The DOI matches its Crossref record; 99 of the 101 references it cites were found in a registry or an index.
Identification of Protein Interactions Involved in Cellular Signaling
Open accessAbstract
Protein-protein interactions drive biological processes. They are critical for all intra- and extracellular functions, and the technologies to analyze them are widely applied throughout the various fields of biological sciences. This study takes an in-depth view of some common principles of cellular regulation and provides a detailed account of approaches required to comprehensively map signaling protein-protein interactions in any particular cellular system or condition. We provide a critical review of the benefits and disadvantages of the yeast two-hybrid method and affinity purification coupled with mass spectrometric procedures for identification of signaling protein-protein interactions. In particular, we emphasize the quantitative and qualitative differences between tandem affinity and one-step purification (such as FLAG and Strep tag) methods. Although applicable to all types of interaction studies, a special section is devoted in this review to aspects that should be considered when attempting to identify signaling protein interactions that often are transient and weak by nature. Finally, we discuss shotgun and quantitative information that can be gleaned by MS-coupled methods for analysis of multiprotein complexes.
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“suggesting that they may be functionally related69–71 or operate together72,73 to mediate phenotypic features associated with UDN-P9’s disease and hypomyelinating leukodystropy-20”
From Few shot learning for phenotype-driven diagnosis of patients with rare genetic diseases (2025) · cites this paper as [72]
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Metadata
- Authors
- Westermarck, J., Ivaska, J., & Corthals, G. L.
- Affiliations
- Åbo Akademi University (FI)
- Corresponding author
- Corthals, Garry L.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 12
- Issue
- 7
- Pages
- 1752-1763
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC3708163
- OpenAlex
- W2147130215
- Cited by
- 143
- References
- 101
- Citations by year
- 2026: 21 · 2025: 19 · 2024: 15 · 2023: 8 · 2022: 13 · 2021: 12 · 2020: 8 · 2019: 12 · 2018: 7 · 2017: 5 · 2016: 7 · 2015: 4 · 2014: 9 · 2013: 1
- FWCI
- 0.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- 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, signal transduction, yeast two-hybrid, affinity purification, tandem affinity purification, FLAG tag, Strep-tag, protein complexes, protein interaction mapping
- MeSH terms
- Humans, Mass Spectrometry, Signal Transduction, Two-Hybrid System Techniques, Protein Interaction Mapping
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