Author

A. R. Ormsby

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· 3 Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:proteomics· 5 Research Focus:cell type annotation· 3 Organism:human· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:metabolism & bioenergetics· 1

Frequent Co-Authors

D. Cox· 6 shared D. M. Hatters· 6 shared G. E. Reid· 2 shared A. Dickson· 1 shared C. B. Raeburn· 1 shared C. J. Rosado· 1 shared C.-S. Ang· 1 shared D. B. Ascher· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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6 shared papersCell Biology

D. Cox

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6 papers

Recent·Most cited

Replicative aging impedes stress-induced assembly of a key human protein disaggregase

Y. Mathangasinghe, N. Alberts, C. J. Rosado, D. Cox, N. L. Payne, A. R. Ormsby, K. M. Alp, R. Sakson, S. Uthishtran, T. Ruppert, S. Arumugam, D. M. Hatters, H. H. Kampinga, N. B. Nillegoda

This study identifies a stress-induced trimeric protein disaggregase in human cells that collapses during replicative aging, contributing to pathophysiological consequences.

bioRxiv · Jun 25, 2022 · PreprintCell Biology

Protein painting reveals pervasive remodeling of conserved proteostasis machinery in response to pharmacological stimuli.

D. Cox, A. R. Ormsby, G. E. Reid, D. M. Hatters

The paper uses protein painting to show how pharmacological stimuli remodel conserved proteostasis machinery across the proteome in whole cells.

bioRxiv · May 14, 2022Cell Biology

Sequence grammar underlying unfolding and phase separation of globular proteins

K. M. Ruff, Y. H. Choi, D. Cox, A. R. Ormsby, Y. Myung, D. B. Ascher, S. E. Radford, R. V. Pappu, D. M. Hatters

The paper investigates how sequence grammars of unfolded globular proteins drive phase separation and formation of UPODs, highlighting the role of hydrophobic residues and their impact on disease-related interactions.

bioRxiv · Aug 20, 2021 · PreprintBiophysics

A biosensor to gauge protein homeostasis resilience differences in the nucleus compared to cytosol of mammalian cells

C. B. Raeburn, A. R. Ormsby, N. S. Moily, D. Cox, S. Ebbinghaus, A. Dickson, G. McColl, D. M. Hatters

The paper develops a biosensor to compare protein homeostasis resilience in the nucleus and cytosol of human cells, finding the nucleus has lower chaperone activity and aggregation suppression capacity.

bioRxiv · Apr 19, 2021 · PreprintBiochemistry

Nascent mutant Huntingtin exon 1 chains do not stall on ribosomes during translation but aggregates do recruit machinery involved in ribosome quality control

A. R. Ormsby, D. Cox, J. Daly, D. Priest, E. Hinde, D. M. Hatters

This study investigates how mutant Huntingtin exon 1 chains form inclusions in cells, finding that nascent chains do not stall on ribosomes but that ribosome quality control proteins are recruited into the aggregates.

bioRxiv · May 13, 2020Cell Biology

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