The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Absolute Quantification of the G Protein-Coupled Receptor Rhodopsin by LC/MS/MS Using Proteolysis Product Peptides and Synthetic Peptide Standards
Abstract
Methods for the absolute quantification of a membrane protein are described using isotopically labeled or unlabeled synthetic peptides as standards. Synthetic peptides are designed to mimic peptides that are cleaved from target analyte proteins by proteolytic or chemical digestion, and the peptides selected serve as standards for quantification by LC/MS/MS on a triple quadrupole mass spectrometer. The technique is complementary to relative quantification techniques in widespread use by providing absolute quantitation of selected targets with greater sensitivity, dynamic range, and precision. Proteins that are found to be of interest by global proteome searches can be selected as targets for quantitation by the present method. This method has a much shorter analytical cycle time (minutes versus hours for the global proteome experiments), making it well suited for high-throughput environments. The present approach using synthetic peptides as standards, in conjunction with proteolytic or chemical cleavage of target proteins, allows mass spectrometry to be used as a highly selective detector for providing absolute quantification of proteins for which no standards are available. We demonstrate that quantification is simple and reliable for the integral membrane protein rhodopsin with reasonable recoveries for replicate experiments using low-micromolar solutions of rhodopsin from rod outer segments.
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Cites
Approved IFCC reference method for the measurement of HbA1c in human blood
Jeppsson, J.-O., Kobold, U., Barr, J., Finke, A., Hoelzel, W., Hoshino, T., Miedema, K., Mosca, A., Mauri, P., Paroni, R., et al. (2002) · Clinical Chemistry and Laboratory Medicine · doi:10.1515/cclm.2002.016 · Cited by 655
Activation of rhodopsin: new insights from structural and biochemical studies
Okada, T., Ernst, O. P., Palczewski, K., & Hofmann, K. P. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01799-6 · Cited by 413
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Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., & Gygi, S. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0832254100 · Cited by 1,733
Bruderer, R., Bernhardt, O. M., Gandhi, T., Miladinović, S. M., Cheng, L.-Y., Messner, S., Ehrenberger, T., Zanotelli, V., Butscheid, Y., Escher, C., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.044305 · Cited by 1,238
Addona, T. A., Abbatiello, S. E., Schilling, B., Skates, S. J., Mani, D. R., Bunk, D. M., Spiegelman, C. H., Zimmerman, L. J., Ham, A.-J. L., Keshishian, H., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1546 · Cited by 1,037
Cheng, D., Hoogenraad, C. C., Rush, J., Ramm, E., Schlager, M. A., Duong, D. M., Xu, P., Wijayawardana, S. R., Hanfelt, J., Nakagawa, T., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.d500009-mcp200 · Cited by 510
Peng, J., Kim, M. J., Cheng, D., Duong, D. M., Gygi, S. P., & Sheng, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400103200 · Cited by 473
Vidova, V., & Spacil, Z. (2017) · Analytica Chimica Acta · doi:10.1016/j.aca.2017.01.059 · Cited by 352
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Quantitative Urinary Proteome Analysis for Biomarker Evaluation in Chronic Kidney Disease
Jantos-Siwy, J., Schiffer, E., Brand, K., Schumann, G., Rossing, K., Delles, C., Mischak, H., & Metzger, J. (2009) · Journal of Proteome Research · doi:10.1021/pr800401m · Cited by 259
Barnidge, D. R., Goodmanson, M. K., Klee, G. G., & Muddiman, D. C. (2004) · Journal of Proteome Research · doi:10.1021/pr049963d · Cited by 253
Self-citationAbbatiello, S. E., Schilling, B., Mani, D. R., Zimmerman, L. J., Hall, S. C., MacLean, B., Albertolle, M., Allen, S., Burgess, M., Cusack, M. P., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.047050 · Cited by 215
Mischak, H., Coon, J. J., Novak, J., Weissinger, E. M., Schanstra, J. P., & Dominiczak, A. F. (2009) · Mass Spectrometry Reviews · doi:10.1002/mas.20205 · Cited by 193
Applications of targeted proteomics in systems biology and translational medicine
Ebhardt, H. A., Root, A., Sander, C., & Aebersold, R. (2015) · PROTEOMICS · doi:10.1002/pmic.201500004 · Cited by 184
Towards comprehensive and quantitative proteomics for diagnosis and therapy of human disease
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Metadata
- Authors
- Barnidge, D. R., Dratz, E. A., Martin, T., Bonilla, L. E., Moran, L. B., & Lindall, A.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-01-01
- Volume
- 75
- Issue
- 3
- Pages
- 445-451
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W1973243635
- Cited by
- 227
- References
- 2
- FWCI
- 6.21
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
