Hsp90 interaction with other proteins

• Grant number: 16/14228-1
• Support type: Scholarships in Brazil - Post-Doctorate
• Effective date (Start): October 01, 2016
• Effective date (End): October 31, 2017
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal researcher: Carlos Henrique Inacio Ramos
• Grantee: Käthe Margareta Dahlström
• Home 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)

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, JUL 2020. Web of Science Citations: 0.