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  Cryoprotectin: a plant lipid-transfer protein homologue that stabilizes membranes during freezing

Hincha, D. K. (2002). Cryoprotectin: a plant lipid-transfer protein homologue that stabilizes membranes during freezing. In Philosophical Transactions of the Royal Society B-Biological Sciences (pp. 909-915).

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 Creators:
Hincha, D. K.1, Author           
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1Transcript Profiling, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753306              

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Free keywords: Phospholipid transfer protein. Broccoli brassica-oleracea. Cell-specific expression. Cold-acclimation. Arabidopsis-thaliana. Low-temperature. Gene family. Secondary structure. Crystal-structure. Thylakoid membranes. Multidisciplinary in Current Contents(R)/Agricultural, Biology & Environmental Sciences Experimental Biology in Current Contents(R)/Life Sciences. 2002 week 35
 Abstract: Plants from temperate and cold climates are able to increase their freezing tolerance during exposure to low non-freezing temperatures. It has been shown that several genes are induced in a coordinated manner during this process of cold acclimation. The functional role of most of the corresponding cold-regulated proteins is not yet known. We summarize our knowledge of those cold-regulated proteins that are able to stabilize membranes during a freeze-thaw cycle. Special emphasis is placed on cryoprotectin, a lipid-transfer protein homologue that was isolated from cold-acclimated cabbage leaves and that protects isolated chloroplast thylakoid membranes from freeze-thaw damage. [References: 77] 77

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Language(s): eng - English
 Dates: 2002
 Publication Status: Issued
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 Identifiers: ISI: ISI:000177132200015
DOI: 10.1098/rstb.2002.1079
URI: ://000177132200015 http://rstb.royalsocietypublishing.org/content/357/1423/909
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Title: Philosophical Transactions of the Royal Society B-Biological Sciences
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Title: Philosophical Transactions of the Royal Society B-Biological Sciences
Source Genre: Proceedings
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Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 909 - 915 Identifier: -