Structural and stability studies of hsp90 co-chaperone p23 suggested that the c-terminal stabilizes the 'beta'-sheet folded domain (2009)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- Assunto: BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq
- Publisher place: São Paulo
- Date published: 2009
- Source:
- Título: Program and Index
- Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society
-
ABNT
BORGES, Julio Cesar e CAGLIARI, Thiago C. e RAMOS, Carlos H. I. Structural and stability studies of hsp90 co-chaperone p23 suggested that the c-terminal stabilizes the 'beta'-sheet folded domain. 2009, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2009. . Acesso em: 29 dez. 2025. -
APA
Borges, J. C., Cagliari, T. C., & Ramos, C. H. I. (2009). Structural and stability studies of hsp90 co-chaperone p23 suggested that the c-terminal stabilizes the 'beta'-sheet folded domain. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. -
NLM
Borges JC, Cagliari TC, Ramos CHI. Structural and stability studies of hsp90 co-chaperone p23 suggested that the c-terminal stabilizes the 'beta'-sheet folded domain. Program and Index. 2009 ;[citado 2025 dez. 29 ] -
Vancouver
Borges JC, Cagliari TC, Ramos CHI. Structural and stability studies of hsp90 co-chaperone p23 suggested that the c-terminal stabilizes the 'beta'-sheet folded domain. Program and Index. 2009 ;[citado 2025 dez. 29 ] - Characterization of nucleoid-induced changes on the quaternary structure of human 70 KDa heat shock protein Hsp70.1 by analytical ultracentrifugation
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