Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry (2012)
- Authors:
- USP affiliated authors: BARBOSA, LEANDRO RAMOS SOUZA - IF ; BORGES, JÚLIO CÉSAR - IQSC
- Unidades: IF; IQSC
- DOI: 10.1016/j.abb.2012.02.009
- Subjects: BIOFÍSICA; BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Source:
- Título: Archives of Biochemistry and Biophysics
- ISSN: 0003-9861
- Volume/Número/Paginação/Ano: v. 520, n. 2, p. 88-98, 2012
- Status:
- Artigo possui versão em acesso aberto em repositório (Green Open Access)
- Versão do Documento:
- Versão submetida (Pré-print)
- Acessar versão aberta:
-
ABNT
DORES-SILVA, Paulo Roberto das et al. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, v. 520, n. 2, p. 88-98, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.02.009. Acesso em: 08 abr. 2026. -
APA
Dores-Silva, P. R. das, Silva, E. R., Gomes, F. E. R., Silva, K. P., Barbosa, L. R. S., & Borges, J. C. (2012). Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, 520( 2), 88-98. doi:10.1016/j.abb.2012.02.009 -
NLM
Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2026 abr. 08 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009 -
Vancouver
Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2026 abr. 08 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009 - 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
- Structural and functional studies of Hsp70-escort protein - Hep1 - of Leishmania braziliensis
- A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
- Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis
- 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
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