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Ryan R. Cupo - Publications

Affiliations: 
University of Pennsylvania, Philadelphia, PA, United States 
Area:
Proteostasis, Mitochondria, Protein Aggregation
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11 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Mack KL, Kim H, Barbieri EM, Lin J, Braganza S, Jackrel ME, DeNizio JE, Yan X, Chuang E, Tariq A, Cupo RR, Castellano LM, Caldwell KA, Caldwell GA, Shorter J. Tuning Hsp104 specificity to selectively detoxify α-synuclein. Molecular Cell. PMID 37625404 DOI: 10.1016/j.molcel.2023.07.029  0.361
2022 Cupo RR, Rizo AN, Braun GA, Tse E, Chuang E, Gupta K, Southworth DR, Shorter J. Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3. Cell Reports. 40: 111408. PMID 36170828 DOI: 10.1016/j.celrep.2022.111408  0.54
2021 Warren JT, Cupo RR, Wattanasirakul P, Spencer D, Locke AE, Makaryan V, Bolyard AA, Kelley ML, Kingston NL, Shorter J, Bellanné-Chantelot C, Donadieu J, Dale DC, Link DC. Heterozygous Variants of CLPB are a Cause of Severe Congenital Neutropenia. Blood. PMID 34115842 DOI: 10.1182/blood.2021010762  0.501
2020 Cupo RR, Shorter J. Expression and Purification of Recombinant Skd3 (Human ClpB) Protein and Tobacco Etch Virus (TEV) Protease from . Bio-Protocol. 10: e3858. PMID 33659495 DOI: 10.21769/BioProtoc.3858  0.537
2020 Cupo RR, Shorter J. Skd3 (human ) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations. Elife. 9. PMID 32573439 DOI: 10.7554/Elife.55279  0.647
2020 Cupo RR, Shorter J. Author response: Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations Elife. DOI: 10.7554/Elife.55279.Sa2  0.542
2018 Cupo RR, Augustine E, Shorter J. Exploring and Enhancing Compartment-Specific Protein Disaggregases to Combat Neurodegenerative Diseases Biophysical Journal. 114: 578a-579a. DOI: 10.1016/J.Bpj.2017.11.3165  0.579
2017 Lavorato M, Iyer VR, Dewight W, Cupo RR, Debattisti V, Gomez L, De la Fuente S, Zhao YT, Valdivia HH, Hajnóczky G, Franzini-Armstrong C. Increased mitochondrial nanotunneling activity, induced by calcium imbalance, affects intermitochondrial matrix exchanges. Proceedings of the National Academy of Sciences of the United States of America. PMID 28096415 DOI: 10.1073/Pnas.1617788113  0.551
2017 Eisner V, Cupo RR, Gao E, Csordás G, Slovinsky WS, Paillard M, Cheng L, Ibetti J, Chen SR, Chuprun JK, Hoek JB, Koch WJ, Hajnóczky G. Mitochondrial fusion dynamics is robust in the heart and depends on calcium oscillations and contractile activity. Proceedings of the National Academy of Sciences of the United States of America. PMID 28096338 DOI: 10.1073/Pnas.1617288114  0.56
2015 Eisner V, Cupo R, Gao E, Csordás G, Cheng L, Ibetti J, Chuprun JK, Koch WJ, Hajnóczky G. Mitochondrial Fusion Dynamics in the Heart Biophysical Journal. 108: 610a. DOI: 10.1016/J.Bpj.2014.11.3322  0.549
2014 Eisner V, Cupo R, Gyorgy C, Cheng L, Koch W, Hajnoczky G. Mitochondrial Dynamics in Neonatal and Adult Cardiomyocytes Biophysical Journal. 106: 592a. DOI: 10.1016/J.Bpj.2013.11.3277  0.548
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