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 (2013)
- Authors:
- USP affiliated authors: BARBOSA, LEANDRO RAMOS SOUZA - IF ; BORGES, JÚLIO CÉSAR - IQSC ; SERAPHIM, THIAGO VARGAS - IQSC ; GOMES, FRANCISCO EDVAN RODRIGUES - IQSC
- Unidades: IF; IQSC
- DOI: 10.1371/journal.pone.0066822
- Subjects: PROTEÍNAS; LEISHMANIA BRASILIENSIS
- Language: Inglês
- Imprenta:
- Publisher place: San Francisco
- Date published: 2013
- Source:
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
SERAPHIM, Thiago Vargas et al. 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. PLoS ONE, v. 8, n. 6, p. e 66822, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0066822. Acesso em: 13 fev. 2026. -
APA
Seraphim, T. V., Alves, M. M., Silva, I. M. da, Gomes, F. E. R., Silva, K. P., Murta, S. M. F., et al. (2013). 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. PLoS ONE, 8( 6), e 66822. doi:10.1371/journal.pone.0066822 -
NLM
Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. 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 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2026 fev. 13 ] Available from: https://doi.org/10.1371/journal.pone.0066822 -
Vancouver
Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. 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 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2026 fev. 13 ] Available from: https://doi.org/10.1371/journal.pone.0066822 - The C-terminal region of the human p23 chaperone modulates its structure and function
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- Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes
- 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
- Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities
- Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization
- Structural and functional studies of Hsp70-escort protein - Hep1 - of Leishmania braziliensis
- Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry
- A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
Informações sobre o DOI: 10.1371/journal.pone.0066822 (Fonte: oaDOI API)
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