A tour de force integration of #cryoEM, #UbAQUA, #XLMS, and #CRISPRCas9 reveals how the human proteasome decodes branched ubiquitin chains.

It has been a long but incredibly valuable journey, filled with ups and downs, culminating in an exhausting publishing process. However, thanks to the tremendous efforts of all the coauthors, our publication is finally out!

If you're curious about how cells quickly eliminate misfolded proteins produced under proteotoxic stress or during cell cycle progression, check out our latest article in @NatureComms https://t.co/LPkcLmvrr5

This is how is looks like in 3D animation https://t.co/HmfxJptqir Credit: @PDraczkowski

What a day! We published two papers describing the lives of proteins from Alpha https://t.co/Jd3tWEktbZ to Omega https://t.co/y4BfTJk0B5 Seeing these processes through the lens of structural biology is so satisfying

We discovered how an engineered ribosome arrest peptide (eRAP) acts as a ���pause button” to precisely control protein synthesis. eRAP merges two natural stalling motifs to stop the ribosome at just the right time — shaping how nascent proteins begin to fold

@PDraczkowski serendipitously found the K11/K48 branch, which is confirmed by Ub-AQUA and Ub-clipping. Amazing support from our #cryoEM and #proteomics MS core at @AcademiaSinica

Excited to share our Nat Comm paper https://t.co/mAANwcSfqf We uncovered by cryoEM how the proteasome recognizes branched K11/K48 ubiquitin chains through a new K11-binding site in the RPN2 subunit, revealing how the proteasome precisely identifies targets for rapid turnover.

Good start of year 2025 with the last publication from my postdoc work where we dissected the role of individual domains in amyloidogenic behavior and soluble toxicity of a light chain associated with AL amyloidosis recently accepted in @JMolBiol 10.1016/j.jmb.2025.168958

Combining SAXS, MD simulations and HDX-MS, we identified a new conformational (H) state in AL LCs. This state could be a better target of LC stabilizers. In @eLife: A conformational fingerprint for amyloidogenic light chains https://t.co/jS4QaT0DDh @stericagno @asibc512

Very pleased to know that our recent work on hCoV-229E S:hAPN recognition has been highlighted by Nature Communications alongside the work of the newly minted Nobel Prize laureate David Baker

We are thrilled to welcome @MakotoShirakaw2 joining @IPMBSinica as a new PI in this fall. Look forward to exciting research expanding our plant development groups

@IPMBSinica summer undergraduate internship program is now open for applications! 🔗 Apply here: https://t.co/pxT8gZU6cd 📆 Deadline: April 30, 2025

We used cryoEM and mass spectrometry glycoproteomics plus GlycoSHIELD to determine the molecular structure of human coronavirus 229E spike protein in complex with its human receptor, hAPN in a 6:2 binding stoichiometry. https://t.co/Cqtc1eV1eQ

@PDraczkowski Here is a more dynamic view of how the K11/K48-branched ubiquitin chain is recognized by the proteasome https://t.co/HmfxJptqir

Here is how the K11/K48-branched ubiquitin chain looks like on the 26S proteasome. And a K11-K48 alternating linkage from proximal ubiquitin! Kudos to @PDraczkowski

Our preprint on the first glimpse of how the human proteasome recognizes a K11/K48-branched ubiquitin chain is out. This work reveals a new multivalent ubiquitin binding mode by the proteasome that could serve as priority checkin signal for proteolysis. https://t.co/Sk2ERBDb9B

The 2024 Franco-Taiwanese Scientific Grand Prize was presented to Danny Shang-te Hsu, deputy director of the Institute of Biological Chemistry at Taipei City-based Academia Sinica, and Cyril Hanus, research fellow at the Institute of Psychiatry and Neuroscience of Paris in Taipei

Happy to share our work on conformational states of amyloidogenic light chains published as preprint in eLife https://t.co/yj5nbgqIv8 Thanks to reviewers for doing great job. We will revise soon to make paper more impactful 💪 carlo camilloni @stericagno @asibc512

Check out our latest invited review published in @FrontiersIn Biophysics explaining why dynamics in deubiquitinase (DUBs) enzymes matter more than their static structures for function and pathological consequences. Check https://t.co/6OYsGLQdEG with @asibc512