Author

M. Radwan

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

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Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:cell-cell communication· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:differential expression· 1 Organism:human· 1

Frequent Co-Authors

C.-S. Ang· 2 shared D. M. Hatters· 2 shared A. R. Ormsby· 1 shared D. Cox· 1 shared G. E. Reid· 1 shared G. Reid· 1 shared J. C. Daly· 1 shared J. Lilley· 1 shared

Activity by Year

2019-2020 · peak 1/yr

Co-Author Collaboration Network

8 top collaborators · 20 mutual co-author links

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2 shared papersBiochemistry

C.-S. Ang

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2 papers

Recent·Most cited

Inclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation

M. Radwan, J. Lilley, C.-S. Ang, G. Reid, D. M. Hatters

The paper compares proteomes enriched in polyGA and polyQ inclusion bodies, finding distinct protein sets but shared degradation-related proteins linked to neurodegenerative diseases.

bioRxiv · May 4, 2020Biochemistry

Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins

M. Radwan, C.-S. Ang, A. R. Ormsby, D. Cox, J. C. Daly, G. E. Reid, D. M. Hatters

This study shows that arginine valency in C9ORF72 DPRs causes promiscuous proteome binding, ribosome stalling, actin cytoskeleton disruption, and arginine hypomethylation.

bioRxiv · Aug 28, 2019 · PreprintBiochemistry