The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Biomarker discovery by CE‐MS enables sequence analysis via MS/MS with platform‐independent separation
Abstract
CE‐MS is a successful proteomic platform for the definition of biomarkers in different body fluids. Besides the biomarker defining experimental parameters, CE migration time and molecular weight, especially biomarker's sequence identity is an indispensable cornerstone for deeper insights into the pathophysiological pathways of diseases or for made‐to‐measure therapeutic drug design. Therefore, this report presents a detailed discussion of different peptide sequencing platforms consisting of high performance separation method either coupled on‐line or off‐line to different MS/MS devices, such as MALDI‐TOF‐TOF, ESI‐IT, ESI‐QTOF and Fourier transform ion cyclotron resonance, for sequencing indicative peptides. This comparison demonstrates the unique feature of CE‐MS technology to serve as a reliable basis for the assignment of peptide sequence data obtained using different separation MS/MS methods to the biomarker defining parameters, CE migration time and molecular weight. Discovery of potential biomarkers by CE‐MS enables sequence analysis via MS/MS with platform‐independent sample separation. This is due to the fact that the number of basic and neutral polar amino acids of biomarkers sequences distinctly correlates with their CE‐MS migration time/molecular weight coordinates. This uniqueness facilitates the independent entry of different sequencing platforms for peptide sequencing of CE‐MS‐defined biomarkers from highly complex mixtures.
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Cites
Thongboonkerd, V., Mcleish, K. R., Arthur, J. M., & Klein, J. B. (2002) · Kidney International · doi:10.1111/j.1523-1755.2002.kid565.x · Cited by 359
Cited by
Decramer, S., de Peredo, A. G., Breuil, B., Mischak, H., Monsarrat, B., Bascands, J.-L., & Schanstra, J. P. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r800001-mcp200 · Cited by 450
Self-citationClinical proteomics: A need to define the field and to begin to set adequate standards
Mischak, H., Apweiler, R., Banks, R. E., Conaway, M., Coon, J., Dominiczak, A., Ehrich, J. H. H., Fliser, D., Girolami, M., Hermjakob, H., et al. (2007) · PROTEOMICS – Clinical Applications · doi:10.1002/prca.200600771 · Cited by 307
Self-citationAdvances in Urinary Proteome Analysis and Biomarker Discovery
Fliser, D., Novak, J., Thongboonkerd, V., Argile[Combining Acute Accent]s, A. G. A., Jankowski, V., Girolami, M. A., Jankowski, J., & Mischak, H. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006090956 · Cited by 286
Self-citationMischak, 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
Self-citationCapillary electrophoresis–mass spectrometry for the analysis of intact proteins
Haselberg, R., de Jong, G. J., & Somsen, G. W. (2007) · Journal of Chromatography A · doi:10.1016/j.chroma.2007.05.048 · Cited by 185
Metadata
- Authors
- Zürbig, P., Renfrow, M. B., Schiffer, E., Novak, J., Walden, M., Wittke, S., Just, I., Pelzing, M., Neusüß, C., Theodorescu, D., Root, K. E., Ross, M. M., & Mischak, H.
- Venue
- ELECTROPHORESIS
- Publisher
- Wiley
- Published
- 2006-05-30
- Volume
- 27
- Issue
- 11
- Pages
- 2111-2125
- ISSN
- 0173-0835 (ISSN-L)
- 1522-2683
- OpenAlex
- W1970252549
- Cited by
- 193
- References
- 1
- FWCI
- 8.88
- Type
- journal article
- Language
- en
- Open access
- closed
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- Zürbig, P., Renfrow, M. B., Schiffer, E., Novak, J., Walden, M., Wittke, S., Just, I., Pelzing, M., Neusüß, C., Theodorescu, D., Root, K. E., Ross, M. M., & Mischak, H. (2006). Biomarker discovery by CE‐MS enables sequence analysis via MS/MS with platform‐independent separation. ELECTROPHORESIS. https://doi.org/10.1002/elps.200500827
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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