Professor in Biological Sciences @unccharlotte Group leader, Charlotte Group for Proteostasis Research Interested in the role of Hsp70 PTMs (Chaperone Code)
We are recruiting! If you are passionate about technology development, protein engineering, computational design, directed evolution, chemical biology - please reach out!
(The setting is pretty nice too…)
We are looking for talented graduate students to join our group for Fall 2026 studying the role and regulation of Hsp70 PTMs! If you are interested please check out trumanlab.org
Trilled and humbled to received the 2025 Outstanding Faculty Research Award by Department of Biological Sciences at UNC Charlotte. Thankful to my mentors, collaborators, current/former lab members, friends and family. @EMGSUS @ASBMB @unccharlotte
Stop the press!!! We are recruiting for an Assistant Professor Position. Particular focus will be given to candidates who strengthen our existing research strengths including proteostasis, genome integrity, immunology, microbiology and virology.
How well do you think you understand chaperones? In our recent @MolSystBiol paper, @fried_lab's Divya Yadav shows that obligate chaperone clients in cells are totally different from the proteins that "need" chaperones during in vitro refolding.
embopress.org/doi/full/10.10…
Great to see this work by our team, lead by PhD student Thomas Walker.
We found that the heat shock protein HSPB5 is a powerful chaperone that prevents TDP-43 fibrillation AND maintains TDP-43 condensate fluidity even more than its sibling HSPB1.
What if proteins that can’t refold in vitro fold perfectly fine inside cells?
Our new News & Views article in Molecular Systems Biology, written with Dr. @TrumanLab , explores this interesting insight from Yadav et al. (2025).
For decades, chaperone-client relationships have been defined using fundamental in vitro refolding assays, where proteins are unfolded by heat or denaturants and refolded with chaperones. But what happens inside a living cell is far more complex. Using proteome-wide LiP-MS, the authors show that in vivo chaperone requirements don’t necessarily match what refolding assays suggest. Many proteins that fail to refold after denaturation can still fold successfully during co-translational synthesis without the chaperones once thought essential.
In our commentary, we discuss how this challenges long-standing assumptions about “chaperone dependence” and highlight the role of the “chaperone code” (post-translational modifications on chaperones) that fine-tunes chaperone functions in the cell.
As someone fascinated by how molecular chaperones and their modifications orchestrate proteostasis, I find these findings a powerful reminder of how dynamic folding is within living cells.
Shan Yan, Ph.D. @unccharlotte shares how the Charlotte Biology and Biotech exchange group has hosted 36 distinguished speaker since 2017. CBB plans to expand the community and collaborations for continued impact. #NCBiotechSummit2025
Shan Yan, Ph.D. @unccharlotte shares how the Charlotte Biology and Biotech exchange group has hosted 36 distinguished speaker since 2017. CBB plans to expand the community and collaborations for continued impact. #NCBiotechSummit2025
Had a wonderful time visiting @MarquetteU Biological Sciences to share our recent work on the Hsp70 Chaperone Code! Such a beautiful campus and loved talking with the students and faculty about the exciting research going on 🔥🔥🔥#hsp70
Excited to share our new work "Dissecting the Cdc37 Co-chaperone Code: Functional Roles in Chaperone-Mediated Stress Adaptation" in press at the Journal of Biological Chemistry jbc.org/article/S0021-9258(2… 🔥🔥🔥
In this work we engineered a collection of 46 yeast strains that express mutations in the 23 known phosphorylation sites of Cdc37. Through phenotypic fingerprinting we have chaaracterized master regulators vs fine tuner sites of this essential co-chaperone!