Understanding how the Grp94 protein helps keep cells healthy and how to target it safely
Official title: Elucidating the Mechanistic Details of the Grp94 Molecular Chaperone through an Integrated Computational and Experimental Approach
Funded at Miami University Oxford · NIH-11336919 · Data updated 2026-11-12
Researchers are studying the Grp94 protein to learn how it helps proteins fold correctly in cells, with implications for diabetes, cancer, heart, and brain diseases.
Quick facts
| Grant type | NIH-funded research |
|---|---|
| Study type | NIH-funded research |
| Funding institution | Miami University Oxford NIH-funded |
| Lab location | 1 site (Oxford, United States) |
| Project start | August 1, 2022 |
| Project end | June 30, 2027 |
| Funding year | 2026 |
| Award (this year) | $343,784 |
| NIH project number | 5R35GM146963-05 |
| Project ID | NIH-11336919 on NIH RePORTER |
Who could benefit from this research
✓Could help
Ideal candidates include adults with or at risk for type 2 diabetes, cancer, cardiovascular or degenerative neurological conditions where ER protein folding is involved.
✕Less likely to help
People without conditions related to ER protein misfolding may receive indirect benefits through broader scientific advances.
What this research studies
This project looks at the Grp94 chaperone in the endoplasmic reticulum, trying to map its workflow and how it uses ATP to assist protein folding. The team combines computer modeling with lab experiments to reveal the details of Grp94’s chaperone cycle. By understanding its structure and function, they aim to identify ways to design safer drugs that disrupt harmful Grp94 activity without harming normal cell processes. The work focuses on how misfolded proteins contribute to diseases like type 2 diabetes, cancer, neurodegenerative and cardiovascular disorders. Results could guide the rational design of therapies that target Grp94 more precisely than current broad Hsp90 inhibitors.
Why it matters
Potential benefit: If successful, the research could inform safer, more targeted therapies for diseases linked to protein misfolding and Grp94 dysfunction.
How similar studies have gone: Similar work on chaperones has advanced understanding of protein folding, but Grp94-specific mechanisms remain an area of active discovery.
Where this research is happening
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Miami University Oxford
Oxford, United States Active
Researchers
- Principal investigator: Kravats, Andrea N — Miami University Oxford
- Study coordinator: Kravats, Andrea N
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.