Here are a number of relevant publications on top-down methods and applications.  Use the search box or browse all below.

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Wang, Q., Wang, Q., Zhu, G. & Sun, L. Capillary Electrophoresis–Mass Spectrometry for Top-Down Proteomics. Annual Review of Analytical Chemistry (2025) http://doi.org/10.1146/annurev-anchem-071124-092242.
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Schairer, J., Römer, J. & Neusüß, C. CE-MS and CE-MS/MS for the multiattribute analysis of monoclonal antibody variants at the subunit level. Journal of Pharmaceutical and Biomedical Analysis 252, 116495 (2025).
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Matzanke, T. et al. Cysteine-Directed Isobaric Labeling Combined with GeLC-FAIMS-MS for Quantitative Top-Down Proteomics. J. Proteome Res. (2025) doi:10.1021/acs.jproteome.4c00835.
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Knott, S. J. et al. Deciphering Proteoform Landscape of Mammary Carcinoma by Top-Down Proteomics. J. Proteome Res. (2025) doi:10.1021/acs.jproteome.4c01044.
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Lutomski, C. A. et al. Defining proteoform-specific interactions for drug targeting in a native cell signalling environment. Nat. Chem. 1–11 (2025) http://doi.org/10.1038/s41557-024-01711-w.
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Benazza, R. et al. Development of Top-Down Mass Spectrometry Strategies in the Chromatographic Time Scale (LC-TD-MS) for the Extended Characterization of an Anti-EGFR Single-Domain Antibody-Drug Conjugate in Both Reduced and Nonreduced Forms. Anal. Chem. 97, 2639–2647 (2025).
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Pavek, J. G. et al. Intact Mass Proteomics Using a Proteoform Atlas. J. Proteome Res. 24, 323–332 (2025).
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Takemori, A., Kaulich, P. T., Tholey, A. & Takemori, N. PEPPI-MS: gel-based sample pre-fractionation for deep top-down and middle-down proteomics. Nat Protoc 1–26 (2025) http://doi.org/10.1038/s41596-024-01100-0.
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Denefeld, B. et al. Revealing Unpredicted Aspartic Acid Isomerization Hotspots by Probing Diagnostic Fragmentation Propensities in Top-Down and Middle-Down Mass Spectrometry. J. Am. Soc. Mass Spectrom. (2025) doi:10.1021/jasms.4c00443.
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Britt, H. M., Ben-Younis, A., Page, N. & Thalassinos, K. A Conformation-Specific Approach to Native Top-down Mass Spectrometry. J. Am. Soc. Mass Spectrom. 35, 3203–3213 (2024).
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Wang, Q. et al. A simple and efficient approach for preparing cationic coating with tunable electroosmotic flow for capillary zone electrophoresis-mass spectrometry-based top-down proteomics. Analytica Chimica Acta 343162 (2024) http://doi.org/10.1016/j.aca.2024.343162.
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Contini, C. et al. A top-down proteomic approach reveals a salivary protein profile able to classify Parkinson's disease with respect to Alzheimer's disease patients and to healthy controls. PROTEOMICS 24, 2300202 (2024).
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Lakis, R. et al. Absolute Quantification of Human Serum Albumin Isoforms by Internal Calibration Based on a Top-Down LC-MS Approach. Anal. Chem. (2024) doi:10.1021/acs.analchem.3c03933.
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Hidayah, S. N. et al. Application of sample displacement batch chromatography for fractionation of proteoforms. PROTEOMICS 24, 2200424 (2024).
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Mikawy, N. N. et al. Are Internal Fragments Observable in Electron Based Top-Down Mass Spectrometry? Molecular & Cellular Proteomics 0, (2024).
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Schwenzer, A.-K., Kruse, L., Jooß, K. & Neusüß, C. Capillary electrophoresis-mass spectrometry for protein analyses under native conditions: Current progress and perspectives. PROTEOMICS 24, 2300135 (2024).
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Wang, Q., Fang, F., Wang, Q. & Sun, L. Capillary zone electrophoresis-high field asymmetric ion mobility spectrometry-tandem mass spectrometry for top-down characterization of histone proteoforms. PROTEOMICS 24, 2200389 (2024).
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Oates, R. N., Lieu, L. B., Srzentić, K., Damoc, E. & Fornelli, L. Characterization of a Monoclonal Antibody by Native and Denaturing Top-Down Mass Spectrometry. J. Am. Soc. Mass Spectrom. 35, 2197–2208 (2024).
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Shah, A., Cui, W., Harrahy, J. & Ivanov, A. R. Characterization of charge variants, including post-translational modifications and proteoforms, of bispecific antigen-binding protein by cation-exchange chromatography coupled to native mass spectrometry. Talanta 266, 125062 (2024).
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Habeck, T., Maciel, E. V. S., Kretschmer, K. & Lermyte, F. Charge site manipulation to enhance top-down fragmentation efficiency. PROTEOMICS 24, 2300082 (2024).
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Fang, F., Gao, G., Wang, Q., Wang, Q. & Sun, L. Combining SDS-PAGE to capillary zone electrophoresis-tandem mass spectrometry for high-resolution top-down proteomics analysis of intact histone proteoforms. PROTEOMICS n/a, 2300650 (2024).
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Zhu, G., Sadeghi, S. A., Mahmoudi, M. & Sun, L. Deciphering nanoparticle protein corona by capillary isoelectric focusing-mass spectrometry-based top-down proteomics. Chem. Commun. (2024) http://doi.org/10.1039/D4CC02666G.
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D’Ippolito, R. A. et al. Determining KRAS4B-Targeting Compound Specificity by Top-Down Mass Spectrometry. Methods Mol Biol 2823, 291–310 (2024).
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Watts, E., Bashyal, A., Dunham, S. D., Crittenden, C. M. & Brodbelt, J. S. Enhanced Characterization of Lysine-Linked Antibody Drug Conjugates Enabled by Middle-Down Mass Spectrometry and Higher-Energy Collisional Dissociation-Triggered Electron-Transfer/Higher-Energy Collisional Dissociation and Ultraviolet Photodissociation. Antibodies 13, 30 (2024).
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Sokratous, K. et al. Enhanced Declustering Enables Native Top-Down Analysis of Membrane Protein Complexes using Ion-Mobility Time-Aligned Fragmentation. J. Am. Soc. Mass Spectrom. 35, 1891–1901 (2024).
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Lieu, L. B. et al. Enhanced Payload Localization in Antibody–Drug Conjugates Using a Middle-Down Mass Spectrometry Approach with Proton Transfer Charge Reduction. Anal. Chem. 96, 18483–18490 (2024).
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Wang, C. R., McFarlane, L. O. & Pukala, T. L. Exploring Snake Venoms Beyond the Primary Sequence: from Proteoforms to Protein-Protein Interactions. Toxicon 107841 (2024) http://doi.org/10.1016/j.toxicon.2024.107841.
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Wang, C. R., Zenaidee, M. A., Snel, M. F. & Pukala, T. L. Exploring Top-Down Mass Spectrometric Approaches To Probe Forest Cobra (Naja melanoleuca) Venom Proteoforms. J. Proteome Res. (2024) doi:10.1021/acs.jproteome.4c00486.
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Zhan, Z. & Wang, L. Fast peak error correction algorithms for proteoform identification using top-down tandem mass spectra. Bioinformatics btae149 (2024) doi:10.1093/bioinformatics/btae149.
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Bailey, A. O., Durbin, K. R., Robey, M. T., Palmer, L. K. & Russell, W. K. Filling the gaps in peptide maps with a platform assay for top-down characterization of purified protein samples. PROTEOMICS n/a, 2400036 (2024).
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Takemori, A. et al. GeLC-FAIMS-MS workflow for in-depth middle-down proteomics. PROTEOMICS 24, 2200431 (2024).
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Kaulich, P. T., Cassidy, L. & Tholey, A. Identification of proteoforms by top-down proteomics using two-dimensional low/low pH reversed-phase liquid chromatography-mass spectrometry. PROTEOMICS 24, 2200542 (2024).
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Hellinger, J. & Brodbelt, J. S. Impact of Charge State on Characterization of Large Middle-Down Sized Peptides by Tandem Mass Spectrometry. J. Am. Soc. Mass Spectrom. 35, 1647–1656 (2024).
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Beaumal, C. et al. Improved characterization of trastuzumab deruxtecan with PTCR and internal fragments implemented in middle-down MS workflows. Anal Bioanal Chem 416, 519–532 (2024).
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Robey, M. T. & Durbin, K. R. Improving Top-Down Sequence Coverage with Targeted Fragment Matching. J. Am. Soc. Mass Spectrom. (2024) doi:10.1021/jasms.4c00161.
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Kaulich, P. T., Jeong, K., Kohlbacher, O. & Tholey, A. Influence of different sample preparation approaches on proteoform identification by top-down proteomics. Nat Methods 1–11 (2024) http://doi.org/10.1038/s41592-024-02481-6.
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Degnan, D. J. et al. IsoForma: An R Package for Quantifying and Visualizing Positional Isomers in Top-Down LC-MS/MS Data. J. Proteome Res. (2024) doi:10.1021/acs.jproteome.3c00681.
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Polák, M., Černý, J. & Novák, P. Isotopic Depletion Increases the Spatial Resolution of FPOP Top-Down Mass Spectrometry Analysis. Anal. Chem. (2024) doi:10.1021/acs.analchem.3c03759.
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Lieu, L. B., Hinkle, J. D., Syka, J. E. P. & Fornelli, L. Leveraging Ion–Ion and Ion–Photon Activation to Improve the Sequencing of Proteins Carrying Multiple Disulfide Bonds: The Human Serum Albumin Case Study. J. Am. Soc. Mass Spectrom. (2024) doi:10.1021/jasms.4c00391.
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Helms, A. & Brodbelt, J. S. Mass Spectrometry Strategies for O-Glycoproteomics. Cells 13, 394 (2024).
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Xu, T., Wang, Q., Wang, Q. & Sun, L. Mass spectrometry-intensive top-down proteomics: an update on technology advancements and biomedical applications. Analytical Methods 16, 4664–4682 (2024).
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Dhenin, J. et al. Monitoring mAb proteoforms in mouse plasma using an automated immunocapture combined with top-down and middle-down mass spectrometry. PROTEOMICS 24, 2300069 (2024).
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Chapman, E. A. et al. Native Top-Down Mass Spectrometry for Characterizing Sarcomeric Proteins Directly from Cardiac Tissue Lysate. J. Am. Soc. Mass Spectrom. 35, 738–745 (2024).
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Fischer, M. S. et al. Online Mixed-Bed Ion Exchange Chromatography for Native Top-Down Proteomics of Complex Mixtures. J. Proteome Res. (2024) doi:10.1021/acs.jproteome.4c00430.
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Sadeghi, S. A. et al. Pilot Evaluation of the Long-Term Reproducibility of Capillary Zone Electrophoresis–Tandem Mass Spectrometry for Top-Down Proteomics of a Complex Proteome Sample. J. Proteome Res. (2024) doi:10.1021/acs.jproteome.3c00872.
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Drown, B. S. et al. Precise Readout of MEK1 Proteoforms upon MAPK Pathway Modulation by Individual Ion Mass Spectrometry. Anal. Chem. (2024) doi:10.1021/acs.analchem.3c04758.
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Jeong, K. et al. Precursor deconvolution error estimation: The missing puzzle piece in false discovery rate in top-down proteomics. PROTEOMICS 24, 2300068 (2024).
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Gant, M. S. & Chamot-Rooke, J. Present and Future Perspectives on Mass Spectrometry for Clinical Microbiology. Microbes and Infection 105296 (2024) http://doi.org/10.1016/j.micinf.2024.105296.
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Pesavento, J. J. et al. pyMS-Vis, an Open-Source Python Application for Visualizing and Investigating Deconvoluted Top-Down Mass Spectrometric Experiments: A Histone Proteoform Case Study. Anal. Chem. (2024) doi:10.1021/acs.analchem.4c02650.
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Chowdhury, T. et al. Quantitative Top-down Proteomics Revealed Kinase Inhibitor-Induced Proteoform-Level Changes in Cancer Cells. J. Proteome Res. (2024) doi:10.1021/acs.jproteome.4c00778.
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Liu, J. et al. Sequencing the Monoclonal Antibody Variable Regions Using Multiple Charge Integration Middle-Down Strategy and Ultraviolet Photodissociation. Analytica Chimica Acta 343450 (2024) http://doi.org/10.1016/j.aca.2024.343450.
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Su, P. et al. Single Cell Analysis of Proteoforms. J. Proteome Res. (2024) doi:10.1021/acs.jproteome.4c00075.
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Carr, A. V., Bollis, N. E., Pavek, J. G., Shortreed, M. R. & Smith, L. M. Spectral averaging with outlier rejection algorithms to increase identifications in top-down proteomics. PROTEOMICS n/a, 2300234 (2024).
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Langford, J. B. et al. Strategies for Top–Down Hydrogen Deuterium Exchange-Mass Spectrometry: A Mini Review and Perspective. Journal of Mass Spectrometry 59, e5097 (2024).
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Walker, J. N., Gautam, A. K. S., Matouschek, A. & Brodbelt, J. S. Structural Analysis of the 20S Proteasome Using Native Mass Spectrometry and Ultraviolet Photodissociation. J. Proteome Res. (2024) doi:10.1021/acs.jproteome.4c00568.
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Lermyte, F. The need for open and FAIR data in top-down proteomics. PROTEOMICS 24, 2300354 (2024).
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Saei, A. A., Sun, L. & Mahmoudi, M. The role of protein corona in advancing plasma proteomics. PROTEOMICS n/a, 2400028 (2024).
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Berthias, F., Bilgin, N., Mecinović, J. & Jensen, O. N. Top-down ion mobility/mass spectrometry reveals enzyme specificity: Separation and sequencing of isomeric proteoforms. PROTEOMICS 24, 2200471 (2024).
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Fernández, J., Chaves, W., Vargas-Diaz, D., Petras, D. & Lomonte, B. Top-down proteomics of venoms from five Micrurus species from Costa Rica: comparative composition of phospholipase A2-rich vs three-finger toxin-rich phenotypes. Toxicon 108187 (2024) http://doi.org/10.1016/j.toxicon.2024.108187.
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Krombholz, S. et al. A combined top-down and bottom-up LC-HRMS/MS method for the quantification of human growth hormone in plasma and serum. Growth Hormone & IGF Research 72–73, 101560 (2023).
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Bhattacharya, S., Joshi, S. & Rathore, A. S. A native multi-dimensional monitoring workflow for at-line characterization of mAb titer, size, charge, and glycoform heterogeneities in cell culture supernatant. Journal of Chromatography A 463983 (2023) http://doi.org/10.1016/j.chroma.2023.463983.
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Ercan, H. et al. A Practical and Analytical Comparative Study of Gel-Based Top-Down and Gel-Free Bottom-Up Proteomics Including Unbiased Proteoform Detection. Cells 12, 747 (2023).
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Blöchl, C. et al. A robust nanoscale RP HPLC-MS approach for sensitive Fc proteoform profiling of IgG allotypes. Analytica Chimica Acta 341795 (2023) http://doi.org/10.1016/j.aca.2023.341795.
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Gabant, G., Stekovic, M., Nemcic, M., Pinêtre, J. & Cadene, M. A sDOE (Simple Design-of-Experiment) Approach for Parameter Optimization in Mass Spectrometry. Part 1. Parameter Selection and Interference Effects in Top-Down ETD Fragmentation of Proteins in a UHR-QTOF Instrument. J. Am. Soc. Mass Spectrom. 34, 27–35 (2023).
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Kandi, S. et al. Amyloid β Proteoforms Elucidated by Quantitative LC/MS in the 5xFAD Mouse Model of Alzheimer's Disease. J. Proteome Res. (2023) doi:10.1021/acs.jproteome.3c00353.
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McGee, J. P. et al. Automated imaging and identification of proteoforms directly from ovarian cancer tissue. Nat Commun 14, 6478 (2023).
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Wang, Q. et al. Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Top-Down Proteomics of Mouse Brain Integral Membrane Proteins. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c02346.
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Lantz, C. et al. Characterization of Molecular Tweezer Binding on α-Synuclein with Native Top-Down Mass Spectrometry and Ion Mobility-Mass Spectrometry Reveals a Mechanism for Aggregation Inhibition. J. Am. Soc. Mass Spectrom. (2023) doi:10.1021/jasms.3c00281.
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Chen, W., Ding, Z., Zang, Y. & Liu, X. Characterization of Proteoform Post-Translational Modifications by Top-Down and Bottom-Up Mass Spectrometry in Conjunction with Annotations. J. Proteome Res. (2023) doi:10.1021/acs.jproteome.3c00207.
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Bashyal, A., Dunham, S. D. & Brodbelt, J. S. Characterization of Unbranched Ubiquitin Tetramers by Combining Ultraviolet Photodissociation with Proton Transfer Charge Reduction Reactions. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c02618.
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Tabb, D. L. et al. Comparing Top-Down Proteoform Identification: Deconvolution, PrSM Overlap, and PTM Detection. J. Proteome Res. 22, 2199–2217 (2023).
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Lanzillotti, M. & Brodbelt, J. S. Comparison of Top-Down Protein Fragmentation Induced by 213 and 193 nm UVPD. J. Am. Soc. Mass Spectrom. (2023) doi:10.1021/jasms.2c00288.
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Xu, T., Wang, Q., Wang, Q. & Sun, L. Coupling High-Field Asymmetric Waveform Ion Mobility Spectrometry with Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Top-Down Proteomics. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c00551.
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Pavek, J. G. et al. Cysteine Counting via Isotopic Chemical Labeling for Intact Mass Proteoform Identifications in Tissue. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c02473.
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Chapman, E. A. et al. Defining the Sarcomeric Proteoform Landscape in Ischemic Cardiomyopathy by Top-Down Proteomics. J. Proteome Res. (2023) doi:10.1021/acs.jproteome.2c00729.
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Lantz, C. et al. Digital Quadrupole Isolation and Electron Capture Dissociation on an Extended Mass Range Q-TOF Provides Sequence and Structure Information on Proteins and Protein Complexes. J. Am. Soc. Mass Spectrom. (2023) doi:10.1021/jasms.3c00184.
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Dunham, S. D. & Brodbelt, J. S. Enhancing Top-Down Analysis of Proteins by Combining Ultraviolet Photodissociation (UVPD), Proton-Transfer Charge Reduction (PTCR), and Gas-Phase Fractionation to Alleviate the Impact of Nondissociated Precursor Ions. J. Am. Soc. Mass Spectrom. (2023) doi:10.1021/jasms.3c00351.
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Sun, Y. et al. Enhancing Top-Down Characterization of Membrane Proteoforms with C8-Functional Amine-Bridged Hybrid Monoliths. Anal. Chem. (2023) doi:10.1021/acs.analchem.2c05401.
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Berthias, F., Cooper-Shepherd, D. A., Holck, F. H. V., Langridge, J. I. & Jensen, O. N. Full Separation and Sequencing of Isomeric Proteoforms in the Middle-Down Mass Range Using Cyclic Ion Mobility and Electron Capture Dissociation. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c02120.
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Melby, J. A. et al. High sensitivity top–down proteomics captures single muscle cell heterogeneity in large proteoforms. Proceedings of the National Academy of Sciences 120, e2222081120 (2023).
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Taylor, B. C. & Young, N. L. Histone H4 proteoforms and post-translational modifications in the Mus musculus brain with quantitative comparison of ages and brain regions. Anal Bioanal Chem (2023) doi:10.1007/s00216-023-04555-4.
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McGee, J. P. et al. Immunocomplexed Antigen Capture and Identification by Native Top-Down Mass Spectrometry. J. Am. Soc. Mass Spectrom. (2023) doi:10.1021/jasms.3c00235.
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Zhang, Y., Cai, Q., Luo, Y., Zhang, Y. & Li, H. Integrated top-down and bottom-up proteomics mass spectrometry for the characterization of endogenous ribosomal protein heterogeneity. Journal of Pharmaceutical Analysis 13, 63–72 (2023).
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Lippold, S., Cadang, L., Schlothauer, T. & Yang, F. Internal Fragment Ions from Higher Energy Collision Dissociation Enable the Glycoform-Resolved Asn325 Deamidation Assessment of Antibodies by Middle-Down Mass Spectrometry. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c03015.
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Adams, L. M. et al. Mapping the KRAS proteoform landscape in colorectal cancer identifies truncated KRAS4B that decreases MAPK signaling. Journal of Biological Chemistry 299, (2023).
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Oluwole, A., Shutin, D. & Bolla, J. R. Mass spectrometry of intact membrane proteins: shifting towards a more native-like context. Essays in Biochemistry EBC20220169 (2023) doi:10.1042/EBC20220169.
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Guo, Y., Cupp-Sutton, K. A., Zhao, Z., Anjum, S. & Wu, S. Multidimensional separations in top–down proteomics. Analytical Science Advances n/a, (2023).
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Ying, Y. & Li, H. Native top-down mass spectrometry for monitoring the rapid chymotrypsin catalyzed hydrolysis reaction. Analytica Chimica Acta 341971 (2023) http://doi.org/10.1016/j.aca.2023.341971.
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Brown, K. A. et al. Nonionic, Cleavable Surfactant for Top-Down Proteomics. Anal. Chem. (2023) doi:10.1021/acs.analchem.2c03916.
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Guo, Y. et al. Optimization of Higher-Energy Collisional Dissociation Fragmentation Energy for Intact Protein-Level Tandem Mass Tag Labeling. J. Proteome Res. (2023) doi:10.1021/acs.jproteome.2c00549.
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Lloyd-Jones, C. et al. Preparative Electrophoresis for HDL Particle Size Separation and Intact-Mass Apolipoprotein Proteoform Analysis. J. Proteome Res. (2023) doi:10.1021/acs.jproteome.2c00804.
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You, J. & Park, H.-M. Progress in Top-Down LC-MS Analysis of Antibodies: Review. Biotechnol Bioproc E 28, 226–233 (2023).
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Chapman, E. A. et al. Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics. Nat Commun 14, 8400 (2023).
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Kellie, J. F. et al. Top-Down Characterization and Intact Mass Quantitation of a Monoclonal Antibody Drug from Serum by Use of a Quadrupole TOF MS System Equipped with Electron-Activated Dissociation. J. Am. Soc. Mass Spectrom. 34, 17–26 (2023).
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Yang, L., Stanisheuski, S., Song, Z., Bracha, S. & Maier, C. S. Top-down mass spectrometry for characterizing the low molecular weight proteome of canine osteosarcoma cell phenotypes. Eur J Mass Spectrom (Chichester) 14690667231202766 (2023) doi:10.1177/14690667231202766.
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Liu, F. C. et al. Top-Down Protein Analysis by Tandem-Trapped Ion Mobility Spectrometry/Mass Spectrometry (Tandem-TIMS/MS) Coupled with Ultraviolet Photodissociation (UVPD) and Parallel Accumulation/Serial Fragmentation (PASEF) MS/MS Analysis. J. Am. Soc. Mass Spectrom. (2023) doi:10.1021/jasms.3c00187.
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Polák, M. et al. Top-Down Proteoform Analysis by 2D MS with Quadrupolar Detection. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c02225.
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Zhao, Z. et al. Top-down Proteomics Analysis of Picogram-level Complex Samples using Spray-Capillary-Based Capillary Electrophoresis Mass Spectrometry. ChemRxiv (2023) http://doi.org/10.26434/chemrxiv-2023-0x5ss.
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Po, A. & Eyers, C. E. Top-Down Proteomics and the Challenges of True Proteoform Characterization. J. Proteome Res. (2023) doi:10.1021/acs.jproteome.3c00416.
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Olianas, A. et al. Top-Down Proteomics Detection of Potential Salivary Biomarkers for Autoimmune Liver Diseases Classification. International Journal of Molecular Sciences 24, 959 (2023).
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Fulcher, J. M. et al. Top-Down Proteomics of Mouse Islets With Beta Cell CPE Deletion Reveals Molecular Details in Prohormone Processing. Endocrinology 164, bqad160 (2023).
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Miller, S. A. et al. Top/Middle-Down Characterization of α-Synuclein Glycoforms. Anal. Chem. (2023) doi:10.1021/acs.analchem.3c02405.
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Martin, E. A., Fulcher, J. M., Zhou, M., Monroe, M. E. & Petyuk, V. A. TopPICR: A Companion R Package for Top-Down Proteomics Data Analysis. J. Proteome Res. (2023) doi:10.1021/acs.jproteome.2c00570.
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Dai, Y., Millikin, R. J., Rolfs, Z., Shortreed, M. R. & Smith, L. M. A Hybrid Spectral Library and Protein Sequence Database Search Strategy for Bottom-Up and Top-Down Proteomic Data Analysis. J. Proteome Res. (2022) doi:10.1021/acs.jproteome.2c00305.
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Luo, R. Y. et al. Accurate Identification of Hemoglobin Variants By Top-Down Protein Analysis Using Capillary Electrophoresis-High-Resolution Mass Spectrometry. Blood 140, 5384–5386 (2022).
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DiStefano, N. et al. Adaptation of Native GELFrEE for HDL Particle Size Subtype Separation and Differential Apolipoprotein Proteoform Quantification. The FASEB Journal 36, (2022).
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Xu, T., Han, L. & Sun, L. Automated Capillary Isoelectric Focusing-Mass Spectrometry with Ultrahigh Resolution for Characterizing Microheterogeneity and Isoelectric Points of Intact Protein Complexes. Anal. Chem. (2022) doi:10.1021/acs.analchem.2c00975.
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Fornelli, L. & Toby, T. K. Characterization of large intact protein ions by mass spectrometry: What directions should we follow? Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1870, 140758 (2022).
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Lin, Y., Agarwal, A. M., Marshall, A. G. & Anderson, L. C. Characterization of Structural Hemoglobin Variants by Top-Down Mass Spectrometry and R Programming Tools for Rapid Identification. J. Am. Soc. Mass Spectrom. 33, 123–130 (2022).
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Cramer, D. A. T., Franc, V., Caval, T. & Heck, A. J. R. Charting the Proteoform Landscape of Serum Proteins in Individual Donors by High-Resolution Native Mass Spectrometry. Anal. Chem. (2022) doi:10.1021/acs.analchem.2c02215.
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Brodbelt, J. S. Deciphering combinatorial post-translational modifications by top-down mass spectrometry. Current Opinion in Chemical Biology 70, 102180 (2022).
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Babović, M., Shliaha, P. V., Gibb, S. & Jensen, O. N. Effective Amino Acid Sequencing of Intact Filgrastim by Multimodal Mass Spectrometry with Topdownr. J. Am. Soc. Mass Spectrom. (2022) doi:10.1021/jasms.2c00193.
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Shaw, J. B. et al. Enhanced Top-Down Protein Characterization with Electron Capture Dissociation and Cyclic Ion Mobility Spectrometry. Anal. Chem. (2022) doi:10.1021/acs.analchem.1c04870.
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Chen, W. et al. Evaluation of Machine Learning Models for Proteoform Retention and Migration Time Prediction in Top-Down Mass Spectrometry. J. Proteome Res. (2022) doi:10.1021/acs.jproteome.2c00124.
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Jeong, K. et al. FLASHIda enables intelligent data acquisition for top–down proteomics to boost proteoform identification counts. Nat Commun 13, 4407 (2022).
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Rojas Ramírez, C., Murtada, R., Gao, J. & Ruotolo, B. T. Free Radical-Based Sequencing for Native Top-Down Mass Spectrometry. J. Am. Soc. Mass Spectrom. (2022) doi:10.1021/jasms.2c00252.
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Su, P. et al. Highly multiplexed, label-free proteoform imaging of tissues by individual ion mass spectrometry. Science Advances 8, eabp9929 (2022).
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