Author

R. R. Cupo

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· 3 Bioengineering· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Research Focus:cell type annotation· 2 Research Focus:drug response / drug discovery· 2 Research Focus:protein folding & dynamics· 2 Organism:C. elegans· 1 Research Focus:differential expression· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

J. Shorter· 4 shared E. Chuang· 3 shared K. L. Mack· 2 shared A. Rizo· 1 shared A. Tariq· 1 shared D. M. Huryn· 1 shared D. R. Southworth· 1 shared E. L. Gorenberg· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersBiochemistry

J. Shorter

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Author profile →

4 papers

Recent·Most cited

Defining a small-molecule stimulator of the human Hsp70-disaggregase system with selectivity for DnaJB proteins

E. Chuang, R. R. Cupo, J. R. Bevan, M. L. Rice, S. Mao, E. L. Gorenberg, K. L. Mack, D. M. Huryn, P. Wipf, J. L. Brodsky, J. Shorter

The paper identifies a small-molecule stimulator of the human Hsp70-disaggregase system that selectively activates DnaJB1- or DnaJB4-containing chaperone complexes.

bioRxiv · Jan 11, 2024 · PreprintBiochemistry

Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3.

R. R. Cupo, A. Rizo, G. A. Braun, E. Tse, E. Chuang, D. R. Southworth, J. Shorter

The paper reports the structure of Skd3-substrate complex, revealing its dodecamer formation and mechanism of protein disaggregation, with implications for SCN and MGCA7.

bioRxiv · Feb 17, 2022Biochemistry

Tuning Hsp104 specificity to selectively detoxify alpha-synuclein

K. L. Mack, H. Kim, M. E. Jackrel, J. Lin, J. E. DeNizio, X. Yan, E. Chuang, A. Tariq, R. R. Cupo, L. M. Castellano, K. A. Caldwell, G. A. Caldwell, J. Shorter

The paper engineers Hsp104 variants with substrate specificity to selectively reduce alpha-synuclein toxicity in a Parkinson's disease model.

bioRxiv · Apr 15, 2020Bioengineering

Skd3 (human CLPB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations

R. R. Cupo, J. Shorter

This study identifies Skd3 (human CLPB) as a mitochondrial protein disaggregase inactivated by mutations causing 3-methylglutaconic aciduria.

bioRxiv · Jan 17, 2020Biochemistry