Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A (2015)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- Subjects: PROTEÍNAS; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Livro de resumos
- Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - UBMB
-
ABNT
DORES-SILVA, Paulo Roberto das e RAMOS, Carlos Henrique Inacio e BORGES, Julio Cesar. Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A. 2015, Anais.. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo, 2015. Disponível em: https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf. Acesso em: 14 out. 2024. -
APA
Dores-Silva, P. R. das, Ramos, C. H. I., & Borges, J. C. (2015). Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A. In Livro de resumos. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf -
NLM
Dores-Silva PR das, Ramos CHI, Borges JC. Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A [Internet]. Livro de resumos. 2015 ;[citado 2024 out. 14 ] Available from: https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf -
Vancouver
Dores-Silva PR das, Ramos CHI, Borges JC. Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A [Internet]. Livro de resumos. 2015 ;[citado 2024 out. 14 ] Available from: https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf - 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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- Obtenção e caracterização da HOP de P. falciparum e L. braziliensis
- Heterologous expression and characterization of n-domain of Hsp90 from Leishmania braziliensis and its co-chaperone p23
- The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism
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