Donald F. Hunt


Primary Appointment

Lecturer in Chemistry, Chemistry


  • BS, Chemistry, University of Massachusetts, Amherst, MA
  • PhD, Organic Chemistry, University of Massachusetts, Amherst, MA
  • Postdoc, Mass Spectrometry, MIT, Cambridge, MA (Klaus Biemann)

Research Disciplines

Biophysics, Biotechnology

Research Interests

Analytical Biochemistry

Research Description

Two areas:
(A) Mass spectrometry applied to immunology:
Cells in the human body communicate their health status to the immune system by degrading cellular proteins and presenting fragments of each on the cell surface in association class I MHC proteins. Appropriately educated, cytotoxic T-lymphocytes (CTL) (CD8+ T-cells) bind to the class I MHC molecules on the cell surface, sample the protein fragments (peptides) being presented and kill those cells that express new peptides as a result of viral, bacterial and parasitic infection, tissue transplantation and cellular transformation (cancer). Since dysregulation of cell signaling pathways is one of the hallmarks of cancer, we hypothesized that class I MHC phosphopeptides that result from these pathways should be excellent candidates for use in the immunotherapy of cancer. Class I MHC phosphopeptides identified in preliminary work on leukemia, melanoma, and colorectal cancers elicit pre-existing, central-memory, T-cell-recall responses in multiple, healthy blood donors. Central memory recall responses to phosphopeptide antigens is absent in some leukemia patients and correlates with clinical outcome. The response is restored following allogenic stem cell transplantation. These results suggest strongly that class I MHC phosphopeptides are tumor targets of immune surveillance in humans and, therefore, are likely candidates for immunotherapy of cancer. Three of the discovered phosphopeptides will be the subject of a phase I clinical trial on melanoma later this spring. Proposed here is additional research to complete our studies on melanoma, leukemia, and colorectal cancer and to begin an effort to characterize class I MHC phosphopetides presented on esophageal, liver and ovarian cancer. Additional research will be conducted to identify the repertoire of altered class I or class II self-peptides that are induced by prescription drugs or environmental agents and lead to life threatening autoimmune disease.
B) Mass spectrometry applied characterization of protein post-translational modifications and antibody sequences.
Proposed here is research to develop a combination of mass spectrometry instrumentation and techniques plus chemical and biochemical methods that will facilitate identification and near complete amino acid sequence analysis of intact proteins or large protein fragments on a chromatographic time scale. This research will make it possible to characterize multiple post-translational modifications, particularly those that exist on the same protein molecule and together regulate its biological activity. This research is driven by five major innovations in my lab: development of (a) electron transfer dissociation (ETD) for fragmentation of intact proteins, (b) ETD and IIPT (ion-ion proton transfer) chemistry to obtain n- and c-terminal sequence information from intact proteins, (c) front end ETD (FETD) that facilitates a 10-50 fold increase in sensitivity for intact proteins, (d) micro-column enzyme reactors that generate 3-10 KDa proteins fragments and provide 96% sequence coverage for monoclonal antibodies and (e) methodology for enrichment of O-GlcNAcylated peptides by boronic acid chemistry in non-aqueous solvents. Going forward, we will implement new IIPT reagents to extend the usable mass range to m/z 4,000, employ a combination of IIPT and parallel ion parking strategies to concentrate multiple charge states observed in protein ESI into a single lower charge state for protein identification by CAD, develop parallel ion parking strategies to minimize second generation ETD reactions and thus allow us to read complete protein sequences from both the n- and c- termini of intact proteins, build a longer linear ion trap to increase the number of protein ions that can be stored for analysis, extend the micro-column enzyme reactor concept to other proteases and solvents and then apply all of this development to the analysis of proteins in outer membrane vesicles secreted by the antibiotic resistant, gram negative bacteria, Neisseria gonorrhoeae. The ultimate goal is to be able to identify bacterial, virulence-factor proteins on a chromatographic time scale. The above technology will also be employed to characterize (a) proteolytic cleavage events on histones that alter the epigenetic code, (b) O-GlcNAc sites on ribosomal proteins, mitochondrial proteins in the heart, and all known human kinases, and (c) protein binding partners for RSK1 (ribosomal protein S6 Kinase) that plays a major role in breast cancer.

Personal Statement

Professor Hunt pioneered efforts to develop methods and instrumentation that set the standard for ultrasensitive detection and characterization of proteins and peptides. These contributions continue to underpin the whole field of proteomics and have had a dramatic impact on research in immunology, cell signaling, cell migration, chromatin biology and cancer. Hunt was the first to use tandem mass spectrometry to characterize peptides presented to the immune system by the class I MHC molecules. This was described in a 1992 Science paper that has recently been re-published as a âPillars of Immunology Articleâ (J of Immunology) along with commentary by Lawrence Stern. Additional studies on class I and class II peptides have appeared in seven Science papers published between 1992 and 1998 and 67 additional papers. Peptides recognized by cytotoxic T-lymphocytes specific for tumors, graft vs host disease, viral and bacterial epitopes, and type 1 diabetes have all been discovered by the Hunt group. Recent work indicates that class I MHC phosphopeptides differentially expressed on cancer cells are likely candidates for immunotherapy of breast cancer, melanoma, ovarian cancer, colorectal cancer and a variety of leukemias.
Professor Hunt has also been a pioneer in characterizing protein post-translational modifications. In 1991, he identified the regulatory phosphorylation sites on MAP kinase. In 1988, he pioneered the use of immobilized metal affinity chromatography to enrich samples for phosphopeptides and reported methodology for the global characterization of phosphopeptides in a yeast cell lysate in 2002. This approach is now the basis for large scale efforts to monitor cell signaling pathways in a variety of biological systems. Professor Hunt also developed instrumentation and chemical derivatization methods that made it possible to elucidate the âhistone codeâ and to characterize the combinatorial nature of histone post-translational modifications on a genome wide scale. Since 2000, his group has published 46 papers on this topic.
Perhaps the most significant of Professor Huntâs recent achievements is the development of instrumentation that makes it possible to use ion-ion chemistry inside the mass spectrometer to determine the sequence of amino acids at both the n-terminus and c-terminus of intact proteins. This technique, electron transfer dissociation (ETD), facilitates identification of proteins in complex mixtures on a chromatographic time-scale (500 msec/protein), and allows one to detect the presence of both splice variants and post-translational modifications. This technology is likely to revolutionize the whole field of proteomics. ETD is also a breakthrough technology for the identification of O-GlcNAcylated peptides. This posttranslational modification on Ser and Thr residues rivals phosphorylation in abundance and constitutes a whole new field of signal transduction. Professor Hunt has now trained more than 120 graduate students and postdoctoral fellows. Many hold academic positions. The list includes: John Yates (Scripps), Andrea Cox (Johns Hopkins), Jarrod Marto (Harvard), Forest White (MIT), Murray Hackett (U. of Washington), Josh Coon (University of Wisconsin), Pat Griffin (Scripps), Nathan Yates, U of Pittsburgh, Beatrix Ueberheide NYU, and Ben Garcia (U. of Pennsylvania Medical School). Professor Hunt is an inventor on more than 30 patents and patent applications and has over 390 scholarly publications to his credit. His Goggle Scholar h-index of 100, (100 papers with 100 or more citations, total citations = 37,000, i10-index = 320) ranks him among the top 130 living chemists in the world. An RG score of 48.82 on ResearchGate places him in the top 97.5% of all members in this scientific community.


  • Training in Molecular Biophysics

Selected Publications


Mahoney, K. E., Shabanowitz, J., & Hunt, D. F. (2021). MHC Phosphopeptides: Promising Targets for Immunotherapy of Cancer and Other Chronic Diseases. MOLECULAR & CELLULAR PROTEOMICS, 20. doi:10.1016/j.mcpro.2021.100112


Cheema, M. S., Good, K. V., Kim, B., Soufari, H., O'Sullivan, C., Freeman, M. E., . . . Ausio, J. (2020). Deciphering the Enigma of the Histone H2A.Z-1/H2A.Z-2 Isoforms: Novel Insights and Remaining Questions. CELLS, 9(5). doi:10.3390/cells9051167

Engelhard, V. H., Obeng, R. C., Cummings, K. L., Petroni, G. R., Ambakhutwala, A. L., Chianese-Bullock, K. A., . . . Slingluff, C. L. J. (2020). MHC-restricted phosphopeptide antigens: preclinical validation and first-in-humans clinical trial in participants with high-risk melanoma. JOURNAL FOR IMMUNOTHERAPY OF CANCER, 8(1). doi:10.1136/jitc-2019-000262


Dinesh, R. K., Barnhill, B., Ilanges, A., Wu, L., Michelson, D. A., Senigl, F., . . . Schatz, D. G. (2020). Transcription factor binding at Ig enhancers is linked to somatic hypermutation targeting. EUROPEAN JOURNAL OF IMMUNOLOGY, 50(3), 380-395. doi:10.1002/eji.201948357

Heather, J. M., Myers, P. T., Shi, F., Aziz-Zanjani, M. O., Mahoney, K. E., Perez, M., . . . Cobbold, M. (2019). Murine xenograft bioreactors for human immunopeptidome discovery. SCIENTIFIC REPORTS, 9. doi:10.1038/s41598-019-54700-2

Hinkle, J. D., D'Ippolito, R. A., Panepinto, M. C., Wang, W. -H., Bai, D. L., Shabanowitz, J., & Hunt, D. F. (2019). Unambiguous Sequence Characterization of a Monoclonal Antibody in a Single Analysis Using a Nonspecific Immobilized Enzyme Reactor. ANALYTICAL CHEMISTRY, 91(21), 13547-13554. doi:10.1021/acs.analchem.9b02666

Ugrin, S. A., English, A. M., Syka, J. E. P., Bai, D. L., Anderson, L. C., Shabanowitz, J., & Hunt, D. F. (2019). Ion-Ion Proton Transfer and Parallel Ion Parking for the Analysis of Mixtures of Intact Proteins on a Modified Orbitrap Mass Analyzer.. Journal of the American Society for Mass Spectrometry, 30(10), 2163-2173. doi:10.1007/s13361-019-02290-8

D'Ippolito, R. A., Minamino, N., Rivera-Casas, C., Cheema, M. S., Bai, D. L., Kasinsky, H. E., . . . Ausio, J. (2019). Protamines from liverwort are produced by post-translational cleavage and C-terminal di-aminopropanelation of several male germ-specific H1 histones. JOURNAL OF BIOLOGICAL CHEMISTRY, 294(44), 16364-16373. doi:10.1074/jbc.RA119.010316

Ugrin, S. A., English, A. M., Syka, J. E. P., Bai, D. L., Anderson, L. C., Shabanowitz, J., & Hunt, D. F. (2019). Ion-Ion Proton Transfer and Parallel Ion Parking for the Analysis of Mixtures of Intact Proteins on a Modified Orbitrap Mass Analyzer. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 30(10), 2163-2173. doi:10.1007/s13361-019-02290-8

Ma, J., Wang, W. -H., Li, Z., Shabanowitz, J., Hunt, D. F., & Hart, G. W. (2019). O-GlcNAc Site Mapping by Using a Combination of Chemoenzymatic Labeling, Copper-Free Click Chemistry, Reductive Cleavage, and Electron-Transfer Dissociation Mass Spectrometry. ANALYTICAL CHEMISTRY, 91(4), 2620-2625. doi:10.1021/acs.analchem.8b05688


Simon, D. N., Wriston, A., Fan, Q., Shabanowitz, J., Florwick, A., Dharmaraj, T., . . . Wilson, K. L. (2018). OGT (O-GlcNAc Transferase) Selectively Modifies Multiple Residues Unique to Lamin A. CELLS, 7(5). doi:10.3390/cells7050044

Martinez-Turino, S., De Jesus Perez, J., Hervas, M., Navajas, R., Ciordia, S., Udeshi, N. D., . . . Antonio Garcia, J. (2018). Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and influences viral infection. MOLECULAR PLANT PATHOLOGY, 19(6), 1427-1443. doi:10.1111/mpp.12626

Grützmann, K., Krimmer, M., Thimme, R., Trantham, P., Penny, S., Curbishley, S., . . . Büttner, N. (2018). The role of phosphopeptide neoantigens in cancer immunotherapy. Zeitschrift für Gastroenterologie, 56(01), E2-E89. doi:10.1055/s-0037-1612842


Pavlos, R., McKinnon, E. J., Ostrov, D. A., Peters, B., Buus, S., Koelle, D., . . . Phillips, E. J. (2017). Shared peptide binding of HLA Class I and II alleles associate with cutaneous nevirapine hypersensitivity and identify novel risk alleles. SCIENTIFIC REPORTS, 7. doi:10.1038/s41598-017-08876-0

Mohammed, F., Stones, D. H., Zarling, A. L., Willcox, C. R., Shabanowitz, J., Cummings, K. L., . . . Willcox, B. E. (2017). The antigenic identity of human class I MHC phosphopeptides is critically dependent upon phosphorylation status.. Oncotarget, 8(33), 54160-54172. doi:10.18632/oncotarget.16952

Weisbrod, C. R., Kaiser, N. K., Syka, J. E. P., Early, L., Mullen, C., Dunyach, J. -J., . . . Hunt, D. F. (2017). Front-End Electron Transfer Dissociation Coupled to a 21 Tesla FT-ICR Mass Spectrometer for Intact Protein Sequence Analysis. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 28(9), 1787-1795. doi:10.1007/s13361-017-1702-3

Mohammed, F., Stones, D. H., Zarling, A. L., Willcox, C. R., Shabanowitz, J., Cummings, K. L., . . . Willcox, B. E. (2017). The antigenic identity of human class I MHC phosphopeptides is critically dependent upon phosphorylation status. ONCOTARGET, 8(33), 54160-54172. doi:10.18632/oncotarget.16952

Bergmann, T., Lindvall, M., Moore, E., Moore, E., Sidney, J., Miller, D., . . . Sette, A. (2017). Peptide-binding motifs of two common equine class I MHC molecules in Thoroughbred horses. IMMUNOGENETICS, 69(5), 351-358. doi:10.1007/s00251-017-0978-6

Malaker, S. A., Penny, S. A., Steadman, L. G., Myers, P. T., Loke, J. C., Raghavan, M., . . . Cobbold, M. (2017). Identification of Glycopeptides as Posttranslationally Modified Neoantigens in Leukemia. CANCER IMMUNOLOGY RESEARCH, 5(5), 376-384. doi:10.1158/2326-6066.CIR-16-0280

Zentella, R., Sui, N., Barnhill, B., Hsieh, W. -P., Hu, J., Shabanowitz, J., . . . Sun, T. -P. (2017). The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA. NATURE CHEMICAL BIOLOGY, 13(5), 479-+. doi:10.1038/NCHEMBIO.2320

Sim, M. J. W., Malaker, S. A., Khan, A., Stowell, J. M., Shabanowitz, J., Peterson, M. E., . . . Boyton, R. J. (2017). Canonic and Cross-reacrtive Binding of NK cell Inhibitory Recweptors to HLA-C Allotypes Is Dication by Peptides Bound to HLA-C. FRONTIERS IN IMMUNOLOGY, 8. doi:10.3389/fimmu.2017.00193


Stankovic, A., Guo, L. Y., Mata, J. F., Bodor, D. L., Cao, X. -J., Bailey, A. O., . . . Jansen, L. E. T. (2017). A Dual Inhibitory Mechanism Sufficient to Maintain Cell-Cycle-Restricted CENP-A Assembly. MOLECULAR CELL, 65(2), 231-246. doi:10.1016/j.molcel.2016.11.021

Malaker, S. A., Ferracane, M. J., Depontieu, F. R., Zarling, A. L., Shabanowitz, J., Bai, D. L., . . . Hunt, D. F. (2017). Identification and Characterization of Complex Glycosylated Peptides Presented by the MHC Class II Processing Pathway in Melanoma. JOURNAL OF PROTEOME RESEARCH, 16(1), 228-237. doi:10.1021/acs.jproteome.6b00496

Penny, S., Abelin, J., Saeed, A., Malaker, S., Trantham, P., Shabanowitz, J., . . . Cobbold, M. (2016). Phosphopeptides as novel tumour antigens in colorectal cancer. European Journal of Cancer, 61, S213. doi:10.1016/s0959-8049(16)61751-3

Penny, S., Malaker, S., Steadman, L., Trantham, P., Bai, D., Shabanowitz, J., . . . Cobbold, M. (2016). Glycosylated and methylated peptides as neoantigens in leukaemia. European Journal of Cancer, 61, S217. doi:10.1016/s0959-8049(16)61765-3

Anderson, L. C., Karch, K. R., Ugrin, S. A., Coradin, M., English, A. M., Sidoli, S., . . . Hunt, D. F. (2016). Analyses of Histone Proteoforms Using Front-end Electron Transfer Dissociation-enabled Orbitrap Instruments. MOLECULAR & CELLULAR PROTEOMICS, 15(3), 975-988. doi:10.1074/mcp.O115.053843

Zentella, R., Hu, J., Hsieh, W. -P., Matsumoto, P. A., Dawdy, A., Barnhill, B., . . . Sun, T. -P. (2016). O-GlcNAcylation of master growth repressor DELLA by SECRET AGENT modulates multiple signaling pathways in Arabidopsis.. Genes & development, 30(2), 164-176. doi:10.1101/gad.270587.115

Sidney, J., Schloss, J., Moore, C., Lindvall, M., Wriston, A., Hunt, D. F., . . . Sette, A. (2016). Characterization of the peptide binding specificity of the HLA class I alleles B*38:01 and B*39:06. IMMUNOGENETICS, 68(3), 231-236. doi:10.1007/s00251-015-0898-2

Zentella, R., Hu, J., Hsieh, W. -P., Matsumoto, P. A., Dawdy, A., Barnhill, B., . . . Sun, T. -P. (2016). O-GlcNAcylation of master growth repressor DELLA by SECRET AGENT modulates multiple signaling pathways in Arabidopsis. GENES & DEVELOPMENT, 30(2), 164-176. doi:10.1101/gad.270587.115


Bailey, A. O., Panchenko, T., Shabanowitz, J., Lehman, S. M., Bai, D. L., Hunt, D. F., . . . Foltz, D. R. (2016). Identification of the Post-translational Modifications Present in Centromeric Chromatin. MOLECULAR & CELLULAR PROTEOMICS, 15(3), 918-931. doi:10.1074/mcp.M115.053710

Zhang, L., English, A. M., Bai, D. L., Ugrin, S. A., Shabanowitz, J., Ross, M. M., . . . Wang, W. -H. (2016). Analysis of Monoclonal Antibody Sequence and Post-translational Modifications by Time-controlled Proteolysis and Tandem Mass Spectrometry. MOLECULAR & CELLULAR PROTEOMICS, 15(4), 1479-1488. doi:10.1074/mcp.O115.056721

Pang, Y., Wang, W. -H., Reid, G. E., Hunt, D. F., & Bruening, M. L. (2015). Pepsin-Containing Membranes for Controlled Monoclonal Antibody Digestion Prior to Mass Spectrometry Analysis. ANALYTICAL CHEMISTRY, 87(21), 10942-10949. doi:10.1021/acs.analchem.5b02739

Bhattacharjee, S., Liu, W., Wang, W. -H., Weitzhandler, I., Li, X., Qi, Y., . . . Chilkoti, A. (2015). Site-Specific Zwitterionic Polymer Conjugates of a Protein Have Long Plasma Circulation. CHEMBIOCHEM, 16(17), 2451-2455. doi:10.1002/cbic.201500439

Bergmann, T., Moore, C., Sidney, J., Miller, D., Tallmadge, R., Harman, R. M., . . . Sette, A. (2015). The common equine class I molecule Eqca-1*00101 (ELA-A3.1) is characterized by narrow peptide binding and T cell epitope repertoires. IMMUNOGENETICS, 67(11-12), 675-689. doi:10.1007/s00251-015-0872-z

Abelin, J. G., Trantham, P. D., Penny, S. A., Patterson, A. M., Ward, S. T., Hildebrand, W. H., . . . Hunt, D. F. (2015). Complementary IMAC enrichment methods for HLA-associated phosphopeptide identification by mass spectrometry. NATURE PROTOCOLS, 10(9), 1308-1318. doi:10.1038/nprot.2015.086

Juanes-Garcia, A., Chapman, J. R., Aguilar-Cuenca, R., Delgado-Arevalo, C., Hodges, J., Whitmore, L. A., . . . Vicente-Manzanares, M. (2015). A regulatory motif in nonmuscle myosin II-B regulates its role in migratory front-back polarity. JOURNAL OF CELL BIOLOGY, 209(1), 23-32. doi:10.1083/jcb.201407059

Hunt, D. F., Shabanowitz, J., & Bai, D. L. (2015). Peptide Sequence Analysis by Electron Transfer Dissociation Mass Spectrometry: A Web-Based Tutorial. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 26(7), 1256-1258. doi:10.1007/s13361-015-1105-2

Onikubo, T., Nicklay, J. J., Xing, L., Warren, C., Anson, B., Wang, W. -L., . . . Shechter, D. (2015). Developmentally Regulated Post-translational Modification of Nucleoplasmin Controls Histone Sequestration and Deposition. CELL REPORTS, 10(10), 1735-1748. doi:10.1016/j.celrep.2015.02.038

Albrecht, L. V., Zhang, L., Shabanowitz, J., Purevjav, E., Towbin, J. A., Hunt, D. F., & Green, K. J. (2015). GSK3-and PRMT-1-dependent modifications of desmoplakin control desmoplakin-cytoskeleton dynamics. JOURNAL OF CELL BIOLOGY, 208(5), 597-612. doi:10.1083/jcb.201406020

Anderson, L. C., English, A. M., Wang, W. -H., Bai, D. L., Shabanowitz, J., & Hunt, D. F. (2015). Protein derivatization and sequential ion/ion reactions to enhance sequence coverage produced by electron transfer dissociation mass spectrometry. INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 377, 617-624. doi:10.1016/j.ijms.2014.06.023

Metushi, I. G., Wriston, A., Banerjee, P., Gohlke, B. O., English, M., Lucas, A., . . . Peters, B. (2015). Acyclovir Has Low but Detectable Influence on HLA-B*57:01 Specificity without Inducing Hypersensitivity. PLOS ONE, 10(5). doi:10.1371/journal.pone.0124878


Papazyan, R., Voronina, E., Chapman, J. R., Luperchio, T. R., Gilbert, T. M., Meier, E., . . . Taverna, S. D. (2014). Methylation of histone H3K23 blocks DNA damage in pericentric heterochromatin during meiosis. ELIFE, 3. doi:10.7554/eLife.02996

Bullen, J. W., Balsbaugh, J. L., Chanda, D., Shabanowitz, J., Hunt, D. F., Neumann, D., & Hart, G. W. (2014). Cross-talk between Two Essential Nutrient-sensitive Enzymes O-GlcNAc TRANSFERASE ( OGT) AND AMP-ACTIVATED PROTEIN KINASE ( AMPK). JOURNAL OF BIOLOGICAL CHEMISTRY, 289(15), 10592-10606. doi:10.1074/jbc.M113.523068

Wang, W. -L., Anderson, L. C., Nicklay, J. J., Chen, H., Gamble, M. J., Shabanowitz, J., . . . Shechter, D. (2014). Phosphorylation and arginine methylation mark histone H2A prior to deposition during Xenopus laevis development. EPIGENETICS & CHROMATIN, 7. doi:10.1186/1756-8935-7-22


Wu, H. -A., Balsbaugh, J. L., Chandler, H., Georgilis, A., Zullow, H., Shabanowitz, J., . . . Bernstein, E. (2013). Mitogen-activated Protein Kinase Signaling Mediates Phosphorylation of Polycomb Ortholog Cbx7. JOURNAL OF BIOLOGICAL CHEMISTRY, 288(51), 36398-36408. doi:10.1074/jbc.M113.486266

Chen, S., Li, Y., Depontieu, F. R., McMiller, T. L., English, A. M., Shabanowitz, J., . . . Topalian, S. L. (2013). Structure-Based Design of Altered MHC Class II-Restricted Peptide Ligands with Heterogeneous Immunogenicity. JOURNAL OF IMMUNOLOGY, 191(10), 5097-5106. doi:10.4049/jimmunol.1300467

Cobbold, M., De La Pena, H., Norris, A., Polefrone, J. M., Qian, J., English, A. M., . . . Engelhard, V. H. (2013). MHC Class I-Associated Phosphopeptides Are the Targets of Memory-like Immunity in Leukemia. SCIENCE TRANSLATIONAL MEDICINE, 5(203). doi:10.1126/scitranslmed.3006061

Berk, J. M., Maitra, S., Dawdy, A. W., Shabanowitz, J., Hunt, D. F., & Wilson, K. L. (2013). O-Linked β-N-Acetylglucosamine (O-GlcNAc) Regulates Emerin Binding to Barrier to Autointegration Factor (BAF) in a Chromatin- and Lamin B-enriched "Niche". JOURNAL OF BIOLOGICAL CHEMISTRY, 288(42), 30192-30209. doi:10.1074/jbc.M113.503060

Earley, L., Anderson, L. C., Bai, D. L., Mullen, C., Syka, J. E. P., English, A. M., . . . Compton, P. D. (2013). Front-End Electron Transfer Dissociation: A New Ionization Source. ANALYTICAL CHEMISTRY, 85(17), 8385-8390. doi:10.1021/ac401783f

Bailey, A. O., Panchenko, T., Sathyan, K. M., Petkowski, J. J., Pai, P. -J., Bai, D. L., . . . Foltz, D. R. (2013). Posttranslational modification of CENP-A influences the conformation of centromeric chromatin. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 110(29), 11827-11832. doi:10.1073/pnas.1300325110

de Jesus Perez, J., Udeshi, N. D., Shabanowitz, J., Ciordia, S., Juarez, S., Scott, C. L., . . . Antonio Garcia, J. (2013). O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection. VIROLOGY, 442(2), 122-131. doi:10.1016/j.virol.2013.03.029

Abreu, C. M., Kumar, R., Hamilton, D., Dawdy, A. W., Creavin, K., Eivers, S., . . . Lowndes, N. F. (2013). Site-Specific Phosphorylation of the DNA Damage Response Mediator Rad9 by Cyclin-Dependent Kinases Regulates Activation of Checkpoint Kinase 1. PLOS GENETICS, 9(4). doi:10.1371/journal.pgen.1003310

Onikubo, T., Nicklav, J. J., Wang, W. -L., Shabanowitz, J., Hunt, D. F., & Shechter, D. (2013). Developmental regulation of nucleoplasmin function by phosphorylation, glutamylation, and methylation. Epigenetics & Chromatin, 6(S1). doi:10.1186/1756-8935-6-s1-p61

Papazvan, R., Voronina, E., Chapman, J. R., Gilbert, T. M., Meier, E., Shabanowitz, J., . . . Taverna, S. D. (2013). Methylation of histone H3 at lysine 23 in meiotic heterochromatin. Epigenetics & Chromatin, 6(S1). doi:10.1186/1756-8935-6-s1-o13

Wang, W. -L., Nicklay, J. J., Anderson, L., Strukl, J., Onikubo, T., Shabanowitz, J., . . . Shechter, D. (2013). Developmental regulation of histone H2A deposition via serine-1 phosphorylation. Epigenetics & Chromatin, 6(S1). doi:10.1186/1756-8935-6-s1-p74

Mothe, B. R., Southwood, S., Sidney, J., English, A. M., Wriston, A., Hoof, I., . . . Sette, A. (2013). Peptide-binding motifs associated with MHC molecules common in Chinese rhesus macaques are analogous to those of human HLA supertypes and include HLA-B27-like alleles. IMMUNOGENETICS, 65(5), 371-386. doi:10.1007/s00251-013-0686-9


Kim, Y. -C., Jahren, N., Stone, M. D., Udeshi, N. D., Markowski, T. W., Witthuhn, B. A., . . . Olszewski, N. E. (2013). Identification and Origin of N-Linked β-D-N-Acetylglucosamine Monosaccharide Modifications on Arabidopsis Proteins. PLANT PHYSIOLOGY, 161(1), 455-464. doi:10.1104/pp.112.208900

Mitchell, D. J., Blasier, K. R., Jeffery, E. D., Ross, M. W., Pullikuth, A. K., Suo, D., . . . Pfister, K. K. (2012). Trk Activation of the ERK1/2 Kinase Pathway Stimulates Intermediate Chain Phosphorylation and Recruits Cytoplasmic Dynein to Signaling Endosomes for Retrograde Axonal Transport. JOURNAL OF NEUROSCIENCE, 32(44), 15495-15510. doi:10.1523/JNEUROSCI.5599-11.2012

Petkowski, J. J., Tooley, C. E. S., Anderson, L. C., Shumilin, I. A., Balsbaugh, J. L., Shabanowitz, J., . . . Macara, I. G. (2012). Substrate Specificity of Mammalian N-Terminal α-Amino Methyltransferase NRMT. BIOCHEMISTRY, 51(30), 5942-5950. doi:10.1021/bi300278f

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