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Hsp90 interaction with other proteins

Grant number: 16/14228-1
Support Opportunities:Scholarships in Brazil - Post-Doctoral
Start date: October 01, 2016
End date: October 31, 2017
Field of knowledge:Biological Sciences - Biochemistry - Chemistry of Macromolecules
Principal Investigator:Carlos Henrique Inacio Ramos
Grantee:Käthe Margareta Dahlström
Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Associated research grant:12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis, AP.TEM

Abstract

The importance of understanding the interaction with other proteins of Hsp90 may be confirmed by the fact that this chaperone is a hub which interacts with at least 10 % of the proteins expressed in eukaryotes. However , little information exists on the regions of interaction. In addition to the above there is also little information about factors that can induce interaction with other proteins and how those interactions affect the structure and function of isolated Hsp90 and the Hsp90-Hsp70 system. In order to generate key information related to the above topics we will use strategies to try to get information on medium and high resolution of isolated and associated proteins . (AU)

News published in Agência FAPESP Newsletter about the scholarship:
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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
GONCALVES, CONRADO DE C.; PINHEIRO, GLAUCIA M. S.; DAHLSTROM, KATHE M.; SOUTO, DENIO E. P.; KUBOTA, LAURO T.; BARBOSA, LEANDRO R. S.; RAMOS, I, CARLOS H.. On the structure and function of Sorghum bicolor CHIP (carboxyl terminus of Hsc70-interacting protein): A link between chaperone and proteasome systems. Plant Science, v. 296, . (17/26158-0, 18/11948-9, 17/26058-6, 14/00076-0, 16/14228-1, 12/50161-8, 15/15822-1)