Tzu-Jing Yang
@tzujingyang.bsky.social
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Membrane protein biogenesis; MPI of Biophysics
reposted by
Tzu-Jing Yang
Desislava Glushkova
10 days ago
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/...
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reposted by
Tzu-Jing Yang
Journal of Cell Biology
12 days ago
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/...
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reposted by
Tzu-Jing Yang
Keenan Lab
27 days ago
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...
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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 ...
https://www.nature.com/articles/s41594-025-01691-6?utm_source=bluesky&utm_medium=social&utm_campaign=nsmb
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reposted by
Tzu-Jing Yang
Melanie McDowell
17 days ago
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
add a skeleton here at some point
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reposted by
Tzu-Jing Yang
about 1 month ago
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/...
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Validate User
https://academic.oup.com/nar/article/53/19/gkaf978/8285789
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reposted by
Tzu-Jing Yang
about 1 month ago
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
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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...
https://rdcu.be/eK7wG
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reposted by
Tzu-Jing Yang
Melanie McDowell
4 months ago
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...
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