Recent technological developments for native mass spectrometry

Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry

Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370 · see citing works

Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process

Zubarev, R. A., Kelleher, N. L., & McLafferty, F. W. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973478k · Cited by 1,881 · see citing works

Ion mobility–mass spectrometry analysis of large protein complexes

Ruotolo, B. T., Benesch, J. L. P., Sandercock, A. M., Hyung, S., & Robinson, C. V. (2008) · Nature Protocols · doi:10.1038/nprot.2008.78 · Cited by 1,095 · see citing works

Collision Cross Sections of Proteins and Their Complexes: A Calibration Framework and Database for Gas-Phase Structural Biology

Bush, M. F., Hall, Z., Giles, K., Hoyes, J. B., Robinson, C. V., & Ruotolo, B. T. (2010) · Analytical Chemistry · doi:10.1021/ac1022953 · Cited by 798 · see citing works

Membrane proteins bind lipids selectively to modulate their structure and function

Laganowsky, A. D., Reading, E., Allison, T. M., Ulmschneider, M. B., Degiacomi, M. T., Baldwin, A. J., & Robinson, C. V. (2014) · Nature · doi:10.1038/nature13419 · Cited by 786 · see citing works

Theory of plasma chromatography/gaseous electrophoresis. Review

Revercomb, H. E., & Mason, E. A. (1975) · Analytical Chemistry · doi:10.1021/ac60357a043 · Cited by 770 · see citing works

Native Mass Spectrometry: What is in the Name?

Leney, A. C., & Heck, A. J. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1545-3 · Cited by 602 · see citing works

Conformational Ordering of Biomolecules in the Gas Phase: Nitrogen Collision Cross Sections Measured on a Prototype High Resolution Drift Tube Ion Mobility-Mass Spectrometer

May, J. C., Goodwin, C. R., Lareau, N. M., Leaptrot, K. L., Morris, C. B., Kurulugama, R. T., Mordehai, A. V., Klein, C., Barry, W., Darland, E. J., et al. (2014) · Analytical Chemistry · doi:10.1021/ac4038448 · Cited by 404 · see citing works

Principles of collisional activation in analytical mass spectrometry

McLuckey, S. A. (1992) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(92)85001-z · Cited by 400 · see citing works

Fundamentals of Trapped Ion Mobility Spectrometry

Michelmann, K., Silveira, J. A., Ridgeway, M. E., & Park, M. A. (2014) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-014-0999-4 · Cited by 379 · see citing works

Enhancements in travelling wave ion mobility resolution

Giles, K., Williams, J. P., & Campuzano, I. D. G. (2011) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.5013 · Cited by 369 · see citing works

Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules

Brodbelt, J. S., Morrison, L. J., & Santos, I. C. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00440 · Cited by 291 · see citing works

21 Tesla Fourier Transform Ion Cyclotron Resonance Mass Spectrometer: A National Resource for Ultrahigh Resolution Mass Analysis

Hendrickson, C. L., Quinn, J. P., Kaiser, N. K., Smith, D. F., Blakney, G. T., Chen, T., Marshall, A. G., Weisbrod, C. R., & Beu, S. C. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1182-2 · Cited by 278 · see citing works

Ion dynamics in a trapped ion mobility spectrometer

Hernandez, D. R., DeBord, J. D., Ridgeway, M. E., Kaplan, D. A., Park, M. A., & Fernandez-Lima, F. A. (2014) · The Analyst · doi:10.1039/c3an02174b · Cited by 271 · see citing works

Collision induced unfolding of isolated proteins in the gas phase: past, present, and future

Dixit, S. M., Polasky, D. A., & Ruotolo, B. T. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.11.010 · Cited by 235 · see citing works

High Resolution Trapped Ion Mobility Spectrometery of Peptides

Silveira, J. A., Ridgeway, M. E., & Park, M. A. (2014) · Analytical Chemistry · doi:10.1021/ac501261h · Cited by 197 · see citing works

Resolving heterogeneous macromolecular assemblies by Orbitrap-based single-particle charge detection mass spectrometry

Wörner, T. P., Snijder, J., Bennett, A., Agbandje-McKenna, M., Makarov, A. A., & Heck, A. J. R. (2020) · Nature Methods · doi:10.1038/s41592-020-0770-7 · Cited by 186 · see citing works

Expanding the structural analysis capabilities on an Orbitrap-based mass spectrometer for large macromolecular complexes

Fort, K. L., van de Waterbeemd, M., Boll, D., Reinhardt-Szyba, M., Belov, M. E., Sasaki, E., Zschoche, R., Hilvert, D., Makarov, A. A., & Heck, A. J. R. (2018) · The Analyst · doi:10.1039/c7an01629h · Cited by 122 · see citing works

21 Tesla Fourier Transform Ion Cyclotron Resonance Mass Spectrometer Greatly Expands Mass Spectrometry Toolbox

Shaw, J., Lin, T., Leach, F. E., Tolmachev, A. V., Tolić, N., Robinson, E. W., Koppenaal, D., & Paša‐Tolić, L. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1507-9 · Cited by 116 · see citing works

Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure

Stiving, A. Q., VanAernum, Z. L., Büsch, F., Harvey, S. R., Sarni, S. H., & Wysocki, V. H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05071 · Cited by 107 · see citing works

Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure

Lermyte, F., Valkenborg, D., Loo, J., & Sobott, F. (2018) · Mass spectrometry reviews (Print) · doi:10.1002/mas.21560 · Cited by 101 · see citing works

On the Dynamics of Fragment Isomerization in Collision-Induced Dissociation of Peptides

Polfer, N. C., Bohrer, B. C., Plasencia, M. D., Paizs, B., & Clemmer, D. E. (2008) · The Journal of Physical Chemistry A · doi:10.1021/jp0763937 · Cited by 90 · see citing works

Fourier Transform-Ion Mobility-Orbitrap Mass Spectrometer: A Next-Generation Instrument for Native Mass Spectrometry

Poltash, M. L., McCabe, J. W., Shirzadeh, M., Laganowsky, A. D., Clowers, B. H., & Russell, D. H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02463 · Cited by 79 · see citing works

Targeted High-Resolution Ion Mobility Separation Coupled to Ultrahigh-Resolution Mass Spectrometry of Endocrine Disruptors in Complex Mixtures

Benigni, P., Thompson, C. J., Ridgeway, M. E., Park, M. A., & Fernandez-Lima, F. A. (2015) · Analytical Chemistry · doi:10.1021/ac504866v · Cited by 78 · see citing works

Noncovalent Protein Tetramers and Pentamers with “n” Charges Yield Monomers with n/4 and n/5 Charges

Beardsley, R. L., Jones, C. M., Galhena, A. S., & Wysocki, V. H. (2009) · Analytical Chemistry · doi:10.1021/ac801883k · Cited by 76 · see citing works

Tandem trapped ion mobility spectrometry

Liu, F. C., Ridgeway, M. E., Park, M. A., & Bleiholder, C. (2018) · The Analyst · doi:10.1039/c7an02054f · Cited by 76 · see citing works

Development of an Ion Mobility Spectrometry-Orbitrap Mass Spectrometer Platform

Ibrahim, Y., Garimella, S., Prost, S. A., Wojcik, R., Norheim, R. V., Baker, E. S., Rusyn, I., & Smith, R. D. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b03027 · Cited by 74 · see citing works

Enhanced Collision Induced Unfolding and Electron Capture Dissociation of Native-like Protein Ions

Gadkari, V. V., Ramírez, C. R., Vallejo, D. D., Kurulugama, R. T., Fjeldsted, J. C., & Ruotolo, B. T. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03372 · Cited by 72 · see citing works

The Effects of Sodium Ions on Ligand Binding and Conformational States of G Protein-Coupled Receptors—Insights from Mass Spectrometry

Agasid, M. T., Sørensen, L., Urner, L. H., Yan, J., & Robinson, C. V. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c11837 · Cited by 69 · see citing works

Heterogeneity of Glycan Processing on Trimeric SARS-CoV-2 Spike Protein Revealed by Charge Detection Mass Spectrometry

Miller, L. M., Barnes, L. F., Raab, S. A., Draper, B. E., El‐Baba, T. J., Lutomski, C. A., Robinson, C. V., Clemmer, D. E., & Jarrold, M. F. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c00353 · Cited by 66 · see citing works

Chemical Probes and Engineered Constructs Reveal a Detailed Unfolding Mechanism for a Solvent-Free Multidomain Protein

Eschweiler, J. D., Martini, R. M., & Ruotolo, B. T. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b11678 · Cited by 65 · see citing works

Recent Developments in Gas-Phase Ion/Ion Reactions for Analytical Mass Spectrometry

Foreman, D. J., & McLuckey, S. A. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05014 · Cited by 65 · see citing works

Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry

Morrison, L. J., & Brodbelt, J. S. (2015) · The Analyst · doi:10.1039/c5an01819f · Cited by 61 · see citing works

Confirmation of intersubunit connectivity and topology of designed protein complexes by native MS

Sahasrabuddhe, A., Hsia, Y., Büsch, F., Sheffler, W., King, N. P., Baker, D. A., & Wysocki, V. H. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713646115 · Cited by 60 · see citing works

Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry

Lermyte, F., Everett, J. L., Lam, Y. P. Y., Wootton, C. A., Brooks, J., Barrow, M. P., Telling, N. D., Sadler, P. J., O’Connor, P. B., & Collingwood, J. F. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02283-7 · Cited by 57 · see citing works

Cyclic Ion Mobility–Collision Activation Experiments Elucidate Protein Behavior in the Gas Phase

Eldrid, C., Ben-Younis, A., Ujma, J., Britt, H. M., Cragnolini, T., Kalfas, S., Cooper-Shepherd, D. A., Tomczyk, N., Giles, K., Morris, M., et al. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00018 · Cited by 56 · see citing works

Higher Resolution Charge Detection Mass Spectrometry

Todd, A. R., Barnes, L. F., Young, K., Zlotnick, A., & Jarrold, M. F. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02133 · Cited by 55 · see citing works

Simple and Minimally Invasive SID Devices for Native Mass Spectrometry

Snyder, D. T., Panczyk, E. M., Somogyi, Á., Kaplan, D. A., & Wysocki, V. H. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c01657 · Cited by 54 · see citing works

Expanding the mass range for UVPD-based native top-down mass spectrometry

Greisch, J.-F., Tamara, S., Scheltema, R. A., Maxwell, H. W. R., Fagerlund, R. D., Fineran, P. C., Tetter, S., Hilvert, D., & Heck, A. J. R. (2019) · Chemical Science · doi:10.1039/c9sc01857c · Cited by 47 · see citing works

Charge Movement and Structural Changes in the Gas-Phase Unfolding of Multimeric Protein Complexes Captured by Native Top-Down Mass Spectrometry

Zhou, M., Liu, W., & Shaw, J. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03469 · Cited by 45 · see citing works

Top-Down Characterization of Denatured Proteins and Native Protein Complexes Using Electron Capture Dissociation Implemented within a Modified Ion Mobility-Mass Spectrometer

Williams, J. P., Morrison, L., Brown, J., Beckman, J., Voinov, V. G., & Lermyte, F. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b04763 · Cited by 43 · see citing works

Enhanced Characterization of Membrane Protein Complexes by Ultraviolet Photodissociation Mass Spectrometry

Sipe, S. N., Patrick, J. W., Laganowsky, A., & Brodbelt, J. S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03689 · Cited by 39 · see citing works

Native Mass Spectrometry, Ion Mobility, Electron-Capture Dissociation, and Modeling Provide Structural Information for Gas-Phase Apolipoprotein E Oligomers

Wang, H., Eschweiler, J. D., Cui, W., Zhang, H., Frieden, C., Ruotolo, B. T., & Gross, M. L. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02148-z · Cited by 36 · see citing works

Native mass spectrometry and gas-phase fragmentation provide rapid and in-depth topological characterization of a PROTAC ternary complex

Song, J. H., Wagner, N. D., Yan, J. R., Li, J., Huang, R. Y. ‐., Balog, A., Newitt, J. A., Chen, G., & Gross, M. L. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.05.005 · Cited by 31 · see citing works

Assessment of biosimilarity under native and heat-stressed conditions: rituximab, bevacizumab, and trastuzumab originators and biosimilars

Kang, J., Halseth, T. A., Vallejo, D. D., Najafabadi, Z. I., Sen, K. I., Ford, M., Ruotolo, B. T., & Schwendeman, A. A. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-02298-9 · Cited by 25 · see citing works

Prediction of Protein Complex Structure Using Surface-Induced Dissociation and Cryo-Electron Microscopy

Seffernick, J. T., Canfield, S. M., Harvey, S. R., Wysocki, V. H., & Lindert, S. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c05468 · Cited by 23 · see citing works

Mapping a Conformational Epitope of Hemagglutinin A Using Native Mass Spectrometry and Ultraviolet Photodissociation

Mehaffey, M. R., Lee, J., Jung, J., Lanzillotti, M. B., Escobar, E. E., Morgenstern, K. R., Georgiou, G., & Brodbelt, J. S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02237 · Cited by 21 · see citing works

An Ion Mobility and Gas-Phase Covalent Labeling Study of the Structure and Reactivity of Gaseous Ubiquitin Ions Electrosprayed from Aqueous and Denaturing Solutions

Carvalho, V. V., Kit, M. C. S., & Webb, I. K. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00138 · Cited by 20 · see citing works

Collision-Induced Unfolding Differentiates Functional Variants of the KCNQ1 Voltage Sensor Domain

Fantin, S. M., Huang, H., Sanders, C. R., & Ruotolo, B. T. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00288 · Cited by 18 · see citing works

Gas-phase ion/ion chemistry for structurally sensitive probes of gaseous protein ion structure: Electrostatic and electrostatic to covalent cross-linking

Kit, M. C. S., Carvalho, V. V., Vilseck, J. Z., & Webb, I. (2021) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2021.116549 · Cited by 16 · see citing works

Determination of the Aggregate Binding Site of Amyloid Protofibrils Using Electron Capture Dissociation Tandem Mass Spectrometry

Lam, Y. P. Y., Wootton, C. A., Hands-Portman, I., Wei, J., Chiu, C. K. C., Romero‐Canelón, I., Lermyte, F., Barrow, M. P., & O’Connor, P. B. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00053 · Cited by 14 · see citing works

Top-Down Analysis of In-Source HDX of Native Protein Ions

Sanguantrakun, N., Chanthamontri, C., & Gross, M. L. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00149 · Cited by 13 · see citing works

Experimental Determination of Activation Energies for Covalent Bond Formation via Ion/Ion Reactions and Competing Processes

Kit, M. C. S., Shepherd, S. O., Prell, J. S., & Webb, I. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00025 · Cited by 13 · see citing works

Solution Condition-Dependent Formation of Gas-Phase Protomers of Alpha-Synuclein in Electrospray Ionization

Lermyte, F., Theisen, A., & O’Connor, P. B. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00373 · Cited by 12 · see citing works

Kinetic Theory of Mobility and Diffusion: Sections 5.1 – 5.2

(1988) · doi:10.1002/3527602852.ch5a · Cited by 8 · see citing works

Native top‐down mass spectrometry for higher‐order structural characterization of proteins and complexes

Liu, R., Xia, S., & Li, H. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21793 · Cited by 59 · see citing works

Analytical methods for obtaining binding parameters of drug–protein interactions: A review

Wang, L., Zhang, W., Shao, Y., Zhang, D., Guo, G., & Wang, X. (2022) · Analytica Chimica Acta · doi:10.1016/j.aca.2022.340012 · Cited by 56 · see citing works

Native metabolomics identifies the rivulariapeptolide family of protease inhibitors

Reher, R., Aron, A. T., Fajtová, P., Stincone, P., Wagner, B., Pérez-Lorente, A. I., Liu, C., Shalom, I. Y. B., Bittremieux, W., Wang, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32016-6 · Cited by 53 · see citing works

A systematic review on the recent advances of wheat allergen detection by mass spectrometry: future prospects

Lu, Y., Ji, H., Chen, Y., Li, Z., & Timira, V. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2101091 · Cited by 23 · see citing works

Mass spectrometric insights into protein aggregation

Pukala, T. L. (2023) · Essays in Biochemistry · doi:10.1042/ebc20220103 · Cited by 19 · see citing works

Simultaneous Native Mass Spectrometry Analysis of Single and Double Mutants To Probe Lipid Binding to Membrane Proteins

Jayasekera, H. S., Mohona, F. A., Ewbank, M. A., & Marty, M. T. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c01704 · Cited by 18 · see citing works

Expanding Orbitrap Collision Cross-Section Measurements to Native Protein Applications Through Kinetic Energy and Signal Decay Analysis

James, V. K., Sanders, J. D., Aizikov, K., Fort, K. L., Grinfeld, D., Makarov, A., & Brodbelt, J. S. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00594 · Cited by 16 · see citing works

Mass spectrometry DDA parameters and global coverage of the metabolome: Spectral molecular networks of momordica cardiospermoides plants

Ramabulana, A., Petras, D., Madala, N. E., & Tugizimana, F. (2023) · Metabolomics · doi:10.1007/s11306-023-01981-4 · Cited by 13 · see citing works

Multiplexed Conformationally Selective, Localized Gas-Phase Hydrogen Deuterium Exchange of Protein Ions Enabled by Transmission-Mode Electron Capture Dissociation

Chaturvedi, R., & Webb, I. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c00942 · Cited by 13 · see citing works

Native mass spectrometry for the investigation of protein structural (dis)order

Santambrogio, C., Ponzini, E., & Grandori, R. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140828 · Cited by 13 · see citing works

Top-Down Proteomics and Comparative 2D-DIGE Analysis

Ohlendieck, K. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2831-7_2 · Cited by 11 · see citing works

Self-packed size-exclusion columns enable versatile high-throughput native, top-down, and ion mobility-mass spectrometry studies on proteins and complexes

Maciel, E. V. S., Habeck, T., Meyners, C., & Lermyte, F. (2025) · Talanta · doi:10.1016/j.talanta.2025.127868 · Cited by 9 · see citing works

Rehydration Post-orientation: Investigating Field-Induced Structural Changes via Computational Rehydration

Brodmerkel, M. N., Santis, E. D., Caleman, C., & Marklund, E. G. (2023) · The Protein Journal · doi:10.1007/s10930-023-10110-y · Cited by 7 · see citing works

LILBID-MS: using lasers to shed light on biomolecular architectures

Hellwig, N., Martin, J., & Morgner, N. (2022) · Biochemical Society Transactions · doi:10.1042/bst20190881 · Cited by 11 · see citing works

Proteomic tools to study phosphorylation of intrinsically disordered proteins

Spolaore, B., Secco, L., Rocca, G., Manfioletti, G., Arrigoni, G., & Sgarra, R. (2023) · Expert Review of Proteomics · doi:10.1080/14789450.2023.2217359 · Cited by 5 · see citing works

FLASHApp: Interactive Data Analysis and Visualization for Top‐Down Proteomics

Müller, T. D., Kim, J., Almaguer, A., Feroz, A., Kim, J., Walter, A., Jung, W., Kohlbacher, O., & Jeong, K. (2025) · PROTEOMICS · doi:10.1002/pmic.70042 · Cited by 4 · see citing works

Tracking Inhibition of Human Small C-Terminal Domain Phosphatase 1 Using 193 nm Ultraviolet Photodissociation Mass Spectrometry

Escobar, E. E., Yang, W., Lanzillotti, M. B., Juetten, K. J., Shields, S., Siegel, D. R., Zhang, Y., & Brodbelt, J. S. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00098 · Cited by 3 · see citing works

A blurry view of fuzzy objects: on the roles of low-resolution structural techniques in discovery and early characterization of intrinsically disordered proteins

Uversky, V. N. (2025) · Frontiers in Biophysics · doi:10.3389/frbis.2025.1693360 · Cited by 3 · see citing works

Native mass spectrometry reveals binding interactions of SARS-CoV-2 PLpro with inhibitors and ISG15Preprint

James, V. K., Godula, R., Perez, J., Butalewicz, J. P., Sipe, S. N., Huibregtse, J. M., & Brodbelt, J. S. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-v6j35 · Cited by 2 · see citing works

Development and Validation of SEC-UV/HRMS Procedure for Simultaneous Determination of BSA and Its Association Products

Hodnik, B., Čamič, Ž., & Pompe, M. (2026) · Molecules · doi:10.3390/molecules31061001 · Cited by 1 · see citing works

Rehydration post-orientation: investigating field-induced structural changes via computational rehydrationPreprint

Brodmerkel, M. N., Santis, E. D., Caleman, C., & Marklund, E. G. (2023) · Research Square · doi:10.21203/rs.3.rs-2625748/v1

Experimental techniques for detecting and evaluating the amyloid fibrils

Farzam, F., & Dabirmanesh, B. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.03.004

Development of Electrostatic-to-Covalent Gas Phase Cross-linkers for Protein Structure Measurements by Mass Spectrometry

Black, K. L., & Webb, I. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00363

Integrated experimental and computational approaches to analyze TNF superfamily ligand–receptor interactions

Favier, A., Salama, C., Cervera, C., Riccobono, D., & Nikovics, K. (2026) · Cytokine · doi:10.1016/j.cyto.2025.157100

Early Detection of Parkinson's Disease through Microfluidics and Ion Mobility - Mass Spectrometry Integration

Figueiredo, I. D. (2024) · theses.fr (ABES) · doi:10.70675/e26318dazc588z42e6z90edz96ccb2ee6e71

Understanding aggregation of proteins in aqueous solutions and methods to study them

Rashid, M. I., Ansari, N. K., Naeem, A., & Rizvi, A. (2026) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2026.129625

Characterizing Antibody-Drug Conjugates with High Molecular Heterogeneity by Native Direct Mass Technology

Chu, P. Y., Fuller, K. E., Dockrey, S. A. B., Wang, I., Lin, C.-W., Harmon, L. P., Wang, D., Compton, P. D., Kafader, J. O., Kelleher, N. L., et al. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c00050

Application of mass spectrometry techniques for analysis of higher order structure of proteins

Herath, D., Walls, K. N., Dollar, A. N., & Webb, I. (2026) · The Analyst · doi:10.1039/d6an00710d

Investigating protein conformational ensembles by native mass spectrometry and complementary biophysical techniques—the case of α-synuclein

Brocca, S., Ponzini, E., Santambrogio, C., & Grandori, R. (2026) · Frontiers in Biophysics · doi:10.3389/frbis.2026.1887194

Native Mass Spectrometry as a Tool in Structural Biology

Lorenzen, K., & van Duijn, E. (2010) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1712s62 · Cited by 54 · see citing works

Revealing the Fates of Proteins in the Gas Phase

Webb, I. K. (2024) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2024.117312 · Cited by 8 · see citing works

Native Mass Spectrometry: Towards High-Throughput Structural Proteomics

Kondrat, F. D. L., Struwe, W. B., & Benesch, J. L. P. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2230-7_18 · Cited by 39 · see citing works

Mass spectrometry beyond the native state

Chandler, S. A., & Benesch, J. L. P. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.11.019 · Cited by 45 · see citing works

DEVELOPMENT OF GAS-PHASE METHODS FOR THE ELUCIDATION OF PROTEIN STRUCTURE USING MASS SPECTROMETRY

Black, K. L. (2026) · Purdue · doi:10.25394/pgs.33104222.v1