ArticleElectrophoresis2006
Using size exclusion chromatography-RPLC and RPLC-CIEF as two-dimensional separation strategies for protein profiling.
Article in Electrophoresis, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 58 citations in OpenAlex.
- Characterizing age-related changes in intact mitochondrial proteoforms in murine hearts using quantitative top-down proteomics.Clinical proteomics · 2024Article
- Multidimensional Separations in Top-Down Proteomics.Analytical science advances · 2023Article
- TopPICR: A Companion R Package for Top-Down Proteomics Data Analysis.Journal of proteome research · 2023Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- A Top-Down Proteomics Platform Coupling Serial Size Exclusion Chromatography and Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.Analytical chemistry · 2019Article
- Two-Dimensional Separation Using High-pH and Low-pH Reversed Phase Liquid Chromatography for Top-down Proteomics.International journal of mass spectrometry · 2018Article
- Top-Down Proteomics of Large Proteins up to 223 kDa Enabled by Serial Size Exclusion Chromatography Strategy.Analytical chemistry · 2017Article
- Complete Characterization of Cardiac Myosin Heavy Chain (223 kDa) Enabled by Size-Exclusion Chromatography and Middle-Down Mass Spectrometry.Analytical chemistry · 2017Article
- It is time for top-down venomics.The journal of venomous animals and toxins including tropical diseases · 2017Review
- Progress in Top-Down Proteomics and the Analysis of Proteoforms.Annual review of analytical chemistry (Palo Alto, Calif.) · 2016Review
- Three dimensional liquid chromatography coupling ion exchange chromatography/hydrophobic interaction chromatography/reverse phase chromatography for effective protein separation in top-down proteomics.Analytical chemistry · 2015Article
- Effective protein separation by coupling hydrophobic interaction and reverse phase chromatography for top-down proteomics.Analytical chemistry · 2014Article
- Review
- Robust two-dimensional separation of intact proteins for bottom-up tandem mass spectrometry of the human CSF proteome.Journal of proteome research · 2012Article
- Comprehensive analysis of protein modifications by top-down mass spectrometry.Circulation. Cardiovascular genetics · 2011Review
- Size-sorting combined with improved nanocapillary liquid chromatography-mass spectrometry for identification of intact proteins up to 80 kDa.Analytical chemistry · 2010Article
- Sensitive and specific identification of wild type and variant proteins from 8 to 669 kDa using top-down mass spectrometry.Molecular & cellular proteomics : MCP · 2009Article
- Capillary electrophoresis applied to proteomic analysis.Journal of separation science · 2009Article
- An integrated top-down and bottom-up strategy for broadly characterizing protein isoforms and modifications.Journal of proteome research · 2009Article
- Fast, comprehensive two-dimensional liquid chromatography.Journal of chromatography. A · 2007Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Bottom-up proteomics (analyzing peptides that result from protein digestion) has demonstrated capability for broad proteome coverage and good throughput. However, due to incomplete sequence coverage, this approach is not ideally suited to the study of modified proteins. The modification complement of a protein can best be elucidated by analyzing the intact protein. 2-DE, typically coupled with the analysis of peptides that result from in-gel digestion, is the most frequently applied protein separation technique in MS-based proteomics. As an alternative, numerous column-based liquid phase techniques, which are generally more amenable to automation, are being investigated. In this work, the combination of size-exclusion chromatography (SEC) fractionation with RPLC-Fourier-transform ion cyclotron resonance (FTICR)-MS is compared with the combination of RPLC fractionation with CIEF-FTICR-MS for the analysis of the Shewanella oneidensis proteome. SEC-RPLC-FTICR-MS allowed the detection of 297 proteins, as opposed to 166 using RPLC-CIEF-FTICR-MS, indicating that approaches based on LC-MS provide better coverage. However, there were significant differences in the sets of proteins detected and both approaches provide a basis for accurately quantifying changes in protein and modified protein abundances.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.