Jason E. Gestwicki, Ph.D.
Affiliations: | 2002 | University of Wisconsin, Madison, Madison, WI |
Area:
Biomolecular recognitionGoogle:
"Jason Gestwicki"Mean distance: 7.84 | S | N | B | C | P |
Parents
Sign in to add mentor| Laura Lee Kiessling | grad student | 2002 | UW Madison | |
| (Synthetic multivalent ligands with diverse architectures in the exploration of receptor function: Studies on concanavalin A, the bacterial chemoreceptors, the selectins, and the B cell receptor.) | ||||
Children
Sign in to add trainee| Jennifer N Rauch | grad student | (Neurotree) | |
| Anne T. Gillies | grad student | 2009-2014 | University of Michigan (Chemistry Tree) |
| Kwadwo A. Opoku-Nsiah | grad student | 2013-2020 | UCSF (Neurotree) |
BETA: Related publications
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Publications
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| Zhang JZ, Greenwood N, Hernandez J, et al. (2023) designed Hsp70 activator dissolves intracellular condensates. Biorxiv : the Preprint Server For Biology |
| Elsasser S, Elia LP, Morimoto RI, et al. (2023) A Comprehensive Enumeration of the Human Proteostasis Network. 2. Components of the Autophagy-Lysosome Pathway. Biorxiv : the Preprint Server For Biology |
| Shao H, Taguwa S, Gilbert L, et al. (2022) A campaign targeting a conserved Hsp70 binding site uncovers how subcellular localization is linked to distinct biological activities. Cell Chemical Biology |
| Johnson OT, Gestwicki JE. (2022) Multivalent protein-protein interactions are pivotal regulators of eukaryotic Hsp70 complexes. Cell Stress & Chaperones |
| Carrettiero DC, Almeida MC, Longhini AP, et al. (2022) Stress routes clients to the proteasome via a BAG2 ubiquitin-independent degradation condensate. Nature Communications. 13: 3074 |
| Opoku-Nsiah KA, de la Pena AH, Williams SK, et al. (2022) The YΦ motif defines the structure-activity relationships of human 20S proteasome activators. Nature Communications. 13: 1226 |
| Johnson OT, Nadel CM, Carroll EC, et al. (2022) Two distinct classes of co-chaperones compete for the EEVD motif in heat shock protein 70 (Hsp70) to tune its chaperone activities. The Journal of Biological Chemistry. 101697 |
| Arhar T, Shkedi A, Nadel CM, et al. (2021) The interactions of molecular chaperones with client proteins: why are they so weak? The Journal of Biological Chemistry. 297: 101282 |
| Lee K, Thwin AC, Nadel CM, et al. (2021) The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state. Molecular Cell |
| Shao H, Li X, Hayashi S, et al. (2021) Inhibitors of heat shock protein 70 (Hsp70) with enhanced metabolic stability reduce tau levels. Bioorganic & Medicinal Chemistry Letters. 41: 128025 |