Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer (2020)
- Authors:
- USP affiliated authors: BORGES, JÚLIO CÉSAR - IQSC ; SILVA, NOELI SOARES MELO DA - IQSC ; TORRICILLAS, MARCELA DA SILVA - IQSC ; BARBOSA, LEANDRO RAMOS SOUZA - IF ; SERAPHIM, THIAGO VARGAS - IQSC
- Unidades: IQSC; IF
- DOI: 10.1016/j.abb.2020.108468
- Assunto: PROTEÍNAS
- Keywords: Hsp90; Molecular chaperone; Plasmodium falciparum
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Título: Archives of Biochemistry and Biophysics
- ISSN: 0003-9861
- Volume/Número/Paginação/Ano: v. 690, p. 108468, Sept.2020
- 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. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Archives of Biochemistry and Biophysics, v. 690, p. 108468, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2020.108468. Acesso em: 13 nov. 2024. -
APA
Silva, N. S. M. da, Torricillas, M. da S., Minari, K., Barbosa, L. R. S., Seraphim, T. V., & Borges, J. C. (2020). Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Archives of Biochemistry and Biophysics, 690, 108468. doi:10.1016/j.abb.2020.108468 -
NLM
Silva NSM da, Torricillas M da S, Minari K, Barbosa LRS, Seraphim TV, Borges JC. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer [Internet]. Archives of Biochemistry and Biophysics. 2020 ; 690 108468.[citado 2024 nov. 13 ] Available from: https://doi.org/10.1016/j.abb.2020.108468 -
Vancouver
Silva NSM da, Torricillas M da S, Minari K, Barbosa LRS, Seraphim TV, Borges JC. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer [Internet]. Archives of Biochemistry and Biophysics. 2020 ; 690 108468.[citado 2024 nov. 13 ] Available from: https://doi.org/10.1016/j.abb.2020.108468 - The C-terminal region of the human p23 chaperone modulates its structure and function
- Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities
- Insights into the full-length SRPK2 structure and its hydrodynamic behavior
- Small-angle X-ray scattering (SAXS) studies on the HSP70 chaperone family
- Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90
- Caracterização dos domínios n- e c-terminais da bip humana(HSPA5)
- Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering
- A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
- Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution
- Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes
Informações sobre o DOI: 10.1016/j.abb.2020.108468 (Fonte: oaDOI API)
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