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Akademický článek
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.
Autor: Thiago V Seraphim, Marina M Alves, Indjara M Silva, Francisco E R Gomes, Kelly P Silva, Silvane M F Murta, Leandro R S Barbosa, Júlio C Borges
Publikováno v: PLoS ONE, Vol 8, Iss 6, p e66822 (2013)
The Hsp90 molecular chaperone is essential for protein homeostasis and in the maturation of proteins involved with cell-cycle control. The low ATPase activity of Hsp90 is critical to drive its functional cycle, which is dependent on the Hsp90 cochape
Externí odkaz: https://doaj.org/article/75618ee561ff457c99dabfc31bb8bc9e
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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
Autor: Júlio César Borges, Indjara M. Silva, Thiago V. Seraphim, K.P. Silva, Francisco E.R. Gomes, Silvane M. F. Murta, Leandro R.S. Barbosa, Marina M. Alves
Publikováno v: PLoS ONE
PLoS ONE, Vol 8, Iss 6, p e66822 (2013)
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
The Hsp90 molecular chaperone is essential for protein homeostasis and in the maturation of proteins involved with cell-cycle control. The low ATPase activity of Hsp90 is critical to drive its functional cycle, which is dependent on the Hsp90 cochape
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1078cbef205169cfb996b451265ee94e
https://pubmed.ncbi.nlm.nih.gov/23826147
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