The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
The Role of Mass Spectrometry in Structure Elucidation of Dynamic Protein Complexes
Abstract
The fact that ions of macromolecular complexes produced by electrospray ionization can be maintained intact in a mass spectrometer has stimulated exciting new lines of research. In this review we chart the progress of this research from the observation of simple homo-oligomers to complex heterogeneous macromolecular assemblies of mega-Dalton proportions. The applications described herein not only confirm the status of mass spectrometry (MS) as a structural biology approach to complement X-ray analysis or electron microscopy, but also highlight unique attributes of the methodology. This is exemplified in studies of the biogenesis of macromolecular complexes and in the exchange of subunits between macromolecular complexes. Moreover, recent successes in revealing the overall subunit architecture of complexes are set to promote MS from a complementary approach to a structural biology tool in its own right.
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Cites
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Cited by
Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000
Self-citationNative mass spectrometry: a bridge between interactomics and structural biology
Heck, A. J. R. (2008) · Nature Methods · doi:10.1038/nmeth.1265 · Cited by 766
Native Mass Spectrometry: What is in the Name?
Leney, A. C., & Heck, A. J. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1545-3 · Cited by 602
High-Resolution Native Mass Spectrometry
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High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies
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Metadata
- Authors
- Sharon, M., & Robinson, C. V.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2007-06-07
- Volume
- 76
- Issue
- 1
- Pages
- 167-193
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2129733824
- Cited by
- 357
- References
- 104
- FWCI
- 1.86
- Type
- journal article
- Language
- en
- Open access
- closed
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