Publications

Harris, R. A.; May, J. C.; Harvey, S. R.; Wysocki, V. H.; McLean, J. A. Evaluation of Surface-Induced Dissociation Ion Mobility-Mass Spectrometry for Lipid Structural Characterization. J. Am. Soc. Mass Spectrom. 2024. https://doi.org/10.1021/jasms.3c00319.
Harvey, S. R.; Gadkari, V. V.; Ruotolo, B. T.; Russell, D. H.; Wysocki, V. H.; Zhou, M. Expanding Native Mass Spectrometry to the Masses. J Am Soc Mass Spectrom 2024. https://doi.org/10.1021/jasms.3c00352.
Li, Y.; Shen, Z.; Zhang, M.; Yang, X.-Y.; Cleary, S. P.; Xie, J.; Marathe, I. A.; Kostelic, M.; Greenwald, J.; Rish, A. D.; Wysocki, V. H.; Chen, C.; Chen, Q.; Fu, T.-M.; Yu, Y PtuA and PtuB Assemble into an Inflammasome-like Oligomer for Anti-Phage Defense. Nat Struct Mol Biol 2024, 1–11. https://doi.org/10.1038/s41594-023-01172-8.
Lyu, J.; Zhang, T.; Marty, M. T.; Clemmer, D.; Russell, D.; Laganowsky, A. Double and Triple Thermodynamic Mutant Cycles Reveal the Basis for Specific MsbA-Lipid Interactions. Elife 2024, 12, RP91094. https://doi.org/10.7554/eLife.91094.
McElroy, C. A.; Ihms, E. C.; Kumar Yadav, D.; Holmquist, M. L.; Wadhwa, V.; Wysocki, V. H.; Gollnick, P.; Foster, M. P. “Solution Structure, Dynamics and Tetrahedral Assembly of Anti-TRAP, a Homo-Trimeric Triskelion-Shaped Regulator of Tryptophan Biosynthesis in Bacillus Subtilis.” Journal of Structural Biology: X 2024, 10, 100103. DOI: 10.1016/j.yjsbx.2024.100103.
Reid, D. J.; Thibert, S. M.; Wilson, J. W.; Soldatova, A. V.; Tebo, B. M.; Spiro, T. G.; Zhou, M. Resolving Metal Binding Properties within Subunits of a Multimeric Enzyme Mnx by Surface Induced Dissociation and Native Ion Mobility Mass Spectrometry. International Journal of Mass Spectrometry 2024, 496, 117172. https://doi.org/10.1016/j.ijms.2023.1171
Roy, J.; Marathe, I.; Wysocki, V.; Pradeep, T. “Observing Atomically Precise Nanocluster Aggregates in Solution by Mass Photometry.” Chem. Commun. 2024, 60 (52), 6655–6658. DOI: 10.1039/D4CC00363B.
Schrader RL, Anderson GA, Russell DH. Increasing Isolation Efficiency Using a Segmented Quadrupole Mass Filter Operated with Rectangular Waveforms. Journal of the American Society for Mass Spectrometry. 2024 April 30. PubMed PMID: 38687674; DOI: 10.1021/jasms.4c00051.
Shaw, J. B.; Harvey, S. R.; Du, C.; Xu, Z.; Edgington, R. M.; Olmedillas, E.; Saphire, E. O.; Wysocki, V. H. Protein Complex Heterogeneity and Topology Revealed by Electron Capture Charge Reduction and Surface Induced Dissociation. ACS Cent. Sci. 2024, 10 (8), 1537–1547. DOI: 10.1021/acscentsci.4c00461.
Thibert, S.; Reid, D.; Wilson, J.; Varikoti, R.; Maltseva, N.; Schultz, K.; Kruel, A.; Babnigg, G.; Joachimiak, A.; Kumar, N.; Zhou, M. Native Mass Spectrometry Dissects the Structural Dynamics of an Allosteric Heterodimer of SARS-CoV-2 Nonstructural Proteins. J. Am. Soc. Mass Spectrom. 2024, 35 (5), 912–921. https://doi.org/10.1021/jasms.3c00453.
Witzel, M. T.; Veltri, L. M.; Kostelic, M.; Elshamy, Y. S.; Lucas, J. A.; Lai, S.; Du, C.; Wysocki, V. H.; Holland, L. A. Protein Analysis Using Capillary Electrophoresis Coupled to Mass Spectrometry through Vibrating Sharp-Edge Spray Ionization. Electrophoresis 2024. https://doi.org/10.1002/elps.202300298.
Yang, X.-Y.; Shen, Z.; Xie, J.; Greenwald, J.; Marathe, I.; Lin, Q.; Xie, W. J.; Wysocki, V. H.; Fu, T.-M. “Molecular Basis of Gabija Anti-Phage Supramolecular Assemblies.” Nat Struct Mol Biol 2024. DOI: 10.1038/s41594-024-01283-w.
Zakharova, K.; Liu, M.; Greenwald, J. R.; Caldwell, B. C.; Qi, Z.; Wysocki, V. H.; Bell, C. E. “Structural Basis for the Interaction of Redβ Single-Strand Annealing Protein with Escherichia Coli Single-Stranded DNA-Binding Protein.” Journal of Molecular Biology 2024, 436 (11), 168590. DOI: 10.1016/j.jmb.2024.168590.
Bermeo, S.; Favor, A.; Chang, Y.-T.; Norris, A.; Boyken, S. E.; Hsia, Y.; Haddox, H. K.; Xu, C.; Brunette, T. J.; Wysocki, V. H.; Bhabha, G.; Ekiert, D. C.; Baker, D. De Novo Design of Obligate ABC-Type Heterotrimeric Proteins.
Biehn, S. E.; Lindert, S. Protein Structure Prediction with Mass Spectrometry Data. Annual Review of Physical Chemistry 2022, 73 (1), 1–19. https://doi.org/10.1146/annurev-physchem-082720-123928.
Boyken, S.E.; Benhaim, M. A.; Busch, F.; Jia, M.; Bick, M. J.; Choi, H.; Klima, J. C.; Chen, Z.; Walkey, C.; Mileant, A.; Sahasrabuddhe, A.; Wei, K. Y.; Hodge, E. A.; Byron, S.; Quijano-Rubio, A.; Sankaran, B.; King, N. P.; Lippincott-Schwartz, J.; Wysocki, V. H.; Lee, K.K.; Baker D. De Novo Design of Tunable, pH-driven Conformational Changes.
Busch, F.; VanAernum, Z.; Lai, S. M.; Gopalan, V.; Wysocki, V. Screening Tagged Proteins Using Tandem Affinity-Buffer Exchange Chromatography Online with Native Mass Spectrometry
Caldwell, B. J.; Norris, A. S.; Karbowski, C. F.; Wiegand, A. M.; Wysocki, V. H.; Bell, C. E. Structure of a RecT/Redβ Family Recombinase in Complex with a Duplex Intermediate of DNA Annealing.
Caldwell, B. J.; Norris, A.; Wysocki, V. H.; Bell, C. E. Structure of a Rad52 Homolog from Bacteriophage in Complex with a Novel Duplex Intermediate of DNA Annealing.
Caldwell, B. J.; Norris, A.; Zakharova, E.; Smith, C. E.; Wheat, C. T.; Choudhary, D.; Sotomayor, M.; Wysocki, V. H.; Bell, C. E. Oligomeric Complexes Formed by Redβ Single Strand Annealing Protein in Its Different DNA Bound States.
Chen, Z.; Kibler, R.D.; Hunt, A.; Busch, F.; Pearl, J.; Jia, M.; VanAernum, Z.L.; Wicky, B.I.M.; Dods, G.; Liao, H.; Wilken, M.S.; Ciarlo, C.; Green, S.; ElpSamad, H.; Stamatoyannopoulos, J.; Wysocki, V.H.; Jewett, M.C.; Boyken, S.E.; Baker, D. De Novo Design of Protein Logic Gates.
Dong, S.; Shirzadeh, M.; Fan, L.; Laganowsky, A.; Russell, D. H. Ag+ Ion Binding to Human Metallothionein-2A Is Cooperative and Domain Specific.
Drake, Z. C.; Seffernick, J. T.; Lindert, S. Protein Complex Prediction Using Rosetta, AlphaFold, and Mass Spectrometry Covalent Labeling.
Du, C.; Cleary, S. P.; Kostelic, M. M.; Jones, B. J.; Kafader, J. O.; Wysocki, V. H. Combining Surface-Induced Dissociation and Charge Detection Mass Spectrometry to Reveal the Native Topology of Heterogeneous Protein Complexes. Anal. Chem. 2023, 95 (37), 13889–13896. https://doi.org/10.1021/acs.analchem.3c02185.
Fan, L.; Russell, D. H. An Ion Mobility-Mass Spectrometry Study of Copper-Metallothionein-2A: Binding Sites and Stabilities of Cu-MT and Mixed Metal Cu–Ag and Cu–Cd Complexes. Analyst 2023, 148 (3), 546–555. https://doi.org/10.1039/D2AN01556K.
Freitas, D. P.; Chen, X.; Hirtzel, E. A.; Edwards, M. E.; Kim, J.; Wang, H.; Sun, Y.; Kocurek, K. I.; Russell, D.; Yan, X. In Situ Droplet-Based on-Tissue Chemical Derivatization for Lipid Isomer Characterization Using LESA. Anal Bioanal Chem 2023, 415 (18), 4197–4208. https://doi.org/10.1007/s00216-023-04653-3.
Gadkari, V. V.; Juliano, B. R.; Mallis, C. S.; May, J. C.; Kurulugama, R. T.; Fjeldsted, J.C.; McLean, J. A.; Russell, D. H.; Ruotolo, B. T. Performance evaluation of in-source ion activation hardware for collision-induced unfolding of proteins and protein complexes on a drift tube ion mobility-mass spectrometer.
Guaglianone, G.; Torrado, B.; Lin, Y.-F.; Watkins, M. C.; Wysocki, V. H.; Gratton, E.; Nowick, J. S. Elucidating the Oligomerization and Cellular Interactions of a Trimer Derived from Aβ through Fluorescence and Mass Spectrometric Studies.
Harvey, S. R.; Ben-Nissan, G.; Sharon, M.; Wysocki, V. H. Surface-Induced Dissociation for Protein Complex Characterization.
Harvey, S. R.; O’Neale, C.; Schey, K. L.; Wysocki, V. H. Native Mass Spectrometry and Surface Induced Dissociation Provide Insight into the Post-Translational Modifications of Tetrameric AQP0 Isolated from Bovine Eye Lens.
Harvey, S. R.; VanAernum, Z. L.; Kostelic, M. M.; Marty, M. T.; Wysocki, V. H. Probing the Structure of Nanodiscs Using Surface-Induced Dissociation Mass Spectrometry
Harvey, S. R.; VanAernum, Z. L.; Wysocki, V. H. Surface-Induced Dissociation of Anionic vs Cationic Native-Like Protein Complexes.
Harvey, S.R.; Seffernick, J.T.; Quintyn, R.S.; Song, Y.; Ju, Y; Yan, J.; Sahasrabuddhe, A.N.; Norris, A.; Zhou, M.; Behrman, E.J.; Lindert, S; Wysocki, V.H. Relative interfacial cleavage energetics of protein complexes revealed by surface collisions.
Holmquist, M.; Ihms, E. C., Gollnick, P.; Wysocki, V. H.; and Foster, M. P. Population distributions from native mass spectrometry titrations reveal nearest-neighbor cooperativity in the ring-shaped oligomeric protein TRAP.
Jia, M.; Sen, S.; Wachnowsky, C.; Fidai, I.; Cowan, J.A. and Wysocki, V. Characterization of [2Fe‐2S]‐Cluster‐Bridged Protein Complexes and Reaction Intermediates by use of Robust Native Mass Spectrometric Methods.
Jia, M.; Song, Y.; Du, C.; Wysocki, V. H. Oxidized and Reduced Dimeric Protein Complexes Illustrate Contrasting CID and SID Charge Partitioning. J. Am. Soc. Mass Spectrom. 2023. https://doi.org/10.1021/jasms.3c00142.
Jimenez-Harrison, D.; Huseby, C. J.; Hoffman, C. N.; Sher, S.; Snyder, D.; Seal, B.; Yuan, C.; Fu, H.; Wysocki, V.; Giorgini, F.; Kuret, J. DJ-1 Molecular Chaperone Activity Depresses Tau Aggregation Propensity through Interaction with Monomers. Biochemistry 2023, 62 (5), 976–988. https://doi.org/10.1021/acs.biochem.2c00581.
Kang, M.; Doddapaneni, K.; Sarni, S.; Heppner, Z.; Wysocki, V.; Wu, Z. Solution Structure of the Nucleotide Hydrolase BlsM: Implication of Its Substrate Specificity.
Karch, K. R.; Snyder, D. T.; Harvey, S. R.; Wysocki, V. H. Native Mass Spectrometry: Recent Progress and Remaining Challenges
Kim, S. S.; Aprahamian, M. L.; Lindert, S. Improving Inverse Docking Target Identification with Z-Score Selection.
Kneuttinger, A.; Zwisele, S.; Straub, K.; Bruckmann, A.; Busch, F.; Kinateder, T.; Gaim, B.; Wysocki, V.; Merkl, R.; Sterner, R. Light-Regulation of Tryptophan Synthase by Combining Protein Design and Enzymology.
Kneuttinger, A.C.; Straub, K.; Bittner, P.; Simeth, N.A.; Bruckmann, A.; Busch, F.; Rajendran, C.; Hupfeld, E.; Wysocki, V.H.; Horinek,D.; König, B.; Merkl, R.; Sterner, R. Light regulation of enzyme allostery through photo-responsive unnatural amino acids.
Kovvali, S.; Gao, Y.; Cool, A.; Lindert, S.; Wysocki, V.H.; Bell, C.E.; Gopalan, V. “Insights into the catalytic mechanism of a bacterial deglycase essential for utilization of fructose-lysine”. Protein Science 2023, 32( 7):e4695. DOI:10.1002/pro.4695.
Kreutzer, A. G.; Guaglianone, G.; Yoo, S.; Parrocha, C. M. T.; Ruttenberg, S. M.; Malonis, R. J.; Tong, K.; Lin, Y.-F.; Nguyen, J. T.; Howitz, W. J.; Diab, M. N.; Hamza, I. L.; Lai, J. R.; Wysocki, V. H.; Nowick, J. S. Probing Differences among Aβ Oligomers with Two Triangular Trimers Derived from Aβ. Proceedings of the National Academy of Sciences 2023, 120 (22), e2219216120. https://doi.org/10.1073/pnas.2219216120.
Kristoff, C. J.; Bwanali, L.; Veltri, L. M.; Gautam, G. P.; Rutto, P. K.; Newton, E. O.; Holland, L. A. Challenging Bioanalyses with Capillary Electrophoresis.
Kristoff, C.J.; Li, C.; Li, P.; Holland, L.A. Low flow voltage free interface for capillary electophoresis and mass spectrometry driven by vibrating sharp-edge spray ionization.
Kulyk, D. S.; Swiner, D. J.; Sahraeian, T.; Badu-Tawiah, A. K. Direct Mass Spectrometry Analysis of Complex Mixtures by Nanoelectrospray with Simultaneous Atmospheric Pressure Chemical Ionization and Electrophoretic Separation Capabilities.
Kuo, S.-T.; Tang, S.; Russell, D. H. Yan, X. Characterization of lipid carbon–carbon double-bond isomerism via ion mobility-mass spectrometry (IMS-MS) combined with cuprous ion-induced fragmentation
Laganowsky A, Clemmer DE, Russell DH. Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions.
Lai, S.M.; Thirugnanasambantham, P.; Sidharthan, V.; Norris, A.S.; Law, J.D.; Gopalan, V.; Wyoscki, V.H. Use of Tandem Affinity-Buffer Exchange Chromatography Online with Native Mass Spectrometry for Optimizing Overexpression and Purification of Recombinant Proteins.
Landeras-Bueno, S.; Wasserman, H.; Oliveira, G.; VanAernum, Z. L.; Busch, F.; Salie, Z. L.; Wysocki, V. H.; Andersen, K.; Saphire, E. O. Cellular MRNA Triggers Structural Transformation of Ebola Virus Matrix Protein VP40 to Its Essential Regulatory Form.
Lantz, C.; Schrader, R.; Meeuwsen, J.; Shaw, J.; Goldberg, N. T.; Tichy, S.; Beckman, J.; Russell, D. H. Digital Quadrupole Isolation and Electron Capture Dissociation on an Extended Mass Range Q-TOF Provides Sequence and Structure Information on Proteins and Protein Complexes.J Am Soc Mass Spectrom 2023, 34 (8), 1753–1760. https://doi.org/10.1021/jasms.3c00
Leelananda, S. P.; Lindert, S. Using NMR Chemical Shifts and Cryo-EM Density Restraints in Iterative Rosetta-MD Protein Structure Refinement.
Li, W.; Norris, A. S.; Lichtenthal, K.; Kelly, S.; Ihms, E. C.; Gollnick, P.; Wysocki, V. H.; Foster, M. P. Thermodynamic Coupling between Neighboring Binding Sites in Homo-Oligomeric Ligand Sensing Proteins from Mass Resolved Ligand-Dependent Population Distributions.
Lin, C.-W.; Oney-Hawthorne, S. D.; Kuo, S.-T.; Barondeau, D. P.; Russell, D. H. Mechanistic Insights of IscU Conformation Regulation for Fe–S Cluster Biogenesis Revealed by Variable-Temperature Electrospray Ionization Native Ion Mobility Mass Spectrometry.
Lin, C.; McCabe, J. W.; Russell, D. H.; Barondeau, D. P. Molecular mechanism of ISC iron-sulfur cluster biogenesis revealed by high-resolution native mass spectrometry.
Liu, Y.; LoCaste, C.E.; Liu, W.; Poltash, M.L.; Russell, D.H.; Laganowsky, A. Selective binding of a toxin and phosphatidylinositides to a mammalian potassium channel.
Lyu, J.; Liu, Y.; McCabe, J.W.; Schrecke, S.; Fang, L.; Russell, D.H.; Laganowsky, A. Discovery of Potent Charge-Reducing Molecules for Native Ion Mobility Mass Spectrometry Studies.
Mallis, C. S.; Zheng, X.; Qiu, X.; McCabe, J. W.; Shirzadeh, M.; Lyu, J.; Laganowsky, A.; Russell, D. H. Development of Native MS Capabilities on an Extended Mass Range Q-TOF MS.
Marathe, I. A.; Lai, S. M.; Zahurancik, W. J.; Poirier, M. G.; Wysocki, V. H.; Gopalan, V. Protein Cofactors and Substrate Influence Mg2+-Dependent Structural Changes in the Catalytic RNA of Archaeal RNase P.
Marciano, S.; Dey, D.; Listov, D.; Fleishman, S. J.; Sonn-Segev, A.; Mertens, H.; Busch, F.; Kim, Y.; Harvey, S. R.; Wysocki, V. H.; Schreiber, G. Protein Quaternary Structures in Solution Are a Mixture of Multiple Forms.
McCabe, J. W.; Hebert, M. J.; Shirzadeh, M.; Mallis, C. S.; Denton, J. K.; Walker, T. E.; Russell, D. H. The Ims Paradox: A Perspective on Structural Ion Mobility-Mass Spectrometry.
McCabe, J. W.; Jones, B. J.; Walker, T. E.; Schrader, R. L.; Huntley, A. P.; Lyu, J.; Hoffman, N. M.; Anderson, G. A.; Reilly, P. T. A.; Laganowsky, A.; Wysocki, V. H.; Russell, D. H. Implementing Digital-Waveform Technology for Extended m/z Range Operation on a Native Dual-Quadrupole FT-IM-Orbitrap Mass Spectrometer.
McCabe, J. W.; Mallis, C. S.; Kocurek, K. I.; Poltash, M. L.; Shirzadeh, M.; Hebert, M. J.; Fan, L.; Walker, T. E.; Zheng, X.; Jiang, T.; Dong, S.; Lin, C.-W.; Laganowsky, A.; Russell, D. H. First-Principles Collision Cross Section Measurements of Large Proteins and Protein Complexes.
McCabe, J. W.; Shirzadeh, M.; Walker, T. E.; Lin, C.-W.; Jones, B. J.; Wysocki, V. H.; Barondeau, D. P.; Clemmer, D. E.; Laganowsky, A.; Russell, D. H. Variable-Temperature Electrospray Ionization for Temperature-Dependent Folding/Refolding Reactions of Proteins and Ligand Binding.
Moghadamchargari Z, Huddleston J, Shirzadeh M, Zheng X, Clemmer DE, M Raushel F, Russell DH, Laganowsky A. Intrinsic GTPase Activity of K-RAS Monitored by Native Mass Spectrometry.
Moghadamchargari, Z.; Shirzadeh, M.; Liu, C.; Schrecke, S.; Packianathan, C.; Russell, D. H.; Zhao, M.; Laganowsky, A. Molecular Assemblies of the Catalytic Domain of SOS with KRas and Oncogenic Mutants.
Norris, A.; Busch, F.; Schupfner, M.; Sterner, R.; Wysocki, V.H. Quaternary structure of the tryptophan synthase α-subunit homolog BX1 from Zea mays,
Novikova I. V.; Zhou M.; Du C.; Parra M., Kim D. N.; VanAernum Z. L.; Shaw J. B.; Hellmann H.; Wysocki V. H.; Evans J. E. Tunable hetero-assembly of a plant pseudoenzyme-enzyme complex.
Pan, H.; Raab, S. A.; El-Baba, T. J.; Schrecke, S. R.; Laganowsky, A.; Russell, D. H.; Clemmer, D. E. Variation of CI-2 Conformers upon Addition of Methanol to Water: An IMS-MS-Based Thermodynamic Analysis. J. Phys. Chem. A 2023, 127 (45), 9399–9408. https://doi.org/10.1021/acs.jpca.3c03651.
Panczyk, E.; Lin, Y.-F.; Snyder, D.; Liu, F.; Ridgeway, M.; Park, M.; Bleiholder, C.; Wysocki, V. Evaluation of a Bruker timsTOF Pro for Native Mass Spectrometry. ChemRxiv September 12, 2023. https://doi.org/10.26434/chemrxiv-2021-qr78t-v2.
Panczyk, E.M.; Gilbert, J.D.; Jagdale, G.S.; Stiving, A.Q.; Baker, L.A. and Wysocki, V.H. Ion Mobility and Surface Collisions: Submicrometer Capillaries Can Produce Native-like Protein Complexes.
Panczyk, E.M.; Snyder, D.T.; Ridgeway, M.E.; Somogyi, A.; Park, M.A.; Wysocki, V.H. Surface-induced dissociation of protein complexes selected by trapped ion mobility spectrometry.
Patra, S.; Lin, C.-W.; Ghosh, M. K.; Havens, S. M.; Cory, S. A.; Russell, D. H.; Barondeau, D. P. Recapitulating the Frataxin Activation Mechanism in an Engineered Bacterial Cysteine Desulfurase Supports the Architectural Switch Model.
Phan, H.-D.; Norris, A. S.; Du, C.; Stachowski, K.; Khairunisa, B. H.; Sidharthan, V.; Mukhopadhyay, B.; Foster, M. P.; Wysocki, V. H.; Gopalan, V. Elucidation of Structure-Function Relationships in Methanocaldococcus Jannaschii RNase P, a Multi-Subunit Catalytic Ribonucleoprotein.
Poltash, M.L.; McCabe, J.W.; Shirzadeh, M.; Laganowsky,; Russell, D.H. Native IM-Orbitrap MS: Resolving what was hidden.
Poltash, M.L.; Shirzadeh, M.; McCabe, J.W.; Moghadamchargari, Z.; Langanowsky, A.; Russell, D.H. New insights into a the metal-induced oxidative degradation pathways of transthyretin.
Purde, V.; Busch, F.; Kudryashova, E.; Wysocki, V.H.; Kudryashov, D.S. Oligomerization affects the ability of human cyclase associated proteins 1 and 2 to promote actin severing by cofilins.
Pyles H, Zhang S, De Yoreo JJ, Baker D. Controlling protein assembly on inorganic crystals through designed protein interfaces.
Qiao, P; Schrecke, S.; Walker, T.; McCabe, J. Lyu, J; Zhu, Y.; Zhang, T.; Kumar, S.; Clemmer, D.; Russell, D.; Laganowsky, A. Entropy in the Molelcular Recognition of Membrane Protein-Lipid Interactions.
Raab S.A., El-Baba T.J., Laganowsky A., Russell D.H., Valentine S.J., Clemmer D.E. 2021. Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations.
Raab, S. A.; El-Baba, T. J.; Woodall, D. W.; Liu, W.; Liu, Y.; Baird, Z.; Hales, D. A.; Laganowsky, A.; Russell, D. H.; Clemmer, D. E. Evidence for Many Unique Solution Structures for Chymotrypsin Inhibitor 2: A Thermodynamic Perspective Derived from vT-ESI-IMS-MS Measurements.
Sahtoe, D. D.; Coscia, A.; Mustafaoglu, N.; Miller, L. M.; Olal, D.; Vulovic, I.; Yu, T.-Y.; Goreshnik, I.; Lin, Y.-R.; Clark, L.; Busch, F.; Stewart, L.; Wysocki, V. H.; Ingber, D. E.; Abraham, J.; Baker, D. Transferrin Receptor Targeting by de Novo Sheet Extension.
Sarni, S. H.; Roca, J.; Du, C.; Jia, M.; Li, H.; Damjanovic, A.; Małecka, E. M.; Wysocki, V. H.; Woodson, S. A. Intrinsically Disordered Interaction Network in an RNA Chaperone Revealed by Native Mass Spectrometry.
Sarni, S.; Biswas, B.; Liu, S.; Olson, E. D.; Kitzrow, J. P.; Rein, A.; Wysocki, V. H.; Musier-Forsyth, K. HIV-1 Gag Protein with or without P6 Specifically Dimerizes on the Viral RNA Packaging Signal.
Schrader, R. L.; Walker, T. E.; Chakravorty, S.; Anderson, G. A.; Reilly, P. T. A.; Russell, D. H. Optimization of a Digital Mass Filter for the Isolation of Intact Protein Complexes in Stability Zone 1,1. Anal Chem 2023, 95 (5), 3062–3068. https://doi.org/10.1021/acs.analchem.2c05221.
Schrader, R. L.; Walker, T. E.; Russell, D. H. Modified Ion Source for the Improved Collisional Activation of Protein Complexes. J Am Soc Mass Spectrom 2023, 34 (5), 977–980. https://doi.org/10.1021/jasms.3c00071.
Schrecke, S.; Zhu, Y.; McCabe, J. W.; Bartz, M.; Packianathan, C.; Zhao, M.; Zhou, M.; Russell, D.; Laganowsky, A. Selective Regulation of Human TRAAK Channels by Biologically Active Phospholipids
Schupfner, M.; Busch F.; Wysocki, V.; Sterner, R. Generation of a stand-alone tryptophan synthase α-subunit by mimicking an evolutionary blueprint.
Seffernick, J. T.; Canfield, S. M.; Harvey, S. R.; Wysocki, V. H.; Lindert, S. Prediction of Protein Complex Structure Using Surface-Induced Dissociation and Cryo-Electron Microscopy.
Seffernick, J. T.; Harvey, S. R.; Wysocki, V. H.; Lindert, S. Predicting Protein Complex Structure from Surface-Induced Dissociation Mass Spectrometry Data.
Seffernick, J. T.; Turzo, S. B. A.; Harvey, S. R.; Kim, Y.; Somogyi, Á.; Marciano, S.; Wysocki, V. H.; Lindert, S. Simulation of Energy-Resolved Mass Spectrometry Distributions from Surface-Induced Dissociation. Anal. Chem. 2022. https://doi.org/10.1021/acs.analchem.2c01869.
Sen, S.; Thompson, Z.; Wachnowsky, C.; Cleary, S.; Harvey, S. R.; Cowan, J. A. Biochemical Impact of a Disease-Causing Ile67Asn Substitution on BOLA3 Protein.
Shirzadeh, M.; Boone, C.D.; Laganowsky, A.; Russell, D.H. Topological Analysis of Transthyretin Disassembly Mechanism: Surface-Induced Dissociation Reveals Hidden Reaction Pathways.
Shirzadeh, M.; Poltash, M.L.; Laganowsky, A.; Russell, D.H. Structural Analysis of the Effect of Dual-FLAG Tag on Transthyretin.
Simmonds, A. L.; Lopez-Clavijo, Andrea F.; Winn, P. J.; Russell, D. H.; Styles, I. B.; Cooper, H. J. Structural Analysis of 14-3-3-ζ-Derived Phosphopeptides Using Electron Capture Dissociation Mass Spectrometry, Traveling Wave Ion Mobility Spectrometry, and Molecular Modeling.
Smith, H.; Pinkerton, N.; Heisler, D. B.; Kudryashova, E.; Hall, A. R.; Karch, K. R.; Norris, A.; Wysocki, V.; Sotomayor, M.; Reisler, E.; Vavylonis, D.; Kudryashov, D. S. Rounding Out the Understanding of ACD Toxicity with the Discovery of Cyclic Forms of Actin Oligomers.
Snyder, D. T.; Harvey, S. R.; Busch, F.; Wysocki, V. H. Chapter 11:Surface-Induced Dissociation in Biomolecular Mass Spectrometry. In Advanced Fragmentation Methods.
Snyder, D. T.; Harvey, S. R.; Wysocki, V. H. Surface-Induced Dissociation Mass Spectrometry as a Structural Biology Tool.
Snyder, D. T.; Jones, B. J.; Lin, Y.-F.; Cooper-Shepherd, D. A.; Hewitt, D.; Wildgoose, J.; Brown, J. M.; Langridge, J. I.; Wysocki, V. H. Surface-Induced Dissociation of Protein Complexes on a Cyclic Ion Mobility Spectrometer.
Snyder, D. T.; Lin, Y.-F.; Somogyi, A.; Wysocki, V. H. Tandem Surface-Induced Dissociation of Protein Complexes on an Ultrahigh Resolution Platform.
Snyder, D. T.; Panczyk, E.; Stiving, A. Q.; Gilbert, J.; Somogyi, A.; Kaplan, D.; Wysocki, V. Design and performance of a second-generation surface-induced dissociation cell for Fourier transform ion cyclotron resonance mass spectrometry of native protein complexes.
Snyder, D.T.; Panczyk, E.M.; Somogyi, A.; Kaplan, D.; Wysocki, V.H. Simple and Minimally Invasive SID Devices for Native Mass Spectrometry.
Stachowski, K.; Norris, A. S.; Potter, D.; Wysocki, V. H.; Foster, M. P. Mechanisms of Cre Recombinase Synaptic Complex Assembly and Activation Illuminated by Cryo-EM.
Stiving AQ, Jones BJ, Ujma J, Giles K, Wysocki VH. Collision Cross Sections of Charge Reduced Proteins and Protein Complexes: A Database for Collision Cross Section Calibration.
Stiving, A. Q.; Gilbert, J. D.; Jones, B. J.; Wysocki, V. H. A Tilted Surface and Ion Carpet Array for SID.
Stiving, A. Q.; VanAernum Z.; Busch, F.; Harvey S. R.; Sarni, S.; Wysocki, V. H. Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure.
Stiving, A.Q; Harvey, S.R.; Jones, B.J.; Bellina, B.; Brown, J.M.; Barran, P.E.; Wysocki, V.H. Coupling 193 nm ultraviolet photodissociation and ion mobility for sequence characterization of conformationally-selected peptides.
Szkoda, B. E.; Di Capua, A.; Shaffer, J.; Behrman, E. J.; Wysocki, V. H.; Gopalan, V. Characterization of a Salmonella Transcription Factor-DNA Complex and Identification of the Inducer by Native Mass Spectrometry.
Thirugnanasambantham, P.; Kovvali, S.; Cool, A.; Gao, Y.; Sabag-Daigle, A.; Boulanger, E. F.; Mitton-Fry, M.; Capua, A. D.; Behrman, E. J.; Wysocki, V. H.; Lindert, S.; Ahmer, B. M. M.; Gopalan, V. Serendipitous Discovery of a Competitive Inhibitor of FraB, a Salmonella Deglycase and Drug Target. Pathogens 2022, 11 (10), 1102. https://doi.org/10.3390/pathogens11101102.
Turzo, S. M. B. A.; Seffernick, J. T.; Lyskov, S.; Lindert, S. Predicting Ion Mobility Collision Cross Sections Using Projection Approximation with ROSIE-PARCS Webserver.
Turzo, S. M. B. A.; Seffernick, J. T.; Rolland, A. D.; Donor, M. T.; Heinze, S.; Prell, J. S.; Wysocki, V. H.; Lindert, S. Protein Shape Sampled by Ion Mobility Mass Spectrometry Consistently Improves Protein Structure Prediction.
VanAernum, Z.; Busch, F.; Jones, B.J.; Jia, M.; Chen, Z.; Boyken, S.E.; Sahasrabuddhe, A.; Baker, D.; Wysocki, V. Rapid Online Buffer Exchange: A Method for Screening of Proteins, Protein Complexes, and Cell Lysates by Native Mass Spectrometry.
VanAernum, Z.L.; Gilbert, J.D.; Belov, M.E.; Makarov, A.A; Horning, S.R.; Wysocki, V.H. Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer.
Vimer, S.; Ben-Nissan, G.; Morgenstern, D.; Kumar-Deshmukh, K.; Polkinghorn, C.; Quintyn R.S.; Vsil’ev, Y.V.; Beckman, J.S.; Elad, N.; Wysocki, V.H.; Sharon, M. Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry.
Vorobieva, A. A.; White, P.; Liang, B.; Horne, J. E.; Bera, A. K.; Chow, C. M.; Gerben, S.; Marx, S.; Kang, A.; Stiving, A. Q.; Harvey, S. R.; Marx, D. C.; Khan, G. N.; Fleming, K. G.; Wysocki, V. H.; Brockwell, D. J.; Tamm, L. K.; Radford, S. E.; Baker, D. De Novo Design of Transmembrane β-Barrels
Vulovic, I.; Yao, Q.; Park, Y.-J.; Courbet, A.; Norris, A.; Busch, F.; Sahasrabuddhe, A.; Merten, H.; Sahtoe, D. D.; Ueda, G.; Fallas, J. A.; Weaver, S. J.; Hsia, Y.; Langan, R. A.; Plückthun, A.; Wysocki, V. H.; Veesler, D.; Jensen, G. J.; Baker, D. Generation of Ordered Protein Assemblies Using Rigid Three-Body Fusion.
Walker, T. E.; Laganowsky, A.; Russell, D. H. Surface Activity of Amines Provides Evidence for the Combined ESI Mechanism of Charge Reduction for Protein Complexes.
Walker, T. E.; Shirzadeh, M.; Sun, He Mirabel; McCabe, J. W.; 1 Roth, A.; Moghadamchargari, Z.; Clemmer, D. E.; Laganowsky, A.; Rye, H.; Russell, D. H. Temperature Regulates Stability, Ligand Binding (Mg2+ and ATP) and Stoichiometry of GroEL/GroES Complexes.
Walker, T.; Sun, H. M.; Gunnels, T.; Wysocki, V.; Laganowsky, A.; Rye, H.; Russell, D. Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time. ACS Cent. Sci. 2023, 9 (3), 466–475. https://doi.org/10.1021/acscentsci.2c01065.
Woodall, D. W.; Brown, C. J.; Raab, S. A.; El-Baba, T. J.; Laganowsky, A.; Russell, D. H.; Clemmer, D. E. Melting of Hemoglobin in Native Solutions as Measured by IMS-MS.
Woodall, D.W.; El-Baba, T.J.; Fuller, D.R.; Liu, W.; Brown, C.J.; Laganowsky, A.; Russell, D.H.; Clemmer, D.E. Variable-Temperature ESI-IMS-MS Analysis of Myohemerythrin Reveals Ligand Losses, Unfolding, and a Non-Native Disulfide Bond.
Woodall, N. B.; Weinberg, Z.; Park, J.; Busch, F.; Johnson, R. S.; Feldbauer, M. J.; Murphy, M.; Ahlrichs, M.; Yousif, I.; MacCoss, M. J.; Wysocki, V. H.; El-Samad, H.; Baker, D. De Novo Design of Tyrosine and Serine Kinase-Driven Protein Switches.
Yang, K. S.; Blankenship, L. R.; Kuo, S.-T. A.; Sheng, Y. J.; Li, P.; Fierke, C. A.; Russell, D. H.; Yan, X.; Xu, S.; Liu, W. R. A Novel Y-Shaped, S–O–N–O–S-Bridged Cross-Link between Three Residues C22, C44, and K61 Is Frequently Observed in the SARS-CoV-2 Main Protease. ACS Chem. Biol. 2023, 18 (3), 449–455. https://doi.org/10.1021/acschembio.2c00695.
Yang, K. S.; Kuo, Sy.-T. Alex; Blankenship, L. R.; Sheng, Y. J.; Sankaran, B.; Li, Pingwei; Fierke, C. A.; Russell, D. H.; Yan, X.; Xu, S.; Liu, W. R. A novel Y-shaped, S-O-N-O-S-bridged crosslink between three residues C22, C44, and K61 is a redox switch of the SARS-CoV-2 main protease.
Yun, S. D.; Scott, E.; Moghadamchargari, Z.; Laganowsky, A. 2′-Deoxy Guanosine Nucleotides Alter the Biochemical Properties of Ras. Biochemistry 2023, 62 (16), 2450–2460. https://doi.org/10.1021/acs.biochem.3c00258.
Zahurancik, W.J.; Norris, A.S.; Lai, S.M.; Snyder, D.T.; Wysocki, V.H.; Gopalan, V. Purification, Reconstitution, and Mass Analysis of Archaeal RNase P, a Multisubunit Ribonucleoprotein Enzyme.
Zhang, S.; Yoo, S.; Snyder, D. T.; Katz, B. B.; Henrickson, A.; Demeler, B.; Wysocki, V. H.; Kreutzer, A. G.; Nowick, J. S. A Disulfide-Stabilized Aβ That Forms Dimers but Does Not Form Fibrils.
Zhang, T.; Lyu, J.; Zhu, Y.; Laganowsky, A. Cardiolipin Regulates the Activity of the Mitochondrial ABC Transporter ABCB10. Biochemistry 2023, 62 (21), 3159–3165. https://doi.org/10.1021/acs.biochem.3c00417.
Zheng, X.; Kurulugama, R. T.; Laganowsky, A.; Russell, D.H. Collision-Induced Unfolding Studies of Proteins and Protein Complexes using Drift Tube Ion Mobility-Mass Spectrometer.
Zhu, Y.; Peng, B.-J.; Kumar, S.; Stover, L.; Chang, J.-Y.; Lyu, J.; Zhang, T.; Schrecke, S.; Azizov, D.; Russell, D. H.; Fang, L.; Laganowsky, A. Polyamine Detergents Tailored for Native Mass Spectrometry Studies of Membrane Proteins. Nat Commun 2023, 14 (1), 5676. https://doi.org/10.1038/s41467-023-41429-w.
Zhu, Y.; Schrecke, S.; Tang, S.; Odenkirk, M. T.; Walker, T.; Stover, L.; Lyu, J.; Zhang, T.; Russell, D.; Baker, E. S.; Yan, X.; Laganowsky, A. Cupric Ions Selectively Modulate TRAAK–Phosphatidylserine Interactions.
Zhu, Y.; Yun, S. D.; Zhang, T.; Chang, J.-Y.; Stover, L.; Laganowsky, A. Native Mass Spectrometry of Proteoliposomes Containing Integral and Peripheral Membrane Proteins. Chem. Sci. 2023, 14 (48), 14243–14255. https://doi.org/10.1039/D3SC04938H.

Native MS Guided Structural Biology Center

Georgia Institute of Technology