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 publish advances in our technology optimization projects, as well as research with our collaborators in Driving Biomedical Projects (DBPs) and Collaboration and Service Projects (CSPs).

Center Publications: 2024

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.

Center Publications: 2019-2023

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.

Nat Struct Mol Biol 2022, 29 (12), 1266–1276. https://doi.org/10.1038/s41594-022-00879-4.

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.

Science, 2019, 364(6441):658-664. DOI: 10.1126/science.aav7897.

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.

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.

 Nat Commun 2022, 13 (1), 7855. https://doi.org/10.1038/s41467-022-35572-z.

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.

bioRxiv March 17, 2022, p 2022.03.17.484533. https://doi.org/10.1101/2022.03.17.484533.

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.

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

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

Drake, Z. C.; Seffernick, J. T.; Lindert, S.
Protein Complex Prediction Using Rosetta, AlphaFold, and Mass Spectrometry Covalent Labeling.

Nat Commun 2022, 13 (1), 7846. https://doi.org/10.1038/s41467-022-35593-8.

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.

ChemRxiv (2022), 1-13 | 10.26434/chemrxiv-2022-njhrw

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.

ACS Chem Neurosci 2022, 13 (16), 2473–2482. https://doi.org/10.1021/acschemneuro.2c00313.

Harvey, S. R.; Ben-Nissan, G.; Sharon, M.; Wysocki, V. H.
Surface-Induced Dissociation for Protein Complex Characterization.

Methods Mol Biol 2022, 2500, 211–237. https://doi.org/10.1007/978-1-0716-2325-1_15.

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.

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

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.

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.

PNAS, 2019; 116 (17)8143-8148. DOI 10.1073/pnas.1817632116.

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

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 

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.

Protein Science 2020, 29 (8), 1760–1773. https://doi.org/10.1002/pro.3812

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.

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

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.

Int. J. Molecular Sciences. 2019, 20, 5106.

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.

Cell Chemical Biology 2019, 19, 30271-5.

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.

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.

Anal. Chem. 2020, 92 (1), 49–66. https://doi.org/10.1021/acs.analchem.9b04718

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

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

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

International Journal of Mass Spectrometry 2022, 479, 116889. https://doi.org/10.1016/j.ijms.2022.116889.

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. 

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)

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.

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.

J. Chem. Inf. Model. 2020, 60 (5), 2522–2532. https://doi.org/10.1021/acs.jcim.9b00932

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.

Protein Sci 2022, 31 (10), e4424. https://doi.org/10.1002/pro.4424.

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.

Biochemistry 2022, 61, 23, 2733–2741. https://doi.org/10.1021/acs.biochem.2c00429

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

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.

Nature Communications, 2019 Mar 22;10(1):1352. DOI 10.1038/s41467-019-09333-4.

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

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

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.

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.

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.; 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.

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

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, 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.

Biochemistry. 2019 Aug 6;58(31):3396-3405. doi:10.1021/acs.biochem.9b00532.

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.

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

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.

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.

Anal. Chem., 2020 Feb 4; 92(3):2460-2467 DOI:10.1021/acs.analchem.9b03666. 

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.

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

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.

Nucleic Acids Res 2022, 50 (14), 8154–8167. https://doi.org/10.1093/nar/gkac595.

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 

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.

Chemical Communications, 2019, 55, 4091-4094. DOI 10.1039/C9CC00682F.

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.

Int. J. Molecular Sciences, 2019, 20, 5647

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

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

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

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.

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.

Proceedings of the National Academy of Sciences 2022, 119 (47), e2208780119. https://doi.org/10.1073/pnas.2208780119.

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.

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.
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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.  

Schupfner, M.; Busch F.; Wysocki, V.; Sterner, R.
Generation of a stand-alone tryptophan synthase α-subunit by mimicking an evolutionary blueprint.

Chembiochem, 2019,20,2747-2751. DOI: 10.1002/cbic.201900323. 

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.

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.

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.

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Biochemical Impact of a Disease-Causing Ile67Asn Substitution on BOLA3 Protein.

Metallomics 2021, 13 (mfab010). https://doi.org/10.1093/mtomcs/mfab010.

Shirzadeh, M.; Boone, C.D.; Laganowsky, A.; Russell, D.H.
Topological Analysis of Transthyretin Disassembly Mechanism: Surface-Induced Dissociation Reveals Hidden Reaction Pathways.

Analytical Chemistry, 2019, 91, 3, 2345-2351 DOI:10.1021/acs.analchem.8b05066

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. 

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 .

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.

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.

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.

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.

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.

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.

Anal. Chem. 2019, 91, 14049-14057. DOI: 10.1021/acs.analchem.9b03746

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

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.

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.

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

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.

Anal Chem., 2019, 91, 190-209.  DOI:10.1021/acs.analchem.8b05071.

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

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.

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.

Briefings in Bioinformatics 2023, bbad308. https://doi.org/10.1093/bib/bbad308.
 

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.

Nat Commun 2022, 13 (1), 4377. https://doi.org/10.1038/s41467-022-32075-9.

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

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.

Anal. Chem., 2019, 91, 3, 2345-2351. DOI: 10.1021/acs.analchem.8b05605.

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

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

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.

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.

Anal. Chem. 2022, 94 (30), 10824–10831. https://doi.org/10.1021/acs.analchem.2c01814.

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

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.

Anal. Chem. 2020, 92 (4), 3440–3446. https://doi.org/10.1021/acs.analchem.9b05561.

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.

Anal. Chem., 2019, 91,10,6808-6814. DOI: 10.1021/acs.analchem.9b00981

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.

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.

bioRxiv (2022), 1-20. doi: https://doi.org/10.1101/2022.04.29.490044.

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.

Methods in Enzymology, 2021, 659, 71-103. (Book chapter)

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.

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.

Anal. Chem. 2020, 92, 10, 7218–7225. DOI: 10.1021/acs.analchem.0c00772

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.

J. Am. Chem. Soc. 2022, 144 (16), 7048–7053. https://doi.org/10.1021/jacs.2c00612.

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.