My interests include: elucidation of signaling networks relevant to human disease and exploring perturbations in phosphorylation patterns induced by pharmacological agents. Quantitative phosphoproteomic analysis by mass spectrometry is a technique that allows efficient profiling of tens of thousands of phosphorylation sites over time from cells and tissues. Our laboratory employs this platform to map complex signaling networks in T cells to more holistically understand the structure of the T cell signaling pathway.

Lab Research Interests

Our laboratory studies how signaling networks control T cell function in health and disease, with a major focus on T cell receptor and CAR T cell signaling using state-of-the-art quantitative LC-MS proteomic workflows. We investigate the phosphorylation-driven pathways that regulate immune cell activation, feedback control, and signaling crosstalk, because these molecular events shape how T cells respond to cancer, infection, and other disease states. By defining these pathways at high resolution, we aim to uncover mechanisms of immune dysfunction and identify signaling nodes that may be leveraged therapeutically.

We also study how CAR T cell design alters signaling in both engineered immune cells and the tumor cells they encounter. This has direct relevance to human health because CAR-driven signaling can influence therapeutic efficacy, persistence, toxicity, and in some cases unintended target-cell responses. Through the integration of advanced phosphoproteomics, biochemical approaches, and computational analysis, our work seeks to define the molecular mechanisms that will guide the development of safer and more effective next-generation cancer immunotherapies.

More broadly, our research is directed toward translating fundamental discoveries in cell signaling into insight that can improve the treatment of cancer and immune-related disease.

Facilities, Resources, and Environment

The Salomon Research Group is located in the Laboratories for Molecular Medicine in the Jewelry District of Providence, Rhode Island, occupying 1,000 square feet of laboratory space on the fourth floor of 70 Ship Street. The laboratory is immediately adjacent to the Brown Proteomics Core Facility, providing direct access to state-of-the-art mass spectrometry instrumentation. Core instrumentation includes an Thermo Scientific Orbitrap Ascend Tribrid Mass Spectrometer equipped with FAIMS (1S10OD036295-01 PI: A. Salomon), a Vanquish Neo UHPLC, two nanospray sources (EasySpray and NanoFlex), and a TECAN A200 for automated proteomic sample preparation. A Thermo Scientific Q Exactive Hybrid Quadrupole-Orbitrap Mass Spectrometer coupled to an UltiMate3000 nanoRSLC UHPLC is also available for pilot studies and method development. The facility is supported by strong institutional commitment, including a PhD-level director (Nicholas A. DaSilva, PhD), PhD-level technical staff, and a service contract that ensures reliable instrument performance. The close integration of the Proteomics Core with the Salomon laboratory has also fostered productive methodological and computational collaboration, strengthening the development of quantitative phosphoproteomic workflows and data analysis strategies. These combined resources provide an exceptional environment for high-sensitivity, reproducible LC-MS studies of T cell and CAR T cell signaling in human disease.

2026

• A. Callahan, R. Puterbaugh, T. Ro, X. Zhang, X. Su, A. Salomon (2026). “Phosphoproteomic analysis of successive Jurkat CD19-CAR generations reveals TCRζ-driven signalling”. Cellular Signalling, 138:112204.

• A. Callahan, S.S. Trychanh, T. Ro, A. Mojumdar, A.R. Salomon. (2026). “Phosphotyrosine proteomics reveals novel Zap70 and Itk pathway targets downstream of TCR and CAR in Jurkat T cells.” Sci. Rep., in press. doi:10.1038/s41598-026-47234-x.

2025

• A. Callahan, A. Mojumdar, A.R. Salomon, N.A. DaSilva. (2025). “Evaluating first-pass, high protein capacity desalting techniques for phosphoproteomics applications.” bioRxiv, 2025.06.03.657744. doi:10.1101/2025.06.03.657744.

• A. Callahan, X. Zhang, A. Wang, A. Mojumdar, L. Zeng, X. Su*, A. Salomon*. (2025). “CSF1R-CAR T cells induce CSF1R signaling and can promote target cell proliferation.” Science Signaling. 18: eadv4112.

• A. Callahan, A. Mojumdar, M. Hu, A. Wang, A. Griffith, N. Huang, X. Chua, N. Mroz, R. Puterbaugh, S. Reilly, A. Salomon (2025). “The phosphatases TCPTP, PTPN22, and SHP1 play unique roles in T cell phosphotyrosine maintenance and feedback regulation of the TCR.” Sci. Rep, 15:27747.
• J. Wan, P. Morse, M. Zurek 1,2, A. Turner, A. Vaishnav, A. Salomon, B. Edwards, T. Arroum, and M. Hüttemann (2025). “Tyrosine 67 Phosphorylation Controls Respiration and Limits the Apoptotic Functions of Cytochrome c”. Cells. 14(3): 951.

2024

• A. Callahan, X. Chua, A. Griffith, T. Hildebrandt, G. Fu, M. Hu, R. Wen, A. Salomon* (2024). “Deep phosphotyrosine characterization of primary murine T cells using broad spectrum optimization of selective triggering”. Proteomics. 24(23-24):e2400106.

2023

• G. Fu, Y. Zheng, G. Xin, Z. Wang, K. Bunting, W. Cui, A. Salomon, R. Wen (2023). “Gab3 Plays an Essential Role in CD8 + T-Cell Expansion through Regulating IL-2-Mediated Activation of PI3K/AKT/mTOR and Erk/FoxO Pathways.” Blood. 142:3931.

2022

• A. Griffith, K. Callahan, N King, Q. Xiao, X. Su, A. Salomon* (2022). “SILAC phosphoproteomics reveals unique signaling circuits in CAR-T cells and the inhibition of B cell-activating phosphorylation in target cells.” J Proteome Res. 21(2):395-409.

2021

• X. Chua, T. Aballo, W. Elnemer, M. Tran, A. Salomon* (2021). “Quantitative interactomics of Lck-TurboID in living human T cells unveils T cell receptor stimulation-induced proximal Lck interactors.” J Proteome Res. 20(1):715-726.
• X. Chua, A. Salomon* (2021). “Ovalbumin antigen-specific activation of T cell receptor closely resembles soluble antibody stimulation as revealed by BOOST phosphotyrosine proteomics.” J. Proteome Res. 20(6):3330-3344.

2020

• X. Chua, T. Mensah, T. Aballo, S. Mackintosh, R. Edmondson, A. Salomon (2020). “Tandem mass tag approach utilizing pervanadate boost channels delivers deeper quantitative characterization of the tyrosine phosphoproteome.” Molecular and Cellular Proteomics, 19(4):730-43.

2019

• M. Curtis, H. Kenny, B. Ashcroft, A. Mukherjee, A. Johnson, Y. Zhang, Y. Helou, R. Batlle, X. Liu, N. Gutierrez, X. Gao, S. Yamada, R. Lastra, A. Montag, N. Ahsan, J. Locasale, A. Salomon, A. Nebreda, E. Lengyel (2019). “Fibroblasts mobilize tumor cell glycogen to promote proliferation and metastasis.” Cell Metabolism, 29:141-155.
• N. Ahsan, J. Boylan, A. Salomon, J. Sanders, P. Gruppuso (2019). “Quantitative proteomics and phosphoproteomics from formalin-fixed, paraffin-embedded tissue samples.” Methods Mol. Biol. In press.

2018

• J. Li, B. Feng, Y. Nie, P. Jiao, X. Lin, M. Huang, R. An, Q. He, H. Zhou, A. Salomon, K. Sigrist, Z. Wu, S. Liu, H. Xu (2018). “Sucrose nonfermenting-related kinase regulates both adipose inflammmation and Energy Homeostasis in mice and humans.” Diabetes, 67:400-11.
• W. Lo, N. Shah, N. Ahsan, V. Horkova, O. Stepanek, A. Salomon, J. Kuriyan, A. Weiss (2018). “Lck promotes Zap70-dependent LAT phosphorylation by bridging Zap70 to LAT.” Nat. Immun., 19:733-41.
• Curtis, H. Kenny, B. Ashcroft, A. Mukherjee, A. Johnson, Y. Zhang, Y. Helou, R. Batlle, X. Liu, N. Gutierrez, X. Gao, S. Yamada, R. Lastra, A. Montag, N. Ahsan, J. Locasale, A. Salomon, A. Nebreda, E. Lengyel (2018). “Fibroblasts mobilize tumor cell glycogen to promote proliferation and metastasis.” Cell Metabolism, 28:1-15.

2017

• J. Belmont, T. Gu, A. Mudd, A. Salomon (2017). “A PLC-g1 feedback pathway regulates Lck substrate phosphorylation at the T cell receptor and SLP-76 Complex.” J. Proteome Res., 16(8):2729-42.
• N. Ahsan, J. Belmont, Z. Chen, J. Clifton, A. Salomon (2017). “Highly reproducible improved label-free quantitative analysis of cellular phosphoproteome by optimization of LC-MS/MS gradient and analytical column construction.” J. Proteomics, 165:69-74.
• N. Ahsan, A. Salomon (2017). “Quantitative phosphoproteomic analysis of T cell receptor signaling.” Methods in Molecular Biology, The Immune Synapse:Methods and Protocols,  1584:369-382.
• A. Qadir, P. Ceppi, S. Brockway, C. Law, L Mu, N. Khodarev, J. Kim, J. Zhao, W. Putzbach, A. Murrmann, Z. Chen, W. Chen, X. Liu, A. Salomon, H. Liu, R. Weichselbaum, J. Yu, M. Peter (2017) “CD95/Fas increases stemness in cancer cells by inducing STAT1 dependent Type I Interferon Response.” Cell Reports, 18:2373-2386.
• A. Michael, N. Ahsan, V. Zabala, H. Francois-Vaughan, S. Post, K. Brilliant, A. Salomon, J. Sanders, and P. Gruppuso (2017). “Proteomic Analysis of Laser Capture Microdissected Focal Lesions in a Rat Model of Progenitor Marker-Positive Hepatocellular Carcinoma.” Oncotarget, 8:26041-56.

2016

• N. Ahsan, R. Rao, P. Gruppuso, B. Ramratnam, A. Salomon (2016). “Targeted proteomics: Current status and future perspectives for quantification of food allergens.” J. Proteomics, 143:15-23.
• G. Mahapatra, A. Varughese, Q. Ji, I. Lee, J. Liu, A. Vaishnav, C. Sinkler, A. Kapralov, C. Moraes, T. Sanderson, T. Stemmler, L. Grossman, V. Kagan, J. Brunzelle, A. Salomon, B. Edwards, M. Huttemann (2016). “Phosphorylation of cytochrome c threonine 28 regulates electron transport chain activity in kidney: Implications for AMP kinase.” J. Biol. Chem., 292(1): 64-79.

2015

• H. Goodfellow, M. Frushicheva, Q. Ji, D. Cheng, T. Kadlecek, A. Cantor, J. Kuriyan, A. Chakraborty*, A. Salomon*, A. Weiss* (2015). “The catalytic activity of the kinase ZAP-70 mediates basal signaling and negative feedback of the T cell receptor pathway.” Science Signaling, 8:ra49. (* co-corresponding authors)
• Q. Ji, Y. Ding, A. Salomon (2015). “SLP-76 N-terminal tyrosine residues regulate a dynamic signaling equilibrium involving feedback of proximal TCR signaling.” Mol Cell Prot., 14(1):30-40.
• Y. Helou, A. Petrashen, A. Salomon (2015). “Vav1 regulates T cell activation through a feedback mechanism and crosstalk between the T cell receptor and CD28.” J. Proteome Research, 14(7):2963-75.
• Q. Ji, A. Salomon (2015). “Wide-scale quantitative phosphoproteomic analysis reveals that cold treatment of T cells closely mimics soluble antibody stimulation.” J. Proteome Research, 14(5):2082-9.
• Y. Helou, A. Salomon (2015). “Protein networks and activation of lymphocytes.” Cur Opin Immun., 33:78-85.
• J. Boylan, A. Salomon, U. Tantravahi, P. Gruppuso (2015). “Adaptation of HepG2 cells to a steady-state reduction in the content of protein phosphatase 6 (PP6) catalytic subunit.” Exp. Cell Res., 335(2):224-37.

2014

• D. Lamming, G. Demirkan, J. Boylan, M. Mihaylova, T. Peng, J. Ferreira, N. Neretti, A. Salomon, D. Sabatini, P. Gruppuso (2014). “Hepatic signaling by the mechanistic target of rapamycin complex 2 (mTORC2).” FASEB J., 28(1):300-15.
• W. Wimuttisuk, M. West, B. Davidge, K. Yu, A. Salomon, JD. Singer (2014). “Novel Cul3 binding proteins function to remodel E3 ligase complexes.” BMC Cell Biol, 15:28.
• B. Feng, P. Jiao, Y. Helou, Y. Li, Q. He, MS. Walters, A. Salomon, H.Xu (2014). “Mitogen-activated protein kinase phosphatase 3 (MKP-3)-deficient mice are resistant to diet-induced obesity.” Diabetes, 63(9):2924-34.

2013

• Y. Helou, V. Nguyen, S. Beik, A. Salomon (2013). “ERK positive feedback regulates a widespread network of tyrosine phosphorylation sites across canonical T cell signaling and actin cytoskeletal proteins in T cells.” PLoS One, 8(7):e69641.
• B. DeNardo, M. Holloway, Q. Ji, K. Nguyen, Y. Cheng, M. Valentine, A. Salomon, R. Altura (2013). “Quantitative phosphoproteomic analysis indetifies activation of the RET and IGF-1R/IR signaling pathways in neuroblastoma.” PLoS One, 8(12):e82513.
• T. Sanderson, G. Mahapatra, P. Pecina, Q. Ji, K. Yu, C. Sinkler, A. Varughese, R. Kumar, M. Bukowski, R. Tousignant, A. Salomon, M. Huttemann (2013). “Cytochrome C is tyrosine 97 phosphorylated by neuroprotective insulin treatment.” PLoS One, 8(11):e78627.
• Y. Li, Y. Nie, Y. Helou, G. Ding, B. Feng, G. Xu, A.Salomon, H. Xu (2013). “Identification of sucrose non-fermenting related kinase (SNRK) as a suppressor of adipocyte inflammation.” Diabetes, 62(7):2396-409.

2012

• X. O’Brien, K. Heflin, L. Lavigne, K. Yu, M. Kim, A. Salomon, J. Reichner (2012). “Lectin site ligation of CR3 induces conformational changes and signaling.” J. Biol. Chem. 287 (5):3337-48.
• G. Demirkan, A. Salomon, P. Gruppuso (2012). “Phosphoproteomic analysis of liver homogenates.” Methods Mol Biol., 909:151-63.
• L. Cao, Y. Ding, N. Hung, K. Yu, A. Ritz, B. Raphael, A. Salomon (2012). “Quantitative phosphoproteomics reveals SLP-76 dependent regulation of PAG and Src family kinases in T cells.” PLoS One, 7(10):e46725.

2011

• G. Demirkan, K. Yu., J. Boylan, A. Salomon, P. Gruppusso (2011). “Phosphoproteomic profiling of in vivo signaling in liver by the mammalian target of rapamycin complex 1 (mTORC1).” PLoS One, 6(6):e21729.

2010

• P. Agrawal, K. Yu, A. Salomon, J. Sedivy (2010). “Proteomic profiling of Myc-associated proteins.” Cell Cycle, 9(24):4908-21.
• K. Yu, A. Salomon (2010). “HTAPP: High-throughput autonomous proteomic pipeline.” Proteomics, 10, 2113-2122. (Paper supplemental website)
• R. Jianu, K. Yu, L. Cao, V. Nguyen, A. Salomon, D. Laidlaw (2010). “Effective visual integration of quantitative proteomic data, pathways, and protein information.” Trans. on Vis. and Comp. Graphics, 16, 609-620. (Paper supplemental website)

2009

• K. Yu, A. Salomon (2009). “PeptideDepot: Flexible relational database for visual analysis of quantitative proteomic data and integration of existing protein information.” Proteomics, 9(23), 5350-58. (Paper supplemental website)
• V. Nguyen, L. Cao, J. T. Lin, N. Hung, A. Rit, K. Yu, R. Jianu, B.J. Raphael, S. Ulin, D.H. Laidlaw, L. Brossay, A. Salomon (2009). “A new approach for quantitative phosphoproteomic dissection of signaling pathways applied to T cell receptor activation.” Mol. Cell Prot, 8:2418-31. (Paper supplemental website)
• K. Yu, A. Sabelli, L. DeKeukelaere, R. Park, S. Sindi, CA. Gatsonis, A. Salomon (2009). “Integrated platform for manual and high-throuput statistical validation of tadem mass spectra.” Proteomics, 9(11), 3115-25. (Paper supplemental website)
• I. Lee, A. Salomon, K. Yu, L. Samavati, P. Pecina, A. Pecinova, M. Huttemann (2009). “Isolation of regulatory-competent, phosphorylated cytochrome c oxidase.” Methods Enzymol. 457, 193-210.
• J. Pezza, S. Langseth, R. Yamamoto, S. Dorris, S. Ulin, A. Salomon, T. Serio (2009). “The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype.” Molec. Biol. Cell.20(3) 1068-80
• A. Ritz, G. Shakhnarovich, A. Salomon, B. Raphael (2009). “Discovery of phosphorylation motif mixtures in phosphoproteomics data.” Bioinformatics. 25 (1) 14-21.

2008

• H. Yu, I. Lee, A. Salomon, K. Yu, M. Huttmann (2008). “Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration.” Biochim. Biophys. Acta. 1777(7-8) 1066-71.

2007

• L. Cao, K. Yu, C. Banh, V. Nguyen, A. Ritz, B. Raphael, Y. Kawakami, T. Kawakami, A. Salomon (2007). “Quantitative Time-Resolved Phosphoproteomic Analysis of Mast Cell Signaling.” J. Immunology. 179(9) 5864-76. (Paper supplemental website)
• T. Nuhse, K. Yu, A. Salomon (2007). “Isolation of Phosphopeptides by Immobilized Metal Ion Affinity Chromatography.”  In Cur. Prot. Mol. Biol., (Ausubel et al., eds.) 18.13.1-18.13.23. John Wiley & Sons, Hoboken, N.J.

2006

• L. Cao, K. Yu, A. Salomon (2006). “Phosphoproteomic Analysis of Lymphocyte Signalling.” In Advances in Experimental Medicine and Biology, Vol. 584, C. Tsoukas, ed. Springer, New York, NY. chapter 19, Pgs. 277-88.
• I. Lee, A. Salomon, K. Yu, J. Doan, L. Grossman, M. Huttemann (2006). “New Prospects for an Old Enzyme: Mammalian Cytochrome c Is Tyrosine Phosphoryalted In Vivo.” Biochemistry. 45(30): 9121-9128.

2005

• S. Ficarro, A. Salomon, L. Brill, D. Mason, M. Stettler-Gill, A. Brock, E. Peters (2005). “Automated immobilized metal affinity chromatography/nano-LC electrospray ionization mass spectrometry platform for profiling protein phosphorylation sites.” Rap. Comm. Mass Spec. 19:57-71.
• I. Lee, A. Salomon, S. Ficarro, I. Mathes, F. Lottspeich, L. Grossman, M. Huttemann (2005). “cAMP-dependent tyrosine phosphorylation of subunit I inhibits cytochrome c oxidase activity.” J. Biol. Chem.280:6094-6100.

2004

• L. Brill, A. Salomon, S. Ficarro, M. Mukherji, M. Stettler-Gill, E. Peters (2004). “Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.” Anal. Chem. 76(10): 2763-2772.

2003

• A. Brock, D. Horn, E. Peters, C. Shaw,  C. Ericson, Q. Phung, A. Salomon (2003). “An automated matrix-assisted laser desorption/ionization quadrupole fourier transform ion cyclotron resonance mass spectrometer for ‘bottom up’ proteomics.” Anal. Chem. 75(14):3419-3428.
• C. Ericson, Q. Phung, D. Horn, E. Peters, J. Fitchett, S. Ficarro, A. Salomon, L. Brill, A. Brock (2003). “An automated noncontact deposition interface for liquid chromatography matrix-assisted laser desorption/ionization mass spectrometry.” Anal. Chem. 75(10): 2309-2315.
• A. Salomon, S. Ficarro, L. Brill, A. Brinker, Q. Phung, C. Ericson, K. Sauer, D. Horn, P. Schultz, E. Peters (2003). “Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.” Proc. Nat. Acad. Sci., 100(2): 443-448.

2002

• A. Brock, D. Horn, C. Shaw, E. Peters, C. Ericson, Q. Phung, S. Ficarro, A. Salomon (2002). “Automated Liquid Chromatography MALDI FT-ICR MS Platform for Proteomics: Automated High Performance Mass Spectrometry and Data Analysis” Am. Pharma. Rev., 5(4): 94-99.
• E. Peters, A. Brock, Q. Phung, J. Fitchett, D. Horn, C. Ericson, S. Ficarro, A. Salomon (2002). “Automated Liquid Chromatography MALDI FT-ICR MS Platform for Proteomics: Rationale for an Off-Line Approach and Optimized Implementation” Am. Pharma. Rev., 5(3): 72-81.
• E. Peters, A. Brock, D. Horn, Q. Phung, C. Ericson, A. Salomon, S. Ficarro, L. Brill (2002). “An automated LC-MALDI FT-ICR MS platform for high-throughput proteomics.” LCGC Europe, 15(7): 423-8.
• J. Pennington, H. Williams, A. Salomon, G. Sulikowski (2002). “Toward a stable apoptolidin derivative: Identification of isoapoptolidin and selective deglycosylation of apoptolidin.” Organic Letters, 4(22): 3823-3825.

2001

• A. Salomon, Y. Zhang, H. Seto, C. Khosla (2001). “Structure-activity relationships within a family of selectively cytotoxic macrolide natural products.” Organic Letters, 3(1): 57-59.
• A. Salomon, D. Voehringer, L. Herzenberg, C. Khosla (2001). “Apoptolidin, a selective cytotoxic agent, is an inhibitor of F0F1-ATPase.” Chemistry and Biology, 8(1): 71-80.

2000

• A.Salomon, D. Voehringer, L. Herzenberg, C. Khosla (2000). “Understanding and exploiting the mechanistic basis for selectivity of polyketide inhibitors of F0F1-ATPase.” Proc. Nat. Acad. Sci., 97(26): 14766-71.
• H. Zeng, H. Shao, N. Menon, J. Yang, A. Salomon, R. Freidland, and M. Zagorski (2000). “Nicotine and Amyloid Formation” Biological Psychiatry 49(3): 248-257.

1997

• H. Shao, K. Marcinowski, E. Clancy, A. Salomon and M. Zagorski (1997). “The Solution Structures of the ß-Amyloid Peptide Provide a Molecular Approach for the Treatment of Alzheimer’s Disease.” In K. Iqbal, B. Winblad, T. Nishimura, M. Takeda and H. M. Wisniewski (eds), Alzheimer’s Disease: Biology, Diagnosis and Therapeutics New York, John Wiley & Sons, pp 729-739.

1996

• A. Salomon, K. Marcinowski, R. Friedland, and M. Zagorski (1996). “Nicotine inhibits amyloid formation by the beta-peptide.” Biochemistry 35(42): 13568-78.

National Institutes of Health Biotechnology Training Grant, 1995-1997
NIH Study Section ZRG1 BST-D(55) National Technology Centers for Networks and Pathways, 2005
NIH Study Section ZRG1 BST-D(51) Continued Development and Maintenance of Software, 2006
Beckman Young Investigator Award, 2006-20010
Session Chair, 96th American Association of Immunologist Annual Meeting "Technological Innovations in Immunology", Seattle, WA, 2009

American Chemistry Society
The American Association of Immunologists

Dr. Salomon teaches across Brown’s undergraduate, graduate, and medical programs, focusing on making biochemistry rigorous, accessible, and relevant to students. His courses have included BIOL 0280 Introductory Biochemistry, BIOL 1270/2270 Advanced Biochemistry, BIOL 2030 Foundations of Advanced Study in the Life Sciences, and BIOL 3642/IMS-I Scientific Foundations in Medicine. Across these settings, he emphasizes conceptual understanding, critical analysis of scientific data and literature, and clear scientific communication.

His teaching spans large undergraduate lecture courses, advanced discussion-based classes, graduate training, and medical education. In BIOL 0280, he has helped introduce hundreds of students each year to the core principles of biochemistry while connecting those fundamentals to modern approaches such as proteomics, genomics, structural biology, and cell signaling. In advanced undergraduate and graduate courses, he combines mechanistic biochemistry with close reading of the primary literature and student presentations. In medical education, he teaches the biochemical foundations of human disease with an emphasis on clinical relevance.

Dr. Salomon’s teaching is grounded in active learning and innovation. He has helped develop and implement tools such as lecture capture, podcasts, online discussion resources, rapid electronic feedback, and in-class response systems to support student engagement and comprehension in fast-paced courses. Across all levels, his goal is to help students build a strong foundation in biochemical thinking while developing the analytical and communication skills essential for success in science and medicine.