Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation (2018)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- DOI: 10.2174/97816810861561180101
- Assunto: PROTEÍNAS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins
- Volume/Número/Paginação/Ano: v. 1
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
BORGES, Julio Cesar e RAMOS, Carlos Henrique Inacio. Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation. Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins. Tradução . Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo, 2018. v. 1. . Disponível em: https://doi.org/10.2174/97816810861561180101. Acesso em: 18 set. 2024. -
APA
Borges, J. C., & Ramos, C. H. I. (2018). Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation. In Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins (Vol. 1). Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo. doi:10.2174/97816810861561180101 -
NLM
Borges JC, Ramos CHI. Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation [Internet]. In: Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins. Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo; 2018. [citado 2024 set. 18 ] Available from: https://doi.org/10.2174/97816810861561180101 -
Vancouver
Borges JC, Ramos CHI. Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation [Internet]. In: Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins. Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo; 2018. [citado 2024 set. 18 ] Available from: https://doi.org/10.2174/97816810861561180101 - 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
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- 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
Informações sobre o DOI: 10.2174/97816810861561180101 (Fonte: oaDOI API)
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