The C-terminal region of the human p23 chaperone modulates its structure and function (2015)
- Authors:
- USP affiliated authors: BORGES, JÚLIO CÉSAR - IQSC ; BARBOSA, LEANDRO RAMOS SOUZA - IF ; SERAPHIM, THIAGO VARGAS - IQSC
- Unidades: IQSC; IF
- DOI: 10.1016/j.abb.2014.10.015
- Subjects: BIOFÍSICA; BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Source:
- Título: Archives of Biochemistry and Biophysics
- ISSN: 0003-9861
- Volume/Número/Paginação/Ano: v. 565, p. 57-67, 2015
- Status:
- Artigo possui versão em acesso aberto em repositório (Green Open Access)
- Versão do Documento:
- Versão submetida (Pré-print)
- Acessar versão aberta:
-
ABNT
SERAPHIM, Thiago Vargas et al. The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, v. 565, p. 57-67, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.10.015. Acesso em: 02 abr. 2026. -
APA
Seraphim, T. V., Gava, L. M., Mokry, D. Z., Cagliari, T. D., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015). The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, 565, 57-67. doi:10.1016/j.abb.2014.10.015 -
NLM
Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2026 abr. 02 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015 -
Vancouver
Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2026 abr. 02 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015 - Insights into the full-length SRPK2 structure and its hydrodynamic behavior
- 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
- 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
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