Increasing the Separation Capacity of Intact Histone Proteoforms Chromatography Coupling Online Weak Cation Exchange-HILIC to Reversed Phase LC UVPD-HRMS
Open accessAbstract
Top-down proteomics is an emerging analytical strategy to characterize combinatorial protein post-translational modifications (PTMs). However, sample complexity and small mass differences between chemically closely related proteoforms often limit the resolution attainable by separations employing a single liquid chromatographic (LC) principle. In particular, for ultramodified proteins like histones, extensive and time-consuming fractionation is needed to achieve deep proteoform coverage. Herein, we present the first online nanoflow comprehensive two-dimensional liquid chromatography (nLC×LC) platform top-down mass spectrometry analysis of histone proteoforms. The described two-dimensional LC system combines weak cation exchange chromatography under hydrophilic interaction LC conditions (i.e., charge- and hydrophilicity-based separation) with reversed phase liquid chromatography (i.e., hydrophobicity-based separation). The two independent chemical selectivities were run at nanoflows (300 nL/min) and coupled online with high-resolution mass spectrometry employing ultraviolet photodissociation (UVPD-HRMS). The nLC×LC workflow increased the number of intact protein masses observable relative to one-dimensional approaches and allowed characterization of hundreds of proteoforms starting from limited sample quantities (∼1.5 μg).
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
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?
Weak-cationic exchange HILIC and RPLC enabled characterization of hundreds of histone proteoforms from ~1.5 μg of protein.
“However, some recent online approaches have been developed which include using weak-cationic exchange HILIC and RPLC to enable the characterization of hundreds of histone proteoforms from ~1.5 μg of protein [90].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [90]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756 · see citing works
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · see citing works
Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,759 · see citing works
Combinatorial patterns of histone acetylations and methylations in the human genome
Wang, Z., Zang, C., Rosenfeld, J. A., Schones, D. E., Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Peng, W., Zhang, M. Q., et al. (2008) · Nature Genetics · doi:10.1038/ng.154 · Cited by 2,331 · see citing works
Proteoform: a single term describing protein complexity
The Consortium for Top Down Proteomics, Smith, L. M., & Kelleher, N. L. (2013) · Nature Methods · doi:10.1038/nmeth.2369 · Cited by 1,528 · see citing works
Progress in Top-Down Proteomics and the Analysis of Proteoforms
Toby, T. K., Fornelli, L., & Kelleher, N. L. (2016) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071015-041550 · Cited by 576 · see citing works
Chemical derivatization of histones for facilitated analysis by mass spectrometry
Garcia, B. A., Mollah, S., Ueberheide, B. M., Busby, S. A., Muratore‐Schroeder, T. L., Shabanowitz, J., & Hunt, D. F. (2007) · Nature Protocols · doi:10.1038/nprot.2007.106 · Cited by 389 · see citing works
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 372 · see citing works
Complete Protein Characterization Using Top-Down Mass Spectrometry and Ultraviolet Photodissociation
Shaw, J. B., Li, W., Holden, D. D., Zhang, Y., Griep-Raming, J., Fellers, R. T., Early, B. P., Thomas, P. M., Kelleher, N. L., & Brodbelt, J. S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4029654 · Cited by 371 · see citing works
Self-citationGiddings, J. C. (1995) · Journal of Chromatography A · doi:10.1016/0021-9673(95)00249-m · Cited by 349 · see citing works
High Throughput Characterization of Combinatorial Histone Codes
Young, N. L., DiMaggio, P. A., Plazas-Mayorca, M. D., Baliban, R. C., Floudas, C. A., & Garcia, B. A. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900238-mcp200 · Cited by 312 · see citing works
EpiProfile 2.0: A Computational Platform for Processing Epi-Proteomics Mass Spectrometry Data
Yuan, Z., Sidoli, S., Marchione, D. M., Simithy, J., Janssen, K. A., Szurgot, M. R., & Garcia, B. A. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00133 · Cited by 187 · see citing works
博一, 長., Bullock, C. R., LeDuc, R. D., Mizzen, C. A., & Kelleher, N. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709796200 · Cited by 185 · see citing works
Informed-Proteomics: open-source software package for top-down proteomics
Park, J., Piehowski, P., Wilkins, C. S., Zhou, M., Mendoza, J., Fujimoto, G. M., Gibbons, B. C., Shaw, J., Shen, Y., Shukla, A. K., et al. (2017) · Nature Methods · doi:10.1038/nmeth.4388 · Cited by 153 · see citing works
Self-citationEnhanced top-down characterization of histone post-translational modifications
Tian, Z., Tolić, N., Zhao, R., Moore, R. J., Hengel, S. M., Robinson, E. W., Stenoien, D. L., Wu, S., Smith, R. D., & Paša‐Tolić, L. (2012) · Genome biology · doi:10.1186/gb-2012-13-10-r86 · Cited by 127 · see citing works
Self-citationBreaking the histone code with quantitative mass spectrometry
Britton, L.-M. P., Gonzales-Cope, M., Zee, B. M., & Garcia, B. A. (2011) · Expert Review of Proteomics · doi:10.1586/epr.11.47 · Cited by 120 · see citing works
Maile, T. M., Izrael-Tomasevic, A., Cheung, T. K., Guler, G. D., Tindell, C., Masselot, A., Liang, J., Zhao, F., Trojer, P., Classon, M., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.046573 · Cited by 118 · see citing works
Separation of acetylated core histones by hydrophilic-interaction liquid chromatography
Lindner, H. H., Sarg, B., Meraner, C., & Helliger, W. (1996) · Journal of Chromatography A · doi:10.1016/0021-9673(96)00131-8 · Cited by 111 · see citing works
Gargano, A., Duffin, M., Navarro, P., & Schoenmakers, P. J. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04051 · Cited by 110 · see citing works
Self-citationVonk, R. J., Gargano, A., Davydova, E., Dekker, H. L., Eeltink, S., de Koning, L. J., & Schoenmakers, P. J. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00708 · Cited by 103 · see citing works
Self-citationCleland, T. P., DeHart, C. J., Fellers, R. T., VanNispen, A. J., Greer, J. B., LeDuc, R. D., Parker, W. R., Thomas, P. M., Kelleher, N. L., & Brodbelt, J. S. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00043 · Cited by 96 · see citing works
Lindner, H. H., Sarg, B., & Helliger, W. (1997) · Journal of Chromatography A · doi:10.1016/s0021-9673(97)00468-8 · Cited by 95 · see citing works
Fort, K. L., Dyachenko, A., Potel, C. M., Corradini, E., Marino, F., Barendregt, A., Makarov, A., Scheltema, R. A., & Heck, A. J. R. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04162 · Cited by 92 · see citing works
LeDuc, R. D., Fellers, R. T., Early, B. P., Greer, J. B., Thomas, P. M., & Kelleher, N. L. (2014) · Journal of Proteome Research · doi:10.1021/pr401277r · Cited by 85 · see citing works
Peach, S. E., Rudomin, E. L., Udeshi, N. D., Carr, S. A., & Jaffe, J. D. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015941 · Cited by 74 · see citing works
Zheng, Y., Fornelli, L., Compton, P. D., Sharma, S., Canterbury, J., Mullen, C., Zabrouskov, V., Fellers, R. T., Thomas, P. M., Licht, J. D., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.053819 · Cited by 73 · see citing works
Epiproteomics: quantitative analysis of histone marks and codes by mass spectrometry
Zheng, Y., Huang, X., & Kelleher, N. L. (2016) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2016.06.007 · Cited by 73 · see citing works
Jung, H. R., Sidoli, S., Haldbo, S. N., Sprenger, R. R., Schwämmle, V., Pasini, D., Helin, K., & Jensen, O. N. (2013) · Analytical Chemistry · doi:10.1021/ac401299w · Cited by 72 · see citing works
Tissue-Specific Expression and Post-Translational Modification of Histone H3 Variants
Garcia, B. A., Thomas, C. E., Kelleher, N. L., & Mizzen, C. A. (2008) · Journal of Proteome Research · doi:10.1021/pr800044q · Cited by 71 · see citing works
Mass Spectrometric Analysis of Histone Proteoforms
Yuan, Z.-F., Arnaudo, A. M., & Garcia, B. A. (2014) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071213-015959 · Cited by 64 · see citing works
Tvardovskiy, A., Wrzesinski, K., Sidoli, S., Fey, S. J., Rogowska-Wrzesińska, A., & Jensen, O. N. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.048975 · Cited by 59 · see citing works
Greer, S. M., & Brodbelt, J. S. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00801 · Cited by 58 · see citing works
Identification and Quantification of Histone PTMs Using High-Resolution Mass Spectrometry
Karch, K. R., Sidoli, S., & Garcia, B. A. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.12.007 · Cited by 56 · see citing works
Identification of Ultramodified Proteins Using Top-Down Tandem Mass Spectra
Liu, X., Hengel, S. M., Wu, S., Tolić, N., Paša‐Tolić, L., & Pevzner, P. A. (2013) · Journal of Proteome Research · doi:10.1021/pr400849y · Cited by 54 · see citing works
Azad, G. K., & Tomar, R. S. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3181-y · Cited by 53 · see citing works
Contrepois, K., Ezan, É., Mann, C., & Fenaille, F. (2010) · Journal of Proteome Research · doi:10.1021/pr100497a · Cited by 49 · see citing works
Two‐dimensional liquid chromatography system for online top‐down mass spectrometry
Tian, Z., Zhao, R., Tolić, N., Moore, R. J., Stenoien, D. L., Robinson, E. W., Smith, R. D., & Paša‐Tolić, L. (2010) · PROTEOMICS · doi:10.1002/pmic.201000367 · Cited by 47 · see citing works
Self-citationCannon, J. R., Holden, D. D., & Brodbelt, J. S. (2014) · Analytical Chemistry · doi:10.1021/ac5036082 · Cited by 46 · see citing works
Dang, X., Singh, A., Spetman, B. D., Nolan, K. D., Isaacs, J. S., Dennis, J. H., Dalton, S., Marshall, A. G., & Young, N. L. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00414 · Cited by 41 · see citing works
Zhou, M., Paša-Tolić, L., & Stenoien, D. L. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00694 · Cited by 39 · see citing works
Self-citationMiddle‐Down and Top‐Down Mass Spectrometric Analysis of Co‐occurring Histone Modifications
Molden, R. C., & Garcia, B. A. (2014) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps2307s77 · Cited by 37 · see citing works
Wang, T., Holt, M. V., & Young, N. L. (2018) · Epigenetics & Chromatin · doi:10.1186/s13072-018-0198-9 · Cited by 35 · see citing works
Analysis of histones, histone variants, and their post‐translationally modified forms
Lindner, H. H. (2008) · Electrophoresis · doi:10.1002/elps.200800094 · Cited by 33 · see citing works
Liquid chromatography mass spectrometry profiling of histones
Su, X., Jacob, N. K., Amunugama, R., Lucas, D. M., Knapp, A. R., Ren, C., Davis, M. E., Marcucci, G., Parthun, M. R., Byrd, J. C., et al. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.12.037 · Cited by 31 · see citing works
Mizzen, C. A., Alpert, A. J., Lévesque, L., Kruck, T. P. A., & McLachlan, D. R. C. (2000) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(00)00210-3 · Cited by 30 · see citing works
Benevento, M., Tonge, P. D., Puri, M. C., Nagy, A., Heck, A. J. R., & Muñoz, J. (2015) · PROTEOMICS · doi:10.1002/pmic.201500031 · Cited by 16 · see citing works
Profiling Changes in Histone Post-translational Modifications by Top-Down Mass Spectrometry
Zhou, M., Wu, S., Stenoien, D. L., Zhang, Z., Connolly, L., Freitag, M., & Paša‐Tolić, L. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6518-2_12 · Cited by 13 · see citing works
Self-citationSeparation and Purification of Multiply Acetylated Proteins Using Cation-Exchange Chromatography
Papazyan, R., & Taverna, S. D. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-305-3_8 · Cited by 7 · see citing works
Mass spectrometry for chromatin biology
Baker, M. (2012) · Nature Methods · doi:10.1038/nmeth.2081 · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Pirok, B. W. J., Stoll, D. R., & Schoenmakers, P. J. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04841 · Cited by 361 · see citing works
Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules
Brodbelt, J. S., Morrison, L. J., & Santos, I. C. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00440 · Cited by 291 · see citing works
Novel Strategies to Address the Challenges in Top-Down Proteomics
Melby, J. A., Roberts, D. S., Larson, E. J., Brown, K. A., Bayne, E. F., Jin, S., & Ge, Y. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00099 · Cited by 191 · see citing works
Top-down proteomics: challenges, innovations, and applications in basic and clinical research
Brown, K. A., Melby, J. A., Roberts, D. S., & Ge, Y. (2020) · Expert Review of Proteomics · doi:10.1080/14789450.2020.1855982 · Cited by 152 · see citing works
Top-Down Proteomics and the Challenges of True Proteoform Characterization
Po, A., & Eyers, C. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00416 · Cited by 94 · see citing works
Sample preparation and fractionation techniques for intact proteins for mass spectrometric analysis.
Thomas, S. L., Thacker, J. B., Schug, K. A., & Maráková, K. (2020) · Journal of Separation Science · doi:10.1002/jssc.202000936 · Cited by 51 · see citing works
Recent advances in top‐down proteome sample processing ahead of MS analysis
Nickerson, J. L., Baghalabadi, V., Rajendran, S. R. C. K., Jakubec, P. J., Said, H., McMillen, T. S., Dang, Z., & Doucette, A. A. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21706 · Cited by 55 · see citing works
Kohler, I., Verhoeven, M., Haselberg, R., & Gargano, A. (2021) · Microchemical journal (Print) · doi:10.1016/j.microc.2021.106986 · Cited by 47 · see citing works
Self-citationChapel, S., & Heinisch, S. (2021) · Journal of Separation Science · doi:10.1002/jssc.202100534 · Cited by 46 · see citing works
Gomes, F. P., Diedrich, J. K., Saviola, A. J., Memili, E., Moura, A. A., & Yates, J. R. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03856 · Cited by 46 · see citing works
Recent Advances in Multidimensional Separation for Proteome Analysis
Yuan, H., Jiang, B., Zhao, B., Zhang, L., & Zhang, Y. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04894 · Cited by 41 · see citing works
Sheng, Q., Liu, M., Lan, M., & Qing, G. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117148 · Cited by 41 · see citing works
Toward a Universal Sample Preparation Method for Denaturing Top-Down Proteomics of Complex Proteomes
Yang, Z.-C., Shen, X., Chen, D.-Y., & Sun, L.-L. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00226 · Cited by 27 · see citing works
Tengattini, S., Massolini, G., Rinaldi, F., Calleri, E., & Temporini, C. (2024) · Trends in Analytical Chemistry (TrAC) · doi:10.1016/j.trac.2024.117702 · Cited by 34 · see citing works
Top-down Mass Spectrometry Analysis of Human Serum Autoantibody Antigen-Binding Fragments
Wang, Z., Liu, X., Muther, J. J., James, J. A., Smith, K., & Wu, S. (2019) · Scientific Reports · doi:10.1038/s41598-018-38380-y · Cited by 34 · see citing works
Jaag, S., Shirokikh, M., & Lämmerhofer, M. (2020) · Journal of Chromatography A · doi:10.1016/j.chroma.2020.461786 · Cited by 30 · see citing works
McIlvin, M. R., & Saito, M. A. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00588 · Cited by 30 · see citing works
Wang, Z., Yu, D., Cupp-Sutton, K. A., Liu, X., Smith, K. J., & Wu, S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03395 · Cited by 23 · see citing works
Multidimensional Separations in Top-Down Proteomics
Guo, Y., Cupp-Sutton, K. A., Zhao, Z.-T., Anjum, S., & Wu, S. (2023) · Analytical Science Advances · doi:10.1002/ansa.202300016 · Cited by 25 · see citing works
Recent advances in on-line upfront devices for sensitive bioanalytical nano LC methods
Røberg‐Larsen, H., Wilson, S. R., & Lundanes, E. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2021.116190 · Cited by 26 · see citing works
Wilson, J., Pena, A. B., Wang, J., Liao, Y., Veličković, D., Wojcik, R., Passamonti, M., Zhao, R., Gargano, A., Gerbasi, V. R., et al. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c00139 · Cited by 25 · see citing works
Self-citationZhou, M., Malhan, N., Ahkami, A. H., Engbrecht, K., Myers, G., Dahlberg, J., Hollingsworth, J., Sievert, J. A., Hutmacher, R., Madera, M., et al. (2020) · Methods · doi:10.1016/j.ymeth.2019.10.007 · Cited by 23 · see citing works
Self-citationvan Schaick, G., Pirok, B. W. J., Haselberg, R., Somsen, G. W., & Gargano, A. (2019) · Journal of Chromatography A · doi:10.1016/j.chroma.2019.03.038 · Cited by 22 · see citing works
Self-citationMcCool, E. N., Chen, D., Li, W., Liu, Y., & Sun, L. (2019) · Analytical Methods · doi:10.1039/c9ay00585d · Cited by 22 · see citing works
Walker, J. N., Lam, R., & Brodbelt, J. S. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.2c05765 · Cited by 22 · see citing works
Kuchaříková, H., Dobrovolná, P., Lochmanová, G., & Zdráhal, Z. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100114 · Cited by 21 · see citing works
Perspectives on the future of multi-dimensional platforms
Groeneveld, G., Pirok, B. W. J., & Schoenmakers, P. J. (2019) · Faraday Discussions · doi:10.1039/c8fd00233a · Cited by 20 · see citing works
Aly, A. A., Muller, M., de Villiers, A. J., Pirok, B. W. J., & Górecki, T. (2020) · Journal of Chromatography A · doi:10.1016/j.chroma.2020.461452 · Cited by 20 · see citing works
Tang, S., & Venkatramani, C. J. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c03572 · Cited by 20 · see citing works
Fang, F., Fries, B. D., Wang, Z., Liu, X., Hummon, A. B., & Sun, L. (2025) · PROTEOMICS · doi:10.1002/pmic.202400336 · Cited by 19 · see citing works
Holt, M. V., Wang, T., & Young, N. L. (2021) · Current Protocols · doi:10.1002/cpz1.26 · Cited by 21 · see citing works
Top-Down Ion Mobility Separations of Isomeric Proteoforms
Berthias, F., Thurman, H. A., Wijegunawardena, G., Wu, H., Shvartsburg, A. A., & Jensen, O. N. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c02948 · Cited by 16 · see citing works
Skeene, K., Khatri, K., Soloviev, Z., & Lapthorn, C. (2021) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140697 · Cited by 17 · see citing works
Sommella, E., Salviati, E., Musella, S., Sarno, V. D., Gasparrini, F., & Campiglia, P. (2020) · Separations · doi:10.3390/separations7020025 · Cited by 16 · 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
Cracking chromatin with proteomics: From chromatome to histone modifications
Sigismondo, G., Papageorgiou, D. N., & Krijgsveld, J. (2022) · PROTEOMICS · doi:10.1002/pmic.202100206 · Cited by 13 · see citing works
TopPICR: A Companion R Package for Top-Down Proteomics Data Analysis
Martin, E. A., Fulcher, J., Zhou, M.-W., Monroe, M. E., & Petyuk, V. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00570 · Cited by 12 · see citing works
Self-citationZheng, R., Govorukhina, N. I., Arrey, T. N., Pynn, C. J., van der Zee, A. G. J., Marko‐Varga, G., Bischoff, R., & Boychenko, O. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c01291 · Cited by 9 · see citing works
Wang, L., & Marcus, R. K. (2020) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-020-02539-2 · Cited by 9 · see citing works
Shahriari, S., & Selvaganapathy, P. R. (2024) · Gels · doi:10.3390/gels10030186 · Cited by 7 · see citing works
Gargano, A., Haselberg, R., & Somsen, G. W. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821447-3.00018-4 · Cited by 6 · see citing works
Self-citationPrSM-Level Side-by-Side Comparison of Online LC-MS Methods with Intact Histone H3 and H4 Proteoforms
Lui, K.-W., & Ngai, S. M. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00308 · Cited by 5 · see citing works
Shahriari, S., Damodara, S., & Selvaganapathy, P. R. (2024) · Microchimica Acta · doi:10.1007/s00604-024-06223-5 · Cited by 4 · see citing works
Richardson, H., Barahona, J., Medwig, G., Johns, A., Pérez, L. M. A., Sode, K., Daniele, M. A.-A., Miller, F. J., Lobaton, E. J., & Pavlidis, S. (2024) · Biosensors and Bioelectronics X · doi:10.1016/j.biosx.2024.100501 · Cited by 4 · see citing works
Top‐down characterization of mouse core histones
Xue, B., Xiao, K., & Tian, Z. (2019) · Journal of Mass Spectrometry · doi:10.1002/jms.4339 · Cited by 4 · see citing works
Poncha, K. F., Paparella, A. T., & Young, N. L. (2025) · Mass spectrometry reviews (Print) · doi:10.1002/mas.21941 · Cited by 6 · see citing works
Ion Activation Methods for Top-Down Proteomics.
Walker, J. N., & Brodbelt, J. (2026) · Mass spectrometry reviews (Print) · doi:10.1002/mas.70023 · Cited by 1 · see citing works
Lui, K.-W., Ngai, S. M., & Chan, T. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00079 · Cited by 1 · see citing works
Pathak, K., & Gomes, F. P. (2026) · Journal of Mass Spectrometry · doi:10.1002/jms.70021 · Cited by 2 · see citing works
Human Coronavirus 229E Infection Alters Histone Proteoforms.
Ives, A. N., Thibert, S. M., Berger, M., Gaffrey, M. J., Mitchell, H., Williams, S., Zhou, M.-W., Waters, K., Sims, A. C., & Zhang, T. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c01015
Self-citationProteoforms: 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
- Authors
- Gargano, A. F. G., Shaw, J. B., Zhou, M., Wilkins, C. S., Fillmore, T. L., Moore, R. J., Somsen, G. W., & Paša-Tolić, L.
- Affiliations
- Vrije Universiteit Amsterdam (NL)
- Pacific Northwest National Laboratory (US)
- Pacific Northwest National Laboratory , , P.O. Box 999, , ,
- Corresponding author
- Gargano, Andrea F. G.
- ORCID
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-09-18
- Volume
- 17
- Issue
- 11
- Pages
- 3791-3800
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- PMC
- PMC6220366
- OpenAlex
- W2890998722
- Cited by
- 53
- References
- 49
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 4 · 2023: 5 · 2022: 5 · 2021: 13 · 2020: 11 · 2019: 7 · 2018: 2
- FWCI
- 3.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of Proteome Research (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UvA-DARE (University of Amsterdam) (publishedVersion)
- VU Research Portal (publishedVersion, other-oa)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Funders
- Universiteit van Amsterdam
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (722.015.009)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Analytical Chemistry and Chromatography
- Keywords
- top-down proteomics, weak cation exchange chromatography, hydrophilic interaction liquid chromatography, reversed-phase liquid chromatography, two-dimensional liquid chromatography, ultraviolet photodissociation, high-resolution mass spectrometry, post-translational modification
- MeSH terms
- Chromatography, Ion Exchange, HeLa Cells, Histones, Humans, Protein Processing, Post-Translational, Spectrophotometry, Ultraviolet, Proteomics, Complex Mixtures, Tandem Mass Spectrometry, Static Electricity, Chromatography, Reverse-Phase, Hydrophobic and Hydrophilic Interactions
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
