个人简介

B.S., 1999, University of Arizona Ph.D. 2004, University of California, Berkeley

研究领域

biological and organic

The overall theme of the lab is understanding the molecular consequences of posttranslational modifications (PTMs) including glycosylation and ubiquitination. These modifications expand the chemical diversity available to cells and living organisms. We specifically focus on the development of chemical tools as attractive methods for dissecting these biochemical pathways. Currently we are applying these chemical approaches to reveal roles for PTMs in cellular responses is processes associated with changes in metabolism and stress. Recent evidence suggests that these pathways are important contributors to a variety of human diseases including neurodegeneration and cancer. To accomplish our scientific goals, members of the lab use combinations of organic synthesis, genetics, protein biochemistry, and cellular biology.

近期论文

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The Extent of Inhibition of α-Synuclein Aggregation In Vitro by SUMOylation is Conjugation Site- and SUMO isoform-selective Abeywardana, T.; Pratt, M. R. Biochemistry (in press). Chemical Methods for the Proteome-Wide Identification of Posttranslationally Modified Proteins Chuh, K. N.; Pratt, M. R. Curr. Opin. Chem. Biol (2015) 24, 27-37. Chemoproteomics Reveals Toll-like Receptor Fatty Acylation Chesarino, N. M.; Hach, J. C.; Chen, J. L.; Zaro B. W.; Rajaram, M. V.; Turner, J; Schlesinger L. S.; Pratt, M. R.; Hang, H. C.; Yount J. S. BMC Biology (2014) 12, 91. Changes in Metabolic Chemical-Reporter Structure Yield a Selective Probe of O-GlcNAc Modification Chuh, K. N.;* Zaro, B. W.;* Piller, F.; Piller, V.; Pratt, M.R. J. Am. Chem. Soc. (2014) 136, 12283-12295. A Chemical Reporter for Visualizing Metabolic Cross-Talk between N-Acetyl-Glucosamine Metabolism and non-Carbohydrate Protein Modification Zaro B. W.; Chuh, K. N.; Pratt, M.R. ACS Chem. Biol. (2014) 9, 1991-1996. Using Chemistry to Investigate the Molecular Consequences of Protein Ubiquitination Abeywardana, T.; Pratt, M.R. ChemBioChem (2014) 15, 1547-1554. Identification of O-GlcNAc Modification Targets in Retinal Pericytes: Implications in the Pathogenesis of Diabetic Retinopathy Gurel, Z.;* Zaro, B. W.; Pratt, M.R.*; Sheibani, N. PLoS One (2014) 9, e95561. *co-corresponding authors A Dual Small-Molecule Rheostat for Precise Control of Protein Concentration in Mammalian Cells Lin, YH.; Pratt, M. R. ChemBioChem (2014) 15, 805-809. Molecular Probes for Protein Glycosylation Hang, H. C.; Pratt, M. R. Book Chapter in: Chemistry, Molecular Sciences and Chemical Engineering (2013) Elsevier Publishing. Site-Specific Differences in Proteasome-Dependent Degradation of Monoubiquitinated α-Synuclein Abeywardana, T.; Lin YH.; Rott R.; Engelender, S.; Pratt, M. R. Chem. Biol. (2013) 20, 1207-1213. An Alkyne-Aspirin Chemical Reporter for the Detection of Aspirin-Dependent Protein Modification in Living Cells Bateman, L. A.; Zaro, B. W.; Miller, S. M.; Pratt, M. R. J. Am. Chem. Soc. (2013) 135,14568-14573. N-Propargyloxycarbamate Monosaccharides as Metabolic Chemical Reporters of Carbohydrate Salvage Pathways and Protein Glycosylation Bateman, L. A.; Zaro, B. W.; Chuh, K. N.; Pratt M. R. ChemComm. (2013) 49, 4328-4330. *‘Emerging Investigators 2013’ themed issue Incorporation of Unnatural Sugars for the Identification of Glycoproteins Zaro, B. W.; Hang, H. C.; Pratt, M. R. Methods Mol. Biol. (2013) 951, 57-67. O-GlcNAc Modification Prevents Peptide-Dependent Acceleration of α-Synuclein Aggregation Marotta, N. P.; Cherwien, C. A.; Abeywardana T.; Pratt M. R. ChemBioChem (2012) 13, 2665-2670. Small-Molecule Reprogramming of Cancer Metabolism Pratt M. R. Chem. Biol. (2012) 19, 1084-1085. *Preview of Kung et al. Chem. Biol. 2012, 19, 1187-1198. Semi-Synthetic, Site-Specific Ubiquitin Modification of α-Synuclein Reveals Differential Effects on Aggregation. Meier, F.; Abeywardana, T.; Dhall, A.; Marotta, N. P.; Varkey, J.; Langen, R.; Chatterjee, C.; Pratt M. R. J. Am. Chem. Soc. (2012) 134, 5468-5471. Robust in-gel Fluorescence Detection of Mucin-type O-Linked Glycosylation. Zaro, B. W.; Bateman, L. A.; Pratt, M. R. Bioorg. Med. Chem. Lett. (2011), 21, 5062-5066. *Issue honoring Prof. Carolyn Bertozzi for 2011 Tetrahedron Young Investigator Award Chemical Reporters for Fluorescent Detection and Identification of O-GlcNAc Modified Proteins Reveal Glycosylation of the Ubiquitin Ligase NEDD4-1. Zaro, B. W.; Yang, Y. Y.; Hang, H. C.; Pratt, M. R. Proc. Natl. Acad. Sci. USA (2011) 108, 8146-8151. Precise Control of Protein Concentration in Living Cells. Lau, H.D., Yaegashi, J.; Zaro, B. W.; Pratt, M. R. Angew. Chem. Int. Ed. (2010) 49, 8458-8461.