The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
MALDI imaging mass spectrometry: Spatial molecular analysis to enable a new age of discovery
Open accessAbstract
Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) combines the sensitivity and selectivity of mass spectrometry with spatial analysis to provide a new dimension for histological analyses to provide unbiased visualization of the arrangement of biomolecules in tissue. As such, MALDI IMS has the capability to become a powerful new molecular technology for the biological and clinical sciences. In this review, we briefly describe several applications of MALDI IMS covering a range of molecular weights, from drugs to proteins. Current limitations and challenges are discussed along with recent developments to address these issues.
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Citations
Cites
Molecular Imaging of Biological Samples: Localization of Peptides and Proteins Using MALDI-TOF MS
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Self-citationStoeckli, M., Chaurand, P., Hallahan, D. E., & Caprioli, R. M. (2001) · Nature Medicine · doi:10.1038/86573 · Cited by 1,172
Self-citationClark, A. E., Kaleta, E. J., Arora, A., & Wolk, D. M. (2013) · Clinical Microbiology Reviews · doi:10.1128/cmr.00072-12 · Cited by 941
Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
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Hankin, J. A., Barkley, R. M., & Murphy, R. C. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.06.010 · Cited by 598
Hebert, A. S., Richards, A. L., Bailey, D. J., Ulbrich, A., Coughlin, E. E., Westphall, M. S., & Coon, J. J. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.034769 · Cited by 528 · cited 1×
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BackgroundDirect Molecular Analysis of Whole-Body Animal Tissue Sections by Imaging MALDI Mass Spectrometry
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Self-citationBiomolecule Analysis by Ion Mobility Spectrometry
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Dynamic range of mass accuracy in LTQ orbitrap hybrid mass spectrometer
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Self-citation
Cited by
Applications of MALDI Mass Spectrometry in Clinical Chemistry
Duncan, M. W., Nedelkov, D., Walsh, R., & Hattan, S. J. (2016) · Clinical Chemistry · doi:10.1373/clinchem.2015.239491 · Cited by 96
Clinical protein science in translational medicine targeting malignant melanoma
Gil, J., Betancourt, L. H., Pla, I., Sanchez, A., Appelqvist, R., Miliotis, T., Kuras, M., Oskolas, H., Kim, Y., Horvath, Z., et al. (2019) · Cell Biology and Toxicology · doi:10.1007/s10565-019-09468-6 · Cited by 45
González de San Román, E., Bidmon, H.-J., Malisic, M., Susnea, I., Küppers, A., Hübbers, R., Wree, A., Nischwitz, V., Amunts, K., & Huesgen, P. F. (2018) · Brain Structure and Function · doi:10.1007/s00429-018-1660-y · Cited by 24
Metadata
- Authors
- Gessel, M. M., Norris, J. L., & Caprioli, R. M.
- Venue
- Journal of Proteomics
- Publisher
- Elsevier BV
- Published
- 2014-07
- Volume
- 107
- Pages
- 71-82
- ISSN
- 1874-3919 (ISSN-L)
- OpenAlex
- W2055881608
- Cited by
- 276
- References
- 59
- FWCI
- 14.97
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
