ArticleJournal of proteome research2011
UNiquant, a program for quantitative proteomics analysis using stable isotope labeling.
Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- A peptide-based method for 13C Metabolic Flux Analysis in microbial communities.PLoS computational biology · 2014Article
- Functional proteomic analysis reveals the involvement of KIAA1199 in breast cancer growth, motility and invasiveness.BMC cancer · 2014Article
- SILAC peptide ratio calculator: a tool for SILAC quantitation of peptides and post-translational modifications.Journal of proteome research · 2014Article
- ISPTM: an iterative search algorithm for systematic identification of post-translational modifications from complex proteome mixtures.Journal of proteome research · 2013Article
- Quantitative analysis of global phosphorylation changes with high-resolution tandem mass spectrometry and stable isotopic labeling.Methods (San Diego, Calif.) · 2013Review
- Quantitative proteomics reveals that miR-155 regulates the PI3K-AKT pathway in diffuse large B-cell lymphoma.The American journal of pathology · 2012Article
- IsoQuant: a software tool for stable isotope labeling by amino acids in cell culture-based mass spectrometry quantitation.Analytical chemistry · 2012Article
- Proteomic analysis of the organ of corti using nanoscale liquid chromatography coupled with tandem mass spectrometry.International journal of molecular sciences · 2012Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Stable isotope labeling (SIL) methods coupled with nanoscale liquid chromatography and high resolution tandem mass spectrometry are increasingly useful for elucidation of the proteome-wide differences between multiple biological samples. Development of more effective programs for the sensitive identification of peptide pairs and accurate measurement of the relative peptide/protein abundance are essential for quantitative proteomic analysis. We developed and evaluated the performance of a new program, termed UNiquant, for analyzing quantitative proteomics data using stable isotope labeling. UNiquant was compared with two other programs, MaxQuant and Mascot Distiller, using SILAC-labeled complex proteome mixtures having either known or unknown heavy/light ratios. For the SILAC-labeled Jeko-1 cell proteome digests with known heavy/light ratios (H/L = 1:1, 1:5, and 1:10), UNiquant quantified a similar number of peptide pairs as MaxQuant for the H/L = 1:1 and 1:5 mixtures. In addition, UNiquant quantified significantly more peptides than MaxQuant and Mascot Distiller in the H/L = 1:10 mixtures. UNiquant accurately measured relative peptide/protein abundance without the need for postmeasurement normalization of peptide ratios, which is required by the other programs.
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