Author

A. K. Rohr

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:clustering· 1 Organism:human· 1 Assay:metagenomics· 1 Approach:simulation· 1 Approach:statistical model· 1

Frequent Co-Authors

B. Bissaro· 2 shared B. Streit· 1 shared B. Westereng· 1 shared E. Martens· 1 shared G. Lo· 1 shared G. T. Beckham· 1 shared G. Vaaje-Kolstad· 1 shared G. Vasconcelos Pereira· 1 shared

Activity by Year

2016-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

B. Bissaro

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Human gut Faecalibacterium prausnitzii deploy a highly efficient conserved system to cross-feed on β-mannan-derived oligosaccharides

L. J. Lindstad, G. Lo, S. A. Leivers, Z. Lu, L. Michalak, G. Vasconcelos Pereira, A. K. Rohr, E. Martens, L. S. McKee, S. Duncan, B. Westereng, P. B. Pope, S. L. La Rosa

This study identifies a conserved system in Faecalibacterium prausnitzii that enables efficient cross-feeding on β-mannan-derived oligosaccharides, enhancing butyrate production in the human gut.

bioRxiv · Dec 23, 2020Microbiology

Molecular mechanism of the chitinolytic monocopper peroxygenase reaction

B. Bissaro, B. Streit, I. Isaksen, V. G. H. Eijsink, G. T. Beckham, J. DuBois, A. K. Rohr

This paper elucidates the H2O2-mediated reaction mechanism of chitinolytic LPMOs using experimental and computational approaches, revealing key kinetic and structural insights.

bioRxiv · Feb 5, 2019Biochemistry

Fenton-type chemistry by a copper enzyme: molecular mechanism of polysaccharide oxidative cleavage

B. Bissaro, A. K. Rohr, M. Skaugen, Z. Forsberg, S. J. Horn, G. Vaaje-Kolstad, V. Eijsink

This study identifies H2O2 as the co-substrate for LPMOs, revealing a mechanism for polysaccharide oxidative cleavage and improving enzymatic stability and activity.

bioRxiv · Dec 27, 2016Biochemistry