ArticleJournal of proteome research2009
High-throughput liquid-liquid fractionation of multiple protein post-translational modifications.
Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Transition from identity to bioactivity-guided proteomics for biomarker discovery with focus on the PF2D platform.Proteomics. Clinical applications · 2016Review
- Serum proteomic signature of human chagasic patients for the identification of novel potential protein biomarkers of disease.Molecular & cellular proteomics : MCP · 2012Article
- An economical high-throughput protocol for multidimensional fractionation of proteins.International journal of proteomics · 2012Article
- The utilization of Triton X-100 for enhanced two-dimensional liquid-phase proteomics.Journal of biomedicine & biotechnology · 2011Article
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Authors and funding
6 authors.
Funding
Abstract
Post-translational protein modifications have contributed significantly to the identification of macromolecular biomarkers of biological processes. We have modified a two-dimensional HPLC system (Beckman Coulter PF2D ProteomeLab) to create proteome maps of post-translational protein modifications. This system resolves complex protein mixtures by anion exchange chromatofocusing in the first dimension and hydrophobicity (reverse phase chromatography) in the second dimension. The simultaneous identification of multiple protein modifications, accomplished by incorporating a photo diode array (PDA) detector into the PF2D system, facilitates the simultaneous production of three-dimensional proteome maps and visualization of both unmodified and post-translationally modified (PTM) proteins at their signature wavelengths within the proteome. We describe procedures for the simultaneous resolution of proteome maps, the identification of proteins modified by nitration, carbonylation, and phosphorylation, and proteins with unique spectra such as the heme containing proteins.
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