Publications

Publication of research in the scientific literature is key to build awareness of the capabilities of a native MS-guided integrated structural biology approach. We aim to publish advances in our technology research and development projects, as well as research with our collaborators in Driving Biomedical Projects (DBPs) and Collaboration and Service (C&S) projects.

Research supported by NIH P41 Resource

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.
Anal. Chem. 2022. https://doi.org/10.1021/acs.analchem.2c01869.
Li, W.; Norris, A. S.; Lichtenthal, K.; Kelly, S.; Ihms, E. C.; Gollnick, P.; Wysocki, V. H.; Foster, M. P. Mechanism of Homotropic Cooperativity from Nearest-Neighbor Statistical Thermodynamic Modelling and Native Mass Spectrometry of Ring-Shaped Homo-Oligomeric Ligand Binding Proteins
Biorxiv, 2022. https://doi.org/10.1101/2022.03.19.484990 (preprint)
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.
bioRxiv March 31, 2022, p 2022.03.30.486392. https://doi.org/10.1101/2022.03.30.486392.
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.
Nucleic Acids Research 2022, 50 (3), 1753–1769. https://doi.org/10.1093/nar/gkac032.
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.
Chemrxix, 2022. https://doi.org/10.26434/chemrxiv-2022-phxng
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.
J. Am. Chem. Soc. 2022, 144, 2667−2678. https://doi.org/10.1021/jacs.1c11341
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.
Journal of Molecular Biology 2022, 434 (7), 167480. https://doi.org/10.1016/j.jmb.2022.167480.
Karch, K. R.; Snyder, D. T.; Harvey, S. R.; Wysocki, V. H. Native Mass Spectrometry: Recent Progress and Remaining Challenges
Annual Review of Biophysics 2022, 51 (1). https://doi.org/10.1146/annurev-biophys-092721-085421.
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.
Anal. Chem. 2022, 94 (3), 1515–1519. https://doi.org/10.1021/acs.analchem.1c04322.
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.
Biochemistry 2022. https://doi.org/10.1021/acs.biochem.1c00739.
Snyder, D. T.; Harvey, S. R.; Wysocki, V. H. Surface-Induced Dissociation Mass Spectrometry as a Structural Biology Tool.
Chem. Rev. 2021. https://doi.org/10.1021/acs.chemrev.1c00309.
Laganowsky A, Clemmer DE, Russell DH. Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions.
Annu Rev Biophys. 2021 Dec 21. doi: 10.1146/annurev-biophys-102221-101121. Epub ahead of print. PMID: 34932911.
El-Baba, T. J.; Raab, S. A.; Buckley, R. P.; Brown, C. J.; Lutomski, C. A.; Henderson, L. W.; Woodall, D. W.; Shen, J.; Trinidad, J. C.; Niu, H.; Jarrold, M. F.; Russell, D. H.; Laganowsky, A.; Clemmer, D. E. Thermal Analysis of a Mixture of Ribosomal Proteins by VT-ESI-MS: Toward a Parallel Approach for Characterizing the Stabilitome.
Anal Chem 2021, 93 (24), 8484–8492. https://doi.org/10.1021/acs.analchem.1c00772
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.
J. Phys. Chem. Lett. 2021, 12, 51, 12218–12224 https://doi.org/10.1021/acs.jpclett.1c03750
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.
J. Am. Soc. Mass Spectrom. 2021, 32, 7, 1553–1561. PMID: 34151568
Harvey, S. R.; VanAernum, Z. L.; Wysocki, V. H. Surface-Induced Dissociation of Anionic vs Cationic Native-Like Protein Complexes.
J. Am. Chem. Soc. 2021. https://doi.org/10.1021/jacs.1c00855.
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.
Nat Struct Mol Biol 2021, 28 (9), 762–770. https://doi.org/10.1038/s41594-021-00649-8.
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.
Nucleic Acids Res 2021, 49 (16), 9444–9458. https://doi.org/10.1093/nar/gkab655.
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.
IJMS 2021, 22 (2), 718. https://doi.org/10.3390/ijms22020718.
Koenig, M. J.; Agana, B. A.; Kaufman, J. M.; Sharpnack, M. F.; Wang, W. Z.; Weigel, C.; Navarro, F. C. P.; Amann, J. M.; Cacciato, N.; Arasada, R. R.; Gerstein, M. B.; Wysocki, V. H.; Oakes, C.; Carbone, D. P. STK11/LKB1 Loss of Function Is Associated with Global DNA Hypomethylation and S-Adenosyl-Methionine Depletion in Human Lung Adenocarcinoma.
Cancer Res 2021, 81 (16), 4194–4204. https://doi.org/10.1158/0008-5472.CAN-20-3199
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.
J. Am. Soc. Mass Spectrom. 2021, 32 (12), 2812–2820. https://doi.org/10.1021/jasms.1c00245.
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.
Analyst 2021, 146 (22), 6861–6873. https://doi.org/10.1039/D1AN01407B.
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. 
Methods in Enzymology 2021, 659, 37-70. (Book chapter)
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.
Methods in Enzymology, 2021, 659, 71-103. (Book chapter)
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.
Anal. Chem. 2021. https://doi.org/10.1021/acs.analchem.0c05468.
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.
Cell Rep 2021, 35 (2), 108986. https://doi.org/10.1016/j.celrep.2021.108986.
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
Biochemistry 2021, 60 (24), 1876–1884. https://doi.org/10.1021/acs.biochem.1c00138.
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.
Metallomics 2021, 13 (mfab010). https://doi.org/10.1093/mtomcs/mfab010.
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.
Anal. Chem. 2021, acs.analchem.0c05373. https://doi.org/10.1021/acs.analchem.0c05373.
Snyder, D. T.; Lin, Y.-F.; Somogyi, A.; Wysocki, V. H. Tandem Surface-Induced Dissociation of Protein Complexes on an Ultrahigh Resolution Platform.
International Journal of Mass Spectrometry 2021, 461, 116503. https://doi.org/10.1016/j.ijms.2020.116503.
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
Science, 2021, 371 (6531), eabc8182, DOI: 10.1126/science.abc8182
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.
Proc Natl Acad Sci U S A 2021, 118 (17). https://doi.org/10.1073/pnas.2021569118.
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.
Nucleic Acids Research 2021, 49 (6), 3441–3460. https://doi.org/10.1093/nar/gkab125.
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.
Anal. Chem. 2021. https://doi.org/10.1021/acs.analchem.1c00870.
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.
Proc Natl Acad Sci USA 2021, 118 (12), e2022403118. https://doi.org/10.1073/pnas.2022403118.
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.
International Journal of Mass Spectrometry 2020, 458, 116451. https://doi.org/10.1016/j.ijms.2020.116451
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.
Mass Spectrometry Reviews 01 July 2020. https://doi.org/10.1002/mas.21642
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.
Anal. Chem. 2020, 92 (16), 11155–11163. https://doi.org/10.1021/acs.analchem.0c01285
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.
bioRxiv 2020, 2020.10.06.326603. https://doi.org/10.1101/2020.10.06.326603
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.
J. Am. Chem. Soc. 2020, 142 (41), 17372–17383. https://doi.org/10.1021/jacs.0c05365
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.
Proc Natl Acad Sci U S A 2021, 118 (23), e2015037118. https://doi.org/10.1073/pnas.2015037118.
Kang, M.; Doddapaneni, K.; Sarni, S.; Heppner, Z.; Wysocki, V.; Wu, Z. Solution Structure of the Nucleotide Hydrolase BlsM: Implication of Its Substrate Specificity.
Protein Science 2020, 29 (8), 1760–1773. https://doi.org/10.1002/pro.3812
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.
Anal. Chem. 2020, 92 (1), 49–66. https://doi.org/10.1021/acs.analchem.9b04718
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.
ACS Chem. Biol. 2021, 16 (11), 2315–2325. https://doi.org/10.1021/acschembio.1c00475.
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.
J Biol Chem 2020, 295 (42), 14391–14401. https://doi.org/10.1074/jbc.RA120.014835.
Snyder, D. T.; Harvey, S. R.; Busch, F.; Wysocki, V. H. Chapter 11:Surface-Induced Dissociation in Biomolecular Mass Spectrometry. In Advanced Fragmentation Methods.
Biomolecular Mass Spectrometry; 2020; pp 281–336. https://doi.org/10.1039/9781839161056-00281.
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
Chem. Commun. 2020. https://doi.org/10.1039/D0CC05531J
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
Nat Chem Biol 2020, 1–7. https://doi.org/10.1038/s41589-020-00659-5.
Dong, S.; Shirzadeh, M.; Fan, L.; Laganowsky, A.; Russell, D. H. Ag+ Ion Binding to Human Metallothionein-2A Is Cooperative and Domain Specific.
Anal. Chem. 2020, 92 (13), 8923–8932. https://doi.org/10.1021/acs.analchem.0c00829
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.
Anal. Chem. 2020, 92 (4), 3440–3446. https://doi.org/10.1021/acs.analchem.9b05561.
Leelananda, S. P.; Lindert, S. Using NMR Chemical Shifts and Cryo-EM Density Restraints in Iterative Rosetta-MD Protein Structure Refinement.
J. Chem. Inf. Model. 2020, 60 (5), 2522–2532. https://doi.org/10.1021/acs.jcim.9b00932
Agana, B. A.; Wysocki, V. H.; Schoenberg, D. R. Cytoplasmic MRNA Recapping Has Limited Impact on Proteome Complexity.
Open Biol. 2020, 10 (11), 200313. https://doi.org/10.1098/rsob.200313.
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.
J. Am. Soc. Mass Spectrom. 2020, 31 (11), 2313–2320. https://doi.org/10.1021/jasms.0c00259
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.
Biochemistry. 2020, DOI: 10.1021/acs.biochem.0c00352
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.
Anal. Chem. 2020, 92, 16, 11242-11. https://doi.org/10.1021/acs.analchem.0c01826
Snyder, D.T.; Panczyk, E.M.; Somogyi, A.; Kaplan, D.; Wysocki, V.H. Simple and Minimally Invasive SID Devices for Native Mass Spectrometry.
Anal. Chem. 2020, 92 (16), 11195–11203. https://doi.org/10.1021/acs.analchem.0c01657
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.
Science, 03 April 2020, 368, 6486, 78-84. DOI: 10.1126/science.aay2790
Stiving, A. Q.; Gilbert, J. D.; Jones, B. J.; Wysocki, V. H.; A Tilted Surface and Ion Carpet Array for SID.
Anal. Chem. 2020, 31, 458-462. DOI: 10.1021/jasms.9b00009
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.
ACS Cent. Sci. 2020, 6, 573-588. DOI:10.1021/acscentsci.0c00080
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.
Anal. Chem. 2020, 92, 10, 7218–7225. DOI: 10.1021/acs.analchem.0c00772
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.
J. Phys. Chem. B 2020, 124, 3, 461-469. DOI: 10.1021/acs.jpcb.9b08506 .
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.
Anal. Chem. 2020 March 17;92(6):4475-4483. DOI: 10.1021/acs.analchem.9b05519.
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.
Angewandte Chemie International Edition. 2020, DOI: 10.1002/anie.201915615
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.
J. Am. Chem. Soc. 2020, 142, 13, 6018-6029. DOI: 10.1021/jacs.9b11454
Shirzadeh, M.; Poltash, M.L.; Laganowsky, A.; Russell, D.H., Structural Analysis of the Effect of Dual-FLAG Tag on Transthyretin.
Biochemistry, 2020, 59, 9, 1013-1022. DOI: 10.1021/acs.biochem.0c00105.
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.
Anal. Chem. 2020, 92, 4, 3006-3013. DOI: 10.1021/acs.analchem.9b03994
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.
Anal. Chem., 2020 Feb 4; 92(3):2460-2467 DOI:10.1021/acs.analchem.9b03666.
Norris, A.; Busch, F.; Schupfner, M.; Sterner, R.; Wysocki, V.H. Quaternary structure of the tryptophan synthase α-subunit homolog BX1 from Zea mays,
J. Am. Soc. Mass. Spectrom., 2020 Feb 5; 31(2):227-233. DOI: 10.1021/jasms9b00068
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.
Nature Protocols 2020, DOI: 10.1038/s41596-019-0281-0
Poltash, M.L.; McCabe, J.W.; Shirzadeh, M.; Laganowsky,; Russell, D.H., Native IM-Orbitrap MS: Resolving what was hidden.
Trends in Analytical Chemistry, 2020, 124:115533. DOI: https://doi.org/10.1016/j.trac.2019.05.035
Pyles H, Zhang S, De Yoreo JJ, Baker D. Controlling protein assembly on inorganic crystals through designed protein interfaces.
Nature. 2019;571(7764):251‐256. doi:10.1038/s41586-019-1361-6
Seffernick, J. T.; Harvey, S. R.; Wysocki, V. H.; Lindert, S. Predicting Protein Complex Structure from Surface-Induced Dissociation Mass Spectrometry Data.
ACS Cent. Sci. 2019, 5 (8), 1330–1341. https://doi.org/10.1021/acscentsci.8b00912.
Liu, Y.; LoCaste, C.E.; Liu, W.; Poltash, M.L.; Russell, D.H.; Laganowsky, A., Selective binging of a toxin and phosphatidylinositides to a mammalian potassium channel.
Nat Commun 2019, 10 (1), 1352. https://doi.org/10.1038/s41467-019-09333-4.
Kim, S. S.; Aprahamian, M. L.; Lindert, S. Improving Inverse Docking Target Identification with Z-Score Selection.
Chemical Biology & Drug Design 2019, 93 (6), 1105–1116. https://doi.org/10.1111/cbdd.13453
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.
Anal. Chem. 2019, 91 (18), 11562–11568. https://doi.org/10.1021/acs.analchem.9b01456
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