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Accounts of Chemical Research|April 4, 2018
Protein-Protein Interactions in the Molecular Chaperone NetworkRebecca Freilich, Taylor Arhar, Jennifer L Abrams, et al.The Journal of Biological Chemistry|October 8, 2021
The interactions of molecular chaperones with client proteins: why are they so weak?Taylor Arhar, Arielle Shkedi, Cory M Nadel, et al.The Journal of Biological Chemistry|February 12, 2022
Two distinct classes of cochaperones compete for the EEVD motif in heat shock protein 70 to tune its chaperone activitiesOleta T Johnson, Cory M Nadel, Emma C Carroll, et al.Cell Stress & Chaperones|February 6, 2021
Functional genomics screen identifies proteostasis targets that modulate prion protein (PrP) stabilityJennifer Abrams, Taylor Arhar, Sue Ann Mok, et al.Journal of Molecular Biology|November 26, 2016
BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock ProteinsJennifer N Rauch, Eric Tse, Rebecca Freilich, et al.ACS Chemical Biology|December 14, 2006
Reclamation of proteins from the cellular scrap heapJason E GestwickiChemistry & Biology|April 27, 2005
Target identification for a promising anti-lupus drugJason E GestwickiNature Structural & Molecular Biology|May 6, 2018
Mapping interactions with the chaperone network reveals factors that protect against tau aggregationSue-Ann Mok, Carlo Condello, Rebecca Freilich, et al.Nature Communications|November 3, 2018
Competing protein-protein interactions regulate binding of Hsp27 to its client protein tauRebecca Freilich, Miguel Betegon, Eric Tse, et al.Pageof 25