The DOI matches its Crossref record; 141 of the 141 references it cites were found in a registry or an index.
Ion mobility mass spectrometry of proteins and proteinassemblies
Abstract
Traditionally, mass spectrometry has been a powerful analytical method enabling the structural analysis of small molecules, and later on peptides and proteins. With the advent of native mass spectrometry, using a combination of electrospray ionisation and time of flight analysis, mass spectrometry could also be applied to the mass determination of large protein complexes such as ribosomes and whole viruses. More recently, ion mobility has been coupled to mass spectrometry providing a new dimension in the analysis of biomolecules, with ion mobility separating ions according to differences in size and shape. In the context of native mass spectrometry, ion mobility mass spectrometry opens up avenues for the detailed structural analysis of large and heterogeneous protein complexes, providing information on the stoichiometry, topology and cross section of these assemblies and their composite subunits. With these characteristics, ion mobility mass spectrometry offers a complementary tool in the context of structural biology. Here, we critically review the development, instrumentation, approaches and applications of ion mobility in combination with mass spectrometry, focusing on the analysis of larger proteins and protein assemblies (185 references).
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Cites
Time-of-Flight Mass Spectrometer with Improved Resolution
Wiley, W. C., & McLaren, I. H. (1955) · Review of Scientific Instruments · doi:10.1063/1.1715212 · Cited by 3,678
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Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
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Studying noncovalent protein complexes by electrospray ionization mass spectrometry
Loo, J. A. (1997) · Mass Spectrometry Reviews · doi:10.1002/(sici)1098-2787(1997)16:1<1::aid-mas1>3.0.co;2-l · Cited by 1,182
Ion mobility–mass spectrometry
Kanu, A. B., Dwivedi, P., Tam, M., Matz, L., & Hill, H. H. (2008) · Journal of Mass Spectrometry · doi:10.1002/jms.1383 · Cited by 1,154
Ion mobility–mass spectrometry analysis of large protein complexes
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Structural Information from Ion Mobility Measurements: Effects of the Long-Range Potential
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An exact hard-spheres scattering model for the mobilities of polyatomic ions
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Self-citation
Cited by
Recommendations for reporting ion mobility Mass Spectrometry measurements
Gabelica, V., Shvartsburg, A. A., Afonso, C., Barran, P., Benesch, J. L. P., Bleiholder, C., Bowers, M. T., Bilbao, A., Bush, M. F., Campbell, J. L., et al. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21585 · Cited by 493
Lapthorn, C., Pullen, F., & Chowdhry, B. Z. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21349 · Cited by 398
Interrogating viral capsid assembly with ion mobility–mass spectrometry
Uetrecht, C., Barbu, I. M., Shoemaker, G. K., van Duijn, E., & Heck, A. J. R. (2011) · Nature Chemistry · doi:10.1038/nchem.947 · Cited by 267
Self-citationThe 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
Self-citationBelov, M. E., Damoc, E., Denisov, E., Compton, P. D., Horning, S., Makarov, A. A., & Kelleher, N. L. (2013) · Analytical Chemistry · doi:10.1021/ac4029328 · Cited by 175
Metadata
- Authors
- Uetrecht, C., Rose, R. J., van Duijn, E., Lorenzen, K., & Heck, A. J. R.
- Venue
- Chem. Soc. Rev.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2010
- Volume
- 39
- Issue
- 5
- Pages
- 1633-1655
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2086145691
- Cited by
- 462
- References
- 141
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- closed
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