ArticleThe Analyst2002
Reconstructed protein arrays from 3D HPLC/tandem mass spectrometry and 2D gels: complementary approaches to Porphyromonas gingivalis protein expression.
Article in The Analyst, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Quantitative proteomics of intracellular Porphyromonas gingivalis.Proteomics · 2007Article
- Differential quantitative proteomics of Porphyromonas gingivalis by linear ion trap mass spectrometry: non-label methods comparison, q-values and LOWESS curve fitting.International journal of mass spectrometry · 2007Article
- Mass spectrometry-based proteomics and its application to studies of Porphyromonas gingivalis invasion and pathogenicity.Infectious disorders drug targets · 2006Review
- Regulation of nitrogenase by 2-oxoglutarate-reversible, direct binding of a PII-like nitrogen sensor protein to dinitrogenase.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Quantitative proteomics of the archaeon Methanococcus maripaludis validated by microarray analysis and real time PCR.Molecular & cellular proteomics : MCP · 2006Article
- Short fimbriae of Porphyromonas gingivalis and their role in coadhesion with Streptococcus gordonii.Infection and immunity · 2005Article
- Differential protein expression by Porphyromonas gingivalis in response to secreted epithelial cell components.Proteomics · 2005Article
- Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.Journal of bacteriology · 2004Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
We compare typical qualitative protein identification data from two-dimensional (2D) polyacrylamide gel electrophoresis and reconstructed protein arrays, in the context of measuring protein expression by the Gram-negative periodontal pathogen Porphyromonas gingivalis. The arrays were assembled computationally from genome annotations and tandem mass spectrometry data from an off-line HPLC fractionation combined with 2D capillary HPLC analysis of whole proteome enzymatic digests. The 2D separation was carried out with a standard binary gradient HPLC system, modified only slightly with readily available components. Compared to 2D gels, the number of annotated open reading frames identified using the 3D HPLC approach was typically larger by at least a factor of 30. However, the newer technology is currently limited in its ability to reflect the many protein variants derived from posttranscriptional and posttranslational processing.
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