The DOI matches its Crossref record.
A Carrot Leucine-Rich-Repeat Protein That Inhibits Ice Recrystallization
Abstract
Many organisms adapted to live at subzero temperatures express antifreeze proteins that improve their tolerance to freezing. Although structurally diverse, all antifreeze proteins interact with ice surfaces, depress the freezing temperature of aqueous solutions, and inhibit ice crystal growth. A protein purified from carrot shares these functional features with antifreeze proteins of fish. Expression of the carrot complementary DNA in tobacco resulted in the accumulation of antifreeze activity in the apoplast of plants grown at greenhouse temperatures. The sequence of carrot antifreeze protein is similar to that of polygalacturonase inhibitor proteins and contains leucine-rich repeats.
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Citations
Cited by
Ice-Binding Proteins and Their Function
Bar Dolev, M., Braslavsky, I., & Davies, P. L. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014546 · Cited by 426
Re-Evaluation of a Bacterial Antifreeze Protein as an Adhesin with Ice-Binding Activity
Guo, S., Garnham, C. P., Whitney, J. C., Graham, L. A., & Davies, P. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048805 · Cited by 67
Metadata
- Authors
- Worrall, D., Elias, L., Ashford, D., Smallwood, M., Sidebottom, C., Lillford, P., Telford, J., Holt, C., & Bowles, D.
- Venue
- Science
- Published
- 1998-10-02
- Volume
- 282
- Issue
- 5386
- Pages
- 115-117
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2044917527
- Cited by
- 271
- References
- 0
- FWCI
- 21.16
- 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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
