The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
At‐HSP17.6A, encoding a small heat‐shock protein in Arabidopsis, can enhance osmotolerance upon overexpression
Abstract
Summary: Owing to their sessile lifestyle, it is crucial for plants to acquire stress tolerance. The function of heat‐shock proteins, including small heat‐shock proteins (smHSPs), in stress tolerance is not fully explored. To gain further knowledge about the smHSPs, the gene that encoded the cytosolic class II smHSP in Arabidopsis thaliana (At‐HSP17.6A) was characterized. The At‐HSP17.6A expression was induced by heat and osmotic stress, as well as during seed development. Accumulation of At‐HSP17.6A proteins could be detected with heat and at a late stage of seed development, but not with osmotic stress, suggesting stress‐induced post‐transcriptional regulation of At‐HSP17.6A expression. Overproduction of At‐HSP17.6A could increase salt and drought tolerance in Arabidopsis. The chaperone activity of At‐HSP17.6A was demonstrated in vitro.
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Current protocols in molecular biology
Sargent, T. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90147-9 · Cited by 7,205
Parsell, D. A., & Lindquist, S. (1993) · Annual Review of Genetics · doi:10.1146/annurev.ge.27.120193.002253 · Cited by 2,273
MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS
Hendrick, J. P., & Hartl, F.-U. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.002025 · Cited by 1,638
The Roles of Heat Shock Proteins in Plants
Vierling, E. (1991) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.42.060191.003051 · Cited by 1,439
The Roles Of Heat Shock Proteins In Plants
Vierling, E. (1991) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.42.1.579 · Cited by 1,319
The Bradford Method for Protein Quantitation
Kruger, N. J. (2003) · Basic Protein and Peptide Protocols · doi:10.1385/0-89603-268-x:9 · Cited by 1,264
Protein disaggregation mediated by heat-shock protein Hspl04
Parsell, D. A., Kowal, A. S., Singer, M. A., & Lindquist, S. (1994) · Nature · doi:10.1038/372475a0 · Cited by 864
Lee, G. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.3.659 · Cited by 779
Evolution, structure and function of the small heat shock proteins in plants
Waters, E. R., Lee, G. J., & Vierling, E. (1996) · Journal of Experimental Botany · doi:10.1093/jxb/47.3.325 · Cited by 675
Regulation of the Heat-Shock Response
Schöffl, F., Prändl, R., & Reindl, A. (1998) · Plant Physiology · doi:10.1104/pp.117.4.1135 · Cited by 434
Cited by
Drought and Salt Tolerance in Plants
Bartels, D., & Sunkar, R. (2005) · Critical Reviews in Plant Sciences · doi:10.1080/07352680590910410 · Cited by 2,615
Physiological, Biochemical, and Molecular Mechanisms of Heat Stress Tolerance in Plants
Hasanuzzaman, M., Nahar, K., Alam, M., Roychowdhury, R., & Fujita, M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14059643 · Cited by 2,313
Mechanisms underlying plant resilience to water deficits: prospects for water-saving agriculture
Chaves, M. M. (2004) · Journal of Experimental Botany · doi:10.1093/jxb/erh269 · Cited by 1,359
Iba, K. (2002) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.53.100201.160729 · Cited by 687
Small heat shock proteins and stress tolerance in plants
Sun, W., Van Montagu, M., & Verbruggen, N. (2002) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(02)00417-7 · Cited by 639
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Metadata
- Authors
- Sun, W., Bernard, C., Van De Cotte, B., Van Montagu, M., & Verbruggen, N.
- Venue
- The Plant Journal
- Publisher
- Wiley
- Published
- 2001-09
- Volume
- 27
- Issue
- 5
- Pages
- 407-415
- ISSN
- 0960-7412 (ISSN-L)
- 1365-313X
- OpenAlex
- W2115547367
- Cited by
- 317
- References
- 20
- FWCI
- 2.93
- Type
- journal article
- Language
- en
- Open access
- closed
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- Sun, W., Bernard, C., Van De Cotte, B., Van Montagu, M., & Verbruggen, N. (2001). At‐HSP17.6A, encoding a small heat‐shock protein in Arabidopsis, can enhance osmotolerance upon overexpression. The Plant Journal. https://doi.org/10.1046/j.1365-313x.2001.01107.x
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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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