Author

L. M. Baehr

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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Physiology· 3 Cell Biology· 1

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Research Focus:cell type annotation· 4 Organism:mouse· 4 Approach:experimental assay· 3 Assay:proteomics· 3 Research Focus:differential expression· 2 Approach:biophysical modeling· 1 Assay:DNA methylation· 1 Research Focus:gene regulatory network inference· 1

Frequent Co-Authors

S. C. Bodine· 4 shared D. C. Hughes· 3 shared A. P. Sharples· 2 shared D. C. Turner· 2 shared D. J. Owens· 2 shared J. C. Jarvis· 2 shared R. A. Seaborne· 2 shared A. K. Larin· 1 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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4 shared papersPhysiology

S. C. Bodine

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Author profile →

4 papers

Recent·Most cited

A Specialized Centrosome-Proteasome Axis Mediates Proteostasis and Influences Cardiac Stress through Txlnb

J. M. McLendon, X. Zhang, C. C. Stein, L. M. Baehr, S. C. Bodine, R. L. Boudreau

This study identifies Txlnb as a centrosome-adapter protein that mediates proteostasis in cardiomyocytes, linking centrosomes to the ubiquitin-proteasome system and influencing cardiac stress responses.

bioRxiv · Feb 12, 2024Physiology

Knockdown of the E3 Ubiquitin ligase UBR5 and its role in skeletal muscle anabolism

D. C. Turner, D. C. Hughes, L. M. Baehr, R. A. Seaborne, M. Viggars, J. C. Jarvis, P. P. Gorski, C. E. Stewart, D. J. Owens, S. C. Bodine, A. P. Sharples

This study shows that knocking down UBR5 leads to skeletal muscle atrophy by disrupting anabolic signaling pathways.

bioRxiv · Jun 5, 2020Cell Biology

Identification and Characterization of Fbxl22, a novel skeletal muscle atrophy-promoting E3 ubiquitin ligase

D. C. Hughes, L. M. Baehr, J. R. Driscoll, S. A. Lynch, D. S. Waddell, S. C. Bodine

This study identifies Fbxl22 and its splice variant as E3 ubiquitin ligases involved in neurogenic muscle atrophy, showing their role in muscle atrophy and potential therapeutic relevance.

bioRxiv · Apr 24, 2020Physiology

UBR5 is a Novel E3 Ubiquitin Ligase involved in Skeletal Muscle Hypertrophy and Recovery from Atrophy

R. A. Seaborne, D. C. Hughes, D. C. Turner, D. J. Owens, L. M. Baehr, P. Gorski, E. A. Semenova, O. V. Borisov, A. K. Larin, D. V. Popov, E. V. Generozov, H. Sutherland, I. I. Ahmetov, J. C. Jarvis, S. C. Bodine, A. P. Sharples

This paper identifies UBR5 as a novel E3 ubiquitin ligase inversely regulated to MuRF1/MAFbx, epigenetically modulated during skeletal muscle recovery from atrophy and hypertrophy, and genetically associated with muscle fiber size and strength traits.

bioRxiv · Apr 29, 2019Physiology