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Christophe V. F. P. Laurent

Researcher at University of Natural Resources and Life Sciences, Vienna

Publications -  19
Citations -  303

Christophe V. F. P. Laurent is an academic researcher from University of Natural Resources and Life Sciences, Vienna. The author has contributed to research in topics: Cellobiose dehydrogenase & Chemistry. The author has an hindex of 8, co-authored 13 publications receiving 171 citations. Previous affiliations of Christophe V. F. P. Laurent include University of Southern Denmark & University of Fribourg.

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Journal ArticleDOI

Multiplicity of enzymatic functions in the CAZy AA3 family.

TL;DR: An overview of the phylogenetic, molecular, and catalytic properties of AA3 enzymes is provided and their interactions with other carbohydrate-active enzymes are discussed.
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Influence of Lytic Polysaccharide Monooxygenase Active Site Segments on Activity and Affinity.

TL;DR: This study investigates the changes in activity induced by shortening the second active site segment (Seg2) or removing the CBM1 from Neurospora crassa LPMO9C and demonstrates that Seg2 is indispensable for substrate recognition and the formation of productive enzyme-substrate complexes.
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Interaction between Cellobiose Dehydrogenase and Lytic Polysaccharide Monooxygenase.

TL;DR: In this work, the interaction of four Neurospora crassa LPMOs and five CDH cytochrome domains from different species is investigated using computational methods and it is found that the LPMO loops are largely responsible for the preferred orientations of the cy tochrome domains.
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Learning from each other: ABC transporter regulation by protein phosphorylation in plant and mammalian systems.

TL;DR: It appears that ABC transporters exhibit an evolutionary conserved but complex regulation by protein phosphorylation, which apparently is, at least in some cases, tightly connected with protein-protein interactions (PPI).
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Direct Electron-Transfer Anisotropy of a Site-Specifically Immobilized Cellobiose Dehydrogenase

TL;DR: A recently published, maleimide-based immobilization method was used in combination with site-directed mutagenesis to establish different orientations on an electrode surface of CDH to study the direct electron transfer of the multicofactor enzyme cellobiose dehydrogenase.