Understanding How Hsp70 Helpers Keep Proteins Healthy in Cancer
Official title: Deciphering the Hsp70 chaperone code
Funded at University of North Carolina Charlotte · NIH-11258077 · Data updated 2026-11-12
This grant looks at how a key protein helper called Hsp70 works and changes in cancer cells to keep proteins correctly folded.
Quick facts
| Grant type | NIH-funded research |
|---|---|
| Study type | NIH-funded research |
| Funding institution | University of North Carolina Charlotte NIH-funded |
| Lab location | 1 site (Charlotte, United States) |
| Project start | August 10, 2026 |
| Project end | May 31, 2031 |
| Funding year | 2026 |
| Award (this year) | $423,500 |
| NIH project number | 1R35GM161217-01 |
| Project ID | NIH-11258077 on NIH RePORTER |
Who could benefit from this research
✓Could help
Patients with cancers where proteostasis and Hsp70 pathways play a role, and those recruited for future translation or biomarker studies linked to chaperone codes.
✕Less likely to help
Individuals without cancers or without involvement of proteostasis pathways may not directly benefit from this basic science work.
What this research studies
Proteins can misfold in many diseases, including cancers, and cells rely on chaperones like Hsp70 to maintain proteostasis. This project will map the various modifications on Hsp70 and on its client proteins to understand how these changes influence protein folding, stress responses, and cell cycle control. Using advanced proteomics and molecular biology, researchers will connect specific modifications to chaperone functions and cancer-related processes, with the aim of identifying points that could be targeted for therapy. The work is grounded in human-relevant biology and could guide new strategies to improve cancer treatments by stabilizing protein folding in tumors.
Why it matters
Potential benefit: If successful, the research could lead to new approaches that improve the effectiveness of cancer treatments by better managing protein folding in cancer cells.
How similar studies have gone: Previous work has shown that chaperone modifications influence protein interactions and stress responses, supporting potential translational value of this direction.
Where this research is happening
-
University of North Carolina Charlotte
Charlotte, United States Active
Researchers
- Principal investigator: Truman, Andrew William — University of North Carolina Charlotte
- Study coordinator: Truman, Andrew William
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.