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:
- Status:
- Artigo publicado em periódico de acesso aberto (Gold Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
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: 01 abr. 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 abr. 01 ] 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 abr. 01 ] 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
- Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry
- Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering
- LbHelp1 is essencial to produce LbmtHsp70 in a structural and functional fashion
- 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
- Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization
- Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities
Informações sobre a disponibilidade de versões do artigo em acesso aberto coletadas automaticamente via oaDOI API (Unpaywall).
Por se tratar de integração com serviço externo, podem existir diferentes versões do trabalho (como preprints ou postprints), que podem diferir da versão publicada.
Download do texto completo
| Tipo | Nome | Link | |
|---|---|---|---|
 |
LEANDROBARBOSA_2013.pdf | Direct link | |
|
LEANDROBARBOSA_2013.pdf | Direct link |
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
