The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Dehydrins: A commonalty in the response of plants to dehydration and low temperature
Abstract
Among proteins that accumulate in plants in response to dehydrative forces or low temperature, dehydrins (late embryogenesis abundant [Lea] D11 family) have been the most commonly observed. Dehydrins are composed of several typical domains joined together in a few characteristic patterns, with numerous minor permutations. These domains include one or more putative amphipathic a‐helix forming consensus regions, a phosphorylatable tract of Ser residues, and an N‐terminal consensus sequence. Lesser conserved domains are also present at various positions, particularly between the putative a‐helix forming domains, where they may occur as tandem repeats. This medley of permutations is mirrored by a wide size range of dehydrin polypeptides from less than 100 to nearly 600 amino acid residues. As of yet, the fundamental biochemical mode of action of dehydrins has not been demonstrated, but a number of immunolocalization and cell fractionation studies have established that dehydrins can be located in the nucleus or cytoplasm. Furthermore, it appears that these proteins associate with macromolecules ranging from nucleoprotein complexes in the nucleus to an endomembrane sheath in the cytoplasm. At present, all observations are consistent with a hypothesis that dehydrins are surfactants capable of inhibiting the coagulation of a range of macromolecules, thereby preserving structural integrity.
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Cites
Escherichia coli and Salmonella typhimurium: Cellular and molecular biology
Lejeune, P. (1988) · Biochimie · doi:10.1016/0300-9084(88)90119-8 · Cited by 4,072
THE MOLECULAR BASIS OF DEHYDRATION TOLERANCE IN PLANTS
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Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteins
Close, T. J. (1996) · Physiologia Plantarum · doi:10.1034/j.1399-3054.1996.970422.x · Cited by 962
Self-citationAbscisic acid and water-stress induce the expression of a novel rice gene.
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Amphipathic helix motif: Classes and properties
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A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn
Close, T. J., Kortt, A. A., & Chandler, P. M. (1989) · Plant Molecular Biology · doi:10.1007/bf00027338 · Cited by 508
Self-citationPlant Responses to Cellular Dehydration During Environmental Stress
Close, T.-J., & Bray, E. A. (1993) · Cited by 273
Self-citationHoude, M., Daniel, C., Lachapelle, M., Allard, F., Laliberté, S., & Sarhan, F. (1995) · The Plant Journal · doi:10.1046/j.1365-313x.1995.8040583.x · Cited by 216
Gene sequence, developmental expression, and protein phosphorylation of RAB-17 in maize
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Clegg, J. S. (2001) · Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(01)00300-1 · Cited by 438
TUBEROSA, R. (2002) · Annals of Botany · doi:10.1093/aob/mcf134 · Cited by 397
Overexpression of Multiple Dehydrin Genes Enhances Tolerance to Freezing Stress in Arabidopsis
Puhakainen, T., Hess, M. W., Mäkelä, P., Svensson, J., Heino, P., & Palva, E. T. (2004) · Plant Molecular Biology · doi:10.1023/b:plan.0000040903.66496.a4 · Cited by 377
Lan, T., Gao, J., & Zeng, Q.-Y. (2013) · Tree Genetics & Genomes · doi:10.1007/s11295-012-0551-2 · Cited by 102
Drought-induced changes in photosynthetic membranes of two wheat (Triticum aestivum L.) cultivars
Huseynova, I. M., Suleymanov, S. Y., Rustamova, S. M., & Aliyev, J. A. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909080124 · Cited by 23
Metadata
- Authors
- Close, T. J.
- Venue
- Physiologia Plantarum
- Publisher
- Wiley
- Published
- 1997-06
- Volume
- 100
- Issue
- 2
- Pages
- 291-296
- ISSN
- 0031-9317 (ISSN-L)
- 1399-3054
- OpenAlex
- W2008316903
- Cited by
- 853
- References
- 15
- FWCI
- 25.46
- Type
- journal article
- Language
- en
- Open access
- closed
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