Author

P. Gorski

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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Biophysics· 1 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Assay:DNA methylation· 1 Research Focus:gene regulatory network inference· 1 Research Focus:genome assembly· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

A. K. Larin· 1 shared A. P. Sharples· 1 shared D. C. Hughes· 1 shared D. C. Turner· 1 shared D. J. Owens· 1 shared D. V. Popov· 1 shared E. A. Semenova· 1 shared E. V. Generozov· 1 shared

Activity by Year

2019-2019 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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1 shared paperPhysiology

A. K. Larin

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2 papers

Recent·Most cited

Interaction of a sarcolipin pentamer and monomer with the sarcoplasmic reticulum calcium pump, SERCA

J. P. Glaves, J. Primeau, P. Gorski, L. M. Espinoza-Fonseca, J. Lemieux, H. S. Young

This paper characterizes the interaction between sarcolipin (SLN) pentamer and monomer with SERCA, revealing structural and functional insights into SLN's regulation of calcium transport and thermogenesis.

bioRxiv · Jul 8, 2019Biophysics

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