Author

N. R. Andersen

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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Cell Biology· 2 Physiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:mouse· 4 Assay:proteomics· 3 Organism:human· 2 Research Focus:metabolism & bioenergetics· 2 Assay:metabolomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

L. L. V. Moller· 3 shared L. Sylow· 3 shared E. A. Richter· 2 shared J. R. Knudsen· 2 shared P. Schjerling· 2 shared R. Kjobsted· 2 shared T. E. Jensen· 2 shared A. Artati· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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3 shared papersCell Biology

L. L. V. Moller

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Pantothenate Kinase 4 controls efficient skeletal muscle energy substrate metabolism via acetyl-CoA

A. Miranda-Cervantes, A. M. Fritzen, S. H. Raun, O. Hodek, L. L. V. Moller, K. Johann, L. Deisen, P. Gregorevic, A. Gudiksen, A. Artati, J. Adamski, N. R. Andersen, P. Schjerling, A. Cebrian-Serrano, M. Jaehnert, , M. Kleinert

This study identifies PanK4 as a regulator of skeletal muscle energy metabolism, showing its role in acetyl-CoA regulation and metabolic flexibility.

bioRxiv · Aug 14, 2023 · PreprintPhysiology

Metformin improves glycemia independently of skeletal muscle AMPK via enhanced intestinal glucose clearance

R. Kjobsted, J. M. Kristensen, J. B. Birk, N. O. Jorgensen, K. Kido, N. R. Andersen, J. K. Larsen, M. Foretz, V. Benoit, F. Nielsen, K. Brosen, N. Jessen, Y. Hellsten, K. Hojlund, J. F. P. Wojtaszewski

This study shows metformin reduces blood glucose through improved intestinal glucose clearance, not via skeletal muscle AMPK activation, challenging current understanding of its mechanism.

bioRxiv · May 22, 2022 · PreprintPhysiology

The role of group I p21-activated kinases in contraction-stimulated skeletal muscle glucose transport

L. L. V. Moller, I. L. Nielsen, J. R. Knudsen, N. R. Andersen, T. E. Jensen, L. Sylow, E. A. Richter

This study investigates the role of group I p21-activated kinases (PAKs) in contraction-stimulated glucose transport in skeletal muscle, finding that PAK2, but not PAK1, contributes to this process in EDL muscle.

bioRxiv · Jan 29, 2020 · PreprintCell Biology

Insulin-stimulated glucose uptake partly relies on p21-activated kinase (PAK)-2, but not PAK1, in mouse skeletal muscle

L. L. V. Moller, M. Jaurji, R. Kjobsted, G. A. Joseph, A. B. Madsen, J. R. Knudsen, A.-M. Lundsgaard, N. R. Andersen, P. Schjerling, T. E. Jensen, R. S. Krauss, E. A. Richter, L. Sylow

This study investigates the role of PAK1 and PAK2 in insulin-stimulated glucose uptake in mouse skeletal muscle, finding that PAK2, not PAK1, contributes to this process.

bioRxiv · Dec 16, 2019Cell Biology