Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis (2016)
- Authors:
- USP affiliated authors: BARBOSA, LEANDRO RAMOS SOUZA - IF ; BORGES, JÚLIO CÉSAR - IQSC
- Unidades: IF; IQSC
- DOI: 10.1016/j.abb.2016.04.008
- Assunto: LEISHMANIA BRASILIENSIS
- Language: Inglês
- Imprenta:
- Source:
- Título: Archives Biochemistry and Biophysics
- ISSN: 0003-9861
- Volume/Número/Paginação/Ano: v. 600, p. 12-22, 2016
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
BATISTA, Fernanda Aparecida Heleno et al. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Archives Biochemistry and Biophysics, v. 600, p. 12-22, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2016.04.008. Acesso em: 27 dez. 2025. -
APA
Batista, F. A. H., Seraphim, T. V., Santos, C. A. dos, Gonzaga, M. R., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2016). Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Archives Biochemistry and Biophysics, 600, 12-22. doi:10.1016/j.abb.2016.04.008 -
NLM
Batista FAH, Seraphim TV, Santos CA dos, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis [Internet]. Archives Biochemistry and Biophysics. 2016 ; 600 12-22.[citado 2025 dez. 27 ] Available from: https://doi.org/10.1016/j.abb.2016.04.008 -
Vancouver
Batista FAH, Seraphim TV, Santos CA dos, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis [Internet]. Archives Biochemistry and Biophysics. 2016 ; 600 12-22.[citado 2025 dez. 27 ] Available from: https://doi.org/10.1016/j.abb.2016.04.008 - A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
- LbHelp1 is essencial to produce LbmtHsp70 in a structural and functional fashion
- 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
- Identification of two p23 co-chaperone isoforms in leihmania braziliensis exhinbiting similar structures and Hsp90 interaction properties despite divergent stabilities
- 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
- Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization
Informações sobre o DOI: 10.1016/j.abb.2016.04.008 (Fonte: oaDOI API)
Download do texto completo
| Tipo | Nome | Link | |
|---|---|---|---|
 |
1-s2.0-S000398611630128X-... | Direct link |
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
