Hydrophilins from distant organisms can protect enzymatic activities from water limitation effects in vitro

By J. Reyes, M. Rodrigo, J. M. Colmenero-Flores, J. Gil, Adriana Garay‐Arroyo, F. Campos, F. Salamini, D. Bartels, A. Covarrubias. 2005

186 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Surgery

View Paper: https://www.semanticscholar.org/paper/eb36637cb5d6c07a87df56d6a3fec5f3726ae92e

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In Cell Biology

1. Michael J. Wise
2. A. Tunnacliffe

In Molecular Biology

1. Michael J. Wise
2. D. Hincha
3. Michaela Hundertmark
4. A. Tunnacliffe
5. O. Leprince

Citations in the corpus

• Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, unknown): “The finding that the CDeT11-24 protein protects the enzymes CS and LDH in vitro against desiccation damage supports a function of the protein as a molecular shield, which has been described previously for LEA proteins (Reyes et al., 2005; Boucher et al., 2010).”
• LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana (2008, background): “A stabilization of lactate dehydrogenase and malate dehydrogenase during freezing and/or drying has been shown for LEA proteins from citrus [42,43], Chlorella [44], barley [45], Arabidopsis, and C. plantagineum [ 46 ,47].”
• The Enigmatic LEA Proteins and Other Hydrophilins1[W] (2008, background): “However, when severe water limitation (greater than 250 bars) is imposed and protein aggregation is evident, hydrophilins have no protective effects, at least in target:hydrophilin ratios in which molecular chaperones are active (1:1–1:5; Reyes et al., 2005).”
• Insights into Late Embryogenesis Abundant (LEA) Proteins in Plants: From Structure to the Functions (2014, background): “But they are distinct in that they lack structure and do not form transient complexes with their client proteins through hydrophobic surfaces, since they are hydrophilic [64] [133].”
• The continuing conundrum of the LEA proteins (2007, background): “…against desiccation (without freezing), and examples from all main LEA protein groups seem able to offer protection to sensitive enzymes such as LDH, malate dehydrogenase, fumarase and citrate synthase (CS; Sanchez-Ballesta et al. 2004; Grelet et al. 2005; Reyes et al. 2005; Goyal et al. 2005a).”
• LEA Proteins: Versatility of Form and Function (2010, background): “Indeed, examples are already known in the literature, such as those formally characterized as hydrophilins (Reyes et al. 2005).”