Tzu-Jing Yang
@tzujingyang.bsky.social
Membrane protein biogenesis; MPI of Biophysics
Reposted by Tzu-Jing Yang
Just published! We share an open-source workflow to measure membrane thickness from tomograms, including a tutorial with 3D visualizations. We analyze thickness variations across organelles and reflect on where to define a membrane boundary. @becklab.bsky.social #teamtomo rupress.org/jcb/article/...
November 6, 2025 at 7:38 AM
Just published! We share an open-source workflow to measure membrane thickness from tomograms, including a tutorial with 3D visualizations. We analyze thickness variations across organelles and reflect on where to define a membrane boundary. @becklab.bsky.social #teamtomo rupress.org/jcb/article/...
Reposted by Tzu-Jing Yang
Glushkova, Böhm, & Beck @maxplanck.de develop a publicly available computational method to measure the thickness of biological membranes in cryo-electron tomograms. Analysis of algae & human cells reveals systematic membrane thickness variations within & across organelles rupress.org/jcb/article/...
November 4, 2025 at 5:30 PM
Glushkova, Böhm, & Beck @maxplanck.de develop a publicly available computational method to measure the thickness of biological membranes in cryo-electron tomograms. Analysis of algae & human cells reveals systematic membrane thickness variations within & across organelles rupress.org/jcb/article/...
Reposted by Tzu-Jing Yang
This was a fun new collaboration using selective ribosome profiling to understand how the subunit composition of the ER translocon is tailored by the nascent chain. Congratulations to everyone involved!
www.nature.com/articles/s41...
www.nature.com/articles/s41...
Global analysis of translocon remodeling during protein synthesis at the ER - Nature Structural & Molecular Biology
The authors use selective ribosome profiling to define how and when factors for N-glycosylation and membrane insertion engage and disengage from the core Sec61 translocation channel during biogenesis ...
www.nature.com
October 20, 2025 at 8:08 PM
This was a fun new collaboration using selective ribosome profiling to understand how the subunit composition of the ER translocon is tailored by the nascent chain. Congratulations to everyone involved!
www.nature.com/articles/s41...
www.nature.com/articles/s41...
Reposted by Tzu-Jing Yang
Our first lab paper is out! We identify and solve the first structure of the SND3 translocon involved in fungal membrane protein insertion. Congratulations @tzujingyang.bsky.social, and our colleagues @saumyakm.bsky.social, @hummerlab.bsky.social and Julian Langer. Read more ⬇️ and ➡️ rdcu.be/eNgIO
SNDing proteins into the membrane! Our new publication from @melaniemcdowell.bsky.social ’s group identifies the SND3 protein as a new route for membrane protein insertion! 🍄 📘 Read more here: www.mpg.de/25599408/102... Image: Louise Duever.
October 30, 2025 at 5:42 PM
Our first lab paper is out! We identify and solve the first structure of the SND3 translocon involved in fungal membrane protein insertion. Congratulations @tzujingyang.bsky.social, and our colleagues @saumyakm.bsky.social, @hummerlab.bsky.social and Julian Langer. Read more ⬇️ and ➡️ rdcu.be/eNgIO
Reposted by Tzu-Jing Yang
We discovered how an engineered ribosome arrest peptide (eRAP) acts as a built-in “pause button” to precisely control protein synthesis. eRAP merges two natural stalling systems to stop the ribosome at just the right time — shaping how nascent proteins begin to fold.
academic.oup.com/nar/article/...
academic.oup.com/nar/article/...
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academic.oup.com
October 15, 2025 at 2:28 AM
We discovered how an engineered ribosome arrest peptide (eRAP) acts as a built-in “pause button” to precisely control protein synthesis. eRAP merges two natural stalling systems to stop the ribosome at just the right time — shaping how nascent proteins begin to fold.
academic.oup.com/nar/article/...
academic.oup.com/nar/article/...
Reposted by Tzu-Jing Yang
Excited to share our Nature Communications paper 🎉 rdcu.be/eK7wG
We uncovered by cryoEM how the human 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. #cryoEM
Structural basis of K11/K48-branched ubiquitin chain recognition by the human 26S proteasome
Nature Communications - K11/K48 branched ubiquitin chains regulate protein degradation and cell cycle progression. Here, the authors report the structural basis of how such a branched ubiquitin...
rdcu.be
October 15, 2025 at 10:16 AM
Excited to share our Nature Communications paper 🎉 rdcu.be/eK7wG
We uncovered by cryoEM how the human 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. #cryoEM
Reposted by Tzu-Jing Yang
Proud to share our first lab pre-print: “SND3 is the membrane insertase within a fungal multipass translocon” where @tzujingyang.bsky.social solved the structure of a ribosome-associated SND3-translocon complex involved in ER membrane protein insertion ➡️ doi.org/10.1101/2025...
July 12, 2025 at 12:49 AM
Proud to share our first lab pre-print: “SND3 is the membrane insertase within a fungal multipass translocon” where @tzujingyang.bsky.social solved the structure of a ribosome-associated SND3-translocon complex involved in ER membrane protein insertion ➡️ doi.org/10.1101/2025...