Literature DB >> 23500044

Computer aided manual validation of mass spectrometry-based proteomic data.

Timothy G Curran1, Bryan D Bryson, Michael Reigelhaupt, Hannah Johnson, Forest M White.   

Abstract

Advances in mass spectrometry-based proteomic technologies have increased the speed of analysis and the depth provided by a single analysis. Computational tools to evaluate the accuracy of peptide identifications from these high-throughput analyses have not kept pace with technological advances; currently the most common quality evaluation methods are based on statistical analysis of the likelihood of false positive identifications in large-scale data sets. While helpful, these calculations do not consider the accuracy of each identification, thus creating a precarious situation for biologists relying on the data to inform experimental design. Manual validation is the gold standard approach to confirm accuracy of database identifications, but is extremely time-intensive. To palliate the increasing time required to manually validate large proteomic datasets, we provide computer aided manual validation software (CAMV) to expedite the process. Relevant spectra are collected, catalogued, and pre-labeled, allowing users to efficiently judge the quality of each identification and summarize applicable quantitative information. CAMV significantly reduces the burden associated with manual validation and will hopefully encourage broader adoption of manual validation in mass spectrometry-based proteomics.
Copyright © 2013 Elsevier Inc. All rights reserved.

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Year:  2013        PMID: 23500044      PMCID: PMC3700613          DOI: 10.1016/j.ymeth.2013.03.004

Source DB:  PubMed          Journal:  Methods        ISSN: 1046-2023            Impact factor:   3.608


  14 in total

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Review 4.  Assigning significance to peptides identified by tandem mass spectrometry using decoy databases.

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Authors:  David M A Martin; Isabelle R E Nett; Franck Vandermoere; Jonathan D Barber; Nicholas A Morrice; Michael A J Ferguson
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Review 3.  System level dynamics of post-translational modifications.

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Journal:  Curr Opin Biotechnol       Date:  2014-01-15       Impact factor: 9.740

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Review 7.  Mass spectrometry-based methods for identifying oxidized proteins in disease: advances and challenges.

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9.  MARQUIS: a multiplex method for absolute quantification of peptides and posttranslational modifications.

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