Standard Proteoforms and Their Complexes for Native Mass Spectrometry

Proteoform: a single term describing protein complexity

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The BioPlex network: a systematic exploration of the human interactome

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A call for transparent reporting to optimize the predictive value of preclinical research

Landis, S. C., Amara, S. G., Asadullah, K., Austin, C. P., Blumenstein, R., Bradley, E. W., Crystal, R. G., Darnell, R. B., Ferrante, R. J., Fillit, H., et al. (2012) · Nature · doi:10.1038/nature11556 · Cited by 1,196 · see citing works

Studying noncovalent protein complexes by electrospray ionization mass spectrometry

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Bayesian Deconvolution of Mass and Ion Mobility Spectra: From Binary Interactions to Polydisperse Ensembles

Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000 · see citing works

Orbitrap Mass Spectrometry

Zubarev, R. A., & Makarov, A. (2013) · Analytical Chemistry · doi:10.1021/ac4001223 · Cited by 662 · 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

Investigation of intact protein complexes by mass spectrometry

Heck, A. J. R., & van den Heuvel, R. H. H. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.10081 · Cited by 584 · see citing works

Electrospray ionization of large multiply charged species proceeds via Dole’s charged residue mechanism

de la Mora, J. F. (2000) · Analytica Chimica Acta · doi:10.1016/s0003-2670(99)00601-7 · Cited by 542 · see citing works

Orbitrap mass spectrometry: Instrumentation, ion motion and applications

Perry, R. H., Cooks, R. G., & Noll, R. J. (2008) · Mass Spectrometry Reviews · doi:10.1002/mas.20186 · Cited by 515 · see citing works

A Tandem Mass Spectrometer for Improved Transmission and Analysis of Large Macromolecular Assemblies

Sobott, F., Hernández, H., McCammon, M. G., Tito, M. A., & Robinson, C. V. (2002) · Analytical Chemistry · doi:10.1021/ac0110552 · Cited by 511 · see citing works

Mass spectrometry of intact membrane protein complexes

Laganowsky, A., Reading, E., Hopper, J. T. S., & Robinson, C. V. (2013) · Nature Protocols · doi:10.1038/nprot.2013.024 · Cited by 409 · see citing works

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

Benesch, J. L. P., Ruotolo, B. T., Simmons, D. A., & Robinson, C. V. (2007) · Chemical Reviews · doi:10.1021/cr068289b · Cited by 408 · see citing works

High-Resolution Mass Spectrometers

Marshall, A. G., & Hendrickson, C. L. (2008) · Annual Review of Analytical Chemistry · doi:10.1146/annurev.anchem.1.031207.112945 · Cited by 397 · see citing works

High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies

Rose, R. J., Damoc, E., Denisov, E., Makarov, A., & Heck, A. J. R. (2012) · Nature Methods · doi:10.1038/nmeth.2208 · Cited by 392 · see citing works

The ‘infinity cell’: A new trapped‐ion cell with radiofrequency covered trapping electrodes for fourier transform ion cyclotron resonance mass spectrometry

Caravatti, P., & Allemann, M. (1991) · Organic Mass Spectrometry · doi:10.1002/oms.1210260527 · Cited by 388 · see citing works

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

Sharon, M., & Robinson, C. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061005.090816 · Cited by 364 · see citing works

Photodissociation mass spectrometry: new tools for characterization of biological molecules

Brodbelt, J. S. (2014) · Chemical Society Reviews · doi:10.1039/c3cs60444f · Cited by 322 · see citing works

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

van den Heuvel, R. H. H., van Duijn, E., Mazon, H., Synowsky, S. A., Lorenzen, K., Versluis, C., Brouns, S. J. J., Langridge, D., John van der, O. O. S. T., Hoyes, J. B., et al. (2006) · Analytical Chemistry · doi:10.1021/ac061039a · Cited by 252 · 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

ProSight Lite: Graphical software to analyze top‐down mass spectrometry data

Fellers, R. T., Greer, J. B., Early, B. P., Yu, X., LeDuc, R. D., Kelleher, N. L., & Thomas, P. M. (2015) · PROTEOMICS · doi:10.1002/pmic.201400313 · Cited by 247 · see citing works

Improving Validation Practices in “Omics” Research

Ioannidis, J. P. A., & Khoury, M. J. (2011) · Science · doi:10.1126/science.1211811 · Cited by 246 · see citing works

Addressing a Common Misconception: Ammonium Acetate as Neutral pH “Buffer” for Native Electrospray Mass Spectrometry

Konermann, L. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1739-3 · Cited by 243 · see citing works

Ion Mobility–Mass Spectrometry Reveals Long‐Lived, Unfolded Intermediates in the Dissociation of Protein Complexes

Ruotolo, B. T., Hyung, S., Robinson, P. M., Giles, K., Bateman, R. H., & Robinson, C. V. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200702161 · Cited by 229 · see citing works

The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes.

Holland, M. J., Holland, J. P., Thill, G. P., & Jackson, K. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69976-x · Cited by 214 · see citing works

Innovative Native MS Methodologies for Antibody Drug Conjugate Characterization: High Resolution Native MS and IM-MS for Average DAR and DAR Distribution Assessment

Debaene, F., Bœuf, A., Wagner‐Rousset, E., Colas, O., Ayoub, D., Corvaı̈a, N., DORSSELAER, A. V., Beck, A., & Cianférani, S. (2014) · Analytical Chemistry · doi:10.1021/ac502593n · Cited by 182 · see citing works

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 · 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

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

Structure of bovine carbonic anhydrase II at 1.95 Å resolution

Saito, R., Sato, T., Ikai, A., & Tanaka, N. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904003166 · Cited by 155 · see citing works

Detergent-free mass spectrometry of membrane protein complexes

Hopper, J. T. S., Yu, Y. T.-C., Li, D., Raymond, A., Bostock, M. J., Liko, I., Mikhailov, V. A., Laganowsky, A. D., Benesch, J. L. P., Caffrey, M., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2691 · Cited by 155 · 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

Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies

Zhang, H., Cui, W., & Gross, M. L. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.11.027 · Cited by 152 · see citing works

Rapid characterization of biotherapeutic proteins by size-exclusion chromatography coupled to native mass spectrometry

Haberger, M., Leiß, M., Heidenreich, A.-K., Pester, O., Hafenmair, G., Hook, M., Bonnington, L. S., Wegele, H., Haindl, M., Reusch, D., et al. (2015) · mAbs · doi:10.1080/19420862.2015.1122150 · Cited by 148 · see citing works

Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry

Hilton, G. R., & Benesch, J. L. P. (2012) · Journal of The Royal Society Interface · doi:10.1098/rsif.2011.0823 · Cited by 140 · see citing works

Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry

Rosati, S., Yang, Y., Barendregt, A., & Heck, A. J. R. (2014) · Nature Protocols · doi:10.1038/nprot.2014.057 · Cited by 138 · see citing works

Surface Induced Dissociation: Dissecting Noncovalent Protein Complexes in the Gas phase

Zhou, M., & Wysocki, V. H. (2014) · Accounts of Chemical Research · doi:10.1021/ar400223t · Cited by 136 · see citing works

Probing the biophysical interplay between a viral genome and its capsid

Snijder, J., Uetrecht, C., Rose, R. J., Sanchez-Eugenia, R., Marti, G. A., Agirre, J., Guérin, D. M. A., Wuite, G. J. L., Heck, A. J. R., & Roos, W. H. (2013) · Nature Chemistry · doi:10.1038/nchem.1627 · Cited by 127 · cited 1× · see citing works

Cover Picture: Proteomics 7'15

Fellers, R. T., Greer, J. B., Early, B. P., Yu, X., LeDuc, R. D., Kelleher, N. L., & Thomas, P. M. (2015) · PROTEOMICS · doi:10.1002/pmic.201570050 · Cited by 122 · 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

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 · see citing works

The Primary Structure of Yeast Alcohol Dehydrogenase

Jörnvall, H. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11267.x · Cited by 117 · see citing works

Probing the Lipid Annular Belt by Gas‐Phase Dissociation of Membrane Proteins in Nanodiscs

Marty, M. T., Hoi, K. K., Gault, J., & Robinson, C. V. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508289 · Cited by 115 · see citing works

Tracking Replicability as a Method of Post-Publication Open Evaluation

Hartshorne, J. K., & Schachner, A. (2012) · Frontiers in Computational Neuroscience · doi:10.3389/fncom.2012.00008 · Cited by 102 · 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

Characterization of Small Protein Aggregates and Oligomers Using Size Exclusion Chromatography with Online Detection by Native Electrospray Ionization Mass Spectrometry

Muneeruddin, K., Thomas, J. J., Salinas, P. A., & Kaltashov, I. A. (2014) · Analytical Chemistry · doi:10.1021/ac502590h · Cited by 96 · see citing works

Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods

van de Waterbeemd, M., Tamara, S., Fort, K. L., Damoc, E., Franc, V., Bieri, P., Itten, M. P., Makarov, A., Ban, N., & Heck, A. J. R. (2018) · Nature Communications · doi:10.1038/s41467-018-04853-x · Cited by 80 · see citing works

Native Proteomics in Discovery Mode Using Size-Exclusion Chromatography–Capillary Zone Electrophoresis–Tandem Mass Spectrometry

Shen, X., Kou, Q., Guo, R., Yang, Z., Chen, D., Liu, X., Hong, H., & Sun, L. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02725 · Cited by 78 · see citing works

Revealing Ligand Binding Sites and Quantifying Subunit Variants of Noncovalent Protein Complexes in a Single Native Top-Down FTICR MS Experiment

Li, H., Wongkongkathep, P., Orden, S. L. V., Loo, R. R. O., & Loo, J. A. (2014) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-014-0928-6 · Cited by 75 · see citing works

Performing native mass spectrometry analysis on therapeutic antibodies

Thompson, N., Rosati, S., & Heck, A. J. R. (2013) · Methods · doi:10.1016/j.ymeth.2013.05.003 · Cited by 72 · see citing works

Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein

Wongkongkathep, P., Han, J. Y., Choi, T. S., Yin, S., Kim, H. I., & Loo, J. A. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-2002-2 · Cited by 71 · see citing works

Analytical Approaches for Size and Mass Analysis of Large Protein Assemblies

Snijder, J., & Heck, A. J. R. (2014) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071213-020015 · Cited by 70 · see citing works

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

Haverland, N. A., Skinner, O. S., Fellers, R. T., Tariq, A., Early, B. P., LeDuc, R. D., Fornelli, L., Compton, P. D., & Kelleher, N. L. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1635-x · Cited by 65 · see citing works

An informatic framework for decoding protein complexes by top-down mass spectrometry

Skinner, O. S., Havugimana, P. C., Haverland, N. A., Fornelli, L., Early, B. P., Greer, J. B., Fellers, R. T., Durbin, K. R., do Vale, L. H. F., Melani, R. D., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3731 · Cited by 64 · see citing works

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Kirshenbaum, N., Michaelevski, I., & Sharon, M. (2010) · Journal of Visualized Experiments · doi:10.3791/1954 · 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

A sheath‐flow nanospray interface for capillary electrophoresis/mass spectrometry

Liu, C. C., Zhang, J., & Dovic̀hi, N. J. (2004) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1769 · Cited by 59 · see citing works

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

Campuzano, I. D. G., Li, H., Bagal, D., Lippens, J. L., Švitel, J., Kurzeja, R. J. M., Xu, H., Schnier, P. D., & Loo, J. A. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b03762 · Cited by 54 · see citing works

Accelerating Biomedical Discoveries through Rigor and Transparency

Hewitt, J., Brown, L. L., Murphy, S. J., Grieder, F. B., & Silberberg, S. D. (2017) · ILAR Journal · doi:10.1093/ilar/ilx011 · Cited by 53 · see citing works

Characterization of Chain Pairing Variants of Bispecific IgG Expressed in a Single Host Cell by High-Resolution Native and Denaturing Mass Spectrometry

Schachner, L. F., Han, G., Dillon, M. A., Zhou, J., McCarty, L., Ellerman, D. A., Yin, Y., Spiess, C., Lill, J. R., Carter, P. J., et al. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02866 · Cited by 48 · see citing works

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

Konijnenberg, A., Bannwarth, L., Yilmaz, D., Koçer, A., Venien‐Bryan, C., & Sobott, F. (2015) · Protein Science · doi:10.1002/pro.2703 · Cited by 45 · see citing works

Hybrid Quadrupole/Time‐of‐Flight Mass Spectrometers for Analysis of Biomolecules

Ens, W., & Standing, K. G. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)02002-1 · Cited by 43 · see citing works

Bioinformatics Analysis of Top-Down Mass Spectrometry Data with ProSight Lite

DeHart, C. J., Fellers, R. T., Fornelli, L., Kelleher, N. L., & Thomas, P. M. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6783-4_18 · Cited by 43 · see citing works

Extracting Charge and Mass Information from Highly Congested Mass Spectra Using Fourier-Domain Harmonics

Cleary, S. P., Li, H., Bagal, D., Loo, J. A., Campuzano, I. D. G., & Prell, J. S. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-2018-7 · Cited by 39 · see citing works

Charge Mediated Compaction and Rearrangement of Gas-Phase Proteins: A Case Study Considering Two Proteins at Opposing Ends of the Structure-Disorder Continuum

Jhingree, J. R., Bellina, B., Pacholarz, K. J., & Barran, P. E. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1692-1 · Cited by 25 · see citing works

Native Mass Spectrometry for the Characterization of Structure and Interactions of Membrane Proteins

van Dyck, J. F., Konijnenberg, A., & Sobott, F. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7151-0_11 · Cited by 22 · see citing works

Repurposed HisC Aminotransferases Complete the Biosynthesis of Some Methanobactins

Park, Y. J., Kenney, G. E., Schachner, L. F., Kelleher, N. L., & Rosenzweig, A. C. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00296 · Cited by 21 · see citing works

A TOF mass spectrometer for the study of noncovalent complexes

Kozlovskiy, V. I., Donald, L. J., Collado, V. M., Spicer, V., Loboda, A. V., Chernushevich, I. V., Ens, W., & Standing, K. G. (2011) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2011.08.009 · Cited by 17 · see citing works

CN-GELFrEE - Clear Native Gel-eluted Liquid Fraction Entrapment Electrophoresis

Melani, R. D., Seckler, H. S., Skinner, O. S., do Vale, L. H. F., Catherman, A. D., Havugimana, P. C., de Sousa, M. V., Domont, G. B., Kelleher, N. L., & Compton, P. D. (2016) · Journal of Visualized Experiments · doi:10.3791/53597 · Cited by 13 · see citing works

Effects of Charge State, Charge Distribution, and Structure on the Ion Mobility of Protein Ions in Helium Gas: Results from Trajectory Method Calculations

Laszlo, K. J., & Bush, M. F. (2017) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.7b08154 · Cited by 13 · see citing works

Intact Antibody Characterization Using Orbitrap Mass Spectrometry

Hao, Z., Zhang, T., Xuan, Y., Wang, H., Qian, J., Lin, S., Chen, J., Horn, D. M., Argoti, D., Beck, A., et al. (2015) · ACS symposium series · doi:10.1021/bk-2015-1202.ch010 · Cited by 3 · 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

Multiplexed mass spectrometry of individual ions improves measurement of proteoforms and their complexes

Kafader, J. O., Melani, R. D., Durbin, K. R., Ikwuagwu, B., Early, B. P., Fellers, R. T., Beu, S. C., Zabrouskov, V., Makarov, A. A., Maze, J. T., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-0764-5 · Cited by 197 · see citing works

Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research

Gomes, F. P., & Yates, J. R. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21599 · Cited by 112 · see citing works

Ion Activation Methods for Peptides and Proteins

Macias, L. A., Santos, I. C., & Brodbelt, J. S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b04859 · Cited by 107 · see citing works

Instrumentation at the Leading Edge of Proteomics

Peters-Clarke, T. M., Coon, J. J., & Riley, N. M. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c04497 · Cited by 84 · 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

Decoding the protein composition of whole nucleosomes with Nuc-MS

Schachner, L. F., Jooß, K., Morgan, M. A., Piunti, A., Meiners, M. J., Kafader, J. O., Lee, A. S., Iwanaszko, M., Cheek, M. A., Burg, J. M., et al. (2021) · Nature Methods · doi:10.1038/s41592-020-01052-9 · Cited by 66 · 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

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

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 49 · see citing works

Top-down mass spectrometry of native proteoforms and their complexes: a community study

Habeck, T., Brown, K. A., Soye, B. J. D., Lantz, C., Zhou, M., Alam, N., Hossain, M. A., Jung, W., Keener, J. E., Volný, M., et al. (2024) · Nature Methods · doi:10.1038/s41592-024-02279-6 · Cited by 49 · see citing works

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

Jooß, K., Schachner, L. F., Watson, R., Gillespie, Z. B., Howard, S. A., Cheek, M. A., Meiners, M. J., Sobh, A., Licht, J. D., Keogh, M., et al. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04975 · Cited by 44 · see citing works

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

Jooss, K., McGee, J., Melani, R., & Kelleher, N. (2020) · bioRxiv · doi:10.1002/elps.202000317 · Cited by 32 · see citing works

Computational Strategies and Challenges for Using Native Ion Mobility Mass Spectrometry in Biophysics and Structural Biology

Allison, T. M., Barran, P., Cianférani, S., Degiacomi, M. T., Gabelica, V., Grandori, R., Marklund, E. G., Menneteau, T., Migas, L. G., Politis, A., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05791 · Cited by 38 · see citing works

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 International Edition · doi:10.1002/anie.202408370 · Cited by 31 · see citing works

Development of native MS capabilities on an extended mass range Q-TOF MS

Mallis, C. S., Zheng, X., Qiu, X., McCabe, J. W., Shirzadeh, M., Lyu, J., Laganowsky, A. D., & Russell, D. H. (2020) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2020.116451 · Cited by 24 · see citing works

Micro-flow size-exclusion chromatography for enhanced native mass spectrometry of proteins and protein complexes

Ventouri, I. K., Veelders, S., Passamonti, M., Endres, P., Roemling, R., Schoenmakers, P. J., Somsen, G. W., Haselberg, R., & Gargano, A. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.341324 · Cited by 27 · see citing works

Uncovering hidden protein modifications with native top-down mass spectrometry

Bennett, J. L., El‐Baba, T. J., Zouboulis, K., Kirschbaum, C., Song, H., Butroid, F. I., Benesch, J. L. P., Lutomski, C. A., & Robinson, C. V. (2025) · Nature Methods · doi:10.1038/s41592-025-02846-5 · Cited by 26 · see citing works

Standardized workflow for multiplexed charge detection mass spectrometry on orbitrap analyzers

Su, P., McGee, J. P., Hollas, M. A. R., Fellers, R. T., Durbin, K. R., Greer, J. B., Early, B. P., Yip, P. F., Zabrouskov, V., Srzentić, K., et al. (2025) · Nature Protocols · doi:10.1038/s41596-024-01091-y · Cited by 23 · see citing works

Voltage Rollercoaster Filtering of Low-Mass Contaminants During Native Protein Analysis

McGee, J. P., Melani, R. D., Goodwin, M., McAlister, G. C., Huguet, R., Senko, M. W., Compton, P. D., & Kelleher, N. L. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00037 · Cited by 21 · see citing works

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 · see citing works

Collision Cross Sections for Native Proteomics: Challenges and Opportunities

Ruotolo, B. T. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00686 · Cited by 20 · see citing works

Automated Control of Injection Times for Unattended Acquisition of Multiplexed Individual Ion Mass Spectra

McGee, J. P., Senko, M. W., Jooß, K., Soye, B. J. D., Compton, P. D., Kelleher, N. L., & Kafader, J. O. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c03495 · Cited by 19 · see citing works

Integrated Approach for Characterizing Bispecific Antibody/Antigens Complexes and Mapping Binding Epitopes with SEC/MALS, Native Mass Spectrometry, and Protein Footprinting

Huang, R. Y. ‐., Wang, F., Wheeler, M. L., Wang, Y., Langish, R. A., Chau, B. H., Dong, J., Morishige, W., Bezman, N., Strop, P., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c01876 · Cited by 18 · see citing works

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 · see citing works

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 · see citing works

Exploring the Chemical Space of Protein Glycosylation in Noncovalent Protein Complexes: An Expedition along Different Structural Levels of Human Chorionic Gonadotropin by Employing Mass Spectrometry

Lebede, M., Marco, F. D., Esser‐Skala, W., Hennig, R., Wohlschlager, T., & Huber, C. G. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c02199 · Cited by 14 · see citing works

Recent Contributions of Proteomics to Our Understanding of Reversible Nε-Lysine Acylation in Bacteria

Popova, L., Carr, R. A., & Carabetta, V. J. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00912 · Cited by 13 · see citing works

Native Mass Spectrometry Facilitates Hit Validation in DNA‐Encoded Library Technology

Bittner, P., Gloger, A., Keller, M., Oehler, S., Lessing, A., Zhang, Q., Ma, Z., Su, W., Satz, A. L., Kuai, L., et al. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202504470 · Cited by 12 · see citing works

Glycoproteomics of a Single Protein: Revealing Tens of Thousands of Myozyme Glycoforms by Hybrid HPLC-MS Approaches

Marco, F. D., Blöchl, C., Esser‐Skala, W., Schäpertöns, V., Zhang, T., Wuhrer, M., Sandra, K., Wohlschlager, T., & Huber, C. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100622 · Cited by 13 · see citing works

Probing the Fundamentals of Native Liquid Extraction Surface Analysis Mass Spectrometry of Proteins: Can Proteins Refold during Extraction?

Illes‐Toth, E., & Cooper, H. J. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02075 · Cited by 11 · see citing works

Nanoflow Size Exclusion Chromatography–Native Mass Spectrometry of Intact Proteoforms and Protein Complexes

Zhai, Z., Holmark, T., van der Zon, A. A. M., Tseliou, V., Mutti, F. G., Astefanei, A., & Gargano, A. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c01019 · Cited by 12 · see citing works

Overcoming aggregation with laser heated nanoelectrospray mass spectrometry: thermal stability and pathways for loss of bicarbonate from carbonic anhydrase II

Jordan, J. S., Lee, K. J., & Williams, E. R. (2024) · The Analyst · doi:10.1039/d4an00229f · Cited by 9 · see citing works

Advances and challenges in preparing membrane proteins for native mass spectrometry

Cheng, D., Guo, Y., Lyu, J., Liu, Y., Xu, W., Zheng, W., Wang, Y., & Qiao, P. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108483 · Cited by 6 · see citing works

Digital Ion Trap Isolation and Mass Analysis of Macromolecular Analytes with Multiply Charged Ion Attachment

Fu, L., Ellin, N. R., Pizzala, N. J., Bolívar, E. G. B., & McLuckey, S. A. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00292 · Cited by 5 · see citing works

Top-down mass spectrometry for protein molecular diagnostics, structure analysis, and biomarker discovery

Patrie, S. M., & Cline, E. N. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818607-7.00017-7 · Cited by 5 · see citing works

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 5 · see citing works

Collision-Induced Unfolding, Tandem MS, Bottom-up Proteomics, and Interactomics for Identification of Protein Complexes in Native Surface Mass Spectrometry

Villacob, R. A., Feizi, N., Beno, S. C., & Solouki, T. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00261 · Cited by 4 · see citing works

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., Melani, R. D., Hinkle, J. D., & Fornelli, L. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00385 · Cited by 3 · 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

Investigating direct current potentials that affect native protein conformation during trapped ion mobility spectrometry–mass spectrometry

Voeten, R. L. C., Majeed, H. A., Bos, T. S., Somsen, G. W., & Haselberg, R. (2024) · Journal of Mass Spectrometry · doi:10.1002/jms.5021 · Cited by 3 · see citing works

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 · see citing works

Applications of native mass spectrometry and ultraviolet photodissociation in protein structure and interaction analysis

Jieying, X. U. E., Liu, Z.-Y., & Wang, F. (2024) · Chinese Journal of Chromatography · doi:10.3724/sp.j.1123.2024.01021 · Cited by 2 · see citing works

Multiplexed Single Ion Mass Spectrometry Improves Measurement of Proteoforms and Their ComplexesPreprint

Kafader, J. O., Melani, R. D., Durbin, K. R., Ikwuagwu, B. C., Early, B. P., Fellers, R. T., Beu, S. C., Zabrouskov, V., Makarov, A., Maze, J. T., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/715425 · Cited by 2 · see citing works

Characterization of Gas-Phase Native(-like) Proteins Using Structures for Lossless Ion Manipulations

Lee, J. Y., Gandhi, V., Harrilal, C., Parvate, A. D., Ives, A. N., Bhotika, H., Thibert, S. M., Zhang, X., Schenter, G. K., Larriba‐Andaluz, C., et al. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c02054 · Cited by 1 · see citing works

Proteoforms: General Concepts and Methodological Process for Identification

Araújo, J. D. S., & Machado, O. L. T. (2019) · Proteoforms - Concept and Applications in Medical Sciences · doi:10.5772/intechopen.89914 · Cited by 1 · see citing works

Mass Spectrometry in Measuring Masses of Atoms, Molecules, and Their Complexes: Brief Review of Progress

Milman, B. L., & Журкович, И. К. (2023) · Journal of Analytical Chemistry · doi:10.1134/s1061934823130099

Native Massenspektrometrie erleichtert die Hit‐Validierung in der DNA‐Encoded Library Technologie

Bittner, P., Gloger, A., Keller, M., Oehler, S., Lessing, A., Zhang, Q., Ma, Z., Su, W., Satz, A. L., Kuai, L., et al. (2025) · Angewandte Chemie · doi:10.1002/ange.202504470

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

Jooss, K., McGee, J., Melani, R., & Kelleher, N. (2020) · bioRxiv · doi:10.1002/elps.202000317 · Cited by 32 · see citing works

Preanalytical Strategies for Native Mass Spectrometry Analysis of Protein Modifications, Complexes, and Higher-Order Structures

Ayon, N. J. (2025) · AppliedChem · doi:10.3390/appliedchem5040035 · Cited by 5 · see citing works

Software for the Analysis and Interpretation of Native Mass Spectrometry DataPreprint

Allison, T. M., Barran, P. E., Benesch, J. L. P., Cianférani, S., Degiacomi, M. T., Gabelica, V., Grandori, R., Marklund, E. G., Menneteau, T., Migas, L. G., et al. (2019) · ChemRxiv · doi:10.26434/chemrxiv.11440254

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 · see citing works

Recent Advances of Native Mass Spectrometry Techniques

Wei, T. C.-R. (2022) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.7538/zpxb.2022.0066