LEA proteins: IDPs with versatile functions in cellular dehydration tolerance: Figure 1
出版年份 2012 全文链接
标题
LEA proteins: IDPs with versatile functions in cellular dehydration tolerance: Figure 1
作者
关键词
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出版物
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 40, Issue 5, Pages 1000-1003
出版商
Portland Press Ltd.
发表日期
2012-11-09
DOI
10.1042/bst20120109
参考文献
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注意:仅列出部分参考文献,下载原文获取全部文献信息。- The STF2p Hydrophilin from Saccharomyces cerevisiae Is Required for Dehydration Stress Tolerance
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- LEA Proteins During Water Stress: Not Just for Plants Anymore
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- Influence of drying on the secondary structure of intrinsically disordered and globular proteins
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- Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes
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- Identification of two hydrophilins that contribute to the desiccation and freezing tolerance of yeast (Saccharomyces cerevisiae) cells
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- Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation
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- A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state
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- Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state
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- The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding
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- MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins
- (2009) VIRGINIE BOUCHER et al. PLANT CELL AND ENVIRONMENT
- The K-Segment of Maize DHN1 Mediates Binding to Anionic Phospholipid Vesicles and Concomitant Structural Changes
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- LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana
- (2008) Michaela Hundertmark et al. BMC GENOMICS
- Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana
- (2008) Natacha Bies-Ethève et al. PLANT MOLECULAR BIOLOGY
- Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse
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- The Enigmatic LEA Proteins and Other Hydrophilins
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