The DOI matches its Crossref record; 86 of the 86 references it cites were found in a registry or an index.
SH3 domains: complexity in moderation
Abstract
The SH3 domain is perhaps the best-characterized member of the growing family of protein-interaction modules. By binding with moderate affinity and selectivity to proline-rich ligands, these domains play critical roles in a wide variety of biological processes ranging from regulation of enzymes by intramolecular interactions, increasing the local concentration or altering the subcellular localization of components of signaling pathways, and mediating the assembly of large multiprotein complexes. SH3 domains and their binding sites have cropped up in many hundreds of proteins in species from yeast to man, which suggests that they provide the cell with an especially handy and adaptable means of bringing proteins together. The wealth of genetic, biochemical and structural information available provides an intimate and detailed portrait of the domain, serving as a framework for understanding other modular protein-interaction domains. Processes regulated by SH3 domains also raise important questions about the nature of specificity and the overall logic governing networks of protein interactions.
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Cited by
Structure and regulation of Src family kinases
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Linear motifs: Evolutionary interaction switches
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RIM Binding Proteins (RBPs) Couple Rab3-Interacting Molecules (RIMs) to Voltage-Gated Ca2+ Channels
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Metadata
- Authors
- Mayer, B. J.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2001-04-01
- Volume
- 114
- Issue
- 7
- Pages
- 1253-1263
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1892578325
- Cited by
- 788
- References
- 86
- FWCI
- 16.18
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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