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Cited by 291

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

PLECKSTRIN HOMOLOGY DOMAINS: A Common Fold with Diverse Functions

Rebecchi, M. J., Scarlata, S.·1998·Annual Review of Biophysics and Biomolecular Structure

Abstract

Pleckstrin homology (PH) motifs are approximately 100 amino-acid residues long and have been identified in nearly 100 different eukaryotic proteins, many of which participate in cell signaling and cytoskeletal regulation. Despite minimal sequence homology, the three-dimensional structures are remarkably conserved. This review gives an overview of the PH domain architecture and examines the best-studied examples in an attempt to understand their function.

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Crossref · 10.1146/annurev.biophys.27.1.503

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Metadata

Authors
Rebecchi, M. J., & Scarlata, S.
Venue
Annual Review of Biophysics and Biomolecular Structure
Published
1998-06
Volume
27
Issue
1
Pages
503-528
ISSN
  • 1056-8700 (ISSN-L)
  • 1545-4266
OpenAlex
W2102436071
Cited by
291
References
2
FWCI
9.57
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: PLECKSTRIN HOMOLOGY DOMAINS: A Common Fold with Diverse Functions. https://app.cochat.ai/papers/10.1146/annurev.biophys.27.1.503
The paper
Rebecchi, M. J., & Scarlata, S. (1998). PLECKSTRIN HOMOLOGY DOMAINS: A Common Fold with Diverse Functions. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.27.1.503

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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.