ArticleCell communication and signaling : CCS2015
High-throughput methods for identification of protein-protein interactions involving short linear motifs.
Article in Cell communication and signaling : CCS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Preparation of μSPOT Lactam-Cyclized Peptides for Ligand Optimization.Methods in molecular biology (Clifton, N.J.) · 2025Article
- FaSTPACE: a fast and scalable tool for peptide alignment and consensus extraction.NAR genomics and bioinformatics · 2024Article
- Proteome-wide assessment of human interactome as a source of capturing domain-motif and domain-domain interactions.Journal of cell communication and signaling · 2024Article
- Prediction of motif-mediated viral mimicry through the integration of host-pathogen interactions.Archives of microbiology · 2024Article
- Discovery and Characterization of Linear Motif Mediated Protein-Protein Complexes.Advances in experimental medicine and biology · 2024Article
- Exploiting the endogenous yeast nuclear proteome to identify short linear motifs in vivo.Cell reports methods · 2023Article
- How different viruses perturb host cellular machinery via short linear motifs.EXCLI journal · 2023Review
- Protein-protein interactions in plant antioxidant defense.Frontiers in plant science · 2022Review
- Protein-protein interactions: Methods, databases, and applications in virus-host study.World journal of virology · 2021Review
- MRBLE-pep Measurements Reveal Accurate Binding Affinities for B56, a PP2A Regulatory Subunit.ACS measurement science au · 2021Article
- Critical assessment of protein intrinsic disorder prediction.Nature methods · 2021Article
- Peptide-based Interaction Proteomics.Molecular & cellular proteomics : MCP · 2020Review
- Screening Intrinsically Disordered Regions for Short Linear Binding Motifs.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Resources to Discover and Use Short Linear Motifs in Viral Proteins.Trends in biotechnology · 2020Review
- Quantitative mapping of protein-peptide affinity landscapes using spectrally encoded beads.eLife · 2019Article
- Improved methods for the detection of histone interactions with peptide microarrays.Scientific reports · 2019Article
- An intrinsically disordered proteins community for ELIXIR.F1000Research · 2019Article
- Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway.PLoS computational biology · 2017Article
- SLiMSearch: a framework for proteome-wide discovery and annotation of functional modules in intrinsically disordered regions.Nucleic acids research · 2017Article
- Assembly and use of high-density recombinant peptide chips for large-scale ligand screening is a practical alternative to synthetic peptide libraries.BMC genomics · 2017Article
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2 authors.
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Abstract
Interactions between modular domains and short linear motifs (3-10 amino acids peptide stretches) are crucial for cell signaling. The motifs typically reside in the disordered regions of the proteome and the interactions are often transient, allowing for rapid changes in response to changing stimuli. The properties that make domain-motif interactions suitable for cell signaling also make them difficult to capture experimentally and they are therefore largely underrepresented in the known protein-protein interaction networks. Most of the knowledge on domain-motif interactions is derived from low-throughput studies, although there exist dedicated high-throughput methods for the identification of domain-motif interactions. The methods include arrays of peptides or proteins, display of peptides on phage or yeast, and yeast-two-hybrid experiments. We here provide a survey of scalable methods for domain-motif interaction profiling. These methods have frequently been applied to a limited number of ubiquitous domain families. It is now time to apply them to a broader set of peptide binding proteins, to provide a comprehensive picture of the linear motifs in the human proteome and to link them to their potential binding partners. Despite the plethora of methods, it is still a challenge for most approaches to identify interactions that rely on post-translational modification or context dependent or conditional interactions, suggesting directions for further method development.
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