Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa.
By Christopher M. Phillips, William T. Beeson, Jamie H. D. Cate, M. Marletta. ACS Chemical Biology, 2011
657 citations recorded by the source corpus.
Subfields: Biomaterials, Biomedical Engineering, Plant Science
View Paper: https://www.semanticscholar.org/paper/d7765b3b96e25b92d65e013afb0b3cc873ed7e15
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In Biomedical Engineering
In Plant Science
Citations in the corpus
- Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes (2013, background): “Iron reductases consist in a cytochrome domain (protoheme IX) of spectral class b. Iron reductase was first described as the N-terminal hemic module found in the bipartite domain organization of the flavocytochrome CDH.”
- Enzymatic breakdown of lignocellulosic biomass: the role of glycosyl hydrolases and lytic polysaccharide monooxygenases (2017, background): “Consequently, a genetic study proved this theory by deleting the key CDH isoform in Neurospora crassa to result in a twofold decrease in secreted cellulase activity on pure cellulose substrate in the mutant enzyme [107].”
- 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].”