Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors (2012)
- Authors:
- Autor USP: MARTÍNEZ, LEANDRO - IFSC
- Unidade: IFSC
- DOI: 10.3390/toxins4080580
- Subjects: MODELAGEM MOLECULAR; TOXINAS; VIRULÊNCIA
- Language: Inglês
- Imprenta:
- Source:
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
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- Cor do Acesso Aberto: gold
- Licença: cc-by
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ABNT
LAINE, Élodie; MARTÍNEZ, Leandro; LADANT, Daniel; MALLIAVIN, Thérèse; BLONDEL, Arnaud. Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors. Toxins, Basel, v. 4, n. 8, p. 580-604, 2012. Disponível em: < http://dx.doi.org/10.3390/toxins4080580 > DOI: 10.3390/toxins4080580. -
APA
Laine, É., Martínez, L., Ladant, D., Malliavin, T., & Blondel, A. (2012). Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors. Toxins, 4( 8), 580-604. doi:10.3390/toxins4080580 -
NLM
Laine É, Martínez L, Ladant D, Malliavin T, Blondel A. Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors [Internet]. Toxins. 2012 ; 4( 8): 580-604.Available from: http://dx.doi.org/10.3390/toxins4080580 -
Vancouver
Laine É, Martínez L, Ladant D, Malliavin T, Blondel A. Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors [Internet]. Toxins. 2012 ; 4( 8): 580-604.Available from: http://dx.doi.org/10.3390/toxins4080580 - Computational study of the temperature dependence of side-chain solvation: implications for protein thermal stability
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Informações sobre o DOI: 10.3390/toxins4080580 (Fonte: oaDOI API)
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