Amyloidogenic properties of a human co-chaperone (2008)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- Assunto: BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology (SBBQ)
-
ABNT
TIROLI, Ana O. et al. Amyloidogenic properties of a human co-chaperone. 2008, Anais.. São Paulo: SBBQ, 2008. . Acesso em: 12 jun. 2024. -
APA
Tiroli, A. O., Borges, J. C., Barbosa, J. A., Sampaio, A. P. W., Rossi, A. P., Zeri, A. C., et al. (2008). Amyloidogenic properties of a human co-chaperone. In . São Paulo: SBBQ. -
NLM
Tiroli AO, Borges JC, Barbosa JA, Sampaio APW, Rossi AP, Zeri AC, Cyr DM, Ferreira ST, Ramos CHI. Amyloidogenic properties of a human co-chaperone. 2008 ;[citado 2024 jun. 12 ] -
Vancouver
Tiroli AO, Borges JC, Barbosa JA, Sampaio APW, Rossi AP, Zeri AC, Cyr DM, Ferreira ST, Ramos CHI. Amyloidogenic properties of a human co-chaperone. 2008 ;[citado 2024 jun. 12 ] - Unfolding studies of yeast HSP40 SIS1 and deleted mutants suggest that c-termini subdomain contacts are important for stabilization and dimerization
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- Structural characterization of the Hsp70-interacting protein-HIP-from Leishmania braziliensis
- Clonagem e expressão heteróloga da HSP70 de Leishmania braziliensis
- Heterologous production and structural studies of the Hsp70/Hsp90 - organization protein - HOP - from leishmania braziliensis
- Cloning and heterologous expression of the human Hsp70 - escort protein - hep1 - and its effect on - solubilization of the mtHsp70
- Human regulatory protein Ki-1/57 has characteristics of an intrinsically unstructured protein
- Thermal- and chemical-unfloding studies of yeast Hsp40 SIS1 and mutants
- Obtenção e caracterização do domínio M da Hsp90 de Leishmania braziliensis
- Expression, purification and characterization of the middle domain of the Hsp90 molecular chaperone from plasmodium falciparum
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