The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Expanding the structural analysis capabilities on an Orbitrap-based mass spectrometer for large macromolecular complexes
Open accessAbstract
Native mass spectrometry can provide insight into the structure of macromolecular biological systems.
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“More recently, instrument hardware improvements have led to enhanced large ion transmission and detection, especially with the implementation of ultra-high mass range (UHMR) Orbitraps that are capable of analyzing species at 70,000 m/z and mass as large as 800 kDa [103,104].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [103]
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Citations
Cites
Electrospray Ionization for Mass Spectrometry of Large Biomolecules
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Studying noncovalent protein complexes by electrospray ionization mass spectrometry
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Electrospray and Taylor-Cone theory, Dole's beam of macromolecules at last?
Wilm, M. S., & Mann, M. (1994) · International Journal of Mass Spectrometry and Ion Processes · doi:10.1016/0168-1176(94)04024-9 · Cited by 976
Native mass spectrometry: a bridge between interactomics and structural biology
Heck, A. J. R. (2008) · Nature Methods · doi:10.1038/nmeth.1265 · Cited by 766
Self-citationDetermining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
Hernández, H., & Robinson, C. V. (2007) · Nature Protocols · doi:10.1038/nprot.2007.73 · Cited by 663
Katta, V., & Chait, B. T. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00022a058 · Cited by 476
High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies
Rose, R. J., Damoc, E., Denisov, E., Makarov, A., & Heck, A. J. R. (2012) · Nature Methods · doi:10.1038/nmeth.2208 · Cited by 392
Self-citationShibuta, Y., Sakane, S., Miyoshi, E., Okita, S., Takaki, T., & Ohno, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00017-5 · Cited by 296
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Evaluation of a Bruker timsTOF Pro for Native Mass SpectrometryPreprint
Panczyk, E. M., Snyder, D. T., Liu, F. C., Lin, Y.-F., Ridgeway, M. E., Park, M., Bleiholder, C., & Wysocki, V. H. (2021) · ChemRxiv · doi:10.26434/chemrxiv-2021-qr78t · Cited by 2
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A Novel Heterometallic Ring {Cr 5 Ni 3 } and New {Cr 6 Co 2 } and {Cr 6 Zn 2 } Rings
Alsuhaymi, A., Geue, N., Brookfield, A., Timco, G. A., Lockyer, S. J., Smith, G. D., Whitehead, G. F. S., Barran, P. E., Collison, D., & Winpenny, R. E. P. (2026) · Chemistry - A European Journal · doi:10.1002/chem.70991 · Cited by 1
Gadallah, M. I., McConnell, K. A., Hager, K. M., James, V. K., Nguyen, A. W., Maynard, J. A., & Brodbelt, J. S. (2026) · Chemical Science · doi:10.1039/d5sc09702a · Cited by 1
Mathew, A., Veloso, L. M. G. D. S., Giskes, F., Eijkel, G. B., Papanastasiou, D. K., Heck, A. J. R., Makarov, A., Ellis, S. R., & Heeren, R. M. A. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.6c00132 · Cited by 1
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High performance interface for boosting ion transmission in native mass spectrometry and beyond.Preprint
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Espectrometria de Massa na Análise de Sistemas Biológicos
Santos, I. C. (2021) · Boletim da Sociedade Portuguesa de Química · doi:10.52590/m3.p696.a30002402
Mathew, A. (2023) · Research Publications (Maastricht University) · doi:10.26481/dis.20231017am
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Mak, J., Famili, A., & Crittenden, C. M. (2025) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2025.117566
Biosensors for Biotoxins Detection and Monitoring
Agerova, A., Juarez, J. F. B., & Peraro, M. D. (2026) · Advanced Sensor Research · doi:10.1002/adsr.70174
Ebberink, E. H. T. M., Giaretta, E., Barendregt, A., Fiala, J., Yin, V. C., Wörner, T. P., Fort, K. L., Makarov, A., & Heck, A. J. R. (2026) · Nature Communications · doi:10.1038/s41467-026-76691-1
Self-citationSetting the STORI Straight: Improved Signal Processing for Charge Detection Mass Spectrometry
Goodwin, M. P., Grinfeld, D., Yip, P., Bowen, K. P., Fu, L., Kafader, J. O., Kelleher, N. L., & Senko, M. W. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.6c00256
Metadata
- Authors
- Fort, K. L., van de Waterbeemd, M., Boll, D., Reinhardt-Szyba, M., Belov, M. E., Sasaki, E., Zschoche, R., Hilvert, D., Makarov, A. A., & Heck, A. J. R.
- Affiliations
- Utrecht University (NL)
- Biomolecular Mass Spectrometry and Proteomics
- Thermo Fisher Scientific (Germany) (DE)
- ETH Zurich (CH)
- Corresponding author
- Heck, Albert J. R.
- Venue
- The Analyst
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2018
- Volume
- 143
- Issue
- 1
- Pages
- 100-105
- ISSN
- 0003-2654 (ISSN-L)
- 1364-5528
- OpenAlex
- W2767559908
- Cited by
- 122
- References
- 16
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 11 · 2023: 12 · 2022: 13 · 2021: 20 · 2020: 18 · 2019: 18 · 2018: 8
- FWCI
- 5.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Analyst (publishedVersion)
- PubMed (publishedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, other-oa)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Funders
- Stichting voor Fundamenteel Onderzoek der Materie (12PR3303-2)
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (184.032.201, 718.015.003)
- H2020 Future and Emerging Technologies (686547)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- native mass spectrometry, macromolecular complexes, signal intensity enhancement, mass resolution
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