Systematic identification of SH3 domain‐mediated human protein–protein interactions by peptide array target screening

@article{Wu2007SystematicIO,
  title={Systematic identification of SH3 domain‐mediated human protein–protein interactions by peptide array target screening},
  author={Chenggang Wu and Mike Haiting Ma and Kevin R. Brown and Matt Geisler and Lei Li and Eve Tzeng and Christina Y. H. Jia and Igor Jurisica and Shawn S.-C. Li},
  journal={PROTEOMICS},
  year={2007},
  volume={7},
  url={https://api.semanticscholar.org/CorpusID:22474278}
}
Compared to protein interactions listed in the online predicted human interaction protein database (OPHID), the majority of interactions identified by PATS are novel, suggesting that, when extended to the large number of peptide interaction domains encoded by the human genome, PATS should aid in the mapping of the human interactome.
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88 Citations
Highly Influential Citations
2
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30
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88 Citations

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The application of oriented peptide array libraries in uncovering specific motifs recognized by an SH2 domain and the use of high-density peptide arrays in identifying interaction networks mediated by the SH3 domain are described.

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The development of a peptide array-based proteomics tool to identify proteins directly interacting with ligand peptides from cell lysates and the results suggest the capacity of arrayed peptide ligands to capture and subsequently identify proteins by mass spectrometry is relatively broad and robust.

The protein interaction network mediated by human SH3 domains.

Large-Scale Screening of Preferred Interactions of Human Src Homology-3 (SH3) Domains Using Native Target Proteins as Affinity Ligands*

The panel of exceptionally robust SH3 interactions identified here provides a rich source of leads and hypotheses for further studies, and indicates that a truly comprehensive characterization of the human SH3 interactome will require novel high-throughput methods based on function instead of absolute binding affinity.

Computational Prediction of PDZ Mediated Protein-protein Interactions

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Prediction of phosphotyrosine signaling networks using a scoring matrix-assisted ligand identification approach

Applying SMALI to a group of SH2 domains identified hundreds of interactions that overlap significantly with known networks mediated by the corresponding SH2 proteins, suggesting SMALi is a useful tool for facile identification of signaling networks mediatedBy modular domains that recognize short linear peptide motifs.

Studying protein-protein interactions using peptide arrays.

The applications, advantages and disadvantages of using peptide arrays as a tool to study protein-protein interactions are discussed and the recent work on this subject is introduced.

The human interaction network mediated by Src Homology-3 domains: enriching the viral-host interactomes with interactions mediated by Src Homology-3 domains

The WISE (Whole Interactome Scanning Experiment) approach was applied to identify interactions between 15 human SH3 domains and viral proline-rich peptides of two oncogenic viruses, HPV (Human papillomavirus type 16) and Ad12 (Human adenovirus A type 12).
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58 References

Identification of preferred protein interactions by phage‐display of the human Src homology‐3 proteome

It is argued that SH3 domains may have a more dominant role in directing cellular protein interactions than has been assumed and led to the discovery of novel signalling proteins, such as the PAK2‐binding adaptor protein POSH2 and the ADAM15‐binding sorting nexin family member SNX30.

Novel Src Homology 3 Domain-binding Motifs Identified from Proteomic Screen of a Pro-rich Region *S

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