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Filtros : "Indexado Science Citation Index" "IF-FGE" Removidos: "Amorim, Sônia Naves David" "Universidad Nacional Autónoma de México (UNAM)" Limpar

Filtros

Artigo de periodico
Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization (2015)
Dores-Silva, Paulo Roberto das; Barbosa, Leandro Ramos Souza; Ramos, Carlos Henrique Inacio; Borges, Julio Cesar
Source: PLoS ONE. Unidades: IF, IQSC
Assunto: PROTEÍNAS
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
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: 14 nov. 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 nov. 14 ] 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 nov. 14 ] Available from: https://doi.org/10.1371/journal.pone.0117170
Artigo de periodico
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 (2013)
Seraphim, Thiago Vargas ; Alves, Marina M; Silva, Indjara Mallmann da; Gomes, Francisco Edvan Rodrigues; Silva, Kelly Prata; Murta, Silvane M. F; Barbosa, Leandro Ramos Souza ; Borges, Julio Cesar
Source: PLoS ONE. Unidades: IF, IQSC
Subjects: PROTEÍNAS, LEISHMANIA BRASILIENSIS
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
SERAPHIM, Thiago Vargas et al. 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. PLoS ONE, v. 8, n. 6, p. e 66822, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0066822. Acesso em: 14 nov. 2024.
APA
Seraphim, T. V., Alves, M. M., Silva, I. M. da, Gomes, F. E. R., Silva, K. P., Murta, S. M. F., et al. (2013). 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. PLoS ONE, 8( 6), e 66822. doi:10.1371/journal.pone.0066822
NLM
Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. 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 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2024 nov. 14 ] Available from: https://doi.org/10.1371/journal.pone.0066822
Vancouver
Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. 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 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2024 nov. 14 ] Available from: https://doi.org/10.1371/journal.pone.0066822

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