Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity (2014)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- DOI: 10.1021/bi500004q
- Assunto: BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Publisher place: Washington
- Date published: 2014
- Source:
- Título: Biochemistry
- ISSN: 0006-2960
- Volume/Número/Paginação/Ano: v. 53, n. 18, p. 2884-2889, 2014
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
ARAUJO, Thaís L. S. et al. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, v. 53, n. 18, p. 2884-2889, 2014Tradução . . Disponível em: https://doi.org/10.1021/bi500004q. Acesso em: 10 nov. 2024. -
APA
Araujo, T. L. S., Borges, J. C., Ramos, C. H. I., Meyer-Fernandes, J. R., Oliveira Júnior, R. S., Pascutti, P. G., et al. (2014). Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, 53( 18), 2884-2889. doi:10.1021/bi500004q -
NLM
Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2024 nov. 10 ] Available from: https://doi.org/10.1021/bi500004q -
Vancouver
Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2024 nov. 10 ] Available from: https://doi.org/10.1021/bi500004q - 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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- Heterologous production and structural studies of the Hsp70/Hsp90 - organization protein - HOP - from leishmania braziliensis
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- 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
Informações sobre o DOI: 10.1021/bi500004q (Fonte: oaDOI API)
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