Michael G. Kearse
Biochemistry, Genetics and Molecular Biology · The Ohio State University
Publications
38
Citations
1,498
Est. group size
~5
Recurring co-author estimate
Active years
17
Publishing since 2010
Michael G. Kearse's research focuses on how cells make proteins from RNA, with particular attention to unconventional translation processes such as non-AUG start codon usage and RAN (repeat-associated non-AUG) translation linked to neurological diseases like fragile X syndrome and C9orf72-associated ALS/FTD. His lab also studies RNA-modifying enzymes and chemical marks on RNA (like m6A), ribosome behavior during stress, and proteins such as TOP3B and FMRP that regulate mRNA processing and translation. This work aims to understand molecular mechanisms underlying neurodevelopmental and neurodegenerative disorders and viral infection.
Publication output has grown notably over the last decade, rising from about 1-2 papers per year in 2017-2021 to 5-7 per year in 2024-2026.
Generated by claude-sonnet-5 from public bibliographic data · Jul 20, 2026
- Selective Isolation of TOP3B•mRNA Covalent Intermediates Using Denaturing Oligo-dT Pulldown
BIO-PROTOCOL · 2026
- Erratum for Huang et al., “Single-base m <sup>6</sup> A epitranscriptomics reveals novel HIV-1 host interaction targets in primary CD4 <sup>+</sup> T cells”
Journal of Virology · 2026
- Unexpected ribosome turnover during prolonged translation inhibition
bioRxiv (Cold Spring Harbor Laboratory) · 2026
- Single-base m <sup>6</sup> A epitranscriptomics reveals novel HIV-1 host interaction targets in primary CD4 <sup>+</sup> T cells
Journal of Virology · 2025
- Unraveling the Role of Topoisomerase 3β (<scp>TOP3B</scp>) in <scp>mRNA</scp> Translation and Human Disease
Wiley Interdisciplinary Reviews - RNA · 2025
- An autism spectrum disorder mutation in Topoisomerase 3β causes accumulation of covalent mRNA intermediates by disrupting metal binding within the zinc finger domain
bioRxiv (Cold Spring Harbor Laboratory) · 2025
- A non-radioactive method to detect and measure 48S initiation complex and 80S ribosome formation in vitro
Methods in enzymology on CD-ROM/Methods in enzymology · 2025
- Increased levels of eIF2A inhibit translation by sequestering 40S ribosomal subunits
Nucleic Acids Research · 2023
- In Vitro Analysis of Stalled Ribosomes using Puromycin Incorporation
BIO-PROTOCOL · 2023
- A noncanonical RNA-binding domain of the fragile X protein, FMRP, elicits translational repression independent of mRNA G-quadruplexes
Journal of Biological Chemistry · 2022
- Increased levels of eIF2A inhibit translation by sequestering 40S ribosomal subunits
bioRxiv (Cold Spring Harbor Laboratory) · 2022
- A non-canonical RNA-binding domain of the Fragile X protein, FMRP, elicits translational repression independent of mRNA G-quadruplexes
bioRxiv (Cold Spring Harbor Laboratory) · 2022
- A double on the Rocs with a twist: Rocaglamide A targets multiple DEAD-box helicases to inhibit translation initiation
Cell chemical biology · 2021
- A native function for RAN translation and CGG repeats in regulating fragile X protein synthesis
Nature Neuroscience · 2020
- High-throughput screening yields several small-molecule inhibitors of repeat-associated non-AUG translation
Journal of Biological Chemistry · 2019
- bioRxiv (Cold Spring Harbor Laboratory)×8
- Journal of Biological Chemistry×4
- Journal of Virology×3
- Nucleic Acids Research×2
- Wiley Interdisciplinary Reviews - RNA×2
- Anita K. Hopper
Biochemistry, Genetics and Molecular Biology · The Ohio State University
- Vollter Anastas
Biochemistry, Genetics and Molecular Biology · The Ohio State University
- Jane E. Jackman
Biochemistry, Genetics and Molecular Biology · The Ohio State University
- Kotaro Nakanishi
Biochemistry, Genetics and Molecular Biology · The Ohio State University
- Wen Zhang
Biochemistry, Genetics and Molecular Biology · Indiana University
This profile was generated automatically from public scholarly data (OpenAlex). Group size and activity levels are estimates derived from co-authorship patterns.
Last updated Jul 19, 2026.
Claim or correct this profile