William B. Pratt
Affiliations: | 1973-2006 | Pharmacology | University of Michigan, Ann Arbor, Ann Arbor, MI |
Area:
Pharmacology, BiochemistryWebsite:
https://www.lib.umich.edu/faculty-history/faculty/william-b-prattGoogle:
"William Pratt"Bio:
Pratt, William Brewster, The Y-glutamyl bond in chick embryo collagen
(1964). Yale Medicine Thesis Digital Library. 3042.
https://elischolar.library.yale.edu/ymtdl/3042
Mean distance: (not calculated yet)
Parents
Sign in to add mentor| Lewis Nelson Lukens | grad student | 1964 | Yale | |
| (M.D. thesis: The Y-glutamyl bond in chick embryo collagen.) | ||||
Children
Sign in to add trainee| Emery H. Bresnick | grad student | 1989 | University of Michigan |
| Kimon C. Kanelakis | grad student | 2002 | University of Michigan |
| Jennifer M. Harrell | grad student | 2004 | University of Michigan |
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Publications
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| Morishima Y, Lau M, Pratt WB, et al. (2022) Dynamic cycling with a unique Hsp90/Hsp70-dependent chaperone machinery and GAPDH is needed for heme insertion and activation of neuronal NO synthase. The Journal of Biological Chemistry. 102856 |
| Mehta RK, Pal S, Kondapi K, et al. (2020) Low dose Hsp90 inhibitor selectively radiosensitizes HNSCC and Pancreatic xenografts. Clinical Cancer Research : An Official Journal of the American Association For Cancer Research |
| Davis AK, Pratt WB, Lieberman AP, et al. (2019) Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases. Cellular and Molecular Life Sciences : Cmls |
| Morishima Y, Mehta RK, Yoshimura M, et al. (2018) Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery. Molecular Pharmacology |
| Elaimy AL, Ahsan A, Marsh K, et al. (2016) ATM is the primary kinase responsible for phosphorylation of Hsp90α after ionizing radiation. Oncotarget |
| Pratt WB, Gestwicki JE, Osawa Y, et al. (2015) Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases. Annual Review of Pharmacology and Toxicology. 55: 353-71 |
| Pratt WB, Morishima Y, Gestwicki JE, et al. (2014) A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseases. Experimental Biology and Medicine (Maywood, N.J.). 239: 1405-13 |
| Ahsan A, Ramanand SG, Bergin IL, et al. (2014) Efficacy of an EGFR-specific peptide against EGFR-dependent cancer cell lines and tumor xenografts. Neoplasia (New York, N.Y.). 16: 105-14 |
| Ahsan A, Ray D, Ramanand SG, et al. (2013) Destabilization of the epidermal growth factor receptor (EGFR) by a peptide that inhibits EGFR binding to heat shock protein 90 and receptor dimerization. The Journal of Biological Chemistry. 288: 26879-86 |
| Wang AM, Miyata Y, Klinedinst S, et al. (2013) Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation. Nature Chemical Biology. 9: 112-8 |