The DOI matches its Crossref record; 493 of the 494 references it cites were found in a registry or an index.
High-Resolution Native Mass Spectrometry
Open accessAbstract
Native mass spectrometry (MS) involves the analysis and characterization of macromolecules, predominantly intact proteins and protein complexes, whereby as much as possible the native structural features of the analytes are retained. As such, native MS enables the study of secondary, tertiary, and even quaternary structure of proteins and other biomolecules. Native MS represents a relatively recent addition to the analytical toolbox of mass spectrometry and has over the past decade experienced immense growth, especially in enhancing sensitivity and resolving power but also in ease of use. With the advent of dedicated mass analyzers, sample preparation and separation approaches, targeted fragmentation techniques, and software solutions, the number of practitioners and novel applications has risen in both academia and industry. This review focuses on recent developments, particularly in high-resolution native MS, describing applications in the structural analysis of protein assemblies, proteoform profiling of─among others─biopharmaceuticals and plasma proteins, and quantitative and qualitative analysis of protein-ligand interactions, with the latter covering lipid, drug, and carbohydrate molecules, to name a few.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Native mass spectrometry has made significant advances over the last decade and has both been applied to analyze intact proteins and protein complexes which have been extensively reviewed.82,85”
From Connecting metabolome and phenotype: recent advances in functional metabolomics tools for the identification of bioactive natural products (2024) · cites this paper as [82]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Electrospray Ionization for Mass Spectrometry of Large Biomolecules
Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., & Whitehouse, C. M. (1989) · Science · doi:10.1126/science.2675315 · Cited by 7,634
Pushko, P., Pumpens, P., & Grens, E. (2013) · Intervirology · doi:10.1159/000346773 · Cited by 5,975
Anion Recognition and Sensing: The State of the Art and Future Perspectives
Beer, P. D., & Gale, P. A. (2001) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20010202)40:3 · Cited by 3,633
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
Mass-spectrometric exploration of proteome structure and function
Aebersold, R., & Mann, M. (2016) · Nature · doi:10.1038/nature19949 · Cited by 2,334
Fourier transform ion cyclotron resonance mass spectrometry: A primer
Marshall, A. G., Hendrickson, C. L., & Jackson, G. S. (1998) · Mass Spectrometry Reviews · doi:10.1002/(sici)1098-2787(1998)17:1 · Cited by 1,992
Lessons from nature about solar light harvesting
Scholes, G. D., Fleming, G. R., Olaya-Castro, A., & van Grondelle, R. (2011) · Nature Chemistry · doi:10.1038/nchem.1145 · Cited by 1,915
Olsen, J. V., de Godoy, L. M. F., Li, G., Maček, B., Mortensen, P., Pesch, R., Makarov, A., Lange, O., Horning, S. R., & Mann, M. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500030-mcp200 · Cited by 1,539
Site-specific glycan analysis of the SARS-CoV-2 spike
Watanabe, Y., Allen, J. D., Wrapp, D., McLellan, J. S., & Crispin, M. (2020) · Science · doi:10.1126/science.abb9983 · Cited by 1,538
Surface Plasmon Resonance: A Versatile Technique for Biosensor Applications
Nguyen, H. H., Park, J., Kang, S., & Kim, M. (2015) · Sensors · doi:10.3390/s150510481 · Cited by 1,372
Flagged first, then by citations
1 of the 494 references couldn’t be matched to a known paper.
Research works printed but not linked: 3
- McNaught A. D., 1997, Compendium of Chemical Terminology: IUPAC Recommendations (The “Gold Book”)
- Mamyrin B. A., 1973, Zh. Ehksp. Teor. Fiz., 64, 82
- Ye B., 2003, Clin. Cancer Res., 9, 2904
Cited by
Sorted by citations
Items 301–400 of 509
Phan, M. Q., Chandrashekaran, I. R., Akhtar, N., Konstantinidou, E., Devine, S. M., Doak, B. C., Nebl, T., Creek, D. J., Scanlon, M. J., & Norton, R. S. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00154 · 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
Fabbrizi, E., Fiorentino, F., Casano, F., Mai, A., & Rotili, D. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2486146 · Cited by 3
“This structural MS method, when combined with nMS, elucidates the three-dimensional architecture and topologies of ternary complexes and other identified intermediate species, therefore delivering conformational details [64,65].”
3D Structure Determination of Protein Complexes using Matrix-Landing Mass SpectrometryPreprint
Westphall, M. S., Lee, K. W., Salome, A. Z., Lodge, J. M., Grant, T., & Coon, J. J. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.13.464253 · Cited by 3
Troutman, M. D. (2023) · Wiley eBooks · doi:10.1002/9781119678496.ch14 · Cited by 3
Ivanova, B. B. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4606434 · Cited by 3
Fast tracking native mass spectrometry: Skipping over buffer exchangePreprint
Grün, A. F. R., Said, F.-A., Schamoni-Kast, K., Damjanović, T., Berikkara, A., Schroeder, J., Brockmann, F. K., Lichtenberg, T., Bosse, J. B., & Uetrecht, C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.22.639503 · Cited by 3
“This can be troublesome when analyzing large protein complexes by nMS. High protein concentration is often crucial for higher-order complex formation.”
InfluentialNative metabolomics for mass spectrometry-based siderophore discovery.
(2024) · Methods in Enzymology · doi:10.1016/bs.mie.2024.07.001 · Cited by 2
Xia, R., Wang, N., Cai, X., Yang, J., Liu, H., Liu, H., Liu, H., Zhang, Q., Tao, Z., & Wang, W. (2024) · Fuel · doi:10.1016/j.fuel.2024.133628 · Cited by 2
Zhang, X., & Gong, X. (2025) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.4c08663 · Cited by 2
Han, J., A, W. C. V. V., Quinn, R. J., & Liu, M. (2025) · Chemosensors · doi:10.3390/chemosensors13050166 · Cited by 2
Lai, C., Liu, Z., Luo, P., Jin, Z., Zhao, H., & Wang, F. (2025) · Chemical Research in Chinese Universities · doi:10.1007/s40242-025-5046-4 · Cited by 2
Fiala, J., Schuster, D., & Heck, A. J. R. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00109 · Cited by 2
Self-citationGroignet, L., Dellemme, D., Duez, Q., Fizazi, A., Colet, J.-M., Brocorens, P., Surin, M., Gerbaux, P., & Winter, J. D. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00259 · Cited by 2
Wu, Y., Li, X., Liao, Z., Lin, H., Liu, X., Sun, Z., Li, Z., & Huang, P. J. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.5c01565 · Cited by 2
Advancing post-genomics research in Mexico: Opportunities and strategies for the next decade
Winkler, R., & Moreno‐Ulloa, A. (2025) · Journal of Proteomics · doi:10.1016/j.jprot.2025.105551 · Cited by 2
Sui, B., Wang, Y., Ma, S., Sun, S., Xi, H., Wang, D., Zhang, S., Zhang, H., & Zhao, W. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c04362 · Cited by 2
Vadivalagan, C., Zhang, J., Dai, J., Liu, S., Singal, A. G., Bass, K., Parikh, N. D., & Lubman, D. M. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00626 · Cited by 2
Sadighi, R., van Paasen, R. M. A., Hutchins, G. H., Jansen, I. D., Neubacher, S., Grossmann, T. N., & Rijs, A. M. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06844 · Cited by 2
Uversky, V. N. (2025) · Frontiers in Biophysics · doi:10.3389/frbis.2025.1693360 · Cited by 3
Stress-Induced Antibody Aggregates: Insights from Native SEC-MS with Postcolumn Denaturation
Ivanov, D. G., Lee, C. M., Delgado, D. A., Brewer, L., Corbo, J., Fitzpatrick, C., Cheng, Z., Albee, K., Lee, K. S., & Tousi, F. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00305 · Cited by 2
Wedasingha, L., Rydberg, M. P., Bruening, M. L., & Manicke, N. E. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06786 · Cited by 2
Bolívar, E. G. B., Fortin, J. S., Ademoye, T. A., & McLuckey, S. A. (2026) · The Analyst · doi:10.1039/d5an01336d · Cited by 2
Unveiling BCL-xL-specific PROTAC efficiency and dissociation pathways using native mass spectrometry
Gadallah, M. I., Nonhof, K. L., Nayak, D., Zhang, P., Dioli, O. E., Zheng, G., Olsen, S. K., Zhou, D., & Brodbelt, J. S. (2026) · Chemical Science · doi:10.1039/d5sc07400b · Cited by 4
“35 – 37 Native MS has been successfully used to study model PROTACs, such as AT1, MZ1, and GNE-987, in complex with Brd4 bromodomains, o ff ering valuable insights into their a ffi nities, complex stoichiometries and cooperativity.”
De Novo Structure Prediction from Tandem Mass Spectra: Algorithms, Benchmarks, and Limitations
Schneider, M. Y., Kholmanskikh, D. D., Romanov, K. Y., Perekina, E. A., Nikolenko, S. A., Lukin, R. Y., & Golov, I. V. (2026) · Molecules · doi:10.3390/molecules31050769 · Cited by 2
Structural mass spectrometry techniques for characterisation of plant and algal proteins
Durant, R. J., Živković, D., & Bolla, J. R. (2026) · The Plant Journal · doi:10.1111/tpj.70780 · Cited by 2
Ion Activation Methods for Top‐Down Proteomics
Walker, J. N., & Brodbelt, J. S. (2026) · Mass Spectrometry Reviews · doi:10.1002/mas.70023 · Cited by 4
Schulte, J., Schwegler, E., Hellmich, U. A., & Morgner, N. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c18602 · Cited by 4
Analyses of Individual Singly Charged Ions Using a High-Field Orbitrap Analyzer
Giaretta, E., Deslignière, E., Ebberink, E. H. T. M., Wörner, T. P., Barendregt, A., Fort, K. L., Makarov, A., & Heck, A. J. R. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c02125 · Cited by 4
Self-citationPathak, K., Brinkman, D., & Gomes, F. P. (2026) · Journal of Mass Spectrometry · doi:10.1002/jms.70075 · Cited by 2
Ying, Y., & Li, H. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.341971 · Cited by 2
A Boron‐Dependent Antibiotic Derived from a Calcium‐Dependent Antibiotic
Chiou, S., Chen, Y., Lee, C., Ho, M. N., Miao, J., Kuo, P., Hsu, C., Lin, Y., & Chu, J. (2023) · Angewandte Chemie · doi:10.1002/ange.202317522 · Cited by 2
Cramer, D. A. T., Yin, V. C., Čaval, T., Franc, V., Yu, D., Wu, G., Lloyd, G., Langendorf, C. G., Whisstock, J. C., Law, R. H. P., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100696 · Cited by 3
Self-citationNative Separation-Mass Spectrometry in Biopharmaceutical Analysis
Jooß, K., & Somsen, G. W. (2023) · LCGC Europe · doi:10.56530/lcgc.eu.mq5567q6 · Cited by 2
Lin, L., Sun, S., & Yu, Q. (2024) · Spectrochimica Acta Part B Atomic Spectroscopy · doi:10.1016/j.sab.2024.106959 · Cited by 2
Yang, J., Hu, X., Zhang, Y., Zhao, L., Yue, C., Cao, Y., Zhang, Y., & Zhao, Z. (2024) · Chinese Chemical Letters · doi:10.1016/j.cclet.2024.110128 · Cited by 2
Harper, C. C., Schloemer, T. H., Jordan, J. S., Heflin, N., Narayanan, P., Zhou, Q., Congreve, D. N., & Williams, E. R. (2024) · ACS Nano · doi:10.1021/acsnano.4c12461 · Cited by 2
Santambrogio, C., Toccafondi, M., Donnici, L., Pesce, E., Francesco, R. D., Grifantini, R., Ponzini, E., Milanesi, F., Fragai, M., Nativi, C., et al. (2025) · ChemBioChem · doi:10.1002/cbic.202500106 · Cited by 2
In‐Cell Fast Photochemical Oxidation Interrogates the Native Structure of Integral Membrane Proteins
Sun, J., Mierxiati, S., Rempel, D. L., Cao, Q., Chai, M., Li, W., & Gross, M. L. (2025) · Angewandte Chemie · doi:10.1002/ange.202424779 · Cited by 2
Analisis Tingkat Stress Orang Tua Ketika Mengasuh Anak Selama Masa Pandemi
Fernianti, A. (2022) · Jurnal Obsesi Jurnal Pendidikan Anak Usia Dini · doi:10.31004/obsesi.v6i3.1957 · Cited by 2
Soft Ionization Mass Spectrometry for Studying Noncovalent Interactions
Zenobi, R. (2022) · CHIMIA International Journal for Chemistry · doi:10.2533/chimia.2022.101 · Cited by 2
Nanni, P., Gehrig, P., & Schlapbach, R. (2022) · CHIMIA International Journal for Chemistry · doi:10.2533/chimia.2022.73 · Cited by 2
Schwartz, E. A., Bravo, J. P. K., Macias, L. A., McCafferty, C. L., Dangerfield, T. L., Walker, J. N., Brodbelt, J. S., Fineran, P. C., Fagerlund, R. D., & Taylor, D. W. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.13.496011 · Cited by 2
Native mass spectrometry reveals binding interactions of SARS-CoV-2 PLpro with inhibitors and ISG15Preprint
James, V. K., Godula, R., Perez, J., Butalewicz, J. P., Sipe, S. N., Huibregtse, J. M., & Brodbelt, J. S. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-v6j35 · Cited by 2
Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactionsPreprint
Lyu, J., Zhang, T., Marty, M. T., Clemmer, D. E., Russell, D. H., & Laganowsky, A. D. (2024) · eLife · doi:10.7554/elife.91094.2 · Cited by 2
Membrane Proteins: Challenging Biotherapeutic Targets
Jayasekera, H. S., Mohona, F. A., & Marty, M. T. (2025) · Wiley eBooks · doi:10.1002/9781394236145.ch18 · Cited by 2
Byrd, E. J., Norgate, E. L., Crossley, J. A., Chau, C. C. C., Schiffrin, B., Kulak, A. N., Radford, S. E., Actis, P., Calabrese, A. N., & Sobott, F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.19.671163 · Cited by 2
Structural Phylogenetics with Protein Mass Spectrometry: A Proof-of-Concept
Todd, B. P., & Downard, K. M. (2024) · The Protein Journal · doi:10.1007/s10930-024-10227-8 · Cited by 1
Unveiling the Molecular Fingerprint: Mass Spectrometry in Metabolomics
Abdi, G., Dhariwal, R., Patil, N., Upadhyay, B., Jain, M., & Tarighat, M. A. (2024) · Springer eBooks · doi:10.1007/978-981-97-7459-3_6 · Cited by 1
In situ characterization of amine‐forming enzymes shows altered oligomeric state
Caparco, A. A., Bommarius, B., Ducrot, L., Champion, J. A., Vergne‐Vaxelaire, C., & Bommarius, A. S. (2024) · Protein Science · doi:10.1002/pro.5248 · Cited by 1
How Native Are Peptides After Activation by Collisions or Photons? A Gas‐Phase FRET Study
Greis, K., Busse, L. F., Benzenberg, L. R., Wu, R., & Zenobi, R. (2025) · Helvetica Chimica Acta · doi:10.1002/hlca.202500043 · Cited by 1
High Abundance of Atmospheric Sulfonates Derived from Light-Duty Gasoline Vehicles
Chen, S., Han, H., Ren, L., Xu, Y., Wu, L., Gao, Y., Yi, Y., Yang, X., Fu, M., Yin, H., et al. (2025) · ACS ES&T Air · doi:10.1021/acsestair.4c00334 · Cited by 1
Kwok, T., Chan, S.-L., Xu, N., Huang, T.-M., & Bo, T. (2025) · Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · doi:10.1016/j.jchromb.2025.124705 · Cited by 1
Nguyen, S. H., & Tran, M. T. (2025) · PLoS ONE · doi:10.1371/journal.pone.0328304 · Cited by 1
Exploring Proteins and Peptides as Natural Excipients
Parekh, N., Patel, M. N., Nandpal, M. N., & Dua, K. (2025) · Springer eBooks · doi:10.1007/978-981-96-7959-1_7 · Cited by 1
James, V. K., Dioli, O. E., & Brodbelt, J. S. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00159 · Cited by 1
Abdelmalek, N., Yousief, S. W., Tanca, A., Bojer, M. S., Alobaidallah, M. S. A., Olsen, J. E., & Paglietti, B. (2025) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2025.107652 · Cited by 1
Wang, W., Ji, X., Gorrea-Acín, P., Lau, K., Pojer, F., Ward, T. R., & Hu, X. (2025) · Nature Synthesis · doi:10.1038/s44160-025-00940-2 · Cited by 1
Luo, P., Zhang, D., Liu, C., Zhao, H., Zhang, W., Xiao, C., Wang, J., Yang, X., Liu, Z., & Wang, F. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00287 · Cited by 1
Zhu, J., Bauzá‐Martinez, J., Gouw, J. W., Zhao, X., Heck, A. J. R., Stahl, B., Reiding, K. R., & Dingess, K. A. (2025) · Frontiers in Nutrition · doi:10.3389/fnut.2025.1697081 · Cited by 1
Self-citationSternicki, L. M., Crowe, C., Wieske, L. H. E., Ciulli, A., & Poulsen, S. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c01970 · Cited by 3
Oney-Hawthorne, S. D., Barondeau, D. P., & Russell, D. H. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00280 · Cited by 1
Integrated Native Mass Spectrometry Imaging of Soluble and Membrane Proteins
Hale, O. J., & Cooper, H. J. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c16821 · Cited by 1
Rox, K. (2026) · ChemMedChem · doi:10.1002/cmdc.202500743 · Cited by 1
Hodnik, B., Čamič, Ž., & Pompe, M. (2026) · Molecules · doi:10.3390/molecules31061001 · Cited by 1
“Despite the conceptual attractiveness of SEC for proteins and aggregate analysis, coupling SEC directly to high-resolution mass spectrometry (HRMS) remains relatively underexplored [18–20].”
Neusüß, C., Lioe, H., Dite, T. A., Ow, S. Y., & Pelzing, M. (2026) · Journal of Mass Spectrometry · doi:10.1002/jms.70048 · Cited by 1
“Native mass spectrometry has become an important technique for studying proteins and protein complexes under near-physiological conditions [1–5].”
Gadallah, M. I., McConnell, K. A., Hager, K. M., James, V. K., Nguyen, A. W., Maynard, J. A., & Brodbelt, J. S. (2026) · Chemical Science · doi:10.1039/d5sc09702a · Cited by 1
“43,46 49 With its exceptional mass accuracy and high resolution, nMS pushes the boundaries of mass analysis, enabling the detailed study of interactions between therapeutic mAbs and di ff erent antigen proteoforms.”
Top‐Down Mass Spectrometry–Based Structural and Functional Proteomics: A Perspective
Cupp‐Sutton, K. A., & Wu, S. (2026) · Journal of Mass Spectrometry · doi:10.1002/jms.70044 · Cited by 1
Štěpánová, S., & Kašička, V. (2026) · Journal of Separation Science · doi:10.1002/jssc.70395 · Cited by 1
Stroganova, I., Ollivier, S., Radić, L., Smyrnakis, A., Kosmopoulou, M., Schinkel, J., Sliepen, K., Greisch, J., & Heck, A. J. R. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c07319 · Cited by 2
Self-citationMitra, A., Chakraborty, A., Upadhye, T. S., Sahu, S., Tawate, M., Chakraborty, S., Chakravarty, R., Vimalnath, K. V., Kar, S., Sengupta, D., et al. (2026) · RSC Advances · doi:10.1039/d5ra07970e · Cited by 1
“58 Furthermore, the orthogonal sampling interface of Q-TOF instruments limits the transmission of solvent clusters into the mass analyser.”
Wu, Y.-H. S., Lin, Y., & Chen, Y. (2026) · Poultry Science · doi:10.1016/j.psj.2026.106956 · Cited by 1
Native mass spectrometry meets X-rays for the elucidation of protein structures
Kierspel, T., Santis, E. D., Schamoni-Kast, K., Blanchet, C. E., Marklund, E. G., Caleman, C., & Uetrecht, C. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250111 · Cited by 1
Time-Resolved Native Mass Spectrometry for Direct Measurement of Biomolecular Kinetics
James, V. K., Stover, L., Bahramimoghaddam, H., Khandelwal, T., Chang, J., Downing, J., Scott, E., Bailey, K. O., Russell, D. H., Baker, L. A., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c21842 · Cited by 1
“21,22 While the technique has been used to determine equilibrium binding constants and thermodynamics, 23 − 28 the use of native MS to determine kinetics of protein − ligand interactions has largely been limited to slow processes (for review see refs 20,29).”
Balıkçı, E., & Akıl, C. (2026) · Sensors · doi:10.3390/s26103105 · Cited by 2
“This trend is especially evident in SPR, MST, and MS-based workflows, where improved fluidics, multiplexing, and automated preparation are increasing experimental throughput while preserving mechanistic depth [7,10,48].”
InfluentialMagnetic Cellulose Nanocrystal Composites: Synthesis, Properties, Applications, and Opportunities
Hasan, M. J., Chand, K., Ureña-Benavides, E. E., & Vasquez, E. S. (2026) · Nanomaterials · doi:10.3390/nano16110645 · Cited by 1
Applying Distinct CDMS Strategies to Observe Nonclassical Virus Capsid Assembly
Thiede, L., Haris, A., Damjanović, T., Kung, J. C. K., Müller-Guhl, J., Pogan, R., Rothe, J., Schultze, W., Ugelstad, S., Eatough, D., et al. (2026) · Journal of Mass Spectrometry · doi:10.1002/jms.70068 · Cited by 1
Zhang, W., Ma, R., Jiang, T., & Xu, W. L. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c01433 · Cited by 1
Charge Loss of Proteins in vacuo: Implications for Native Mass Spectrometry and Ion Mobility
Bejoy, M., Österlund, N., Jordan, J. S., Pagel, K., & Geue, N. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c04928 · Cited by 1
Krichel, B., Chan, H., Bandura, L. J., Gao, Z., Wang, M., Rogers, H. T., McIlwain, S. J., Uetrecht, C., & Ge, Y. (2026) · Science Advances · doi:10.1126/sciadv.aeg5294 · Cited by 1
A butterfly effect: From a single nucleotide to altered immunity
Bechtella, L., & Pagel, K. (2023) · Chem · doi:10.1016/j.chempr.2023.02.014 · Cited by 1
A Bayesian approach for constituent estimation in nucleic acid mixture models
Tomono, T., Hara, S., Nakai, Y., Takahara, K., Iida, J., & Washio, T. (2024) · Frontiers in Analytical Science · doi:10.3389/frans.2023.1301602 · Cited by 1
Eronen, V., Iljin, K., Pääkkönen, J., Jänis, J., Rouvinen, J., Nevanen, T. K., & Hakulinen, N. (2024) · ACS Omega · doi:10.1021/acsomega.3c09027 · Cited by 1
Mutational Analysis of RIP Type I Dianthin-30 Suggests a Role for Arg24 in Endocytosis
Schlaak, L., Weise, C., Kuropka, B., & Weng, A. (2024) · Toxins · doi:10.3390/toxins16050219 · Cited by 1
“His His His To circumvent the drawbacks of SPR measurements of surface-active compounds (unspeci fi c binding to the sensor surface) such as triterpene saponins, native mass spectrometry (MS) was chosen, which detects binding in the gas phase under non-denaturing conditions [42,43].”
MethodCharge Detection Mass Spectrometry for Megadalton Protein Analysis
Yamaguchi, Y. (2024) · Journal of the Mass Spectrometry Society of Japan · doi:10.5702/massspec.s24-12 · Cited by 1
Fe-S cluster biosynthesis and maturation: Mass spectrometry-based methods advancing the field
Oney-Hawthorne, S. D., & Barondeau, D. P. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119784 · Cited by 1
Unraveling Clinical Glycoproteome by Integrating Affinity Enrichment with Nanopore Sequencing
Ali, I., Ali, M. M., Liu, Q., & Hu, L. (2024) · ChemBioChem · doi:10.1002/cbic.202400419 · Cited by 1
Crack, J. C., & Brun, N. E. L. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119865 · Cited by 1
Gel electrophoresis-based proteoform separation and analysis
Dowling, P., & Ohlendieck, K. (2025) · Advances in clinical chemistry · doi:10.1016/bs.acc.2025.04.002 · Cited by 1
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
Hoppe, I. J., Prommegger, B., Uhl, A., Lohrig, U., Huber, C. G., & Brandstetter, H. (2022) · ChemBioChem · doi:10.1002/cbic.202200399 · Cited by 1
Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactionsPreprint
Lyu, J., Zhang, T., Marty, M. T., Clemmer, D. E., Russell, D. H., & Laganowsky, A. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.03.547565 · Cited by 1
Single-molecule digital sizing of proteins in solutionPreprint
Krainer, G., Jacquat, R. P. B., Schneider, M. M., Welsh, T. J., Fan, J., Peter, Q. A. E., Andrzejewska, E. A., Šneiderienė, G., Czekalska, M. A., Ausserwӧger, H., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.12.548675 · Cited by 1
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.18.567687 · Cited by 1
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2024) · eLife · doi:10.7554/elife.94407.1 · Cited by 1
Adapting a trapped ion mobility spectrometry-Q-TOF for native mass spectrometryPreprint
Lin, Y.-F., Jones, B., Ridgeway, M. E., Panczyk, E. M., Somogyi, Á., Kaplan, D. A., Marathe, I. A., Yun, S., Laganowsky, A. D., Park, M. A., et al. (2024) · ChemRxiv · doi:10.26434/chemrxiv-2024-xmjml · Cited by 1
Stochastic Dynamics Mass Spectrometry of Caffeine MetabolitesPreprint
Ivanova, B. B. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4825115 · Cited by 1
Lotay, N., Suarez, C. M., Franier, B. D. L., Jockusch, R. A., & Thompson, M. E. (2024) · Preprints.org · doi:10.20944/preprints202407.1589.v1 · Cited by 1
Membrane Proteins: Challenging Biotherapeutic TargetsPreprint
Jayasekera, H. S., Mohona, F. A., & Marty, M. T. (2024) · ChemRxiv · doi:10.26434/chemrxiv-2024-dz7rf · Cited by 1
Tandem Mass Spectrometry for Peptide Sequencing
Mishra, S., & Rathod, N. V. (2025) · doi:10.1002/9781394314133.ch17 · Cited by 1
Metadata
- Authors
- Tamara, S., den Boer, M. A., & Heck, A. J. R.
- Affiliations
- Utrecht University (NL)
- Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands
- Corresponding author
- Heck, Albert J. R.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2021-08-20
- Volume
- 122
- Issue
- 8
- Pages
- 7269-7326
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- PMC
- PMC9052423
- OpenAlex
- W3194897413
- Cited by
- 511
- References
- 494
- Citations by year
- 2026: 95 · 2025: 138 · 2024: 123 · 2023: 95 · 2022: 54 · 2021: 6
- FWCI
- 7.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Chemical Reviews (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NACTAR 16442, SPI.2017.028)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- native mass spectrometry, high-resolution mass spectrometry, protein structure, protein complexes, protein assembly, biopharmaceuticals, plasma proteins, protein-ligand interactions, protein-lipid interactions, drug-protein interactions, carbohydrate-protein interactions, mass analyzers
- MeSH terms
- Ligands, Proteins, Mass Spectrometry, Macromolecular Substances
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review