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Cited by 547

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

MODULAR PEPTIDE RECOGNITION DOMAINS IN EUKARYOTIC SIGNALING

Kuriyan, John, Cowburn, David·1997·Annual Review of Biophysics and Biomolecular Structure

Abstract

A characteristic feature of cellular signal transduction pathways in eukaryotes is the separation of catalysis from target recognition. Several modular domains that recognize short peptide sequences and target signaling proteins to these sequences have been identified. The structural bases of the specificities of recognition by SH2, SH3, and PTB domains have been elucidated by X-ray crystallography and NMR, and these results are reviewed here. In addition, the mechanism of cooperative interactions between these domains is discussed.

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Crossref · 10.1146/annurev.biophys.26.1.259

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Metadata

Authors
Kuriyan, J., & Cowburn, D.
Venue
Annual Review of Biophysics and Biomolecular Structure
Published
1997-06
Volume
26
Issue
1
Pages
259-288
ISSN
  • 1056-8700 (ISSN-L)
  • 1545-4266
OpenAlex
W2107532817
Cited by
547
References
2
FWCI
11.70
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: MODULAR PEPTIDE RECOGNITION DOMAINS IN EUKARYOTIC SIGNALING. https://app.cochat.ai/papers/10.1146/annurev.biophys.26.1.259
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Kuriyan, J., & Cowburn, D. (1997). MODULAR PEPTIDE RECOGNITION DOMAINS IN EUKARYOTIC SIGNALING. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.26.1.259

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.