Mechanism of Drug Action, Proteomics and Protein Modification
Guoqiang Xu
B.S. & M.S. Fudan University, Shanghai, China 1996 & 1999
Ph.D. The University of Akron, Akron, OH, USA 2002

The research in Dr. Xu’s laboratory is mainly focusing on the development of new mass spectrometry-based proteomic approaches to study protein post-translationally modified by ubiquitin and ubiquitin-like modifiers; to study protease processing in cell signaling pathways; to study the biological functions of these modifications in disease development and treatment.
SELECTED Peer-reviewed publication (* Corresponding Author)
1.Xu, G.*; Jiang, X.; Jaffrey, S. R.* A mental retardation-linked nonsense mutation in cereblon is rescued by proteasome inhibition. J. Biol. Chem. 2013, 288, 29573-29585.
2.Yoon, Y.; McKenna, M. C.; Rollins, D. A.; Song, M.; Nuriel, T.; Gross, S. S.; Xu, G.; Glatt, C. E. Anxiety-associated alternative polyadenylation of the serotonin transporter mRNA confers translational regulation by hnRNPK. Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 11624-11629.
3.Xu, G.*; Jaffrey, S. R.* Proteomic identification of protein ubiquitination events. Biotech. Genet. Eng. Rev. 2013, 29, 73-109.
4.Xu, G.*; Jaffrey, S. R. Comprehensive profiling of protein ubiquitination for drug discovery. Curr. Pharm. Des. 2013, 19, 3315-3328.
5.Li H., Wan A., Xu G., Ye D. Small changes huge impact: the role of thioredoxin 1 in the regulation of apoptosis by S-nitrosylation. Acta Biochim. Biophys. Sin. 2013, 45, 153-161.
6.Xu, G.; Jaffrey, S. R. The new landscape of protein ubiquitination. Nat. Biotechnol. (News & Views) 2011, 29, 1098-1100.
7.Xu, G.; Shin, S. Y.; Jaffrey, S. R. Chemoenzymatic labeling of protein C-termini for positive selection of C-terminal peptides. ACS Chem. Biol. 2011, 6, 1015-1020.
8.Xu, G.; Jaffrey, S. R. N-CLAP: global profiling of N-termini by chemoselective labeling of the  amine of proteins. Cold Spring Harb. Protoc. 2010, 11, pdb.prot5528.
9.Xu, G.; Paige, J. S.; Jaffrey, S. R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 2010, 28, 868-873.
10.Xu, G.; Shin, S. Y.; Jaffrey, S. R. Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 19310-19315.
11.Gahl, R. F.; Pradeep, L.; Siegel, C. R.; Xu, G.; Scheraga, H. A. Effects of tyrosine mutations on the conformational and oxidative folding of ribonuclease A: a comparative study. Biochemistry 2009, 48, 3887-3893.
12.Paige, J. S.; Xu, G.; Stancevic, B.; Jaffrey, S. R. Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability. Chem. Biol. 2008, 15, 1307-1316.
13.Narayan, M.; Welker, E.; Zhai, H.; Han, X.; Xu, G.; McLafferty, F. W.; Scheraga, H. A. Detecting native folds in mixtures of proteins that contain disulfide bonds. Nat. Biotechnol. 2008, 26, 427-429.
14.Gahl, R. F.; Narayan, M.; Xu, G.; Scheraga, H. A. Dissimilarity in the oxidative folding of onconase and ribonuclease A, two structural homologues. Protein Eng. Des. Sel. 2008, 21, 223-231.
15.Welker, E.; Hathaway, L.; Xu, G.; Narayan, M.; Pradeep, L.; Shin, H. C.; Scheraga, H. A. Oxidative folding and N-terminal cyclization of onconase. Biochemistry 2007, 46, 5485-5493.
16.Xu, G.; Narayan, M.; Kurinov, I.; Ripoll, D. R.; Welker, E.; Khalili, M.; Ealick, S. E.; Scheraga, H. A. A localized specific interaction alters the unfolding pathways of structural homologues. J. Am. Chem. Soc. 2006, 128, 1204-1213.
17.Leung, H. J.; Xu, G.; Narayan, M.; Scheraga, H. A. Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins. J. Pep. Res., 2005, 65, 47-54.
18.Xu, G.; Narayan, M.; Scheraga, H. A. The oxidative folding rate of bovine pancreatic ribonuclease is enhanced by a covalently attached oligosaccharide. Biochemistry 2005, 44, 9817-9823.
19.Xu, G.; Zhai, H.; Narayan, M.; McLafferty, F. W.; Scheraga, H. A. Simultaneous characterization of the reductive unfolding pathways of RNase B isoforms by top-down mass spectrometry. Chem. Biol. 2004, 11, 517-524.
20.Xu, G.; Narayan, M.; Welker, E.; Scheraga, H. A. Characterization of the fast-forming intermediate, des [30-75], in the reductive unfolding of onconase. Biochemistry 2004, 43, 3246-3254.
21.Narayan, M.; Xu, G.; Ripoll, D.; Zhai, H.; Breuker, K.; Wanjalla, C.; Leung, H. J.; Navon, A.; Welker, E.; McLafferty, F. W.; Scheraga, H. A. Disimilarity in the reductive unfolding of two ribonuclease homologues. J. Mol. Biol. 2004, 338, 795-809.
22.Gahl, R. F.; Narayan, M.; Xu, G.; Scheraga, H. A. Trimethylamine-N-oxide modulates the reductive unfolding of onconase. Biochem. Biophys. Res. Commun. 2004, 325, 707-710.
23.Narayan, M.; Xu, G.; Schultz, S. K.; Scheraga, H. A. Assessing the magnitude of folding forces along the oxidative folding pathway of multi-disulfide-containing proteins. J. Am. Chem. Soc. 2003, 125, 16184-16185.
24.Xu, G.; Narayan, M.; Welker, E.; Scheraga, H. A. A novel method to determine thermal transition curves of disulfide-containing proteins and their structured folding intermediates. Biochem. Biophys. Res. Commun. 2003, 311, 514-517.
25.Narayan, M.; Welker, E.; Wanjalla, C.; Xu, G.; Scheraga, H. A. Shifting the competition between the intramolecular reshuffling reaction and the direct oxidation reaction during the oxidative folding of kinetically trapped disulfide-insecure intermediates. Biochemistry 2003, 42, 10783-10789.
Xu, G.
; Deglincerti, A.; Paige, J. S.; Lundquist, M. R.; Jaffrey, S. R. Profiling lysine ubiquitination by selective enrichment of ubiquitin remnant-containing peptides. Meth. Mol. Biol. 2014, 1174, 57-71.
Xu, G.; Jaffrey, S. R. Antibodies for ubiquitinated proteins. U.S. Patent, Application #: 12/455,496, June 2, 2009.
1.Profiling of protein ubiquitination and its potential application in drug discovery, International Symposium on “Futures in Drug Research and Development in Pharmaceutical Sciences”, Yeungnam University, Gyeongsan, Korea, Jan 17, 2014.
2.The function of cereblon ubiquitination in human disease, International Symposium Current Trends and Future Prospects in Pharmaceutical Sciences, Pokhara, Kaski, Nepal, July 6-7, 2014.
1.Molecular mechanism of lenalidomide in the treatment of multiple myeloma. National Natural Science Foundation of China (2013-2016).
2.National Basic Research Program of China (973 Program) (2013-2016)
·Double Innovative Program of Jiangsu Province (2013)
·One Thousand Youth Talents Program (2012)
·Jinji Lake Double Hundred Talents Program (Suzhou Industrial Park, 2012)
·Omnova Signature Award (The University of Akron, 2002)
·Ticona Award (The University of Akron, 2001)

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