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Optimized C-Trap Timing of an Orbitrap 240 Mass Spectrometer for High-Throughput Screening and Native MS by IR-MALDESI

Knizner, K. T., Bagley, M. C., Garrard, K. P., Hauschild, J.-P., Pu, F., Elsen, N. L., Williams, J. D., & Muddiman, D. C. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00319 · Cited by 33 · see citing works

Native Mass Spectrometry-Based Screening for Optimal Sample Preparation in Single-Particle Cryo-EM

Olinares, P. D. B., Kang, J. Y., Llewellyn, E., Chiu, C., Chen, J., Malone, B., Saecker, R. M., Campbell, E. A., Darst, S. A., & Chait, B. T. (2020) · Structure · doi:10.1016/j.str.2020.11.001 · Cited by 32 · see citing works

De novo design of tyrosine and serine kinase-driven protein switches

Woodall, N. B., Weinberg, Z. Y., Park, J., Büsch, F., Johnson, R. S., Feldbauer, M. J., Murphy, M., Ahlrichs, M., Yousif, I., MacCoss, M. J., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00649-8 · Cited by 32 · see citing works

Dissecting the structural heterogeneity of proteins by native mass spectrometry

Reid, D. J., Thibert, S. M., & Zhou, M.-W. (2023) · Protein Science · doi:10.1002/pro.4612 · Cited by 23 · see citing works

Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics

Chapman, E. A., Roberts, D. S., Tiambeng, T. N., Andrews, J., Wang, M.-D., Reasoner, E. A., Melby, J. A., Li, B. H., Kim, D., Alpert, A. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43321-z · Cited by 28 · 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

De novo design of obligate ABC-type heterotrimeric proteins

Bermeo, S., Favor, A., Chang, Y., Norris, A. S., Boyken, S. E., Hsia, Y., Haddox, H. K., Xu, C., Brunette, T., Wysocki, V. H., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00879-4 · Cited by 25 · 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

Mass Spectrometry Analysis of Intact Proteins from Crude Samples

Vimer, S., Ben-Nissan, G., & Sharon, M. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02162 · Cited by 22 · see citing works

Ion Mobility and Surface Collisions: Submicrometer Capillaries Can Produce Native-like Protein Complexes

Panczyk, E. M., Gilbert, J. D., Jagdale, G. S., Stiving, A. Q., Baker, L. A., & Wysocki, V. H. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03666 · Cited by 23 · see citing works

Characterization of [2Fe–2S]‐Cluster‐Bridged Protein Complexes and Reaction Intermediates by use of Native Mass Spectrometric Methods

Jia, M., Sen, S., Wachnowsky, C., Fidai, I., Cowan, J. A., & Wysocki, V. H. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.201915615 · Cited by 24 · see citing works

Collision-Induced Affinity Selection Mass Spectrometry for Identification of Ligands

Mak, T., Rossjohn, J., Littler, D. R., Liu, M., & Quinn, R. J. (2022) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.2c00021 · Cited by 24 · 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

Symmetry of 4-Oxalocrotonate Tautomerase Trimers Influences Unfolding and Fragmentation in the Gas Phase

Sipe, S. N., Lancaster, E. B., Butalewicz, J. P., Whitman, C. P., & Brodbelt, J. S. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c03564 · Cited by 23 · see citing works

Seeing the complete picture: proteins in top-down mass spectrometry.

Habeck, T., & Lermyte, F. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220098 · Cited by 15 · see citing works

In-Depth Structure and Function Characterization of Heterogeneous Interchain Cysteine-Conjugated Antibody–Drug Conjugates

Chen, H., Qiu, D., Shi, J., Wang, N., Li, M., Wu, Y. H., Tian, Y., Bu, X., Liu, Q., Jiang, Y., et al. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00235 · Cited by 22 · see citing works

Not All Arms of IgM Are Equal: Following Hinge-Directed Cleavage by Online Native SEC-Orbitrap-Based CDMS

Yin, V. C., Deslignière, E., Mokiem, N. J., Gazi, I., Lood, R., de Haas, C. J. C., Rooijakkers, S. H. M., & Heck, A. J. R. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00094 · Cited by 22 · see citing works

A Combination of Native LC-MS Approaches for the Comprehensive Characterization of the Antibody-Drug Conjugate Trastuzumab Deruxtecan

Deslignière, E., Diemer, H., Erb, S., Coliat, P., Pivot, X. B., Detappe, A., Hernandez‐Alba, O., & Cianférani, S. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2710290 · Cited by 21 · see citing works

Analysis of Tagged Proteins Using Tandem Affinity-Buffer Exchange Chromatography Online with Native Mass Spectrometry

Büsch, F., VanAernum, Z. L., Lai, S. M., Gopalan, V., & Wysocki, V. H. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00138 · Cited by 21 · 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 22 · see citing works

Cellular mRNA triggers structural transformation of Ebola virus matrix protein VP40 to its essential regulatory form

Landeras-Bueno, S., Wasserman, H., Oliveira, G., VanAernum, Z. L., Büsch, F., Salie, Z. L., Wysocki, V. H., Andersen, K. G., & Saphire, E. O. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108986 · Cited by 18 · see citing works

Light-Regulation of Tryptophan Synthase by Combining Protein Design and Enzymology

Kneuttinger, A. C., Zwisele, S., Straub, K., Bruckmann, A., Büsch, F., Kinateder, T., Gaim, B., Wysocki, V. H., Merkl, R., & Sterner, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205106 · Cited by 18 · see citing works

Microflow size exclusion chromatography to preserve micromolar affinity complexes and achieve subunit separations for native state mass spectrometry

Hecht, E. S., Obiorah, E., Liu, X., Morrison, L. J., Shion, H., & Lauber, M. A. (2022) · Journal of Chromatography A · doi:10.1016/j.chroma.2022.463638 · Cited by 18 · see citing works

Ultra-high-throughput mass spectrometry in drug discovery: fundamentals and recent advances

Williams, J. D., Pu, F., Sawicki, J. W., & Elsen, N. L. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2293153 · Cited by 18 · see citing works

Ion–Ion Charge Reduction Addresses Multiple Challenges Common to Denaturing Intact Mass Analysis

Bailey, A. O., Huguet, R., Mullen, C., Syka, J. E. P., & Russell, W. K. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.1c04973 · Cited by 18 · see citing works

Development of an Automated, High-Throughput Methodology for Native Mass Spectrometry and Collision-Induced Unfolding

Juliano, B. R., Keating, J. W., Li, H. W., Anders, A. G., Xie, Z., & Ruotolo, B. T. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c03788 · Cited by 18 · see citing works

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

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

In a flash of light: X-ray free electron lasers meet native mass spectrometry

Kádek, A., Lorenzen, K., & Uetrecht, C. (2021) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2021.07.001 · Cited by 16 · see citing works

Desalting strategies for native mass spectrometry

Li, Y., Li, W., Zheng, Y., Wang, T., Pu, R., & Zhang, Z. (2024) · Talanta · doi:10.1016/j.talanta.2024.126824 · Cited by 16 · see citing works

UniDec Processing Pipeline for Rapid Analysis of Biotherapeutic Mass Spectrometry Data

Phung, W., Bakalarski, C. E., Hinkle, T. B., Sandoval, W. N., & Marty, M. T. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c02010 · Cited by 16 · see citing works

From inflammation to remodelling: A novel BASP1+ monocyte subset as a catalyst for acute aortic dissection

He, W., Yu, S., Li, J., Li, S., Chen, Z., Zhang, J., Liu, Y., Zhou, M., Yang, T., Cheng, W., et al. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.03.003 · Cited by 15 · see citing works

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

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

Chromatographic separation of peptides and proteins for characterization of proteomes

Liang, Y., Zhang, L., & Zhang, Y. (2022) · Chemical Communications · doi:10.1039/d2cc05568f · Cited by 15 · see citing works

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

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

Nanoscale Methods for Longitudinal Extraction of Intracellular Contents

Quek, Y. J., & Tay, A. K. P. (2024) · Advanced Materials · doi:10.1002/adma.202314184 · Cited by 14 · see citing works

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

Fischer, M. S., Rogers, H. T., Chapman, E. A., Jin, S., & Ge, Y. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c02341 · Cited by 13 · see citing works

Taylor–Aris Dispersion-Assisted Mass Spectrometry for the Analysis of Native Proteins

Szabó, R., Gyémánt, G., Nagy, C., Andrási, M., & Gáspár, A. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c01270 · Cited by 13 · see citing works

Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)2CO group during maturation of E. coli [NiFe]-hydrogenase 2

Arlt, C., Nutschan, K., Haase, A., Ihling, C. H., Tänzler, D., Sinz, A., & Sawers, R. G. (2021) · Scientific Reports · doi:10.1038/s41598-021-03900-w · Cited by 13 · see citing works

Online Buffer Exchange Enables Automated Membrane Protein Analysis by Native Mass Spectrometry

Liu, W., Jayasekera, H. S., Sanders, J. D., Zhang, G., Viner, R., & Marty, M. T. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c02164 · Cited by 13 · see citing works

Impact of Excipient Extraction and Buffer Exchange on Recombinant Monoclonal Antibody Stability

Sarin, D., Krishna, K., Nejadnik, M. R., Suryanarayanan, R., & Rathore, A. S. (2024) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c01157 · Cited by 12 · see citing works

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

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

Toward routine utilisation of native mass spectrometry as an enabler of contemporary drug development

Sternicki, L. M., & Poulsen, S. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00617a · Cited by 12 · see citing works

Digital ion trap mass analysis of high mass protein complexes using IR activation coupled with ion/ion reactions

Lee, K. W., Harrilal, C., Fu, L., Eakins, G. S., & McLuckey, S. A. (2020) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2020.116437 · Cited by 12 · see citing works

Surface-Induced Dissociation for Protein Complex Characterization

Harvey, S. R., Ben‐Nissan, G., Sharon, M., & Wysocki, V. H. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2325-1_15 · Cited by 12 · see citing works

Expanding Native Mass Spectrometry to the Masses

Harvey, S. R., Gadkari, V. V., Ruotolo, B. T., Russell, D. H., Wysocki, V. H., & Zhou, M. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00352 · Cited by 11 · see citing works

An Online Native Mass Spectrometry Approach for Fast, Sensitive, and Quantitative Assessment of Adeno-Associated Virus Capsid Content Ratios

Cotham, V. C., Wang, S., & Li, N. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00151 · Cited by 11 · see citing works

Characterization of adeno-associated virus capsid proteins using denaturing size-exclusion chromatography coupled with mass spectrometry

Tiambeng, T. N., Yan, Y., Patel, S. K., Cotham, V. C., Wang, S., & Li, N. (2024) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2024.116524 · Cited by 11 · see citing works

Progress in Tandem Mass Spectrometry Data Analysis for Nucleic Acids

Lanzillotti, M. B., & Brodbelt, J. S. (2025) · Mass Spectrometry Reviews · doi:10.1002/mas.21923 · Cited by 11 · see citing works

Separation and Collision Cross Section Measurements of Protein Complexes Afforded by a Modular Drift Tube Coupled to an Orbitrap Mass Spectrometer

Sipe, S. N., Sanders, J. D., Reinecke, T., Clowers, B. H., & Brodbelt, J. S. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c01653 · Cited by 13 · see citing works

A High-Throughput Workflow for Mass Spectrometry Analysis of Nucleic Acids by Nanoflow Desalting

Lanzillotti, M. B., & Brodbelt, J. S. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c05428 · Cited by 10 · see citing works

A native SEC-MS workflow and validation for analyzing drug-to-antibody ratio and drug load distribution in cysteine-linked antibody-drug conjugates

Wu, G., Yu, C., Yin, S., Du, J., Zhang, Y., Fu, Z., Wang, L., & Wang, J. (2024) · Journal of Chromatography B · doi:10.1016/j.jchromb.2024.124167 · Cited by 10 · see citing works

Recent advances in gas phase unfolding: Instrumentation and applications

Matney, R., & Gadkari, V. V. (2024) · Journal of Mass Spectrometry · doi:10.1002/jms.5059 · Cited by 10 · see citing works

Oligomeric complexes formed by Redβ single strand annealing protein in its different DNA bound states

Caldwell, B. J., Norris, A. S., Zakharova, E., Smith, C. E., Wheat, C. T., Choudhary, D., Sotomayor, M. M., Wysocki, V. H., & Bell, C. E. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab125 · Cited by 10 · see citing works

Characterizing Non-covalent Protein Complexes Using Asymmetrical Flow Field-Flow Fractionation On-Line Coupled to Native Mass Spectrometry

Ventouri, I. K., Chang, W., Meier, F., Drexel, R., Somsen, G. W., Schoenmakers, P. J., de Spiegeleer, B., Haselberg, R., & Astefanei, A. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.2c05049 · Cited by 10 · see citing works

Multi-dimensional plug-and-play liquid chromatography-native ion mobility mass spectrometry method for the analysis of biotherapeutics

Jia, M., Mozziconacci, O., Abend, A. M., Wuelfing, W. P., & Pennington, J. P. (2021) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2021.116725 · Cited by 10 · see citing works

Use of tandem affinity–buffer exchange chromatography online with native mass spectrometry for optimizing overexpression and purification of recombinant proteins

Lai, S. M., Thirugnanasambantham, P., Sidharthan, V., Norris, A. S., Law, J. D., Gopalan, V., & Wysocki, V. H. (2021) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2021.07.007 · Cited by 10 · see citing works

Direct‐MS analysis of antibody‐antigen complexes

Vimer, S., Ben‐Nissan, G., Marty, M. T., Fleishman, S. J., & Sharon, M. (2021) · PROTEOMICS · doi:10.1002/pmic.202000300 · Cited by 10 · see citing works

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

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

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

The road less taken: Dihydroflavonol 4‐reductase inactivation and delphinidin anthocyanin loss underpins a natural intraspecific flower colour variation

Wong, D. C. J., Wang, Z., Perkins, J., Jin, X., Marsh, G. E., John, E. G., & Peakall, R. (2024) · Molecular Ecology · doi:10.1111/mec.17334 · Cited by 9 · see citing works

Rapid Profiling of the Glycosylation Effects on the Binding of SARS-CoV-2 Spike Protein to Angiotensin-Converting Enzyme 2 Using MALDI-MS with High Mass Detection

Zhou, Y., Tan, C., & Zenobi, R. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c03930 · Cited by 8 · see citing works

Native Mass Spectrometry Dissects the Structural Dynamics of an Allosteric Heterodimer of SARS-CoV‑2 Nonstructural Proteins

Thibert, S. M., Reid, D. J., Wilson, J., Varikoti, R. A., Maltseva, N., Schultz, K., Kruel, A., Babnigg, G., Joachimiak, A., Kumar, N., et al. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00453 · Cited by 8 · see citing works

Coupling Online Size Exclusion Chromatography with Charge Detection-Mass Spectrometry Using Hadamard Transform Multiplexing

Sanders, J. D., Owen, O. N., Tran, B., Mosqueira, J., & Marty, M. T. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c03248 · Cited by 8 · see citing works

Design of pseudosymmetric protein hetero-oligomers

Kibler, R. D., Lee, S., Kennedy, M. A., Wicky, B. I. M., Lai, S. M., Kostelic, M. M., Carr, A., Li, X., Chow, C. M., Nguyen, T. K., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54913-8 · Cited by 13 · see citing works

Determination of ultra-trace metal-protein interactions in co-formulated monoclonal antibody drug product by SEC-ICP-MS

Whitty-Léveillé, L., VanAernum, Z. L., Pavon, J. A., Murphy, C., Neal, K., Forrest, W. P., Gao, X., Zhong, W., Richardson, D. D., & Schuessler, H. A. (2023) · mAbs · doi:10.1080/19420862.2023.2199466 · Cited by 7 · see citing works

Characterization of a Salmonella Transcription Factor-DNA Complex and Identification of the Inducer by Native Mass Spectrometry

Szkoda, B. E., Capua, A. D., Shaffer, J., Behrman, E. J., Wysocki, V. H., & Gopalan, V. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167480 · Cited by 7 · see citing works

Isobaric Stable Isotope N‐Phosphorylation Labeling (iSIPL) for Ultrasensitive Proteome Quantification

Wang, X., Chen, C., He, Y., Ding, L., Wu, Y., Huang, C., Wu, J., Ding, R., Xue, Y., Lin, Z., et al. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202303656 · Cited by 7 · see citing works

Dissecting the Heterogeneous Glycan Profiles of Recombinant Coronavirus Spike Proteins with Individual Ion Mass Spectrometry

Stiving, A. Q., Foreman, D. J., VanAernum, Z. L., Dürr, E., Wang, S., Vlasak, J., Galli, J. D., Kafader, J. O., Tsukidate, T., Li, X., et al. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00309 · Cited by 7 · see citing works

Native Taylor/Non‐Taylor Dispersion–Mass Spectrometry (TNT‐MS) Allows Rapid Protein Desalting and Multiplexed, Label‐Free Ligand Screening

Eisert, J., Maciel, E. V. S., Dederer, V., Berwanger, A., Bailey, H., Đikić, I., Knapp, S., Empting, M., Mathea, S., Jensen, H. M., et al. (2025) · Small Methods · doi:10.1002/smtd.202500658 · Cited by 6 · see citing works

Oxidized and Reduced Dimeric Protein Complexes Illustrate Contrasting CID and SID Charge Partitioning

Jia, M., Song, Y., Du, C., & Wysocki, V. H. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00142 · Cited by 6 · see citing works

Rapid Online Buffer Exchange: A Method for Screening of Proteins, Protein Complexes, and Cell Lysates by Native Mass SpectrometryPreprint

VanAernum, Z. L., Büsch, F., Jones, B. J., Jia, M., Chen, Z., Boyken, S. E., Sahasrabuddhe, A., Baker, D. A., & Wysocki, V. H. (2019) · ChemRxiv · doi:10.26434/chemrxiv.8792177

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 · see citing works

Online Buffer Exchange Enables Automated Membrane Protein Analysis by Native Mass Spectrometry

Liu, W., Jayasekera, H. S., Sanders, J. D., Zhang, G., Viner, R., & Marty, M. T. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c02164 · Cited by 13 · see citing works

Screening Tagged Proteins Using Tandem Affinity-Buffer Exchange Chromatography Online with Native Mass SpectrometryPreprint

Büsch, F., VanAernum, Z. L., Lai, S. M., Gopalan, V., & Wysocki, V. H. (2021) · ChemRxiv · doi:10.26434/chemrxiv.14035691

Development of native mass spectrometry with nanoelectrospray ionization coupled to size exclusion chromatography for proteins

Saikusa, K., Kinumi, T., & Kato, M. (2022) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.9395 · Cited by 3 · see citing works