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Fibroin-Hybrid Systems: Current Advances in Biomedical Applications.

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Laboratório de Bioengenharia, Universidade Federal de Itajubá, Itabira 35903-087, Minas Gerais, Brazil.

Fibroin, a protein extracted from silk, offers advantageous properties such as non-immunogenicity, biocompatibility, and ease of surface modification, which have been widely utilized for a variety of biomedical applications. However, in vivo studies have revealed critical challenges, including rapid enzymatic degradation and limited stability. To widen the scope of this natural biomacromolecule, the grafting of polymers onto the protein surface has been advanced as a platform to enhance protein stability and develop smart conjugates.

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RNA editing is a significant mechanism underlying genetic variation and protein molecule alteration; C-to-U RNA editing, specifically, is important in the regulation of mammalian genetic diversity. The ability to define and limit accesses of enzymatic machinery to avoid the modification of unintended targets is key to the success of RNA editing. Identification of the core component of the apoB RNA editing holoenzyme, APOBEC, and investigation into new candidate genes encoding other elements of the complex could reveal further details regarding APOBEC-mediated mRNA editing.

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[Directed evolution improves the catalytic activity of laccase in papermaking].

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As a biocatalyst, laccase has been widely studied and applied in the papermaking industry. However, the low catalytic efficiency and poor stability of natural laccase limit its application in the pulping process. To develop the laccase with high activity and strong tolerance, we carried out directed evolution for modification of the laccase derived from and screened out the mutants F282L/F306L and Q275P from the random mutant library by high-throughput screening.

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Poly(ADP-ribose) polymerase-1 (PARP-1) is the key enzyme among other PARPs for post-translational modification of DNA repair proteins. It has four functional domains for DNA-binding, automodification and enzymatic activity. PARP-1 participates in poly-ADP-ribosylation of itself or other proteins during DNA damage response.

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