Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization (2015)
- Authors:
- USP affiliated authors: BARBOSA, LEANDRO RAMOS SOUZA - IF ; BORGES, JÚLIO CÉSAR - IQSC
- Unidades: IF; IQSC
- DOI: 10.1371/journal.pone.0117170
- Assunto: PROTEÍNAS
- Language: Inglês
- Imprenta:
- Publisher place: San Francisco
- Date published: 2015
- Source:
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by
-
ABNT
DORES-SILVA, Paulo Roberto das et al. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization. PLOS ONE, v. 10, n. 1, 2015Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0117170. Acesso em: 02 maio 2024. -
APA
Dores-Silva, P. R. das, Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015). Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization. PLOS ONE, 10( 1). doi:10.1371/journal.pone.0117170 -
NLM
Dores-Silva PR das, Barbosa LRS, Ramos CHI, Borges JC. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization [Internet]. PLOS ONE. 2015 ; 10( 1):[citado 2024 maio 02 ] Available from: https://doi.org/10.1371/journal.pone.0117170 -
Vancouver
Dores-Silva PR das, Barbosa LRS, Ramos CHI, Borges JC. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization [Internet]. PLOS ONE. 2015 ; 10( 1):[citado 2024 maio 02 ] Available from: https://doi.org/10.1371/journal.pone.0117170 - A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
- Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering
- Structural and functional studies of Hsp70-escort protein - Hep1 - of Leishmania braziliensis
- Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes
- 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
- Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis
- The C-terminal region of the human p23 chaperone modulates its structure and function
Informações sobre o DOI: 10.1371/journal.pone.0117170 (Fonte: oaDOI API)
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