Identification of two p23 co-chaperone isoforms inLeishmania braziliensisexhibiting similar structures and Hsp90 interaction properties despite divergent stabilities

Author:

Batista Fernanda A.H.1,Almeida Glessler S.2,Seraphim Thiago V.1,Silva Kelly P.1,Murta Silvane M.F.3,Barbosa Leandro R.S.4,Borges Júlio C.1

Affiliation:

1. Instituto de Química de São Carlos; Universidade de São Paulo - USP; São Carlos, SP, Brazil

2. Programa de Pós-Graduação em Genética Evolutiva e Biologia Molecular; Departamento de Genética e Evolução; Universidade Federal de São Carlos; São Carlos, SP, Brazil

3. Centro de Pesquisa René Rachou; Fiocruz; Belo Horizonte MG, Brazil

4. Instituto de Física; Universidade de São Paulo - USP; São Paulo SP, Brazil

Funder

FAPESP (Fundação de Amparo à Pesquisa do Estado de São Paulo)

CNPq (Conselho Nacional de Pesquisa e Desenvolvimento)

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference53 articles.

1. Protein folding assisted by chaperones;Borges;Protein Pept Lett,2005

2. Conformational dynamics of the molecular chaperone Hsp90;Krukenberg;Q Rev Biophys,2011

3. The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones;Li;Biochim Biophys Acta,2012

4. The Interaction Networks of Hsp70 and Hsp90 in the Plasmodium and Leishmania Parasites

5. A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23;Johnson;J Biol Chem,1994

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