Cloning and expression of the Hsp70-interacting protein - hip-from leishmania braziliensis (2010)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- Assunto: BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq
- Publisher place: São Paulo
- Date published: 2010
- Source:
- Título do periódico: Program and Index
- Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society - SBBq
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ABNT
SILVA, E R et al. Cloning and expression of the Hsp70-interacting protein - hip-from leishmania braziliensis. 2010, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2010. . Acesso em: 04 fev. 2023. -
APA
Silva, E. R., Gomes, F. E. R., Silva, K. P., & Borges, J. C. (2010). Cloning and expression of the Hsp70-interacting protein - hip-from leishmania braziliensis. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. -
NLM
Silva ER, Gomes FER, Silva KP, Borges JC. Cloning and expression of the Hsp70-interacting protein - hip-from leishmania braziliensis. Program and Index. 2010 ;[citado 2023 fev. 04 ] -
Vancouver
Silva ER, Gomes FER, Silva KP, Borges JC. Cloning and expression of the Hsp70-interacting protein - hip-from leishmania braziliensis. Program and Index. 2010 ;[citado 2023 fev. 04 ] - Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity
- Amyloidogenic properties of a human co-chaperone
- Expressão e caracterização da AHA1 de Leishmania braziliensis
- Structural and functional studies of the HSP90 of the leishmania braziliensis
- Human, yeast, and leishmania P23 confer different stress response tolerances as deemed by in vivo yeast complementation assays
- Clonagem e expressão heteróloga da chaperona molecular Hsp70 citoplasmática de Plasmodium falciparum (PfHsp70) para caracterização estrutural e funcional
- Analysis of molecular targets of mycobacterium tuberculosis by analytical ultrcentrifugation
- Characterization of HSP90 molecular chaperone from leishmania braziliensis: structural features, ATPASE activity and inhibition studies
- Structural studies of prephenate dehydratase from Mycobacterium tuberculosis H37Rv by SAXS, ultracentrifugation, and computational analysis
- Activation of leishmania braziliensis HSP90 by AHA1 co-chaporone occurs through a cooperative mechanism
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