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

The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

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Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry

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Structure of the 30S ribosomal subunit

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Analytical Properties of the Nanoelectrospray Ion Source

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Studying noncovalent protein complexes by electrospray ionization mass spectrometry

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Ion mobility–mass spectrometry analysis of large protein complexes

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An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-ToF instrument

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Native mass spectrometry: a bridge between interactomics and structural biology

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Applications of a travelling wave‐based radio‐frequency‐only stacked ring ion guide

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Evidence for Macromolecular Protein Rings in the Absence of Bulk Water

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Structural characterization of proteins and complexes using small-angle X-ray solution scattering

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The molecular sociology of the cell

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Mapping protein-protein interactions in solution by NMR spectroscopy.

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Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry

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Detection of noncovalent receptor-ligand complexes by mass spectrometry

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A dual pressure linear ion trap orbitrap instrument with very high sequencing speed

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Ion mobility mass spectrometry of proteins and proteinassemblies

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Stepwise evolution of protein native structure with electrospray into the gas phase, 10 −12 to 10 2 s

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High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies

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Complete Protein Characterization Using Top-Down Mass Spectrometry and Ultraviolet Photodissociation

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The role of mass spectrometry in structure elucidation of dynamic protein complexes.

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Micelles Protect Membrane Complexes from Solution to Vacuum

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Electron-capture dissociation tandem mass spectrometry

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Extending Top-Down Mass Spectrometry to Proteins with Masses Greater Than 200 Kilodaltons

Han, X., Jin, M., Breuker, K., & McLafferty, F. W. (2006) · Science · doi:10.1126/science.1128868 · Cited by 328 · see citing works

Native protein mass spectrometry: from intact oligomers to functional machineries

van den Heuvel, R. H. H., & Heck, A. J. R. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.08.006 · Cited by 303 · see citing works

Mass spectrometry: come of age for structural and dynamical biology

Benesch, J. L. P., & Ruotolo, B. T. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.08.002 · Cited by 264 · see citing works

Improving the Performance of a Quadrupole Time-of-Flight Instrument for Macromolecular Mass Spectrometry

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Mass spectrometry–based functional proteomics: from molecular machines to protein networks

Köcher, T., & Superti‐Furga, G. (2007) · Nature Methods · doi:10.1038/nmeth1093 · Cited by 240 · see citing works

High-resolution mass spectrometry of viral assemblies: Molecular composition and stability of dimorphic hepatitis B virus capsids

Uetrecht, C., Versluis, C., Watts, N. R. M., Roos, W. H., Wuite, G. J. L., Wingfield, P. T., Steven, A. C., & Heck, A. J. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800406105 · Cited by 220 · see citing works

Refinement of Multidomain Protein Structures by Combination of Solution Small-Angle X-ray Scattering and NMR Data

Grishaev, A., Wu, J., Trewhella, J., & Bax, A. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054342m · Cited by 211 · see citing works

Collisional activation of protein complexes: Picking up the pieces

Benesch, J. L. P. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.11.014 · Cited by 195 · see citing works

Nonergodic and conformational control of the electron capture dissociation of protein cations

Breuker, K., Oh, H. B., Lin, C., Carpenter, B. K., & McLafferty, F. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406095101 · Cited by 170 · see citing works

Integrated Ultramicroelectrode−Nanopipet Probe for Concurrent Scanning Electrochemical Microscopy and Scanning Ion Conductance Microscopy

Comstock, D. J., Elam, J. W., Pellin, M. J., & Hersam, M. C. (2010) · Analytical Chemistry · doi:10.1021/ac902224q · Cited by 170 · see citing works

Zeptomole-Sensitivity Electrospray Ionization−Fourier Transform Ion Cyclotron Resonance Mass Spectrometry of Proteins

Belov, M. E., Gorshkov, M. V., Udseth, H. R., Anderson, G., & Smith, R. D. (2000) · Analytical Chemistry · doi:10.1021/ac991360b · Cited by 164 · see citing works

Chaperonin Complexes Monitored by Ion Mobility Mass Spectrometry

van Duijn, E., Barendregt, A., Synowsky, S. A., Versluis, C., & Heck, A. J. R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8055134 · Cited by 152 · see citing works

Increasing charge while preserving noncovalent protein complexes for ESI-MS

Lomeli, S. H., Yin, S., Loo, R. R. O., & Loo, J. A. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.11.013 · Cited by 144 · see citing works

NMR studies of protein interactions

Takeuchi, K., & Wagner, G. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.01.006 · Cited by 128 · see citing works

Native electrospray and electron-capture dissociation in FTICR mass spectrometry provide top-down sequencing of a protein component in an intact protein assembly

Zhang, H., Cui, W., Wen, J., Blankenship, R. E., & Gross, M. L. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2010.08.006 · Cited by 121 · see citing works

Stability and Shape of Hepatitis B Virus Capsids In Vacuo

Uetrecht, C., Versluis, C., Watts, N. R. M., Wingfield, P. T., Steven, A. C., & Heck, A. J. R. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802410 · Cited by 108 · see citing works

The social network of a cell: Recent advances in interactome mapping

Charbonnier, S., Gallego, O., & Gavin, A. (2008) · Biotechnology annual review · doi:10.1016/s1387-2656(08)00001-x · Cited by 97 · see citing works

Tandem Mass Spectrometry of Intact GroEL−Substrate Complexes Reveals Substrate-Specific Conformational Changes in thetransRing

van Duijn, E., Simmons, D. A., van den Heuvel, R. H. H., Bakkes, P. J., van Heerikhuizen, H., Heeren, R. M. A., Robinson, C. V., van der Vies, S. M., & Heck, A. J. R. (2006) · Journal of the American Chemical Society · doi:10.1021/ja056756l · Cited by 87 · see citing works

Revealing the Quaternary Structure of a Heterogeneous Noncovalent Protein Complex through Surface-Induced Dissociation

Blackwell, A. E., Dodds, E. D., Bandarian, V., & Wysocki, V. H. (2011) · Analytical Chemistry · doi:10.1021/ac200452b · Cited by 84 · see citing works

Current limitations in native mass spectrometry based structural biology

van Duijn, E. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2009.12.010 · Cited by 83 · see citing works

Initial implementation of an electrodynamic ion funnel with fourier transform ion cyclotron resonance mass spectrometry

Belov, M. E., Gorshkov, M. V., Udseth, H. R., Anderson, G., Tolmachev, A. V., Prior, D. C., Harkewicz, R., & Smith, R. D. (2000) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(99)00121-x · Cited by 79 · see citing works

Automated Gain Control and Internal Calibration with External Ion Accumulation Capillary Liquid Chromatography-Electrospray Ionization-Fourier Transform Ion Cyclotron Resonance

Belov, M. E., Zhang, R., Strittmatter, E. F., Prior, D. C., Tang, K., & Smith, R. D. (2003) · Analytical Chemistry · doi:10.1021/ac0206770 · Cited by 79 · see citing works

Interaction networks for systems biology

Bader, S. L., Kühner, S., & Gavin, A. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.015 · Cited by 76 · see citing works

Dynamically Multiplexed Ion Mobility Time-of-Flight Mass Spectrometry

Belov, M. E., Clowers, B. H., Prior, D. C., Danielson, W., Liyu, A. V., Petritis, B. O., & Smith, R. D. (2008) · Analytical Chemistry · doi:10.1021/ac8003665 · Cited by 74 · see citing works

The changing impact of the collision-induced decomposition of ions on mass spectrometry

Jennings, K. R. (2000) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(00)00325-0 · Cited by 74 · see citing works

Robust Analysis of the Yeast Proteome under 50 kDa by Molecular-Mass-Based Fractionation and Top-Down Mass Spectrometry

Kellie, J. F., Catherman, A. D., Durbin, K. R., Tran, J. C., Tipton, J., Norris, J. L., Witkowski, C. E., Thomas, P. M., & Kelleher, N. (2011) · Analytical Chemistry · doi:10.1021/ac202384v · Cited by 62 · see citing works

Quadrupole-Time-of-Flight Mass Spectrometer Modified for Higher-Energy Dissociation Reduces Protein Assemblies to Peptide Fragments

Benesch, J. L. P., Ruotolo, B. T., Sobott, F., Wildgoose, J. L., Gilbert, A. A., Bateman, R. H., & Robinson, C. V. (2008) · Analytical Chemistry · doi:10.1021/ac801950u · Cited by 60 · see citing works

Use of an automated chromium reduction system for hydrogen isotope ratio analysis of physiological fluids applied to doubly labeled water analysis

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Native mass spectrometry of photosynthetic pigment–protein complexes

Zhang, H., Cui, W., Gross, M. L., & Blankenship, R. E. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.005 · Cited by 53 · see citing works

Macromolecular mass spectrometry and electron microscopy as complementary tools for investigation of the heterogeneity of bacteriophage portal assemblies

Poliakov, A., van Duijn, E., Lander, G. C., Fu, C., Johnson, J. E., Prevelige, P. E., & Heck, A. J. R. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.09.003 · Cited by 46 · see citing works

Methyl Proton Contacts Obtained Using Heteronuclear Through-Bond Transfers in Solid-State NMR Spectroscopy

Loquet, A., Laage, S., Gardiennet, C., Elena‐Herrmann, B., Emsley, L., Böckmann, A., & Lesage, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801464g · Cited by 22 · see citing works

Purification of GroEL from an Overproducing E. coli Strain

Quaite-Randall, E., & Joachimiak, A. (2003) · Humana Press eBooks · doi:10.1385/1-59259-061-6:29 · Cited by 22 · see citing works

Structure and function of large cellular assemblies

Ban, N., & Egelman, E. H. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.02.003 · Cited by 4 · see citing works

High-Resolution Native Mass Spectrometry

Tamara, S., den Boer, M. A., & Heck, A. J. R. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00212 · Cited by 511 · see citing works

Top Down proteomics: Facts and perspectives

Catherman, A. D., Skinner, O. S., & Kelleher, N. L. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.02.041 · Cited by 507 · see citing works

Evolution of Orbitrap Mass Spectrometry Instrumentation

Eliuk, S. M., & Makarov, A. (2015) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071114-040325 · Cited by 460 · see citing works

The Q Exactive HF, a Benchtop Mass Spectrometer with a Pre-filter, High-performance Quadrupole and an Ultra-high-field Orbitrap Analyzer

Scheltema, R. A., Hauschild, J.-P., Lange, O., Hornburg, D., Denisov, E. V., Damoc, E., Kuehn, A., Makarov, A., & Mann, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.043489 · Cited by 321 · 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

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

Li, H., Nguyen, H. H., Ogorzalek Loo, R. R., Campuzano, I. D. G., & Loo, J. A. (2018) · Nature Chemistry · doi:10.1038/nchem.2908 · Cited by 249 · see citing works

Ion Activation Methods for Peptides and Proteins

Brodbelt, J. S. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04563 · Cited by 245 · see citing works

Top-Down Proteomics: Ready for Prime Time?

Chen, B., Brown, K. A., Lin, Z., & Ge, Y. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04747 · Cited by 210 · see citing works

High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

van de Waterbeemd, M., Fort, K. L., Boll, D., Reinhardt-Szyba, M., Routh, A., Makarov, A., & Heck, A. J. R. (2017) · Nature Methods · doi:10.1038/nmeth.4147 · Cited by 168 · see citing works

Defining the Stoichiometry and Cargo Load of Viral and Bacterial Nanoparticles by Orbitrap Mass Spectrometry

Snijder, J., van de Waterbeemd, M., Damoc, E., Denisov, E., Grinfeld, D., Bennett, A., Agbandje-McKenna, M., Makarov, A., & Heck, A. J. R. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502616y · Cited by 168 · see citing works

Hybrid mass spectrometry approaches in glycoprotein analysis and their usage in scoring biosimilarity

Yang, Y., Liu, F., Franc, V., Halim, L. A., Schellekens, H., & Heck, A. J. R. (2016) · Nature Communications · doi:10.1038/ncomms13397 · Cited by 152 · see citing works

The biosynthesis of methanobactin

Kenney, G. E., Dassama, L. M. K., Pandelia, M., Gizzi, A. S., Martinie, R. J., Gao, P., DeHart, C. J., Schachner, L. F., Skinner, O. S., Ro, S. Y., et al. (2018) · Science · doi:10.1126/science.aap9437 · Cited by 156 · see citing works

Top-down characterization of endogenous protein complexes with native proteomics

Skinner, O. S., Haverland, N. A., Fornelli, L., Melani, R. D., Do Vale, L. H. F., Seckler, H. S., Doubleday, P. F., Schachner, L. F., Srzentić, K., Kelleher, N. L., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2515 · Cited by 155 · see citing works

Protein–Small Molecule Interactions in Native Mass Spectrometry

Bennett, J. L., Nguyen, G. T. H., & Donald, W. A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00293 · Cited by 158 · see citing works

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

Zhou, M., Lantz, C., Brown, K. A., Ge, Y., Paša-Tolić, L., Loo, J. A., & Lermyte, F. (2020) · Chemical Science · doi:10.1039/d0sc04392c · Cited by 146 · see citing works

Top or Middle? Up or Down? Toward a Standard Lexicon for Protein Top-Down and Allied Mass Spectrometry Approaches

Lermyte, F., Tsybin, Y. O., O’Connor, P. B., & Loo, J. A. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02201-x · Cited by 132 · see citing works

The Blood Proteoform Atlas: A reference map of proteoforms in human hematopoietic cells

Melani, R. D., Gerbasi, V. R., Anderson, L. C., Sikora, J. W., Toby, T. K., Hutton, J. E., Butcher, D. S., Negrão, F., Seckler, H. S., Srzentić, K., et al. (2022) · Science · doi:10.1126/science.aaz5284 · Cited by 140 · see citing works

Boundaries of Mass Resolution in Native Mass Spectrometry

Lössl, P., Snijder, J., & Heck, A. J. R. (2014) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-014-0874-3 · Cited by 136 · see citing works

Characterization of Native Protein Complexes Using Ultraviolet Photodissociation Mass Spectrometry

O’Brien, J. P., Li, W., Zhang, Y., & Brodbelt, J. S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505217w · Cited by 135 · see citing works

Chemical cross‐linking and native mass spectrometry: A fruitful combination for structural biology

Sinz, A., Arlt, C., Chorev, D. S., & Sharon, M. (2015) · Protein Science · doi:10.1002/pro.2696 · Cited by 130 · see citing works

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 116 · see citing works

Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals

Wohlschlager, T., Scheffler, K., Forstenlehner, I. C., Esser‐Skala, W., Senn, S., Damoc, E., Holzmann, J., & Huber, C. G. (2018) · Nature Communications · doi:10.1038/s41467-018-04061-7 · Cited by 109 · see citing works

Native top-down mass spectrometry provides insights into the copper centers of membrane-bound methane monooxygenase

Ro, S., Schachner, L. F., Koo, C. W., Purohit, R., Remis, J., Kenney, G. E., Liauw, B., Thomas, P. M., Patrie, S. M., Kelleher, N., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10590-6 · Cited by 85 · see citing works

Design and Performance of a Novel Interface for Combined Matrix-Assisted Laser Desorption Ionization at Elevated Pressure and Electrospray Ionization with Orbitrap Mass Spectrometry

Belov, M. E., Ellis, S. R., Dilillo, M., Paine, M. R. L., Danielson, W., Anderson, G., de Graaf, E. L., Eijkel, G. B., Heeren, R. M. A., & McDonnell, L. A. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01168 · Cited by 100 · see citing works

Analysis of Proteins, Protein Complexes, and Organellar Proteomes Using Sheathless Capillary Zone Electrophoresis - Native Mass Spectrometry

Belov, A. M., Viner, R., Santos, M. R., Horn, D. M., Bern, M., Karger, B. L., & Ivanov, A. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1781-1 · Cited by 97 · see citing works

Implementation of Ultraviolet Photodissociation on a Benchtop Q Exactive Mass Spectrometer and Its Application to Phosphoproteomics

Fort, K. L., Dyachenko, A., Potel, C. M., Corradini, E., Marino, F., Barendregt, A., Makarov, A., Scheltema, R. A., & Heck, A. J. R. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04162 · Cited by 92 · see citing works

Tandem Native Mass-Spectrometry on Antibody–Drug Conjugates and Submillion Da Antibody–Antigen Protein Assemblies on an Orbitrap EMR Equipped with a High-Mass Quadrupole Mass Selector

Dyachenko, A., Wang, G., Belov, M., Makarov, A., de Jong, R. N., van den Bremer, E. T. J., Parren, P. W. H. I., & Heck, A. J. R. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00788 · Cited by 90 · see citing works

Measurement of Individual Ions Sharply Increases the Resolution of Orbitrap Mass Spectra of Proteins

Kafader, J. O., Melani, R. D., Senko, M. W., Makarov, A. A., Kelleher, N. L., & Compton, P. D. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04519 · Cited by 87 · see citing works

Mapping Proteoforms and Protein Complexes From King Cobra Venom Using Both Denaturing and Native Top-down Proteomics

Melani, R. D., Skinner, O. S., Fornelli, L., Domont, G. B., Compton, P. D., & Kelleher, N. L. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.056523 · Cited by 85 · see citing works

Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool

Snyder, D. T., Harvey, S. R., & Wysocki, V. H. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00309 · Cited by 86 · see citing works

Structural characterization of holo- and apo-myoglobin in the gas phase by ultraviolet photodissociation mass spectrometry

Cammarata, M. B., & Brodbelt, J. S. (2014) · Chemical Science · doi:10.1039/c4sc03200d · Cited by 84 · see citing works

Structural Characterization of Dihydrofolate Reductase Complexes by Top-Down Ultraviolet Photodissociation Mass Spectrometry

Cammarata, M. B., Thyer, R. T., Rosenberg, J. A., Ellington, A. D., & Brodbelt, J. S. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b04628 · Cited by 81 · see citing works

Native mass spectrometry—A valuable tool in structural biology

Barth, M., & Schmidt, C. (2020) · Journal of Mass Spectrometry · doi:10.1002/jms.4578 · Cited by 82 · see citing works

Individual Ion Mass Spectrometry Enhances the Sensitivity and Sequence Coverage of Top-Down Mass Spectrometry

Kafader, J. O., Durbin, K. R., Melani, R. D., Des Soye, B. J., Schachner, L. F., Senko, M. W., Compton, P. D., & Kelleher, N. L. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00797 · Cited by 76 · see citing works

Ion traps in modern mass spectrometry

Nolting, D., Malek, R., & Makarov, A. (2017) · Mass Spectrometry Reviews · doi:10.1002/mas.21549 · Cited by 71 · see citing works

Fundamentals and Advances of Orbitrap Mass Spectrometry

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

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Mass spectrometry captures off-target drug binding and provides mechanistic insights into the human metalloprotease ZMPSTE24

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Native Mass Spectrometry of Recombinant Proteins from Crude Cell Lysates

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Defining Gas-Phase Fragmentation Propensities of Intact Proteins During Native Top-Down Mass Spectrometry

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Structural Analysis of the Glycoprotein Complex Avidin by Tandem-Trapped Ion Mobility Spectrometry–Mass Spectrometry (Tandem-TIMS/MS)

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Decoding the Protein Composition of Whole Nucleosomes with Nuc-MS

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Native vs Denatured: An in Depth Investigation of Charge State and Isotope Distributions

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Capillary electrophoresis‐mass spectrometry for protein analyses under native conditions: Current progress and perspectives

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Deciphering combinatorial post-translational modifications by top-down mass spectrometry

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Design and performance of a high-flux electrospray ionization source for ion soft landing

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Triple-Stage Mass Spectrometry Unravels the Heterogeneity of an Endogenous Protein Complex

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Native MS Analysis of Bacteriorhodopsin and an Empty Nanodisc by Orthogonal Acceleration Time-of-Flight, Orbitrap and Ion Cyclotron Resonance

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Symmetry of Charge Partitioning in Collisional and UV Photon-Induced Dissociation of Protein Assemblies

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Simple and Minimally Invasive SID Devices for Native Mass Spectrometry

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Uniting Native Capillary Electrophoresis and Multistage Ultraviolet Photodissociation Mass Spectrometry for Online Separation and Characterization of Escherichia coli Ribosomal Proteins and Protein Complexes

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β-Glucocerebrosidase Modulators Promote Dimerization of β-Glucocerebrosidase and Reveal an Allosteric Binding Site

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

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Integral membrane proteins: bottom-up, top-down and structural proteomics

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Design and Performance of a Dual-Polarity Instrument for Ion Soft Landing

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Denaturing and Native Mass Spectrometric Analytics for Biotherapeutic Drug Discovery Research: Historical, Current, and Future Personal Perspectives

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Standard Proteoforms and Their Complexes for Native Mass Spectrometry

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Mass spectrometry beyond the native state

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

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It is time for top-down venomics

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Native GELFrEE: A New Separation Technique for Biomolecular Assemblies

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Resonance methods in quadrupole ion traps

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Top‐down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment

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Native-MS Analysis of Monoclonal Antibody Conjugates by Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

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Native and Denaturing MS Protein Deconvolution for Biopharma: Monoclonal Antibodies and Antibody–Drug Conjugates to Polydisperse Membrane Proteins and Beyond

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Separation and Characterization of Endogenous Nucleosomes by Native Capillary Zone Electrophoresis–Top-Down Mass Spectrometry

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Quantitative collision‐induced unfolding differentiates model antibody–drug conjugates

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Standard procedures for native CZE-MS of proteins and protein complexes up to 800 kDa

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Multi-Stage Ultraviolet Photodissociation Mass Spectrometry to Characterize Single Amino Acid Variants of Human Mitochondrial BCAT2

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Structural mass spectrometry comes of age: new insight into protein structure, function and interactions

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Formaldehyde cross-linking and structural proteomics: Bridging the gap

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Tandem‐trapped ion mobility spectrometry/mass spectrometry coupled with ultraviolet photodissociation

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Exposing the molecular heterogeneity of glycosylated biotherapeutics

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The growing role of structural mass spectrometry in the discovery and development of therapeutic antibodies

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Infrared Laser Activation of Soluble and Membrane Protein Assemblies in the Gas Phase

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Direct Mass Spectrometry Analysis of Protein Complexes and Intact Proteins up to >70 kDa from Tissue

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Top-Down Mass Spectrometry: Proteomics to Proteoforms

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Ion Mobility and Mass Spectrometry Measurements of the Humanized IgGk NIST Monoclonal Antibody

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Using 10,000 Fragment Ions to Inform Scoring in Native Top-down Proteomics

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Towards integrative structural mass spectrometry: Benefits from hybrid approaches

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Application of the Exactive Plus EMR for automated protein–ligand screening by non‐covalent mass spectrometry

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Measuring masses of large biomolecules and bioparticles using mass spectrometric techniques

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Surface Induced Dissociation Coupled with High Resolution Mass Spectrometry Unveils Heterogeneity of a 211 kDa Multicopper Oxidase Protein Complex

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Native Mass Spectrometry Analysis of Affinity-Captured Endogenous Yeast RNA Exosome Complexes

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Sensing mechanisms of iron–sulfur cluster regulatory proteins elucidated using native mass spectrometry

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A novel crosslinking protocol stabilizes amyloid β oligomers capable of inducing Alzheimer's‐associated pathologies

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Structural Evaluation of Protein/Metal Complexes via Native Electrospray Ultraviolet Photodissociation Mass Spectrometry

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Native Mass Spectrometry and Surface Induced Dissociation Provide Insight into the Post-Translational Modifications of Tetrameric AQP0 Isolated from Bovine Eye Lens

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Uncovering hidden protein modifications with native top-down mass spectrometry

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Enhancing Top-Down Analysis Using Chromophore-Assisted Infrared Multiphoton Dissociation from (Phospho)peptides to Protein Assemblies

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Native Mass Spectrometry Gives Insight into the Allosteric Binding Mechanism of M2 Pyruvate Kinase to Fructose-1,6-Bisphosphate

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Developments in FTICR-MS and Its Potential for Body Fluid Signatures

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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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Native Mass Spectrometry at the Convergence of Structural Biology and Compositional Proteomics

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

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Native Mass Spectrometry as a Tool in Structural Biology

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