The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
ProSight Lite: Graphical software to analyze top‐down mass spectrometry data
Abstract
Many top‐down proteomics experiments focus on identifying and localizing PTMs and other potential sources of “mass shift” on a known protein sequence. A simple application to match ion masses and facilitate the iterative hypothesis testing of PTM presence and location would assist with the data analysis in these experiments. ProSight Lite is a free software tool for matching a single candidate sequence against a set of mass spectrometric observations. Fixed or variable modifications, including both PTMs and a select number of glycosylations, can be applied to the amino acid sequence. The application reports multiple scores and a matching fragment list. Fragmentation maps can be exported for publication in either portable network graphic (PNG) or scalable vector graphic (SVG) format. ProSight Lite can be freely downloaded from http://prosightlite.northwestern.edu , installs and updates from the web, and requires Windows 7 or a higher version.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Data interpretation for complex-down spectra is similar to TDMS of denatured proteins; therefore, many existing software packages for TDMS can be retrofitted for complex-down data, including ProSight PTM 2.0,115 ProSight Lite,116 MASH Suite,117–119 ProteinGoggle,120 TopPIC,121 Informed-Proteomics,122 Masstodon,123 and others.”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [116]
Citations
Cites
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
Self-citationTyers, M., & Mann, M. (2003) · Nature · doi:10.1038/nature01510 · Cited by 1,026
Automated reduction and interpretation of
Horn, D. M., Zubarev, R. A., & McLafferty, F. W. (2000) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(99)00157-9 · Cited by 507
Decoding protein modifications using top-down mass spectrometry
Siuti, N., & Kelleher, N. L. (2007) · Nature Methods · doi:10.1038/nmeth1097 · Cited by 503
Self-citationPeer Reviewed: Top-Down Proteomics
Kelleher, N. (2004) · Analytical Chemistry · doi:10.1021/ac0415657 · Cited by 386
Self-citationComplete 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
Self-citationActivated Ion Electron Capture Dissociation for Mass Spectral Sequencing of Larger (42 kDa) Proteins
Horn, D. M., Ge, Y., & McLafferty, F. W. (2000) · Analytical Chemistry · doi:10.1021/ac000494i · Cited by 334
Frese, C. K., Altelaar, M. A. F., van den Toorn, H., Nolting, D., Griep‐Raming, J., Heck, A. J. R., & Mohammed, S. (2012) · Analytical Chemistry · doi:10.1021/ac3025366 · Cited by 304
Zamdborg, L., LeDuc, R. D., Glowacz, K. J., Kim, Y.-B., Viswanathan, V., Spaulding, I. T., Early, B. P., Bluhm, E. J., Babai, S., & Kelleher, N. L. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm371 · Cited by 251
Self-citationInformatics and multiplexing of intact protein identification in bacteria and the archaea
Meng, F., Cargile, B. J., Miller, L. M., Forbes, A. J., Johnson, J. R., & Kelleher, N. L. (2001) · Nature Biotechnology · doi:10.1038/nbt1001-952 · Cited by 210
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
The MaxQuant computational platform for mass spectrometry-based shotgun proteomics
Tyanova, S., Temu, T., & Cox, J. (2016) · Nature Protocols · doi:10.1038/nprot.2016.136 · Cited by 4,858
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
Self-citationProteome Discoverer—A Community Enhanced Data Processing Suite for Protein Informatics
Orsburn, B. C. (2021) · Proteomes · doi:10.3390/proteomes9010015 · Cited by 341
Hendrickson, C. L., Quinn, J. P., Kaiser, N. K., Smith, D. F., Blakney, G. T., Chen, T., Marshall, A. G., Weisbrod, C. R., & Beu, S. C. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1182-2 · Cited by 278
The diverse and expanding role of mass spectrometry in structural and molecular biology
Lössl, P., van de Waterbeemd, M., & Heck, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694818 · Cited by 222
Top-Down Proteomics: Ready for Prime Time?
Chen, B., Brown, K. A., Lin, Z., & Ge, Y. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04747 · Cited by 210
The Role of Electron Transfer Dissociation in Modern Proteomics
Riley, N. M., & Coon, J. J. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04810 · Cited by 184
The biosynthesis of methanobactin
Kenney, G. E., Dassama, L. M. K., Pandelia, M., Gizzi, A. S., Martinie, R. J., Gao, P., DeHart, C. J., Schachner, L. F., Skinner, O. S., Ro, S. Y., et al. (2018) · Science · doi:10.1126/science.aap9437 · Cited by 159
Self-citationFornelli, L., Srzentić, K., Huguet, R., Mullen, C., Sharma, S., Zabrouskov, V., Fellers, R. T., Durbin, K. R., Compton, P. D., & Kelleher, N. L. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b00984 · Cited by 150
Self-citationRoberts, D. S., Loo, J. A., Tsybin, Y. O., Liu, X., Wu, S., Chamot-Rooke, J., Agar, J. N., Paša-Tolić, L., Smith, L. M., & Ge, Y. (2024) · Nature Reviews Methods Primers · doi:10.1038/s43586-024-00318-2 · Cited by 161
Zhou, M., Lantz, C., Brown, K. A., Ge, Y., Paša-Tolić, L., Loo, J. A., & Lermyte, F. (2020) · Chemical Science · doi:10.1039/d0sc04392c · Cited by 146
MASH Suite Pro: A Comprehensive Software Tool for Top-Down Proteomics
Cai, W., Guner, H., Gregorich, Z. R., Chen, A. J., Ayaz-Guner, S., Peng, Y., Valeja, S. G., Liu, X., & Ge, Y. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.054387 · Cited by 132
GlyConnect: Glycoproteomics Goes Visual, Interactive, and Analytical
Alocci, D., Mariethoz, J. A., Gastaldello, A., Gasteiger, E., Karlsson, N. G., Kolarich, D., Packer, N. H., & Lisacek, F. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00766 · Cited by 128
Srzentić, K., Fornelli, L., Tsybin, Y. O., Loo, J. A., Seckler, H. S., Agar, J. N., Anderson, L. C., Bai, D. L., Beck, A., Brodbelt, J. S., et al. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00036 · Cited by 124
Self-citationA photocleavable surfactant for top-down proteomics
Brown, K. A., Chen, B., Guardado-Alvarez, T. M., Lin, Z., Hwang, L., Ayaz-Guner, S., Jin, S., & Ge, Y. (2019) · Nature Methods · doi:10.1038/s41592-019-0391-1 · Cited by 111
Top-Down Proteomics and the Challenges of True Proteoform Characterization
Po, A., & Eyers, C. E. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00416 · Cited by 117
Ro, S. Y., Schachner, L. F., Koo, C. W., Purohit, R., Remis, J. P., Kenney, G. E., Liauw, B. W.-H., Thomas, P. M., Patrie, S. M., Kelleher, N. L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10590-6 · Cited by 107
Self-citationPetras, D., Heiss, P., Süßmuth, R. D., & Calvete, J. J. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00305 · Cited by 102
Fornelli, L., Durbin, K. R., Fellers, R. T., Early, B. P., Greer, J. B., LeDuc, R. D., Compton, P. D., & Kelleher, N. L. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00698 · Cited by 88
Self-citationMiddle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry
Pandeswari, P. B., & Sabareesh, V. (2019) · RSC Advances · doi:10.1039/c8ra07200k · Cited by 94
A comprehensive pipeline for translational top-down proteomics from a single blood draw
Toby, T. K., Fornelli, L., Srzentić, K., DeHart, C. J., Levitsky, J., Friedewald, J., & Kelleher, N. L. (2019) · Nature Protocols · doi:10.1038/s41596-018-0085-7 · Cited by 86
Self-citationMelani, R. D., Skinner, O. S., Fornelli, L., Domont, G. B., Compton, P. D., & Kelleher, N. L. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.056523 · Cited by 85
Self-citationPascovici, D., Wu, J. X., McKay, M. J., Joseph, C., Noor, Z., Kamath, K. S., Wu, Y., Ranganathan, S., Gupta, V., & Mirzaei, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010016 · Cited by 82
Activated Ion-Electron Transfer Dissociation Enables Comprehensive Top-Down Protein Fragmentation
Riley, N. M., Westphall, M. S., & Coon, J. J. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00249 · Cited by 81
Emerging Computational Methods in Mass Spectrometry Imaging
Hu, H., & Laskin, J. (2022) · Advanced Science · doi:10.1002/advs.202203339 · Cited by 79
Exploring ECD on a Benchtop Q Exactive Orbitrap Mass Spectrometer
Fort, K. L., Cramer, C. N., Voinov, V. G., Vasil’ev, Y. V., Lopez, N. I., Beckman, J. S., & Heck, A. J. R. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00622 · Cited by 76
Kafader, J. O., Durbin, K. R., Melani, R. D., Des Soye, B. J., Schachner, L. F., Senko, M. W., Compton, P. D., & Kelleher, N. L. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00797 · Cited by 76
Self-citationThorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics
Fornelli, L., Srzentić, K., Toby, T. K., Doubleday, P. F., Huguet, R., Mullen, C., Melani, R. D., Seckler, H. S., DeHart, C. J., Weisbrod, C. R., et al. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir119.001638 · Cited by 79
Self-citationZheng, 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
Self-citationpTop 1.0: A High-Accuracy and High-Efficiency Search Engine for Intact Protein Identification
Sun, R.-X., Luo, L., Wu, L., Wang, R.-M., Zeng, W.-F., Chi, H., Liu, C., & He, S.-M. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b03963 · Cited by 71
Fundamentals and Advances of Orbitrap Mass Spectrometry
Hecht, E. S., Ščigelová, M., Eliuk, S. M., & Makarov, A. (2019) · Wiley eBooks · doi:10.1002/9780470027318.a9309.pub2 · Cited by 93
Fornelli, L., Ayoub, D., Aizikov, K., Liu, X., Damoc, E., Pevzner, P. A., Makarov, A., Beck, A., & Tsybin, Y. O. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.02.013 · Cited by 72
Sequencing Larger Intact Proteins (30-70 kDa) with Activated Ion Electron Transfer Dissociation
Riley, N. M., Westphall, M. S., & Coon, J. J. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1808-7 · Cited by 70
An informatic framework for decoding protein complexes by top-down mass spectrometry
Skinner, O. S., Havugimana, P. C., Haverland, N. A., Fornelli, L., Early, B. P., Greer, J. B., Fellers, R. T., Durbin, K. R., do Vale, L. H. F., Melani, R. D., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3731 · Cited by 65
Self-citationHaverland, N. A., Skinner, O. S., Fellers, R. T., Tariq, A., Early, B. P., LeDuc, R. D., Fornelli, L., Compton, P. D., & Kelleher, N. L. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1635-x · Cited by 69
Self-citationDecoding the protein composition of whole nucleosomes with Nuc-MS
Schachner, L. F., Jooß, K., Morgan, M. A., Piunti, A., Meiners, M. J., Kafader, J. O., Lee, A. S., Iwanaszko, M., Cheek, M. A., Burg, J. M., et al. (2021) · Nature Methods · doi:10.1038/s41592-020-01052-9 · Cited by 67
Self-citationTop-down proteomics for the analysis of proteolytic events - Methods, applications and perspectives
Tholey, A., & Becker, A. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.07.002 · Cited by 65
Enhanced Dissociation of Intact Proteins with High Capacity Electron Transfer Dissociation
Riley, N. M., Mullen, C., Weisbrod, C. R., Sharma, S., Senko, M. W., Zabrouskov, V., Westphall, M. S., Syka, J. E. P., & Coon, J. J. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1306-8 · Cited by 62
Liu, R., Xia, S., & Li, H. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21793 · Cited by 64
Delcourt, V., Franck, J., Quanico, J. P., Gimeno, J., Wisztorski, M., Raffo‐Romero, A., Kobeissy, F. H., Roucou, X., Salzet, M., & Fournier, I. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.065755 · Cited by 59
Srzentić, K., Nagornov, K. O., Fornelli, L., Lobas, A. A., Ayoub, D., Kozhinov, A. N., Gasilova, N., Menin, L., Beck, A., Gorshkov, M. V., et al. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02398 · Cited by 56
He, L., Anderson, L. C., Barnidge, D. R., Murray, D. L., Hendrickson, C. L., & Marshall, A. G. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1602-6 · Cited by 56
Phosphoproteomics with Activated Ion Electron Transfer Dissociation
Riley, N. M., Hebert, A. S., Dürnberger, G., Stanek, F., Mechtler, K., Westphall, M. S., & Coon, J. J. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b00212 · Cited by 55
Quantitative Top-Down Proteomics in Complex Samples Using Protein-Level Tandem Mass Tag Labeling
Yu, D., Wang, Z., Cupp‐Sutton, K. A., Guo, Y., Kou, Q., Smith, K., Liu, X., & Wu, S. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00464 · Cited by 54
Zheng, J., Chen, L., Skinner, O. S., Ysselstein, D., Remis, J. P., Lansbury, P. T., Skerlj, R. T., Mrosek, M., Heunisch, U., Krapp, S., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.7b13003 · Cited by 50
Self-citationType III-B CRISPR-Cas cascade of proteolytic cleavages
Steens, J. A., Bravo, J. P. K., Salazar, C. R. P., Yildiz, Ç., Amieiro, A. M., Köstlbacher, S., Prinsen, S. H. P., Andres, A. S., Patinios, C., Bardis, A., et al. (2024) · Science · doi:10.1126/science.adk0378 · Cited by 50
Weisbrod, C. R., Kaiser, N. K., Syka, J. E. P., Early, L., Mullen, C., Dunyach, J., English, A. M., Anderson, L. C., Blakney, G. T., Shabanowitz, J., et al. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1702-3 · Cited by 52
Campuzano, I. D. G., & Sandoval, W. N. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00036 · Cited by 51
Standard Proteoforms and Their Complexes for Native Mass Spectrometry
Schachner, L. F., Ives, A. N., McGee, J. P., Melani, R. D., Kafader, J. O., Compton, P. D., Patrie, S. M., & Kelleher, N. L. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02191-w · Cited by 48
Self-citationExtensive regulation of enzyme activity by phosphorylation in Escherichia coli
Schastnaya, E., Nakic, Z. R., Gruber, C., Doubleday, P. F., Krishnan, A., Johns, N. I., Park, J., Wang, H. H., & Sauer, U. (2021) · Nature Communications · doi:10.1038/s41467-021-25988-4 · Cited by 50
Native GELFrEE: A New Separation Technique for Biomolecular Assemblies
Skinner, O. S., do Vale, L. H. F., Catherman, A. D., Havugimana, P. C., de Sousa, M. V., Compton, P. D., & Kelleher, N. L. (2015) · Analytical Chemistry · doi:10.1021/ac504678d · Cited by 50
Self-citationGomes, 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
ProSight Native: Defining Protein Complex Composition from Native Top-Down Mass Spectrometry Data
Durbin, K. R., Robey, M. T., Voong, L. N., Fellers, R. T., Lutomski, C. A., El‐Baba, T. J., Robinson, C. V., & Kelleher, N. L. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00171 · Cited by 48
Self-citationBioinformatics Analysis of Top-Down Mass Spectrometry Data with ProSight Lite
DeHart, C. J., Fellers, R. T., Fornelli, L., Kelleher, N. L., & Thomas, P. M. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6783-4_18 · Cited by 44
Self-citationBrodie, N. I., Huguet, R., Zhang, T., Viner, R., Zabrouskov, V., Pan, J., Petrotchenko, E. V., & Borchers, C. H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b03655 · Cited by 43
Mayfield, J. E., Irani, S., Escobar, E. E., Zhang, Z., Burkholder, N. T., Robinson, M., Mehaffey, M. R., Sipe, S. N., Yang, W., Prescott, N. A., et al. (2019) · eLife · doi:10.7554/elife.48725 · Cited by 43
Kline, J. T., Mullen, C., Durbin, K. R., Oates, R. N., Huguet, R., Syka, J. E. P., & Fornelli, L. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00062 · Cited by 47
Halim, M. A., Girod, M., MacAleese, L., Lemoine, J., Antoine, R., & Dugourd, P. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1419-8 · Cited by 42
Characterization of microbial mixtures by mass spectrometry
Sandrin, T. R., & Demirev, P. A. (2017) · Mass Spectrometry Reviews · doi:10.1002/mas.21534 · Cited by 44
Seckler, H. S., Fornelli, L., Mutharasan, R. K., Thaxton, C. S., Fellers, R. T., Daviglus, M. L., Sniderman, A. D., Rader, D. J., Kelleher, N. L., Lloyd‐Jones, D. M., et al. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00100 · Cited by 41
Self-citationEscobar, E. E., King, D. T., Serrano-Negrón, J. E., Alteen, M. G., Vocadlo, D. J., & Brodbelt, J. S. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c04710 · Cited by 40
Yu, D., Wang, Z., Cupp-Sutton, K. A., Liu, X., & Wu, S. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02315-2 · Cited by 39
The benefits (and misfortunes) of SDS in top-down proteomics
Kachuk, C., & Doucette, A. A. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2017.03.002 · Cited by 39
Sipe, S. N., Patrick, J. W., Laganowsky, A., & Brodbelt, J. S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03689 · Cited by 39
Adams, L. M., DeHart, C. J., Drown, B., Anderson, L. C., Bocik, W., Boja, E. S., Hiltke, T., Hendrickson, C. L., Rodriguez, H., Caldwell, M. A., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102768 · Cited by 37
Self-citationMASH Native: a unified solution for native top-down proteomics data processing
Larson, E. J., Pergande, M. R., Moss, M. E., Rossler, K. J., Wenger, R. K., Krichel, B., Josyer, H., Melby, J. A., Roberts, D. S., Pike, K. A., et al. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad359 · Cited by 43
Production of Recombinant Chemokines and Validation of Refolding
Veldkamp, C. T., Koplinski, C. A., Jensen, D. R., Peterson, F. C., Smits, K., Smith, B. L., Johnson, S. K., Lettieri, C. K., Buchholz, W. G., Solheim, J. C., et al. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.09.031 · Cited by 37
Sadeghi, S. A., Ashkarran, A. A., Wang, Q., Zhu, G., Mahmoudi, M., & Sun, L. (2024) · ACS Nano · doi:10.1021/acsnano.4c04675 · Cited by 33
Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes
Sipe, S. N., & Brodbelt, J. S. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp01144g · Cited by 37
Shaw, J., Robinson, E. W., & Paša‐Tolić, L. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00148 · Cited by 35
Top-Down Mass Spectrometry: Proteomics to Proteoforms
Patrie, S. M. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-41448-5_8 · Cited by 38
Regl, C., Wohlschlager, T., Holzmann, J., & Huber, C. G. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01755 · Cited by 34
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
Protein-species quantitative venomics: looking through a crystal ball
Calvete, J. J., Petras, D., Calderón‐Celis, F., Lomonte, B., Encinar, J. R., & Sanz‐Medel, A. (2017) · The Journal of venomous animals and toxins including tropical diseases · doi:10.1186/s40409-017-0116-9 · Cited by 33
Top-Down Analysis of Proteins in Low Charge States
Bashyal, A., Sanders, J. D., Holden, D. D., & Brodbelt, J. S. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02146-1 · Cited by 37
Top-Down and Middle-Down Mass Spectrometry of Antibodies
Khristenko, N. A., Nagornov, K. O., Garcia, C., Gasilova, N., Gant, M. S., Druart, K., Kozhinov, A. N., Menin, L., Chamot‐Rooke, J., & Tsybin, Y. O. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.100989 · Cited by 31
Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli
Schastnaya, E., Doubleday, P. F., Maurer, L., & Sauer, U. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111950 · Cited by 33
Prospects and challenges of cancer systems medicine: from genes to disease networks
Karimi, M. R., Karimi, A. H., Abolmaali, S., Sadeghi, M., & Schmitz, U. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab343 · Cited by 33
Guo, Y., Yu, D., Cupp‐Sutton, K. A., Liu, X., & Wu, S. (2022) · Analytica Chimica Acta · doi:10.1016/j.aca.2022.340037 · Cited by 30
Berghmans, E., Jacobs, J., Deben, C., Hermans, C., Broeckx, G., Smits, E., Maes, E., Raskin, J., Pauwels, P., & Baggerman, G. (2020) · Cancers · doi:10.3390/cancers12040863 · Cited by 29
Nagornov, K. O., Kozhinov, A. N., Gasilova, N., Menin, L., & Tsybin, Y. O. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00190 · Cited by 32
Khan, A., Eikani, C. K., Khan, H., Iavarone, A. T., & Pesavento, J. J. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00780 · Cited by 28
He, L., Anderson, L. C., Barnidge, D. R., Murray, D. L., Dasari, S., Dispenzieri, A. A., Hendrickson, C. L., & Marshall, A. G. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03294 · Cited by 29
Blöchl, C., Holzner, C., Luciano, M., Bauer, R., Horejs‐Hoeck, J., Eckhard, U., Brandstetter, H., & Huber, C. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010412 · Cited by 26
Cline, E. N., Das, A., Bicca, M. A., Mohammad, S. N., Schachner, L. F., Kamel, J. M., DiNunno, N., Weng, A., Paschall, J. D., Bu, R. L., et al. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14647 · Cited by 25
Self-citationWeisbrod, C. R., Anderson, L. C., Hendrickson, C. L., Schaffer, L. V., Shortreed, M. R., Smith, L. M., Shabanowitz, J., & Hunt, D. F. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c00847 · Cited by 28
Moe, M. K., Haug, T., Sydnes, M. O., Sperstad, S. V., Li, C., Vaagsfjord, L. C., de la Vega, E., & Stensvåg, K. (2018) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00780 · Cited by 25
Rosenberg, J. A., Parker, W. R., Cammarata, M. B., & Brodbelt, J. S. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-1918-x · Cited by 25
Rommelfanger, S. R., Zhou, M., Shaghasi, H., Tzeng, S., Evans, B. S., Paša‐Tolić, L., Umen, J., & Pesavento, J. J. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00029 · Cited by 24
Large‐scale top‐down proteomics of the Arabidopsis thaliana leaf and chloroplast proteomes
Wang, Q., Sun, L., & Lundquist, P. K. (2022) · PROTEOMICS · doi:10.1002/pmic.202100377 · Cited by 25
Peng, W., den Boer, M. A., Tamara, S., Mokiem, N. J., van der Lans, S. P. A., Bondt, A., Schulte, D., Haas, P., Minnema, M. C., Rooijakkers, S. H. M., et al. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00330 · Cited by 24
Peris‐Díaz, M. D., Guráň, R., Zítka, O., Adam, V., & Krężel, A. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00651 · Cited by 22
Seckler, H. D. S., Park, H.-M., Lloyd-Jones, C., Melani, R., Camarillo, J., Wilkins, J., Compton, P. D., & Kelleher, N. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00026 · Cited by 21
Self-citationJeong, K., Babović, M., Gorshkov, V., Kim, J., Jensen, O. N., & Kohlbacher, O. (2022) · Nature Communications · doi:10.1038/s41467-022-31922-z · Cited by 25
Chen, C., Kuo, T.-H., Chung, H., Huang, P., Lin, L., & Hsu, C. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00354 · Cited by 23
Soler-Ventura, A., Gay, M., Jodar, M., Vilanova, M., Castillo, J., Arauz-Garofalo, G., Villarreal, L., Ballescà, J., Vilaseca, M., & Oliva, R. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00499 · Cited by 14
Liu, F. C., Ridgeway, M. E., Wootton, C. A., Theisen, A., Panczyk, E. M., Meier, F., Park, M. A., & Bleiholder, C. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00187 · Cited by 21
Top-down protein identification using isotopic envelope fingerprinting
Xiao, K., Yu, F., & Tian, Z. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.10.010 · Cited by 21
Modulation of Protein Fragmentation Through Carbamylation of Primary Amines
Greer, S. M., Holden, D. D., Fellers, R. T., Kelleher, N. L., & Brodbelt, J. S. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1648-5 · Cited by 21
Self-citation
Metadata
- Authors
- Fellers, R. T., Greer, J. B., Early, B. P., Yu, X., LeDuc, R. D., Kelleher, N. L., & Thomas, P. M.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Kelleher, Neil L.
- Thomas, Paul M.
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2015-02-26
- Volume
- 15
- Issue
- 7
- Pages
- 1235-1238
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- OpenAlex
- W1983285663
- Cited by
- 247
- References
- 15
- Citations by year
- 2026: 6 · 2025: 21 · 2024: 22 · 2023: 18 · 2022: 21 · 2021: 36 · 2020: 19 · 2019: 27 · 2018: 20 · 2017: 28 · 2016: 18 · 2015: 10
- FWCI
- 7.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- PROTEOMICS (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Drug Abuse (P30DA018310)
- National Institute of General Medical Sciences (R01GM067193)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- top-down mass spectrometry, post-translational modification, mass shift, glycosylation, graphics software, open source software
- MeSH terms
- Amino Acid Sequence, Humans, Molecular Weight, Protein Processing, Post-Translational, Software, Proteome, Databases, Protein, Proteomics, Tandem Mass Spectrometry, Molecular Sequence Annotation
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