The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Molecular Analysis of Tumor Margins by MALDI Mass Spectrometry in Renal Carcinoma
Open accessAbstract
The rate of tumor recurrence post resection suggests that there are underlying molecular changes in nearby histologically normal tissue that go undetected by conventional diagnostic methods that utilize contrast agents and immunohistochemistry. MALDI MS is a molecular technology that has the specificity and sensitivity to monitor and identify molecular species indicative of these changes. The current study utilizes this technology to assess molecular distributions within a tumor and adjacent normal tissue in clear cell renal cell carcinoma biopsies. Results indicate that the histologically normal tissue adjacent to the tumor expresses many of the molecular characteristics of the tumor. Proteins of the mitochondrial electron transport system are examples of such distributions. This work demonstrates the utility of MALDI MS for the analysis of tumor tissue in the elucidation of aberrant molecular changes in the tumor microenvironment.
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Citations
Cites
Statistical significance for genomewide studies
Storey, J. D., & Tibshirani, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1530509100 · Cited by 9,692
Molecular Imaging of Biological Samples: Localization of Peptides and Proteins Using MALDI-TOF MS
Caprioli, R. M., Farmer, T. B., & Gile, J. (1997) · Analytical Chemistry · doi:10.1021/ac970888i · Cited by 2,234
Self-citationGuzy, R. D., & Schumacker, P. T. (2006) · Experimental Physiology · doi:10.1113/expphysiol.2006.033506 · Cited by 881
The biology of hypoxia: the role of oxygen sensing in development, normal function, and disease
Giaccia, A. J., Simon, M. C., & Johnson, R. (2004) · Genes & Development · doi:10.1101/gad.1243304 · Cited by 380
Cited by
MALDI Imaging of Lipid Biochemistry in Tissues by Mass Spectrometry
Zemski Berry, K. A., Hankin, J. A., Barkley, R. M., Spraggins, J. M., Caprioli, R. M., & Murphy, R. C. (2011) · Chemical Reviews · doi:10.1021/cr200280p · Cited by 386
Self-citationMALDI imaging mass spectrometry of human tissue: method challenges and clinical perspectives
Seeley, E. H., & Caprioli, R. M. (2011) · Trends in Biotechnology · doi:10.1016/j.tibtech.2010.12.002 · Cited by 197
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Metadata
- Authors
- Oppenheimer, S. R., Mi, D., Sanders, M. E., & Caprioli, R. M.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-03-24
- Volume
- 9
- Issue
- 5
- Pages
- 2182-2190
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W1987355385
- Cited by
- 167
- References
- 4
- FWCI
- 10.23
- Type
- journal article
- Language
- en
- Open access
- green
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.