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- aggregation classification "A1".
- aggregation creator B605516.
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- aggregation date "2013".
- aggregation format "application/pdf".
- aggregation hasFormat 3209094.bibtex.
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- aggregation isPartOf urn:issn:1535-9476.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Deep proteome coverage based on ribosome profiling aids mass spectrometry-based protein and peptide discovery and provides evidence of alternative translation products and near-cognate translation initiation events".
- aggregation abstract "An increasing number of studies involve integrative analysis of gene and protein expression data, taking advantage of new technologies such as next-generation transcriptome sequencing (RNA-Seq) and highly sensitive mass spectrometry (MS) instrumentation. Recently, a strategy, termed ribosome profiling (or RIBO-seq), based on deep sequencing of ribosome-protected mRNA fragments, indirectly monitoring protein synthesis, has been described. We devised a proteogenomic approach constructing a custom protein sequence search space, built from both SwissProt and RIBO-seq derived translation products, applicable for MS/MS spectrum identification. To record the impact of using the constructed deep proteome database we performed two alternative MS-based proteomic strategies: (I) a regular shotgun proteomic and (II) an N-terminal COFRADIC approach. While the former technique gives an overall assessment on the protein and peptide level, the latter technique, specifically enabling the isolation of N-terminal peptides, is very appropriate in validating the RIBO-seq derived (alternative) translation initiation site profile. We demonstrate that this proteogenomic approach increases the overall protein identification rate with 2.5% (e.g. new protein products, new protein splice variants, SNP variant proteins, and N-terminally extended forms of known proteins) as compared to only searching UniProtKB-SwissProt. Furthermore, using this custom database, identification of N-terminal COFRADIC data resulted in detection of 16 alternative start sites giving rise to N-terminally extended protein variants besides the identification of four translated uORFs. Notably, the characterization of these new translation products revealed the use of multiple near-cognate (non-AUG) start codons. As deep sequencing techniques are becoming more standard, less expensive, and widespread, we anticipate that mRNA-seq and especially custom-tailored RIBO-seq will become indispensible in the MS-based protein or peptide identification process.".
- aggregation authorList BK961447.
- aggregation endPage "1790".
- aggregation issue "7".
- aggregation startPage "1780".
- aggregation volume "12".
- aggregation aggregates 3209099.
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- aggregation similarTo mcp.M113.027540.
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