How the speed of protein production changes protein shape and cell behavior in cancer
Translation Kinetics and their Effects on Protein Structure and Function, mRNA half-lives, and Cellular Phenotype
Researchers are looking at how the speed that cells make proteins can change protein shape, mRNA lifetimes, and behaviors linked to cancer.
Quick facts
| Grant type | NIH-funded research |
|---|---|
| Study type | NIH-funded research |
| Funding institution | Pennsylvania State University, the NIH-funded |
| Lab location | 1 site (University Park, United States) |
| Project ID | NIH-11162481 on NIH RePORTER |
What this research studies
The team will combine computer modeling and big-data analysis with lab techniques such as mass spectrometry, cryo-electron microscopy, and NMR to track how translation speed affects protein folding and function. They will examine synonymous codon changes (DNA changes that don't alter the amino acid sequence but change how fast a protein is made) to see how these changes influence enzyme activity and mRNA degradation. Experiments will span organisms from bacteria and yeast to fruit flies and human-derived samples to connect molecular events to cell behaviors like migration and circadian rhythm. The goal is to produce predictive models that link ribosome traffic, translation-dependent mRNA decay, and downstream cellular effects.
Who could benefit from this research
Good fit: This project does not enroll patients directly, but its findings are most relevant to people with cancers linked to gene changes that alter how proteins are produced or folded.
Not a fit: Patients whose cancers are driven by unrelated mechanisms or who lack mutations that affect translation speed are unlikely to receive direct benefit from this work.
Why it matters
Potential benefit: If successful, this work could uncover hidden genetic mechanisms that drive some cancers and suggest new targets for diagnostics or therapies.
How similar studies have performed: Prior studies have shown that synonymous codon changes can affect protein behavior, but this comprehensive mix of big-data modeling and high-resolution structural methods is relatively novel.
Where this research is happening
University Park, United States
- Pennsylvania State University, the — University Park, United States (Active)
Researchers
- Principal investigator: O'brien, Edward Patrick — Pennsylvania State University, the
- Study coordinator: O'brien, Edward Patrick
About this research
- This is an active NIH-funded research project — typically early-stage science, not a clinical trial accepting patient enrollment.
- Some NIH-funded labs run parallel clinical studies or seek volunteers for related work. To check, contact the principal investigator or institution listed above.
- For full project details, budget, and progress reports, visit the official NIH RePORTER page below.