Correction: Recent advances in self-healing polyurethane based on dynamic covalent bonds combined with other self-healing methods.

Correction for 'Recent advances in self-healing polyurethane based on dynamic covalent bonds combined with other self-healing methods' by Ze-Wei An , , 2023, , 6505-6520, https://doi.org/10.1039/D2NR07110J.

Recent advances in self-healing polyurethane based on dynamic covalent bonds combined with other self-healing methods.

To meet more application requirements, improving mechanical properties and self-healing efficiency has become the focus of current research on self-healing PU. The competitive relationship between self-healing ability and mechanical properties cannot be avoided by a single self-healing method. To address this problem, a growing number of studies have combined dynamic covalent bonding with other self-healing methods to construct the PU structure.

Inhibition of MSK1 Promotes Inflammation and Apoptosis and Inhibits Functional Recovery After Spinal Cord Injury.

Mitogen- and stress-activated kinase (MSK) 1 is a nuclear serine/threonine kinase. In the central nervous system, it plays an important role in regulating cell proliferation and neuronal survival; it is also involved in astrocyte inflammation and the inhibition of inflammatory cytokine production. However, its specific role in spinal cord injury is not clear.

Development of a whole-cell biocatalyst with NADPH regeneration system for biosulfoxidation.

A formate dehydrogenase gene (fdh) originated from Candida boidinii was co-expressed in E. coli BL21 (DE3) with the cyclohexanone monooxygenase gene (chmo) cloned from Acinetobacter calcoaceticus NCIMB 9871. The co-expression system was then used as a whole-cell biocatalyst to synthesize chiral phenyl methyl sulfoxide (PMSO) from thioanisole (PMS) and the reaction conditions were investigated.

Characterization of an aldo-keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum.

A novel aldo-keto reductase gene, Tm1743, from Thermotoga maritima was overexpressed in Escherichia coli. The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C.

Biocatalytic characterization of a short-chain alcohol dehydrogenase with broad substrate specificity from thermophilic Carboxydothermus hydrogenoformans.

The gene encoding a novel short-chain alcohol dehydrogenase in the thermophilic bacterium, Carboxydothermus hydrogenoformans, was identified and overexpressed in Escherichia coli. The enzyme was thermally stable and displayed the highest activity at 70 °C and pH 6.0.