Academic Appointments

  • Basic Life Science Research Associate, Biology

All Publications

  • Defining Hsp70 Subnetworks in Dengue Virus Replication Reveals Key Vulnerability in Flavivirus Infection. Cell Taguwa, S., Maringer, K., Li, X., Bernal-Rubio, D., Rauch, J. N., Gestwicki, J. E., Andino, R., Fernandez-Sesma, A., Frydman, J. 2015; 163 (5): 1108-1123

    View details for DOI 10.1016/j.cell.2015.10.046

    View details for PubMedID 26582131

  • The significance of Hsp70 subnetwork for Dengue virus lifecycle. Uirusu Taguwa, S., Frydman, J. 2015; 65 (2): 179-186


    Viruses hijack host machineries for replicating themselves efficiently. Host protein quality control machineries (QC) not only assist protein folding to form bona fide proteins with active functions but also get rid of un/misfolded proteins via degradation to maintain the protein homeostasis. Previous studies have reported that viruses utilize QC at various steps for their lifecycles. Recently we defined Hsp70s and their cochaperones, DnaJs functions on Dengue lifecycle. Here we summarize the significance of QC on Dengue virus.

    View details for PubMedID 27760916

  • Broad action of Hsp90 as a host chaperone required for viral replication BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH Geller, R., Taguwa, S., Frydman, J. 2012; 1823 (3): 698-706


    Viruses are intracellular pathogens responsible for a vast number of human diseases. Due to their small genome size, viruses rely primarily on the biosynthetic apparatus of the host for their replication. Recent work has shown that the molecular chaperone Hsp90 is nearly universally required for viral protein homeostasis. As observed for many endogenous cellular proteins, numerous different viral proteins have been shown to require Hsp90 for their folding, assembly, and maturation. Importantly, the unique characteristics of viral replication cause viruses to be hypersensitive to Hsp90 inhibition, thus providing a novel therapeutic avenue for the development of broad-spectrum antiviral drugs. The major developments in this emerging field are hereby discussed. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).

    View details for DOI 10.1016/j.bbamcr.2011.11.007

    View details for Web of Science ID 000301628700012

    View details for PubMedID 22154817