Super excited to share our latest work on the Hsp70 chaperone code "Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response" out now in @NatureComms :nature.com/articles/s41467-0…. @UNCCBiology @unccharlotte #hsp70

Last Friday @phdsadikbay presented some of our latest research at the 22nd Anderson Cancer Symposium. More to come! #interactome #mitochondria #HSP90 #proteomics #heatshockprotein #PTMs #posttranslationalmodification #cancer #omics

Like it or not, there is zero chance that major journals will not have “AI-assisted review” within 3 years

Today in @NatureBiotech we report OptiPrime, a mechanism-based machine learning model for predicting prime editing (PE) efficiencies and suggesting pegRNAs to achieve a user-specified edit. OptiPrime incorporates biochemical knowledge about PE into its mathematical structure, enabling training on ~300,000 PE efficiencies collected using 40 experimental conditions in multiple labs, and outcome predictions of PE variants such as twin prime editing not used in its training. OptiPrime enabled the rapid identification of efficient PE strategies across a variety of applications in vitro and in vivo, and could outperform months or years of manual experimental optimization. Try out OptiPrime here: optipri.me PDF: drive.google.com/file/d/13JZ… 1/15

UNC Charlotte ranks No. 17 in the nation and No. 1 in NC on SmartAsset’s 2026 list of America’s Best Value Public Universities. The ranking reflects what matters most: affordability, graduation and strong career outcomes. smartasset.com/data-studies/…

We are looking for motivated postdocs to join our lab starting Spring 2027 to study the Hsp70 Chaperone Code and Proteostasis, see here for more details: trumanlab.org/open-positions

Can someone start a journal called “Cell Atlases” so that the rest of the journals can go back to publishing interesting things?

Our paper in @Nature today 🥳 We tracked 6,438 mice from puberty to death and mapped the genetics of *when* you die, not just whether a gene associates with lifespan. nature.com/articles/s41586-0… 59 loci. Two decades of data. Thread 👇 #Longevity #Aging #Genetics #Healthspan

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…)

New article about our research: science.charlotte.edu/2026/0…

Adjusted Timeline for NIHs Implementation of Common Forms grants.nih.gov/grants/guide/…

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

New preprint! We measured temperature- and pH-induced aggregation for over 18,000 natural and de novo designed protein domains!

We are recruiting! open position for Asst Professor in Biological Sciences--Apply online at jobs.charlotte.edu, position number #006728

Didn’t think I could love @TwistBioscience more, but then they sent me a goodie bag of cool stuff for my 11 year old daughter 🔥🔥🔥

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.

Fantastic review!