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.
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“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]
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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
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Items 201–247 of 247
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Adhikari, S., Dziekonski, E. T., Londry, F. A., & McLuckey, S. A. (2019) · Journal of Mass Spectrometry · doi:10.1002/jms.4352 · Cited by 4
Chaihu, L., Yao, X., Xu, X., Zhu, Z., Chen, D. D. Y., & Wang, G. (2021) · Journal of Visualized Experiments · doi:10.3791/62672 · Cited by 4
Pediatric Brain Tumors: Signatures from the Intact Proteome
Rossetti, D. V., Inserra, I., Nesticò, A., Vincenzoni, F., Iavarone, F., Messana, I., Castagnola, M., Massimi, L., Tamburrini, G., Caldarelli, M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063196 · Cited by 4
McGee, W. M., Faron, M. L., Neil, J. R., Kronewitter, S. R., Buchan, B. W., Ledeboer, N. A., & Stephenson, J. L. (2020) · Clinical mass spectrometry · doi:10.1016/j.clinms.2020.07.001 · Cited by 4
Native Multidimensional Protein Complex Identification and Topology Characterization (Native MudPIT)
Qi, Z., Fang, F., Moeller, W. J., Zhu, G., Wang, Q., Wang, Q., Gao, G., Sun, L., & Wysocki, V. H. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c01693 · Cited by 4
Immunocomplexed Antigen Capture and Identification by Native Top-Down Mass Spectrometry
McGee, J. P., Melani, R. D., Soye, B. J. D., Croote, D., Winton, V. J., Quake, S. R., Kafader, J. O., & Kelleher, N. L. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00235 · Cited by 4
Self-citationCastillo, J., Gay, M., de la Iglesia, A., Arauz‐Garofalo, G., Vilanova, M., Leiva, M., Corral, J. M., Guimerà, M., Manau, D., Vilaseca, M., et al. (2025) · Molecular Human Reproduction · doi:10.1093/molehr/gaaf019 · Cited by 3
Mao, Y., Daly, T. J., & Li, N. (2019) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.8574 · Cited by 3
Muneeruddin, K., Kaltashov, I. A., & Wang, G. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1859-2_27 · Cited by 3
Tracking proteasome degradation: A cross-organ analysis via intact degradomics mass spectrometry
Zittlau, K. I., Zachor-Movshovitz, D., Leushkin, Y., Brener, R. S., Morgenstern, D., Ben‐Nissan, G., & Sharon, M. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419607122 · Cited by 4
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TDFragMapper: a visualization tool for evaluating experimental parameters in top-down proteomics
Dhenin, J., Lima, D. B., Dupré, M., & Chamot‐Rooke, J. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btab784 · Cited by 4
McGee, W. M., Verma, A., Viirtola, M., Kronewitter, S. R., Neil, J. R., & Stephenson, J. L. (2021) · Journal of Mass Spectrometry and Advances in the Clinical Lab · doi:10.1016/j.jmsacl.2021.05.001 · Cited by 3
Delfino, D., Rossetti, D. V., Martelli, C., Inserra, I., Vincenzoni, F., Castagnola, M., Urbani, A., Scarpa, S., Fuso, A., Cavallaro, R. A., et al. (2019) · Journal of Chromatography B · doi:10.1016/j.jchromb.2019.06.005 · Cited by 3
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Renbarger, E. A., & Webb, I. (2026) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2026.117570 · Cited by 2
Cain, R. L., & Webb, I. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00388 · Cited by 2
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Chang, H.-Y., Chen, C.-T., Ko, C.-L., Chen, Y., Chen, Y., Hsu, W., Juo, C., & Sung, T. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b02343 · Cited by 2
Kline, J. T., Mullen, C., Durbin, K. R., Oates, R. N., Huguet, R., Syka, J. E. P., & Fornelli, L. (2021) · ChemRxiv · doi:10.26434/chemrxiv.14036810 · Cited by 2
Yang, L., Stanisheuski, S., Song, Z., Bracha, S., & Maier, C. S. (2023) · European Journal of Mass Spectrometry · doi:10.1177/14690667231202766 · Cited by 1
Determining KRAS4B-Targeting Compound Specificity by Top–Down Mass Spectrometry
D’Ippolito, R. A., Scheidemantle, G. M., Rabara, D., Blanco, M. A., Ramakrishnan, N., Widmeyer, S. R. T., Messing, S., Turner, D., Maciag, A. E., Stephen, A. G., et al. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3922-1_18 · Cited by 1
Karamonová, L., Procházková, B., Volný, M., Nemeškalová, A., Sýkora, D., Kuchař, M., Fukal, L., & Holubová, B. (2025) · Journal of Analytical Methods in Chemistry · doi:10.1155/jamc/3021570 · Cited by 2
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Ives, A. N., Thibert, S. M., Berger, M. R., Gaffrey, M. J., Mitchell, H. D., Williams, S. M., Zhou, M., Waters, K. M., Sims, A. C., & Zhang, T. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c01015 · Cited by 1
Lane, N. M., Gregorich, Z. R., & Ge, Y. (2016) · Springer eBooks · doi:10.1007/978-3-319-31828-8_8 · Cited by 1
Lanzillotti, M. B., Dunham, S. D., Juetten, K. J., & Brodbelt, J. S. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00607 · Cited by 1
Olson, L. J., Jensen, D. R., Volkman, B. F., Kim, J. J., Peterson, F. C., Gundry, R. L., & Dahms, N. M. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.04.002 · Cited by 1
Using TDFragMapper: a high-performance tool to assess experimental parameters in top-down proteomicsPreprint
Lima, D. B., Dhenin, J., Dupré, M., & Chamot‐Rooke, J. (2021) · Research Square · doi:10.21203/rs.3.pex-1051/v1 · Cited by 1
Lisacek, F. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.20479-2 · Cited by 1
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Dollar, A. N., & Webb, I. K. (2025) · bioRxiv · doi:10.1101/2025.02.20.639338
Galluzzi, F. (2021) · theses.fr (ABES) · doi:10.70675/544c95bfz2ddbz4ecaza12dz64e75d212990 · Cited by 1
Waas, M., Farris, S. D., Kropp, E. M., Beckman, J. A., Stempien‐Otero, A., Mahr, C., & Gundry, R. L. (2016) · Springer eBooks · doi:10.1007/978-3-319-31828-8_6
Bioinformatics Support for Farm Animal Proteomics
Pena, A. B., & Lisacek, F. (2018) · Springer eBooks · doi:10.1007/978-3-319-69682-9_18
Wang, Y. (2017) · Digital Repository Service (Northeastern University) · doi:10.17760/d20252417
Jeong, K., Babović, M., Gorshkov, V., Kim, J., Jensen, O. N., & Kohlbacher, O. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.11.468203
Qin, S., & Tian, Z. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2325-1_10
Proteomic applications for studies of bull fertility
Viana, A. G. D. A. (2022) · doi:10.47328/ufvbbt.2022.651
Recent Advances in Top-Down Proteomics for Proteoform Analysis
Yu, J., Kim, M.-J., & Park, H.-M. (2023) · KSBB Journal · doi:10.7841/ksbbj.2023.38.1.12
De novo antibody sequencing based on mass spectrometry
Peng, W. (2024) · Utrecht University Repository (Utrecht University) · doi:10.33540/2133
Black, K. L., & Webb, I. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00363
Liao, Y., Qian, R., Zhang, M., Sun, C., Wen, H., Weinan, E., Zhang, W., & Zhou, M. (2025) · PROTEOMICS · doi:10.1002/pmic.70031
Halim, M. A. (2017) · theses.fr (ABES) · doi:10.70675/1987b0d6z615ez491dz9468z6cb2816294cf
Evidence for an Organometallic Species Formed in the ArsL ReactionPreprint
Serrano, D. A., Wang, B., Booker, S. J., & Silakov, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.29.721666
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Gao, Y., Greguš, M., Kostas, J. C., Marie, A., & Ivanov, A. R. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c01310
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Colón-Rosado, J. A., Fang, F., & Sun, L. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c03571
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
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