The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism (2011)
- Authors:
- Autor USP: BORGES, JÚLIO CÉSAR - IQSC
- Unidade: IQSC
- Subjects: BIOLOGIA MOLECULAR; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Protein and Peptide Letters
- ISSN: 0929-8665
- Volume/Número/Paginação/Ano: v. 18, n.2, p. 132-142, 2011
-
ABNT
SILVA, Kelly P da e BORGES, Julio Cesar. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters, v. 18, n. 2, p. 132-142, 2011Tradução . . Acesso em: 17 fev. 2026. -
APA
Silva, K. P. da, & Borges, J. C. (2011). The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters, 18( 2), 132-142. -
NLM
Silva KP da, Borges JC. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters. 2011 ; 18( 2): 132-142.[citado 2026 fev. 17 ] -
Vancouver
Silva KP da, Borges JC. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters. 2011 ; 18( 2): 132-142.[citado 2026 fev. 17 ] - Preparation and characterization of Aha1 from leishmania braziliensis
- Low resolution structural studies of human RACK-1
- Efeito da co-chaperona Hep1 e de seus mutantes de deleção, na solubilização da Hsp70 mitocondrial de Leishmania braziliensis em sistemas de co-expressão
- Human regulatory ki-1/57 is a novel intrinsically unstructured protein involved in mechanisms of pre-mRNA splicing
- Produção e caracterização biofísica incial dos mutantes de delação de Hep1 de leishmania braziliensis
- Structural characterization of the Hsp70-interacting protein-HIP-from Leishmania braziliensis
- Obtenção e caracterização da chaperona mtHSP70 de Leishmania braziliensis
- Structural studies of plasmodium falciparum activator of Hsp90 ATPase 1 – PfAha1
- Heterologous expression and characterization of n-domain of Hsp90 from Leishmania braziliensis and its co-chaperone p23
- Structural studies of prephenate dehydratase from Mycobacterium tuberculosis H37Rv by SAXS, ultracentrifugation, and computational analysis
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