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Understanding viral proteostasis and translationregulation offers novel and exciting targets for antiviral therapies. Check out this cool article by Ranen Aviner defining SARS-CoV2 translation, in another great collaboration with the Andino lab at UCSF journals.plos.org/plospathogens/…

We are proud and excited to share the new study from our lab, led by the amazing Ranen Aviner. It uncovers an important pathogenic mechanism causing cellular dysfunction in Huntington's Disease. We hope this work will inspire new and effective therapies nature.com/articles/s4155…

Popular diet practiced for weight loss may cause accelerated aging: study suggests that ketogenic diet promotes cellular senescence in multiple organs by stabilizing p53 in an AMPK dependent manner. science.org/doi/10.1126/sc…

My choice this week in Science Magazine nature.com/articles/s4155… Frydman Lab Ranen Aviner

1. Check out our MS just out! Amazing Mauricio Aguilar developed a new ML pipeline that identifies ribosome pausing sites as an Anomaly Detection problem to overcome spurious signals that arise when analyzing RiboSeq data. science.org/doi/10.1126/sc…

2. Mauricio and Kevin Stein combined ML with experiments to understand how codon choice and tRNA pools are tuned to harmonize elongation rate with cotranslational folding and minimize unwanted ribosome pausing. Major and important findings of our study are.....

3. i) We dissect the interdependence and distinct contributions of amino acid properties and tRNA abundance on elongation pausing ii) We find that competition between tRNAs leads to wobble pairing playing a preeminent role in decoding the translatome

4. iii) We identify nascent chain sequences in the exit tunnel that contribute to sequence-specific pausing iv) We find that ribosome collisions arise from an elongation rate mismatch of proximal ribosomes translating sequences with opposite elongation rates.

5. We hope others use this robust strategy for reliably detecting pausing events even in low coverage data. Our approach may open the way to understand translation dynamics in rare and valuable samples, such as donor tissues or single cell analyses.

1. Check out our latest and exciting MS describing a new class of neurodevelopmental diseases caused by mutations in most subunits of the chaperonin TRiC/CCT. science.org/doi/10.1126/sc… (part 1 of series)

2. Despite its ubiquitous expression, de novo mutations in seven out of the eight CCT-genes led to brain malformations, intellectual disability, and seizures in a total of 22 patients. Thus, insufficient TRiC folding capacity becomes a bottleneck in brain development.

3. From a clinical perspective, these patients with "TRiCopathies" may be at an extreme end of a spectrum, with frequent but less-severe TRiC genetic variants causing milder intellectual disability and seizure phenotypes.

4. The concept of chaperonin function as central in brain development is a new paradigm opening the door to many additional mysteries. Thanks to all: Ingo,  Miriam, Stephen, Florian, Piere for the fun collaboration and to Manu Sharma for the highlight: science.org/doi/10.1126/sc…

A really nice piece on our recent study: med.stanford.edu/news/all-news/…

Check out our MS describing the in vivo cycle of chaperonin TRiC/CCT, in a wonderful collaboration with Martin Beck's lab: nature.com/articles/s4158… 1) The study established TRiC's important function in folding newly translated proteins and defines its ATP-driven cycle

2) The MS also quantified TRiC-Prefoldin cooperation in vivo. Importantly it establishes that closed TRiC engages in specific interactions with quasi-folded substrate folding intermediates in its closed folding chamber, which is clearly NOT an "Anfinsen cage"

3) Two surprises that could only be revealed by cryoET raise new cool future questions (I) It uncovered a new cofactor, PDCD5 which binds to ALL open TRiC complexes (and was missed by biochemical studies) and (II) closed TRiC forms stereotypic clusters of mysterious function.

Closing an unforgettable chapter at Stanford. Grateful for the science, the growth, and the incredible people who shaped this journey—especially Judith, with whom I had the privilege of doing great science. This place and its people will always mean a lot to me. Very excited!

It was a pleasure to participate in the "Protein folding & Chaperones" platform session this morning in #bps2025 sharing our story from the Frydman Lab about TRiC mutations and their link with brain malformations. A session with a nice mix of cool stories focused protein folding