ArticlePloS one2012
Computational and statistical analyses of amino acid usage and physico-chemical properties of the twelve late embryogenesis abundant protein classes.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
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- Cloning and function analysis of aFrontiers in plant science · 2022Article
- Genome-wide identification and analysis ofFrontiers in plant science · 2022Article
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- Late Embryogenesis Abundant (LEA)5 Regulates Translation in Mitochondria and Chloroplasts to Enhance Growth and Stress Tolerance.Frontiers in plant science · 2022Article
- The in vitro structure and functions of the disordered late embryogenesis abundant three proteins.Protein science : a publication of the Protein Society · 2021Article
- Structural and Functional Characterization of the ABA-Water Deficit Stress Domain from Wheat and Barley: An Intrinsically Disordered Domain behind the Versatile Functions of the Plant Abscissic Acid, Stress and Ripening Protein Family.International journal of molecular sciences · 2021Article
- Questing functions and structures of hypothetical proteins from Campylobacter jejuni: a computer-aided approach.Bioscience reports · 2020Article
- Common Functions of Disordered Proteins across Evolutionary Distant Organisms.International journal of molecular sciences · 2020Review
- Conserved sequence motifs in the abiotic stress response protein late embryogenesis abundant 3.PloS one · 2020Article
- Structural properties and cellular expression of AfrLEA6, a group 6 late embryogenesis abundant protein from embryos of Artemia franciscana.Cell stress & chaperones · 2019Article
- Preferential adsorption to air-water interfaces: a novel cryoprotective mechanism for LEA proteins.The Biochemical journal · 2019Article
- Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat.Scientific reports · 2019Article
- Analysis of pcC13-62 promoters predicts a link between cis-element variations and desiccation tolerance in Linderniaceae.Journal of experimental botany · 2018Article
- Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.Scientific reports · 2017Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Late Embryogenesis Abundant Proteins (LEAPs) are ubiquitous proteins expected to play major roles in desiccation tolerance. Little is known about their structure - function relationships because of the scarcity of 3-D structures for LEAPs. The previous building of LEAPdb, a database dedicated to LEAPs from plants and other organisms, led to the classification of 710 LEAPs into 12 non-overlapping classes with distinct properties. Using this resource, numerous physico-chemical properties of LEAPs and amino acid usage by LEAPs have been computed and statistically analyzed, revealing distinctive features for each class. This unprecedented analysis allowed a rigorous characterization of the 12 LEAP classes, which differed also in multiple structural and physico-chemical features. Although most LEAPs can be predicted as intrinsically disordered proteins, the analysis indicates that LEAP class 7 (PF03168) and probably LEAP class 11 (PF04927) are natively folded proteins. This study thus provides a detailed description of the structural properties of this protein family opening the path toward further LEAP structure - function analysis. Finally, since each LEAP class can be clearly characterized by a unique set of physico-chemical properties, this will allow development of software to predict proteins as LEAPs.
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