An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes

Fourier transform ion cyclotron resonance mass spectrometry: A primer

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Proteoform: a single term describing protein complexity

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Current Protocols in Protein Science

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Native mass spectrometry: a bridge between interactomics and structural biology

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Three-dimensional structure of β-galactosidase from E. coli.

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Current Protocols in Protein Science

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Decoding protein modifications using top-down mass spectrometry

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Protein Complexes in the Gas Phase: Technology for Structural Genomics and Proteomics

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Design and Performance of a Second-Generation Surface-Induced Dissociation Cell for Fourier Transform Ion Cyclotron Resonance Mass Spectrometry of Native Protein Complexes

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Tandem Trapped Ion Mobility Spectrometry/Mass Spectrometry (tTIMS/MS) Reveals Sequence-Specific Determinants of Top-Down Protein Fragment Ion Cross Sections

Liu, F. C., Kirk, S. R., Caldwell, K. A., Pedrete, T. D. A., Meier, F., & Bleiholder, C. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.1c05171 · Cited by 23

Top-down mass spectrometry and assigning internal fragments for determining disulfide bond positions in proteins

Wei, B., Zenaidee, M. A., Lantz, C., Williams, B. J., Totten, S. M., Loo, R. R. O., & Loo, J. A. (2022) · The Analyst · doi:10.1039/d2an01517j · Cited by 21

Proteomic profiling of giant skeletal muscle proteins

Murphy, S., Dowling, P., Zweyer, M., Swandulla, D., & Ohlendieck, K. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1575205 · Cited by 21

High Mass Analysis with a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer: From Inorganic Salt Clusters to Antibody Conjugates and Beyond

Campuzano, I. D. G., Nshanian, M., Spahr, C. S., Lantz, C., Netirojjanakul, C., Li, H., Wongkongkathep, P., Wolff, J. J., & Loo, J. A. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00030 · Cited by 21

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

Pervasive Charge Solvation Permeates Native-like Protein Ions and Dramatically Influences Top-down Sequencing Data

Polasky, D. A., Dixit, S. M., Keating, M. F., Gadkari, V. V., Andrews, P., & Ruotolo, B. T. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c01076 · Cited by 20

Isotope Depletion Mass Spectrometry (ID-MS) for Accurate Mass Determination and Improved Top-Down Sequence Coverage of Intact Proteins

Gallagher, K. J., Palasser, M., Hughes, S., Mackay, C. L., Kilgour, D. P. A., & Clarke, D. J. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00119 · Cited by 18

Mass Analysis of Macro-molecular Analytes via Multiply-Charged Ion Attachment

Abdillahi, A. M., Lee, K. W., & McLuckey, S. A. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04335 · Cited by 22

Towards understanding the formation of internal fragments generated by collisionally activated dissociation for top-down mass spectrometry

Wei, B., Zenaidee, M. A., Lantz, C., Loo, R. R. O., & Loo, J. A. (2021) · Analytica Chimica Acta · doi:10.1016/j.aca.2021.339400 · Cited by 21

Recent advances in structural mass spectrometry methods in the context of biosimilarity assessment: from sequence heterogeneities to higher order structures

Castel, J.-G., Delaux, S., Hernandez‐Alba, O., & Cianférani, S. (2023) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2023.115696 · Cited by 21

Advances in mass spectrometry-based approaches for characterizing monoclonal antibodies: resolving structural complexity and analytical challenges

Mojumdar, A., Yoo, H.-J., Kim, D., Park, J., Park, S., Jeon, E., Choi, S., Choi, J. H., Park, M., Bang, G., et al. (2024) · Journal of Analytical Science & Technology · doi:10.1186/s40543-024-00437-1 · Cited by 19

Onto Grid Purification and 3D Reconstruction of Protein Complexes Using Matrix-Landing Native Mass Spectrometry

Lee, K. W., Salome, A. Z., Westphall, M. S., Grant, T., & Coon, J. J. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00595 · Cited by 18

Evaluation of a Commercial TIMS-Q-TOF Platform for Native Mass Spectrometry

Panczyk, E. M., Lin, Y.-F., Harvey, S. R., Snyder, D. T., Liu, F. C., Ridgeway, M. E., Park, M. A., Bleiholder, C., & Wysocki, V. H. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00320 · Cited by 17

Integrative Molecular Dynamics Simulations Untangle Cross‐Linking Data to Unveil Mitochondrial Protein Distributions

Schuhmann, F., Akkaya, K. C., Puchkov, D., Hohensee, S., Lehmann, M., Liu, F., & Pezeshkian, W. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202417804 · Cited by 18

Evolution of Mass Spectrometers for High m/z Biological Ion Formation, Transmission, Analysis and Detection: A Personal Perspective

Campuzano, I. D. G., & Loo, J. A. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00348 · Cited by 20

Internal Fragment Ions Disambiguate and Increase Identifications in Top-Down Proteomics

Rolfs, Z., & Smith, L. M. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00599 · Cited by 17

Fundamentals and Advances of Orbitrap Mass Spectrometry

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Two-Dimensional Partial Covariance Mass Spectrometry for the Top–Down Analysis of Intact Proteins

Driver, T., Averbukh, V., Frasinski, L. J., Marangos, J. P., & Edelson‐Averbukh, M. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c00332 · Cited by 16

High-Pressure Electrospray Ionization Yields Supercharged Protein Complexes from Native Solutions While Preserving Noncovalent Interactions

Yin, Z., Huang, J., Miao, H., Hu, O., & Li, H. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c01965 · Cited by 16

Relative Strength of Noncovalent Interactions and Covalent Backbone Bonds in Gaseous RNA–Peptide Complexes

Vušurović, J., & Breuker, K. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05387 · Cited by 16

An Orbitrap/Time-of-Flight Mass Spectrometer for Photofragment Ion Imaging and High-Resolution Mass Analysis of Native Macromolecular Assemblies

Mathew, A., Giskes, F., Lekkas, A., Greisch, J., Eijkel, G. B., Anthony, I. G. M., Fort, K. L., Heck, A. J. R., Papanastasiou, D. K., Makarov, A., et al. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00053 · Cited by 16

Online Mixed-Bed Ion Exchange Chromatography for Native Top-Down Proteomics of Complex Mixtures

Fischer, M. S., Rogers, H. T., Chapman, E. A., Chan, H., Krichel, B., Gao, Z., Larson, E. J., & Ge, Y. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00430 · Cited by 17

Reassembling protein complexes after controlled disassembly by top-down mass spectrometry in native mode

Schachner, L. F., Tran, D. P., Lee, A. S., McGee, J. P., Jooß, K., Durbin, K. R., Seckler, H. S., Adams, L. M., Cline, E. N., Melani, R. D., et al. (2021) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2021.116591 · Cited by 15

Insights into Phosphorylation-Induced Protein Allostery and Conformational Dynamics of Glycogen Phosphorylase via Integrative Structural Mass Spectrometry and In Silico Modeling

Huang, J., Chu, X., Luo, Y., Wang, Y., Zhang, Y., Zhang, Y., & Li, H. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00393 · Cited by 13

Integrated mass spectrometry strategy for functional protein complex discovery and structural characterization

Liu, Z., Chen, X., Yang, S., Tian, R., & Wang, F. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102305 · Cited by 15

Digital Quadrupole Isolation and Electron Capture Dissociation on an Extended Mass Range Q-TOF Provides Sequence and Structure Information on Proteins and Protein Complexes

Lantz, C., Schrader, R., Meeuwsen, J. C., Shaw, J., Goldberg, N. T., Tichy, S. E., Beckman, J., & Russell, D. H. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00184 · Cited by 12

Internal Fragments Enhance Middle-Down Mass Spectrometry Structural Characterization of Monoclonal Antibodies and Antibody-Drug Conjugates

Wei, B., Lantz, C., Loo, R. R. O., Campuzano, I. D. G., & Loo, J. A. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c04526 · Cited by 12

Origins and clinical relevance of proteoforms in pediatric malignancies

Lorentzian, A. C., Uzozie, A. C., & Lange, P. F. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1575206 · Cited by 14

Proteomics: Tools of the Trade

Bose, U., Wijffels, G. L., Howitt, C. A., & Colgrave, M. L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-12298-0_1 · Cited by 18

Native Top-Down Proteomics of Endogenous Protein Complexes Enabled by Online Two-Dimensional Liquid Chromatography

Fischer, M. S., Rogers, H. T., Chapman, E. A., Jin, S., & Ge, Y. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c02341 · Cited by 16

Determining the Location of the α-Synuclein Dimer Interface Using Native Top-Down Fragmentation and Isotope Depletion-Mass Spectrometry

Jeacock, K., Chappard, A., Gallagher, K. J., Mackay, C. L., Kilgour, D. P. A., Horrocks, M. H., Kunath, T., & Clarke, D. J. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00339 · Cited by 14

Photochemical bromination and iodination of peptides and proteins by photoexcitation of aqueous halides

Luo, P., Liu, Z., Zhang, T., Wang, X., Liu, J., Liu, Y., Zhou, X.-H., Chen, Y., Hou, G., Dong, W., et al. (2021) · Chemical Communications · doi:10.1039/d1cc04906b · Cited by 13

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

Microfluidic devices for protein analysis using intact and top‐down mass spectrometry

Shao, X., Huang, Y., & Wang, G. (2022) · Open Research (University of Surrey) · doi:10.1002/viw.20220032 · Cited by 15

Studying Membrane Protein–Lipid Specificity through Direct Native Mass Spectrometric Analysis from Tunable Proteoliposomes

Panda, A., Brown, C., & Gupta, K. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00110 · Cited by 14

Native Top-Down Mass Spectrometry for Characterizing Sarcomeric Proteins Directly from Cardiac Tissue Lysate

Chapman, E. A., Li, B. H., Krichel, B., Chan, H., Buck, K. M., Roberts, D. S., & Ge, Y. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00430 · Cited by 11

Achievable accuracy of resonating nanomechanical systems for mass sensing of larger analytes in GDa range

Stachiv, I., Machů, Z., Ševeček, O., Jeng, Y., Li, W.-L., Kotoul, M., & Prášek, J. (2022) · International Journal of Mechanical Sciences · doi:10.1016/j.ijmecsci.2022.107353 · Cited by 12

Interrogating the Quaternary Structure of Noncanonical Hemoglobin Complexes by Electrospray Mass Spectrometry and Collision-Induced Dissociation

Sever, A. I. M., Yin, V. C., & Konermann, L. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00320 · Cited by 12

Degronomics: Mapping the Interacting Peptidome of a Ubiquitin Ligase Using an Integrative Mass Spectrometry Strategy

Canzani, D., Rusnac, D.-V., Zheng, N., & Bush, M. F. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02331 · Cited by 11

Resolving the geometric structure of trastuzumab by mobility capillary electrophoresis and native mass spectrometry

Zhang, W., Hong, J., Yang, L., Xu, Z., Xiang, Y., & Xu, W. L. (2023) · Chinese Chemical Letters · doi:10.1016/j.cclet.2023.108695 · Cited by 11

Elucidating the molecular mechanisms of perfluorooctanoic acid-serum protein interactions by structural mass spectrometry

Zhang, W., Liu, Z., Zhou, Y., Lai, C., Sun, B., He, M., Zhai, Z., Wang, J., Wang, Q., Wang, X., et al. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.132945 · Cited by 11

Development of a High-Field “Brick” Mass Spectrometer with Extended Mass Range and Capable of Characterizing Native Proteins

Zhang, H., Jia, H., Hong, J., Zhang, M., Jiang, T., & Xu, W. L. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c01769 · Cited by 13

Testing the Robustness of Solution Force Fields for MD Simulations on Gaseous Protein Ions

Lee, J., Pollert, K., & Konermann, L. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b04014 · Cited by 11

A Conformation-Specific Approach to Native Top-down Mass Spectrometry

Britt, H. M., Ben-Younis, A., Page, N., & Thalassinos, K. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00361 · Cited by 10

Binding mechanism and distant regulation of histone deacetylase 8 by PCI-34051

Luo, Y., Yan, Z., Chu, X., Zhang, Y., Qiu, Y., & Li, H. (2025) · Communications Biology · doi:10.1038/s42003-025-07649-0 · Cited by 10

High-spatial-resolution multi-spectroscopic provides insights into the interaction and release of δ-decanolactone and decanoic acid with β-lactoglobulin

Zhang, R., & Jia, W. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107787 · Cited by 10

Native Top–Down Analysis of Membrane Protein Complexes Directly From In Vitro and Native Membranes

Jung, W., Panda, A., Lee, J., Ghosh, S., Shaw, J., & Gupta, K. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.100993 · Cited by 11

Exploring the Conformations and Binding Location of HMGA2·DNA Complexes Using Ion Mobility Spectrometry and 193 nm Ultraviolet Photodissociation Mass Spectrometry

Sipe, S. N., Fouque, K. J. D., Garabedian, A., Leng, F., Fernandez-Lima, F. A., & Brodbelt, J. S. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00083 · Cited by 9

High-Throughput, Quantitative Analysis of Peptide-Exchanged MHCI Complexes by Native Mass Spectrometry

Schachner, L. F., Phung, W., Han, G., Darwish, M., Bell, A., Mellors, J. S., Srzentić, K., Huguet, R., Blanchette, C., & Sandoval, W. N. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c02423 · Cited by 9

Decoding the molecular interplay in the central dogma: An overview of mass spectrometry‐based methods to investigate protein‐metabolite interactions

Stincone, P., Naimi, A., Saviola, A. J., Reher, R., & Petras, D. (2023) · PROTEOMICS · doi:10.1002/pmic.202200533 · Cited by 9

Atomistic Insights into the Formation of Nonspecific Protein Complexes during Electrospray Ionization

Aliyari, E., & Konermann, L. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c02836 · Cited by 8

Connecting ‘multi-omics’ approaches to endogenous protein complexes

Wu, D., & Robinson, C. V. (2021) · Trends in Chemistry · doi:10.1016/j.trechm.2021.03.007 · Cited by 8

Analysis of oligonucleotides by ion-pair reversed-phase liquid chromatography coupled with positive mode electrospray ionization mass spectrometry

Weng, G., Sun, B., Liu, Z., Wang, F., & Pan, Y. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-01819-w · Cited by 8

Infrared Multiphoton Dissociation Enables Top‐Down Characterization of Membrane Protein Complexes and G Protein‐Coupled Receptors

Lutomski, C. A., El‐Baba, T. J., Hinkle, J. D., Liko, I., Bennett, J. L., Kalmankar, N. V., Dolan, A., Kirschbaum, C., Greis, K., Urner, L. H., et al. (2023) · Angewandte Chemie · doi:10.1002/ange.202305694 · Cited by 8

Mass spectrometry: Raw protein from the top down.

Breuker, K. (2018) · Nature Chemistry · doi:10.1038/nchem.2936 · Cited by 6

Graph theory-based reaction pathway searches and DFT calculations for the mechanism studies of free radical-initiated peptide sequencing mass spectrometry (FRIPS MS): a model gas-phase reaction of GGR tri-peptide

Lee, J.-U., Kim, Y., Kim, W. Y., & Oh, H. B. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp05433b · Cited by 8

Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform

Snyder, D. T., Lin, Y.-F., Somogyi, Á., & Wysocki, V. H. (2021) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2020.116503 · Cited by 9

Programmable Plasma-Microdroplet Cascade Reactions for Multicomponent Systems

Grooms, A. J., Marcelo, I. M., Huttner, R. T., & Badu-Tawiah, A. K. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c07053 · Cited by 8

Advances in protein sequencing: Techniques, challenges and prospects

Luo, X., Ng, C. C. A., Lam, H., & Yao, Z. (2025) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2025.118341 · Cited by 7

Mass spectrometry-based proteomics in forensic investigations: a focused review of LC-MS applications

Athira Raj, T., Aravind, G. B., Arun, M., & Aneesh, E. M. (2025) · Egyptian Journal of Forensic Sciences · doi:10.1186/s41935-025-00484-8 · Cited by 7

Sample preparation for structural mass spectrometry via polyacrylamide gel electrophoresis

Takemori, A., & Takemori, N. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.051 · Cited by 7

In-depth structural proteomics integrating mass spectrometry and polyacrylamide gel electrophoresis

Takemori, N., & Takemori, A. (2023) · Frontiers in Analytical Science · doi:10.3389/frans.2022.1107183 · Cited by 8

Free Radical-Based Sequencing for Native Top-Down Mass Spectrometry

Rojas Ramírez, C., Murtada, R., Gao, J., & Ruotolo, B. T. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00252 · Cited by 7

Peptidomics as a Tool to Assess the Cleavage of Wine Haze Proteins by Peptidases from Drosophila suzukii Larvae

Albuquerque, W. W. C., Ghezellou, P., Lee, K., Schneider, Q., Gross, P., Kessel, T., Omokungbe, B., Spengler, B., Vilcinskas, A., Zorn, H., et al. (2023) · Biomolecules · doi:10.3390/biom13030451 · Cited by 7

Covalent Cross-Linking as an Enabler for Structural Mass Spectrometry

Hanozin, E., Grifnée, E., Gattuso, H., Matagne, A., Morsa, D., & Pauw, E. D. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02491 · Cited by 7

Probing Protein Interaction Networks by Combining MS-Based Proteomics and Structural Data Integration

Postic, G., Marcoux, J., Reys, V., Andréani, J., Vandenbrouck, Y., Bousquet, M., Mouton‐Barbosa, E., Cianférani, S., Burlet‐Schiltz, O., Guérois, R., et al. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00066 · Cited by 8

Native Top-Down Mass Spectrometry Characterization of Model Integral Membrane Protein Bacteriorhodopsin

Le, J., & Loo, J. A. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00439 · Cited by 6

Recent Advancements and Applications of Size Exclusion Chromatography in Modern Analysis

Bhatia, R., Kumari, Y., & Chopra, A. (2023) · Current Analytical Chemistry · doi:10.2174/1573411019666230526144816 · Cited by 7

Biofunctionalized dissolvable hydrogel microbeads enable efficient characterization of native protein complexes

Shao, X., Tian, M., Yin, J., Duan, H., Tian, Y., Wang, H. Z., Xia, C., Wang, Z., Zhu, Y., Wang, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52948-5 · Cited by 9

Native mass spectrometry prescreening of G protein-coupled receptor complexes for cryo-EM structure determination

Kim, D., Liu, W., Viner, R., & Cherezov, V. (2024) · Structure · doi:10.1016/j.str.2024.10.004 · Cited by 6

Dissecting Hidden Liraglutide Oligomerization Pathways via Direct Mass Technology, Electron-Capture Dissociation, and Molecular Dynamics

Kuo, S.-T. A., Xi, Z., Cong, X., Yan, X., & Russell, D. H. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c01851 · Cited by 6

Structural basis for L-isoaspartyl-containing protein recognition by the human PCMTD1 cullin-RING E3 ubiquitin ligase

Pang, E. Z., Zhao, B., Flowers, C., Oroudjeva, E., Winter, J. B., Pandey, V., Sawaya, M. R., Wohlschlegel, J. A., Loo, J. A., Rodríguez, J. A., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110735 · Cited by 5

Advancing Native Mass Spectrometry Toward Cellular Biology

Saikusa, K. (2024) · Journal of Mass Spectrometry · doi:10.1002/jms.5095 · Cited by 5

Rational Design of a Foldon-Derived Heterotrimer Guided by Quantitative Native Mass Spectrometry

Liu, X., Roberts, D. S., Bingman, C. A., Jin, S., Ge, Y., & Ge, Y. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c06094 · Cited by 4

Oxidative aggregation of hemoglobin–a mechanism for low-temperature plasma-mediated wound healing

Oganesyan, I., Begley, A., Mrđenović, D., Harrison, J. A., & Zenobi, R. (2024) · Journal of Physics D Applied Physics · doi:10.1088/1361-6463/ad6e99 · Cited by 5

Roughhousing with Ions: Surface-Induced Dissociation and Electron Capture Dissociation as Diagnostics of Q-Cyclic IMS-TOF Instrument Tuning Gentleness

Arslanian, A. J., & Wysocki, V. H. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00417 · Cited by 6

Solving Complex Biologics Truncation Problems by Top-Down Mass Spectrometry

Zhang, Z., Hug, C., Tao, Y., Bitsch, F., & Yang, Y. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00343 · Cited by 5

Mass Spectrometry and Its Applications

Jovcevski‬, B., & Pukala, T. L. (2019) · Wiley eBooks · doi:10.1002/9781119483977.ch10 · Cited by 5

Structural Heterogeneity of Proteoform-Ligand Complexes in Adenosine Monophosphate-Activated Protein Kinase Uncovered by Integrated Top-Down Mass Spectrometry

Chan, H., Krichel, B., Bandura, L. J., Chapman, E. A., Rogers, H. T., Fischer, M. S., Roberts, D. S., Gao, Z., Wang, M., Wu, J., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c06950 · Cited by 7

Retention and Rearrangement of Membrane Protein Complexes’ Higher Order Structure by Collisionally Activated Dissociation- and Electron Capture Dissociation-Mass Spectrometry

Le, J., Jung, W., Arbing, M. A., Egea, P. F., Loo, R. R. O., & Loo, J. A. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c05797 · Cited by 4

Simultaneous Quantification of Apolipoprotein C-III O-Glycoforms by Protein-MRM

Kim, H., Cheon, D. H., Yang, W. S., & Baek, J. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00490 · Cited by 4

Improved Annotation of Internal Fragments via Trapped‐Ion Mobility Enhanced Top‐Down Sequencing of Protein Ions

Graham, K., Lawlor, C., Reddy, R. S., Prertprawnon, S., Akinola, O., Grisolia, V. J., Kunwor, K., & Borotto, N. B. (2025) · Journal of Mass Spectrometry · doi:10.1002/jms.5158 · Cited by 3

Dual Electrospray Ionization Enhancement of Proteins Enabled by DMSO Supercharging Reagent

Eremin, D. B., & Fokin, V. V. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00280 · Cited by 4

Multiplexed screening of thousands of natural products for protein-ligand binding in native mass spectrometryPreprint

Nguyen, G. T. H., Bennett, J., Liu, S., Hancock, S. E., Winter, D. L., Glover, D. J., & Donald, W. A. (2021) · doi:10.33774/chemrxiv-2021-sc39c-v2 · Cited by 4

A Research Journey: Over a Decade of Denaturing and Native-MS Analyses of Hydrophobic and Membrane Proteins in Amgen Therapeutic Discovery

Campuzano, I. D. G. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00175 · Cited by 4

Dynamic Spray Mass Spectrometry for Direct Analysis of Complex Mixtures

Damale, P. S., Kulyk, D. S., Zumock, A. P., & Badu-Tawiah, A. K. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c04327 · Cited by 3

Native Multidimensional Protein Complex Identification and Topology Characterization (Native MudPIT)

Qi, Z., Fang, F., Moeller, W. J., Zhu, G., Wang, Q., Wang, Q., Gao, G., Sun, L., & Wysocki, V. H. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c01693 · Cited by 4

Quantitative Mapping of NHS Ester–Protein Reactivity Using Native Top-Down Mass Spectrometry

Bennett, J. L., Ramsay, O. B., Lutomski, C. A., Kirschbaum, C., & Robinson, C. V. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00395 · Cited by 3

On the Utility of Infrared Photoactivation for Native Top-Down and Complex-Down Orbitrap Mass Spectrometry of Soluble Proteoform Complexes

Nagy, C., Lieu, L. B., Mullen, C., McAlister, G. C., Melani, R. D., Hinkle, J. D., & Fornelli, L. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00385 · Cited by 4

Top–Down Proteomics of Skinned Human Muscle Fibers Reveals Proteoform‐Resolved Fiber‐to‐Fiber Variability

Wilson, M. C., Gao, Z., Lopez, J. R., Zhu, Y., Olszewski, S. S., Konopka, A. R., Diffee, G. M., & Ge, Y. (2026) · Journal of Mass Spectrometry · doi:10.1002/jms.70040 · Cited by 3

Native-Like Protein Structures in Vacuo: Steric Cooperativity as a Kinetic Barrier to Denaturation

Bleiholder, C., Pedrete, T. D. A., Lee, J., & Liu, F. C. (2026) · JACS Au · doi:10.1021/jacsau.5c01759 · Cited by 3

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

Decoding Ubiquitin Modifications by Mass Spectrometry

Gong, Y., & Dai, L. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-981-97-7288-9_1 · Cited by 3

Development of automated proteomic workflows utilizing silicon-based coupling agents

Frey, C., Arad, M., Ku, K., Hare, R., Balagtas, R., Shi, Y., Moon, K., Foster, L. J., & Ghafourifar, G. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105215 · Cited by 3

Native Proteomics by Capillary Zone Electrophoresis‐Mass Spectrometry

Wang, Q., Wang, Q., Qi, Z., Moeller, W. J., Wysocki, V. H., & Sun, L. (2024) · Angewandte Chemie · doi:10.1002/ange.202408370 · Cited by 3

Evaluation of a Bruker timsTOF Pro for Native Mass SpectrometryPreprint

Panczyk, E. M., Snyder, D. T., Liu, F. C., Lin, Y.-F., Ridgeway, M. E., Park, M., Bleiholder, C., & Wysocki, V. H. (2021) · doi:10.33774/chemrxiv-2021-qr78t · Cited by 3

Evaluation of a Bruker timsTOF Pro for Native Mass SpectrometryPreprint

Panczyk, E. M., Lin, Y.-F., Snyder, D. T., Liu, F. C., Ridgeway, M. E., Park, M., Bleiholder, C., & Wysocki, V. H. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2021-qr78t-v2 · Cited by 5

Characterization of proteoforms within α-synuclein complexes in living cells by cleavable cross-linking combined with top-down mass spectrometry

Yang, X., Zhong, B., Chen, J., Sun, Y., Zhao, B., Zhao, Q., Liang, Z., Zhang, Y., Liang, Y., & Zhang, L. (2026) · Talanta · doi:10.1016/j.talanta.2026.129914 · Cited by 2

Deciphering the molecular organization of GET pathway chaperones through native mass spectrometry

Giska, F., Mariappan, M., Bhattacharyya, M., & Gupta, K. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.02.026 · Cited by 2

Exploring the structure and dynamics of macromolecular complexes by native mass spectrometry

Erba, E. B., Signor, L., & Petosa, C. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103799 · Cited by 52

The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes

Erba, E. B., & Petosa, C. (2015) · Protein Science · doi:10.1002/pro.2661 · Cited by 132

Native Top-Down Electrospray Ionization-Mass Spectrometry of 158 kDa Protein Complex by High-Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Li, H., Wolff, J. J., Orden, S. L. V., & Loo, J. A. (2013) · Analytical Chemistry · doi:10.1021/ac4033214 · Cited by 119

From Protein Complexes to Subunit Backbone Fragments: A Multi-stage Approach to Native Mass Spectrometry

Belov, M. E., Damoc, E., Denisov, E., Compton, P. D., Horning, S., Makarov, A. A., & Kelleher, N. L. (2013) · Analytical Chemistry · doi:10.1021/ac4029328 · Cited by 175

Methods | Mass Spectrometry of Native Complexes

Rose, R., & Heck, A. J. R. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00586-7