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Cited by 609

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Structural Basis for FGF Receptor Dimerization and Activation

Open access
Plotnikov, Alexander N, Schlessinger, Joseph, Hubbard, Stevan R, Mohammadi, Moosa·1999·Cell

Abstract

The crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3 as well as with the linker between the two domains. The dimer is stabilized by interactions between FGF2 and D2 of the adjoining complex and by a direct interaction between D2 of each receptor. A positively charged canyon formed by a cluster of exposed basic residues likely represents the heparin-binding site. A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data.

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Crossref · 10.1016/s0092-8674(00)80051-3

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Metadata

Authors
Plotnikov, A. N., Schlessinger, J., Hubbard, S. R., & Mohammadi, M.
Venue
Cell
Publisher
Elsevier BV
Published
1999-09
Volume
98
Issue
5
Pages
641-650
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2169147580
Cited by
609
References
3
FWCI
16.53
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structural Basis for FGF Receptor Dimerization and Activation. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80051-3
The paper
Plotnikov, A. N., Schlessinger, J., Hubbard, S. R., & Mohammadi, M. (1999). Structural Basis for FGF Receptor Dimerization and Activation. Cell. https://doi.org/10.1016/s0092-8674(00)80051-3

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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.