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: 03 jan. 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 jan. 03 ] -
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 jan. 03 ] - Thermal-and chemical-unfolding studies of yeast Hsp40 Sis1 and mutants
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- Central domain deletions affect the SAXS solution structure and function of yeast Hsp40 proteins Sis1 and Ydj1
- Comparative biopohysical studies to two Co-chaperones of leishmania braziliensis-Lbp23A and Lbp23B
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