The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Defensins - Components of the Innate Immune System in Plants
Abstract
Plant defensins are small (c.a. 5 kDa), basic, cysteine-rich proteins with antimicrobial activities. They are ubiquitous in plants and form part of the innate immunity arsenal. Plant defensins are encoded by small multigene families and are expressed in various plant tissues, but are best characterized in seeds. They are typically produced as preproteins, however, a small subset are produced as larger precursors with C-terminal prodomains. To date, the three-dimensional solution structures of seven seed- and two floral-derived defensins have been elucidated by (1)H-NMR spectroscopy. Despite limited amino acid sequence identities, these defensins have comparable global folds with features that are characteristic of the cysteine-stabilized alphabeta (CSalphabeta) motif. Interestingly, their structures are remarkably similar to those of insect defensins and scorpion toxins. Functionally, these proteins exhibit a diverse array of biological activities, although they all serve a common function as defenders of their hosts. This review describes the distribution, biosynthesis, structure, function and mode of action of plant defensins and reflects on their potential in agribiotechnological applications.
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Cites
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Thionins: properties, possible biological roles and mechanisms of action
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Molecular cloning and analysis of four potato tuber mRNAs
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Cited by
Significance of Inducible Defense-related Proteins in Infected Plants
van Loon, L. C., Rep, M., & Pieterse, C. M. J. (2006) · Annual Review of Phytopathology · doi:10.1146/annurev.phyto.44.070505.143425 · Cited by 3,410
Plant pathogenesis-related (PR) proteins: A focus on PR peptides
Sels, J., Mathys, J., De Coninck, B. M. A., Cammue, B. P. A., & De Bolle, M. F. C. (2008) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2008.06.011 · Cited by 836
Antimicrobial peptides and plant disease control
Montesinos, E. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00683.x · Cited by 376
Sagaram, U. S., Pandurangi, R., Kaur, J., Smith, T. J., & Shah, D. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018550 · Cited by 185
Antimicrobial peptides: promising compounds against pathogenic microorganisms
Cruz, J., Ortiz, C., Guzmán, F., Fernández-Lafuente, R., & Torres, R. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140217110155 · Cited by 166
Metadata
- Authors
- Lay, F., & Anderson, M.
- Venue
- Current Protein & Peptide Science
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2005-02-01
- Volume
- 6
- Issue
- 1
- Pages
- 85-101
- ISSN
- 1389-2037 (ISSN-L)
- OpenAlex
- W1971644830
- Cited by
- 494
- References
- 15
- FWCI
- 16.29
- Type
- journal article
- Language
- en
- Open access
- closed
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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).
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