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Cited by 285

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

The Cystine-Knot Growth-Factor Superfamily

Open access
Sun, P D, Davies, D R·1995·Annual Review of Biophysics and Biomolecular Structure

Abstract

Four recent crystal structures of growth factors--nerve growth factor, transforming growth factor-beta, platelet-derived growth factor, and human chorionic gonadotropin--from four separate superfamilies revealed that these proteins are structurally related and share a common overall topology. These proteins have very little sequence homology, but they all have an unusual arrangement of six cysteines linked to form a "cystine-knot" conformation. The active forms of these proteins are dimers, either homo- or heterodimers. Despite the overall topological similarity between the monomers, the interfaces used to form the dimer are in each case quite different. Because the surfaces used for dimer formation are mostly hydrophobic, the uniqueness of each dimer accounts for the lack of sequence homology and raises questions about the effectiveness of reverse sequence fitting in this kind of structure as a predictor of structural homology.

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Crossref · 10.1146/annurev.bb.24.060195.001413

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Metadata

Authors
Sun, P. D., & Davies, D. R.
Venue
Annual Review of Biophysics and Biomolecular Structure
Published
1995-06
Volume
24
Issue
1
Pages
269-292
ISSN
  • 1056-8700 (ISSN-L)
  • 1545-4266
OpenAlex
W2176052107
Cited by
285
References
34
FWCI
3.91
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The Cystine-Knot Growth-Factor Superfamily. https://app.cochat.ai/papers/10.1146/annurev.bb.24.060195.001413
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Sun, P. D., & Davies, D. R. (1995). The Cystine-Knot Growth-Factor Superfamily. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.bb.24.060195.001413

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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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