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https://hdl.handle.net/2440/90997
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dc.contributor.author | Arentz, G. | - |
dc.contributor.author | Weiland, F. | - |
dc.contributor.author | Oehler, M. | - |
dc.contributor.author | Hoffmann, P. | - |
dc.date.issued | 2015 | - |
dc.identifier.citation | Proteomics: Clinical Applications, 2015; 9(3-4):277-288 | - |
dc.identifier.issn | 1862-8346 | - |
dc.identifier.issn | 1862-8354 | - |
dc.identifier.uri | http://hdl.handle.net/2440/90997 | - |
dc.description.abstract | Difference gel electrophoresis enables the accurate quantification of changes in the proteome including combinations of PTMs and protein isoform expression. Here, we review recent advances in study design, image acquisition, and statistical analysis. We also compare DIGE to established and emerging mass spectrometric analysis technologies. Despite these recent advances in MS and the still unsolved limitations of 2DE to map hydrophobic, high molecular weight proteins with extreme pIs, DIGE remains the most comprehensive top-down method to study changes in abundance of intact proteins. | - |
dc.description.statementofresponsibility | Georgia Arentz, Florian Weiland, Martin K. Oehler, and Peter Hoffmann | - |
dc.language.iso | en | - |
dc.publisher | Wiley-VCH Verlag | - |
dc.rights | © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim | - |
dc.source.uri | http://dx.doi.org/10.1002/prca.201400119 | - |
dc.subject | 2DE | - |
dc.subject | DIGE | - |
dc.subject | Gel electrophoresis | - |
dc.subject | MS | - |
dc.title | State of the art of 2D DIGE | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1002/prca.201400119 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Weiland, F. [0000-0001-9702-9245] | - |
dc.identifier.orcid | Oehler, M. [0000-0002-2651-5913] | - |
Appears in Collections: | Aurora harvest 2 Molecular and Biomedical Science publications |
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