Characterization of nucleoid-induced changes on the quaternary structure of human 70 KDa heat shock protein Hsp70.1 by analytical ultracentrifugation (2009)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- DOI: 10.5483/bmbrep.2009.42.3.166
- Assunto: NUCLÉOLO
- Language: Inglês
- Imprenta:
- Source:
- Título: Journal of Biochemistry Molecular Biology Reports - BMB Reports
- ISSN: 1976-6696
- Volume/Número/Paginação/Ano: v. 42, n. 3, p. 166-171, 2009
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by-nc
-
ABNT
BORGES, Julio Cesar e RAMOS, Carlos H. I. Characterization of nucleoid-induced changes on the quaternary structure of human 70 KDa heat shock protein Hsp70.1 by analytical ultracentrifugation. Journal of Biochemistry Molecular Biology Reports - BMB Reports, v. 42, n. 3, p. 166-171, 2009Tradução . . Disponível em: https://doi.org/10.5483/bmbrep.2009.42.3.166. Acesso em: 30 dez. 2025. -
APA
Borges, J. C., & Ramos, C. H. I. (2009). Characterization of nucleoid-induced changes on the quaternary structure of human 70 KDa heat shock protein Hsp70.1 by analytical ultracentrifugation. Journal of Biochemistry Molecular Biology Reports - BMB Reports, 42( 3), 166-171. doi:10.5483/bmbrep.2009.42.3.166 -
NLM
Borges JC, Ramos CHI. Characterization of nucleoid-induced changes on the quaternary structure of human 70 KDa heat shock protein Hsp70.1 by analytical ultracentrifugation [Internet]. Journal of Biochemistry Molecular Biology Reports - BMB Reports. 2009 ; 42( 3): 166-171.[citado 2025 dez. 30 ] Available from: https://doi.org/10.5483/bmbrep.2009.42.3.166 -
Vancouver
Borges JC, Ramos CHI. Characterization of nucleoid-induced changes on the quaternary structure of human 70 KDa heat shock protein Hsp70.1 by analytical ultracentrifugation [Internet]. Journal of Biochemistry Molecular Biology Reports - BMB Reports. 2009 ; 42( 3): 166-171.[citado 2025 dez. 30 ] Available from: https://doi.org/10.5483/bmbrep.2009.42.3.166 - 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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- Expression, purification and characterization of the middle domain of the Hsp90 molecular chaperone from plasmodium falciparum
- Expression and purification of the human mitochondrial Hsp70 (mortalin) for structural studies
Informações sobre o DOI: 10.5483/bmbrep.2009.42.3.166 (Fonte: oaDOI API)
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