Complexity of the heat-soluble LEA proteome in Artemia species.
about
Molecular approaches for improving desiccation tolerance: insights from the brine shrimp Artemia franciscanaGroup 1 LEA proteins contribute to the desiccation and freeze tolerance of Artemia franciscana embryos during diapause.Study of model systems to test the potential function of Artemia group 1 late embryogenesis abundant (LEA) proteins.Late embryogenesis abundant proteins protect human hepatoma cells during acute desiccation.Mechanisms of animal diapause: recent developments from nematodes, crustaceans, insects, and fish.Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana.Towards water-free biobanks: long-term dry-preservation at room temperature of desiccation-sensitive enzyme luciferase in air-dried insect cells.Potential functions of LEA proteins from the brine shrimp Artemia franciscana - anhydrobiosis meets bioinformatics.
P2860
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P2860
Complexity of the heat-soluble LEA proteome in Artemia species.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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2012年学术文章
@zh-cn
2012年学术文章
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2012年学术文章
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2012年学术文章
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2012年學術文章
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2012年學術文章
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name
Complexity of the heat-soluble LEA proteome in Artemia species.
@en
Complexity of the heat-soluble LEA proteome in Artemia species.
@nl
type
label
Complexity of the heat-soluble LEA proteome in Artemia species.
@en
Complexity of the heat-soluble LEA proteome in Artemia species.
@nl
prefLabel
Complexity of the heat-soluble LEA proteome in Artemia species.
@en
Complexity of the heat-soluble LEA proteome in Artemia species.
@nl
P2093
P1476
Complexity of the heat-soluble LEA proteome in Artemia species.
@en
P2093
Alden H Warner
James S Clegg
Sohini Chakrabortee
P304
P356
10.1016/J.CBD.2012.04.002
P577
2012-04-28T00:00:00Z