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 é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by
-
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: 28 dez. 2025. -
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 2025 dez. 28 ] 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 2025 dez. 28 ] Available from: https://doi.org/10.1371/journal.pone.0066822 - The C-terminal region of the human p23 chaperone modulates its structure and function
- Insights into the full-length SRPK2 structure and its hydrodynamic behavior
- LbHelp1 is essencial to produce LbmtHsp70 in a structural and functional fashion
- 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
- 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
- Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry
Informações sobre o DOI: 10.1371/journal.pone.0066822 (Fonte: oaDOI API)
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