Unfolding studies of yeast HSP40 SIS1 and deleted mutants suggest that c-termini subdomain contacts are important for stabilization and dimerization (2008)
- Authors:
- USP affiliated author: BORGES, JÚLIO CÉSAR - IQSC
- School: IQSC
- Subject: BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Conference title: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology (SBBQ)
-
ABNT
BORGES, Júlio Cesar e CYR, D. M. e RAMOS, C. H. I. Unfolding studies of yeast HSP40 SIS1 and deleted mutants suggest that c-termini subdomain contacts are important for stabilization and dimerization. 2008, Anais.. São Paulo: SBBQ, 2008. . Acesso em: 06 jul. 2022. -
APA
Borges, J. C., Cyr, D. M., & Ramos, C. H. I. (2008). Unfolding studies of yeast HSP40 SIS1 and deleted mutants suggest that c-termini subdomain contacts are important for stabilization and dimerization. In . São Paulo: SBBQ. -
NLM
Borges JC, Cyr DM, Ramos CHI. Unfolding studies of yeast HSP40 SIS1 and deleted mutants suggest that c-termini subdomain contacts are important for stabilization and dimerization. 2008 ;[citado 2022 jul. 06 ] -
Vancouver
Borges JC, Cyr DM, Ramos CHI. Unfolding studies of yeast HSP40 SIS1 and deleted mutants suggest that c-termini subdomain contacts are important for stabilization and dimerization. 2008 ;[citado 2022 jul. 06 ] - Human regulatory ki-1/57 is a novel intrinsically unstructured protein involved in mechanisms of pre-mRNA splicing
- Preparation and characterization of Aha1 from leishmania braziliensis
- Low resolution structural studies of human RACK-1
- Cloning and expression of the middle domain of Hsp90 protein (Hsp90M) from leishmania braziliensis
- Expression and purification of Hsp90 from leishmania braziliensis and its interaction with two Co-chaperones p23
- Heterologous expression and structural characterization of two p23 - Hsp90's Co-chaperone - from leishmania braziliensis
- Low resolution structural studies of the activator of Hsp70 ATPase activity - Aha1- from leishmania braziliensis
- Structural study of the splicing regulatory kinase SRPK2
- Structural and thermodynamic studies of the HSP70/HSP90 organizing protein-HOP from leishmania braziliensis
- Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A
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