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Updated: Aug 17, 2026

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
Published on: July 27, 2017
Lessons from nature: On the molecular recognition elements of the phosphoprotein binding-domains
A Cecília A Roque1, Christopher R Lowe
1Institute of Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, United Kingdom. car38@cam.ac.uk
Abstract:
The reversible phosphorylation of proteins regulates many biological processes. Despite the technological advances in the enrichment and detection of phosphorylated proteins, the currently available techniques still struggle with the complexity of the human proteome. The aim of this review is to highlight the molecular recognition elements of the interaction between phosphorylated proteins and peptides and pTyr or pSer/Thr-binding domains. The identification of the recognition features of the naturally occurring pTyr- and pSer/Thr-binding domains can contribute to an understanding of the molecular aspects of the affinity and specificity for phosphorylated residues. This might inspire the design of small "biomimetic" molecules with potential applications in assessing the extent of the phosphoproteome using affinity-based strategies.
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