Andy Truman PhD

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Andy Truman PhD

Andy Truman PhD

@TrumanLab

Professor in Biological Sciences @unccharlotte Group leader, Charlotte Group for Proteostasis Research Interested in the role of Hsp70 PTMs (Chaperone Code)

Charlotte, NC Beigetreten Aralık 2018
4.2K Folgt6.1K Follower
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Alice Ting
Alice Ting@aliceyting·
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…)
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Melissa Perreault 🇨🇦
So many new STEM PhDs pumping out 20+ low impact papers/year. ECRs over 50, and they train their students to do the same. We need to stop rewarding this behaviour as we are the ones responsible. It's us who sit on the awards, promotion, membership, and hiring committees.
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Michał Jastrzębski
Michał Jastrzębski@_inc0_·
Hey bio hackers! Where do you order your DNA from? Addgene is useless unfortunately..
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Andy Truman PhD
Andy Truman PhD@TrumanLab·
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
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Shan Yan
Shan Yan@ShanYanLab·
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
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Gabriel Rocklin
Gabriel Rocklin@grocklin·
New preprint! We measured temperature- and pH-induced aggregation for over 18,000 natural and de novo designed protein domains!
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Andy Truman PhD
Andy Truman PhD@TrumanLab·
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 🔥🔥🔥
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Oded Rechavi
Oded Rechavi@OdedRechavi·
“The bad review will come from your list of suggested reviewers”
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Stephen Fried JHU
Stephen Fried JHU@fried_lab·
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…
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Luke McAlary
Luke McAlary@LukeMcAlary·
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.
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biorxiv_biochem@biorxiv_biochem

Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP-43 low complexity domain biorxiv.org/content/10.110… #biorxiv_biochem

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Yevheniia Bushman
Yevheniia Bushman@whybee_yb·
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.
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Andy Truman PhD
Andy Truman PhD@TrumanLab·
@jdpereira Love it! We are currently working on a project that stems from an observation I made over 20 years ago as a grad student. It turns out that the little dots I saw under the microscope then weren’t artifacts but phase separation lol
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Joao Pereira
Joao Pereira@jdpereira·
When I was doing my postdoc there was an experiment I would have loved to do. We couldn’t. I moved on to industry, it was in my mind. Became a core director, it was in my mind. Became an assistant professor and it was in my mind. We just did it.
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Andy Truman PhD
Andy Truman PhD@TrumanLab·
@OdedRechavi Grant rejections are more damaging because they are needed to keep lab members employed. However I find the publication process way more stressful
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Oded Rechavi
Oded Rechavi@OdedRechavi·
What hurts you more - getting a paper rejected or getting a grant rejected? I know grant rejections are probably worst in terms of consequences, but paper rejections are somehow more emotional (for me). Depends on the paper and grant of course (and how urgently you need the money or publication), but I’m asking in general.
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Brian S. Kim
Brian S. Kim@itchdoctor·
Our lab prides itself on knowing how well our papers fit into specific journals. We never submit a paper to a journal that we think is out of reach in terms of the reviews we will get. I am amazed at how well AI aligns with our internal adjudication. We will use for all pre-subs.
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John Streicher
John Streicher@JohnStreicher1·
@drugmonkeyblog It is profoundly demoralizing to bust my ass finishing reviews by tomorrow for a meeting it seems won’t happen.
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