Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome (2018)
- Authors:
- USP affiliated authors: BARBOSA, LEANDRO RAMOS SOUZA - IF ; BORGES, JÚLIO CÉSAR - IQSC
- Unidades: IF; IQSC
- DOI: 10.1016/j.ijbiomac.2017.11.161
- Assunto: BIOQUÍMICA CELULAR
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: International Journal of Biological Macromolecules
- ISSN: 0141-8130
- Volume/Número/Paginação/Ano: v. 108, p. 193-204, 2018
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
SILVA, Noeli Soares Melo da et al. Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome. International Journal of Biological Macromolecules, v. 108, p. 193-204, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2017.11.161. Acesso em: 20 abr. 2024. -
APA
Silva, N. S. M. da, Seraphim, T. V., Minari, K., Barbosa, L. R. S., & Borges, J. C. (2018). Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome. International Journal of Biological Macromolecules, 108, 193-204. doi:10.1016/j.ijbiomac.2017.11.161 -
NLM
Silva NSM da, Seraphim TV, Minari K, Barbosa LRS, Borges JC. Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome [Internet]. International Journal of Biological Macromolecules. 2018 ; 108 193-204.[citado 2024 abr. 20 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.11.161 -
Vancouver
Silva NSM da, Seraphim TV, Minari K, Barbosa LRS, Borges JC. Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome [Internet]. International Journal of Biological Macromolecules. 2018 ; 108 193-204.[citado 2024 abr. 20 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.11.161 - A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
- Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering
- Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes
- Structural and functional studies of Hsp70-escort protein - Hep1 - of Leishmania braziliensis
- Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide
- Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry
- Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities
- Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis
- Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization
- The C-terminal region of the human p23 chaperone modulates its structure and function
Informações sobre o DOI: 10.1016/j.ijbiomac.2017.11.161 (Fonte: oaDOI API)
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