Research Interests for Michael C. Fitzgerald

Dr. Fitzgerald’s research group is focused on studies of protein folding and function. The group utilizes a combination of covalent labeling strategies (e.g. protein amide H/D exchange and methionine oxidiation) and mass spectrometry techniques to investigate the thermodynamic properties of protein folding and ligand binding reactions. Current research efforts involve: (1) the development new biophysical methods that enable protein folding and stability measurements to be performed on the proteomic scale; and (2) the application of these new methods in the areas of disease detection, diagnosis, and therapy.

Keywords:

Adenocarcinoma, Adult, Aged, Aged, 80 and over, Algorithms, Alleles, Amidines, Amino Acid Sequence, Amino Acid Substitution, Amino Acids, Animals, Anions, Antioxidants, Arginine, Automation, Bacterial Outer Membrane Proteins, Bacterial Proteins, Bacteriophage lambda, Base Sequence, bcl-X Protein, Binding Sites, Biological Markers, Biological Transport, Biophysical Phenomena, Biophysics, Blood Proteins, Buffers, Calcineurin, Calmodulin, Calorimetry, Carbonic Anhydrase II, Carcinoma, Non-Small-Cell Lung, Carrier Proteins, Catalysis, Cattle, Cell Line, Chromatography, Chromatography, Gel, Chromatography, High Pressure Liquid, Chromatography, Liquid, Circular Dichroism, Citrate (si)-Synthase, Coenzymes, Combinatorial Chemistry Techniques, Complex Mixtures, Copper, Cyclophilin A, Cyclosporine, Cytochromes c, Databases, Protein, Deuterium, Deuterium Exchange Measurement, Deuterium Oxide, Dimerization, Diterpenes, DNA, DNA-Binding Proteins, Dose-Response Relationship, Drug, Drug Discovery, Enzyme Activation, Enzyme Stability, Enzyme-Linked Immunosorbent Assay, Escherichia coli, Escherichia coli Proteins, Esters, Fatty Acid-Binding Proteins, Female, Ferric Compounds, Fluorescent Dyes, Fructose-Bisphosphate Aldolase, Fusarium, Gallium, Gene Expression Profiling, Genetic Complementation Test, Glutamate Dehydrogenase, Gonorrhea, Guanidine, Haemophilus influenzae, Heat-Shock Proteins, Histidine, Horses, Humans, Hydro-Lyases, Hydrogen, Hydrogen Bonding, Hydrogen Peroxide, Hydrogen-Ion Concentration, Hyperoxaluria, Primary, Immunoblotting, Immunohistochemistry, Immunosuppressive Agents, Indicators and Reagents, Iron, Iron-Binding Proteins, Isoelectric Focusing, Isomerases, Isotope Labeling, Kinetics, L-Lactate Dehydrogenase, Lactalbumin, Ligands, Lung Neoplasms, Lysine, Macrophage Migration-Inhibitory Factors, Malate Dehydrogenase, Male, Maltose, Maltose-Binding Proteins, Mass Spectrometry, Metalloproteins, Methionine, Mice, Microbial Sensitivity Tests, Microchemistry, Middle Aged, Models, Biological, Models, Chemical, Models, Molecular, Models, Theoretical, Molecular Chaperones, Molecular Sequence Data, Molecular Weight, Muser Mentor, Mutagenesis, Site-Directed, Mutation, Myoglobin, NAD, Neisseria gonorrhoeae, Neoplasms, Squamous Cell, Organometallic Compounds, Oxamic Acid, Oxidants, Oxidation-Reduction, Oxygen Isotopes, Peptide Biosynthesis, Peptide Fragments, Peptide Hydrolases, Peptide Mapping, Peptides, Peptostreptococcus, Periplasmic Binding Proteins, Pharmaceutical Preparations, Polymorphism, Genetic, Predictive Value of Tests, Prognosis, Protein Array Analysis, Protein Binding, Protein Conformation, Protein Denaturation, Protein Folding, Protein Footprinting, Protein Interaction Mapping, Protein Kinases, Protein Stability, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Proteins, Proteome, Proteomics, Protons, Pteridines, Pyridoxal Phosphate, Pyrones, Quantum Theory, Rabbits, Recombinant Fusion Proteins, Recombinant Proteins, Repressor Proteins, Reproducibility of Results, Ribonuclease, Pancreatic, Ribonucleases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sensitivity and Specificity, Sequence Homology, Amino Acid, Small Molecule Libraries, Sorbic Acid, Spectrometry, Fluorescence, Spectrometry, Mass, Electrospray Ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectrophotometry, Spectrophotometry, Ultraviolet, src Homology Domains, Stereoisomerism, Stilbenes, Streptococcus, Structure-Activity Relationship, Substrate Specificity, Sulfonium Compounds, Sulfurtransferases, Superoxide Dismutase, Survival Analysis, Swine, Tandem Mass Spectrometry, Temperature, Thermodynamics, Time, Time Factors, Transaminases, Transcription Factors, Transferrin, Transferrin-Binding Protein A, Transferrin-Binding Protein B, Trypsin, Tumor Markers, Biological, Ubiquitin, UDPglucose 4-Epimerase, Ultraviolet Rays, Urea, Variation, Viral Proteins, Viral Regulatory and Accessory Proteins, Vitamin B Complex, Yeasts

Recent Publications

1. Gurysh, EG; Zahid, MSH; Johnson, MM; Landavazo, A; Namjoshi, OA; Wilson, JW; Varma, DM; Woodring, RN; Hendricksen, AT; Vath, JF; Quan, B; Pino, EN; Fitzgerald, MC; Bachelder, EM; Blough, BE; Ainslie, KM, Discovery of Host-Directed Small Molecules with Broad Anti-Leishmanial Efficacy., bioRxiv (November, 2025) [doi] [abs]
2. Denning-Jannace, CA; James, KJ; Monteagudo, CR; Sturrock, GR; Robison, ATR; Vaccaro, FA; Kuhn, SA; Fitzgerald, MC; Franz, KJ, Leveraging Vulnerabilities in Copper Trafficking for Synergistic Antifungal Activity., ACS chemical biology, vol. 20 no. 11 (November, 2025), pp. 2659-2670 [doi] [abs]
3. Outlaw, TC; Robison, ATR; Schulte, NB; Vaccaro, FA; Williams, IG; Repala, S; Diaz, D; Sturrock, GR; Fitzgerald, MC; Franz, KJ, Copper Activates a Redox Switch to Reversibly Inhibit Glyceraldehyde-3-Phosphate Dehydrogenase., Biochemistry, vol. 64 no. 21 (November, 2025), pp. 4400-4413 [doi] [abs]
4. Truong, A; Hu, R; Quan, B; Bailey, MA; Schroeder, EA; Sylvester, K; Neveu, G; Kafsack, BFC; Fitzgerald, MC; Derbyshire, ER, Covalent inhibition of <i>Plasmodium falciparum</i> Ubc13 impairs global protein synthesis., iScience, vol. 28 no. 6 (June, 2025), pp. 112545 [doi] [abs]
5. Sturrock, GR; Robison, ATR; Dharani, A; Monson, EE; Franz, KJ; Fitzgerald, MC, Extrinsic and intrinsic factors affect copper-induced protein precipitation across eukaryotic and prokaryotic proteomes., Protein science : a publication of the Protein Society, vol. 34 no. 6 (June, 2025), pp. e70158 [doi] [abs]