Beyond hairballs: The use of quantitative mass spectrometry data to understand protein–protein interactions
Open accessAbstract
The past 10 years have witnessed a dramatic proliferation in the availability of protein interaction data. However, for interaction mapping based on affinity purification coupled with mass spectrometry (AP‐MS), there is a wealth of information present in the datasets that often goes unrecorded in public repositories, and as such remains largely unexplored. Further, how this type of data is represented and used by bioinformaticians has not been well established. Here, we point out some common mistakes in how AP‐MS data are handled, and describe how protein complex organization and interaction dynamics can be inferred using quantitative AP‐MS approaches.
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Affinity-purification mass spectrometry (AP-MS) of serine/threonine phosphatases
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“can help to maintain interactors that would otherwise be lost [48,89].”
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PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4
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Self-citationFunctional protein microarray technology
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Ceccarelli, D. F. J., Laister, R. C., Mulligan, V. K., Kean, M. J., Goudreault, M., Scott, I. C., Derry, W. B., Chakrabartty, A., Gingras, A., & Sicheri, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213777 · Cited by 74 · see citing works
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Defining the budding yeast chromatin‐associated interactome
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Modeling Contaminants in AP-MS/MS Experiments
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The full-ORF clone resource of the German cDNA Consortium
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A Biomedically Enriched Collection of 7000 Human ORF Clones
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Mapping physical interactions within chromatin by proteomic approaches
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Self-citationProfiling Protein Interaction Networks with Functional Protein Microarrays
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Flagged first, then by citations
Cited by
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Protein Analysis by Shotgun/Bottom-up Proteomics
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- Authors
- Gingras, A.-C., & Raught, B.
- Affiliations
- Mount Sinai Hospital (CA)
- University of Toronto (CA)
- Corresponding author
- Gingras, Anne-Claude
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2012-04-10
- Volume
- 586
- Issue
- 17
- Pages
- 2723-2731
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- PMC
- PMC3669394
- OpenAlex
- W2064661383
- Cited by
- 34
- References
- 117
- Citations by year
- 2023: 1 · 2022: 2 · 2021: 9 · 2020: 3 · 2018: 2 · 2017: 1 · 2016: 2 · 2015: 5 · 2014: 3 · 2013: 5 · 2012: 1
- FWCI
- 0.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- CIHR (MOP-84314, MOP-81268, MOP-119289)
- NIH (R01RR024031)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- protein-protein interaction, affinity purification mass spectrometry, quantitative mass spectrometry, protein complex organization, interaction dynamics, interaction mapping, data curation
- MeSH terms
- Animals, Cell Line, Humans, Models, Biological, Peptides, Proteins, Software, Mass Spectrometry, Open Reading Frames, DNA, Complementary, Computational Biology, Protein Interaction Mapping, Databases, Protein, Proteomics
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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