The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems
Open accessAbstract
Solution-phase hydrogen/deuterium exchange (HDX) coupled to mass spectrometry (MS) is a widespread tool for structural analysis across academia and the biopharmaceutical industry. By monitoring the exchangeability of backbone amide protons, HDX-MS can reveal information about higher-order structure and dynamics throughout a protein, can track protein folding pathways, map interaction sites, and assess conformational states of protein samples. The combination of the versatility of the hydrogen/deuterium exchange reaction with the sensitivity of mass spectrometry has enabled the study of extremely challenging protein systems, some of which cannot be suitably studied using other techniques. Improvements over the past three decades have continually increased throughput, robustness, and expanded the limits of what is feasible for HDX-MS investigations. To provide an overview for researchers seeking to utilize and derive the most from HDX-MS for protein structural analysis, we summarize the fundamental principles, basic methodology, strengths and weaknesses, and the established applications of HDX-MS while highlighting new developments and applications.
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Walls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532
Self-citationKey interactions in HIV-1 maturation identified by hydrogen-deuterium exchange
Lanman, J., Lam, T. T., Emmett, M. R., Marshall, A. G., Sakalian, M., & Prevelige, P. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb790 · Cited by 164
Direct protein-lipid interactions shape the conformational landscape of secondary transporters
Martens, C., Shekhar, M., Borysik, A. J., Lau, A. M., Reading, E., Tajkhorshid, E., Booth, P. J., & Politis, A. (2018) · Nature Communications · doi:10.1038/s41467-018-06704-1 · Cited by 134
Toward an Optimized Workflow for Middle-Down Proteomics
Cristobal, A., Marino, F., Post, H., van den Toorn, H. W. P., Mohammed, S., & Heck, A. J. R. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b03756 · Cited by 130
Impact of Fc N-glycan sialylation on IgG structure
Zhang, Z., Shah, B., & Richardson, J. (2019) · mAbs · doi:10.1080/19420862.2019.1655377 · Cited by 46
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Self-citationCorey, R. A., Ahdash, Z., Shah, A., Pyle, E., Allen, W. J., Fessl, T., Lovett, J. E., Politis, A., & Collinson, I. (2019) · eLife · doi:10.7554/elife.41803 · Cited by 30
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Dissecting the molecular basis for the modulation of neurotransmitter GPCR signaling by GINIP
Luebbers, A., Gonzalez-Hernandez, A. J., Zhou, M., Eyles, S. J., Levitz, J., & Garcia-Marcos, M. (2024) · Structure · doi:10.1016/j.str.2023.10.010 · Cited by 13
Palhano Zanela, T. M., Woudenberg, A., Romero Bello, K. G., & Underbakke, E. S. (2023) · Structure · doi:10.1016/j.str.2023.02.003 · Cited by 12
Bimai, O., Banerjee, I., Rozman Grinberg, I., Huang, P., Hultgren, L., Ekström, S., Lundin, D., Sjöberg, B.-M., & Logan, D. T. (2024) · eLife · doi:10.7554/elife.89292 · Cited by 3
Metadata
- Authors
- James, E. I., Murphree, T. A., Vorauer, C., Engen, J. R., & Guttman, M.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2021-09-07
- Volume
- 122
- Issue
- 8
- Pages
- 7562-7623
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W3197273087
- Cited by
- 305
- References
- 8
- FWCI
- 2.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- James, E. I., Murphree, T. A., Vorauer, C., Engen, J. R., & Guttman, M. (2022). Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.1c00279
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