A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering (2016)
- Authors:
- USP affiliated authors: BORGES, JÚLIO CÉSAR - IQSC ; BARBOSA, LEANDRO RAMOS SOUZA - IF
- Unidades: IQSC; IF
- DOI: 10.1007/s12551-016-0194-x
- Subjects: PROTEÍNAS; BIOQUÍMICA CELULAR
- Language: Inglês
- Imprenta:
- Publisher place: Heidelberg
- Date published: 2016
- Source:
- Título: Biophysical Reviews
- ISSN: 1867-2469
- Volume/Número/Paginação/Ano: on line, 2016
- Status:
- Artigo possui acesso gratuito no site do editor (Bronze Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
ABNT
BORGES, Julio Cesar et al. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophysical Reviews, 2016Tradução . . Disponível em: https://doi.org/10.1007/s12551-016-0194-x. Acesso em: 01 abr. 2026. -
APA
Borges, J. C., Seraphim, T. V., Dores-Silva, P. R. das, & Barbosa, L. R. S. (2016). A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophysical Reviews. doi:10.1007/s12551-016-0194-x -
NLM
Borges JC, Seraphim TV, Dores-Silva PR das, Barbosa LRS. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering [Internet]. Biophysical Reviews. 2016 ;[citado 2026 abr. 01 ] Available from: https://doi.org/10.1007/s12551-016-0194-x -
Vancouver
Borges JC, Seraphim TV, Dores-Silva PR das, Barbosa LRS. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering [Internet]. Biophysical Reviews. 2016 ;[citado 2026 abr. 01 ] Available from: https://doi.org/10.1007/s12551-016-0194-x - 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
- Structural and functional studies of Hsp70-escort protein - Hep1 - of Leishmania braziliensis
- Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis
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