Insights into the structural mechanism behind complex formation between a snake venom metalloproteinase and its natural inhibitor by synchrotron small-angle x-ray solution scattering (2002)
- Authors:
- USP affiliated authors: GARRATT, RICHARD CHARLES - IFSC ; CRAIEVICH, ALDO FELIX - IF
- Unidades: IFSC; IF
- Subjects: BIOLOGIA MOLECULAR; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Publisher: Blackwell Munksgaard
- Publisher place: Copenhagen
- Date published: 2002
- Source:
- Título do periódico: Acta Crystallographica A
- Conference titles: Congress and General Assembly of the International Union of Crystallography
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ABNT
FISCHER, H. et al. Insights into the structural mechanism behind complex formation between a snake venom metalloproteinase and its natural inhibitor by synchrotron small-angle x-ray solution scattering. Acta Crystallographica A. Copenhagen: Blackwell Munksgaard. . Acesso em: 19 abr. 2024. , 2002 -
APA
Fischer, H., Neves-Ferreira, A. G. C., Perales, J., Moura da Silva, A. M., Domont, G. B., Souza, D. H. F., et al. (2002). Insights into the structural mechanism behind complex formation between a snake venom metalloproteinase and its natural inhibitor by synchrotron small-angle x-ray solution scattering. Acta Crystallographica A. Copenhagen: Blackwell Munksgaard. -
NLM
Fischer H, Neves-Ferreira AGC, Perales J, Moura da Silva AM, Domont GB, Souza DHF, Garratt RC, Craievich AF. Insights into the structural mechanism behind complex formation between a snake venom metalloproteinase and its natural inhibitor by synchrotron small-angle x-ray solution scattering. Acta Crystallographica A. 2002 ;[citado 2024 abr. 19 ] -
Vancouver
Fischer H, Neves-Ferreira AGC, Perales J, Moura da Silva AM, Domont GB, Souza DHF, Garratt RC, Craievich AF. Insights into the structural mechanism behind complex formation between a snake venom metalloproteinase and its natural inhibitor by synchrotron small-angle x-ray solution scattering. Acta Crystallographica A. 2002 ;[citado 2024 abr. 19 ] - Domain motions and quartenary packing of phosphofructokinase-2 from Escherichia coli studied by small angle x-ray scattering and homology modeling
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