y Técnicas
Publisher
American Chemical Society (ACS)
Subject
General Chemistry,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/pr500185a
Reference60 articles.
1. Structural Aspects of the Metzincin Clan of Metalloendopeptidases
2. Families of zinc metalloproteases
3. Catalytic Domain Architecture of Metzincin Metalloproteases
4. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’
5. The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc-peptidases
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