How the Grp94 helper protein folds insulin-like growth factors
Official title: Mechanism by which the Grp94 molecular chaperone folds insulin-like growth factors
Funded at Brandeis University · NIH-11329533 · Data updated 2026-11-12
This research looks at how a helper protein called Grp94 works with another chaperone to correctly shape insulin-like growth factors, which matters for people with cancers and other IGF-related conditions.
Quick facts
| Grant type | NIH-funded research |
|---|---|
| Study type | NIH-funded research |
| Funding institution | Brandeis University NIH-funded |
| Lab location | 1 site (Waltham, United States) |
| Project start | May 15, 2025 |
| Project end | February 28, 2030 |
| Funding year | 2026 |
| Award (this year) | $435,116 |
| NIH project number | 5R35GM157973-02 |
| Project ID | NIH-11329533 on NIH RePORTER |
Who could benefit from this research
✓Could help
People with cancers or other conditions linked to abnormal IGF signaling, or those interested in contributing tissue or biospecimens for IGF biology research, would be most relevant.
✕Less likely to help
Patients without IGF-related conditions or those seeking immediate clinical treatments are unlikely to benefit directly from this basic laboratory research.
What this research studies
Researchers will examine how Grp94 and the chaperone BiP interact to decide whether insulin-like growth factors are folded for secretion or kept for degradation. They will use purified proteins, structural and biochemical experiments, and cell-based assays to watch docking, conformational changes, and client transfer between BiP and Grp94. The team aims to identify the conditions that favor transfer of IGF clients onto Grp94 and to determine what folding benefit that transfer provides. The work focuses on molecular mechanisms that could point to targets for future therapies.
Why it matters
Potential benefit: If successful, the findings could reveal new molecular steps to target that might help control IGF-related pathways in cancer or growth disorders.
How similar studies have gone: Previous laboratory studies have shown that chaperones like Grp94 and BiP guide protein folding, but translating that knowledge into therapies remains largely untested.
Where this research is happening
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Brandeis University
Waltham, United States Active
Researchers
- Principal investigator: Street, Timothy Oliver — Brandeis University
- Study coordinator: Street, Timothy Oliver
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.