Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components
By R. Quinlan, Matthew D. Sweeney, L. Lo Leggio, Harm Otten, J. Poulsen, K. Johansen, K. B. Krogh, C. I. Jørgensen, Morten Tovborg, A. Anthonsen and 6 more. Proceedings of the National Academy of Sciences of the United States of America, 2011
982 citations recorded by the source corpus.
Subfields: Biomaterials, Biomedical Engineering, Plant Science
View Paper: https://www.semanticscholar.org/paper/75647d855ae498ce8a7b0359e2859116628b0f8a
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Citations in the corpus
- Enzymatic breakdown of lignocellulosic biomass: the role of glycosyl hydrolases and lytic polysaccharide monooxygenases (2017, background): “The oxidative cleavage by LPMOs can also be affected by reducing agents such as glutathione or gallate ascorbic acid [102,108,109].”
- Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes (2013, methodology): “This family includes the lytic polysaccharide monooxygenases previously classified as family GH61 glycoside hydrolases [8,53].”
- Novel enzymes for the degradation of cellulose (2012, background): “At the same time, a series of elegant studies showed that GH61s are functionally very similar to CBM33s [13,14,16-18].”