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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
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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.
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Chem. Rev. 2021. https://doi.org/10.1021/acs.chemrev.1c00309.
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Annu Rev Biophys. 2021 Dec 21. doi: 10.1146/annurev-biophys-102221-101121. Epub ahead of print. PMID: 34932911.
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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.
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Cancer Res 2021, 81 (16), 4194–4204. https://doi.org/10.1158/0008-5472.CAN-20-3199
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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.
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International Journal of Mass Spectrometry 2021, 461, 116503. https://doi.org/10.1016/j.ijms.2020.116503.
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Science, 2021, 371 (6531), eabc8182, DOI: 10.1126/science.abc8182
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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
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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.
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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
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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.
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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.
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