Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities (2015)
- Authors:
- USP affiliated authors: BARBOSA, LEANDRO RAMOS SOUZA - IF ; BORGES, JÚLIO CÉSAR - IQSC
- Unidades: IF; IQSC
- DOI: 10.1111/febs.13141
- Assunto: LEISHMANIA BRASILIENSIS
- Language: Inglês
- Imprenta:
- Source:
- Título: FEBS Journal
- Volume/Número/Paginação/Ano: v. 282, n. 2, p. 388-406, 2015
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: green
- Licença: other-oa
-
ABNT
BATISTA, Fernanda Aparecida Heleno et al. Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS Journal, v. 282, n. 2, p. 388-406, 2015Tradução . . Disponível em: https://doi.org/10.1111/febs.13141. Acesso em: 14 out. 2024. -
APA
Batista, F. A. H., Almeida, G. S., Seraphim, T. V., Silva, K. P., Murta, S. M. F., Barbosa, L. R. S., & Borges, J. C. (2015). Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS Journal, 282( 2), 388-406. doi:10.1111/febs.13141 -
NLM
Batista FAH, Almeida GS, Seraphim TV, Silva KP, Murta SMF, Barbosa LRS, Borges JC. Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities [Internet]. FEBS Journal. 2015 ; 282( 2): 388-406.[citado 2024 out. 14 ] Available from: https://doi.org/10.1111/febs.13141 -
Vancouver
Batista FAH, Almeida GS, Seraphim TV, Silva KP, Murta SMF, Barbosa LRS, Borges JC. Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities [Internet]. FEBS Journal. 2015 ; 282( 2): 388-406.[citado 2024 out. 14 ] Available from: https://doi.org/10.1111/febs.13141 - 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
- Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry
- Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome
- Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide
- 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
- 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: 10.1111/febs.13141 (Fonte: oaDOI API)
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