Happy to share my first adventure in #TeamTomo in collaboration with the talented @inaharasimov.bsky.social. It was a fun experience experience with a lot of learning along the way.
Posts by Haselbach Lab
Excited to share our work on the structure and function of cytoplasmic lattices within mouse embryos. A collaborative effort with @niakanlab.bsky.social and work led by @kashishsingh.bsky.social and @inaharasimov.bsky.social . It is now out on BioRxiv: www.biorxiv.org/content/10.6...
The @natsmb.nature.com March issue is out! Though always interested in proteostasis, in 2026 we have published and will continue to do so relevant content. Our editorial www.nature.com/articles/s41... recaps why the processes and mechanisms of proteostasis continue to interest us.
You asked, we listened. Millions of AI-predicted protein complex structures are now available in the #AlphaFold Database.
This spans homodimers from 20 of the most studied species, including humans, as well as the World Health Organization’s priority pathogens list.
www.ebi.ac.uk/about/news/t...
Learn more about the collaboration possibilities offered at Vienna BioCenter as Victoria Deneke shares her insights as a Postdoc at the Research Institute of Molecular Pathology.
The VIP³ PostDoc Program call is open – apply now! training.vbc.ac.at/post-docs/vi...
#VBCPostDoc
Our Spring call is now open with over 30+ fully funded positions in the life sciences. Want to know more? Join our Info Session on 26 March, 1600 (CET). Register now: www.vbcphd.at
Institute of Molecular Biotechnology, Max Perutz Labs Vienna, IMP, Gregor Mendel Institute of Molecular Plant Biology
Welcome to the vbc and the wonderful Vienna cryo EM community
Review from Fia B. Larsen in @rhp-lab.bsky.social with everything you always wanted to know about proteasomal control of transcription factors (but were afraid to ask about)
Proteasomal control of transcription factors: mechanisms, regulation and dysregulation.
doi.org/10.1007/s000...
A consortium of group leaders from IMP, IMBA (Vienna BioCenter) and ISTA has been awarded an FWF Emerging Fields grant to study how germ cells safeguard and pass on genetic information across generations.
Congrats Leo!
#pictureofthemonth: March shows a “Cross-section” of the endoplasmic reticulum, a kind of membrane-labyrinth, using cryo-electron microscopy.
More: www.biochem.mpg.de/plitzko
March – Calendar of @mpiforbi.bsky.social and @mpibiochem.bsky.social
📸 Illustration by Jürgen Plitzko & Sven Klumpe
Job opening for Research Group Leader in Structural Studies at MRC Laboratory of Molecular Biology, focusing on macromolecular structures.
Are you a structural biologist pushing the boundaries of molecular science with an ambitious research programme?
Join our Structural Studies Division as a tenure-track Group Leader, with core funding, world-leading facilities & enthusiastic colleagues.
Apply by 16 MAR
www.nature.com/naturecareer...
SAVE THE DATE: Ubiquitin & Friends Symposium 2026 on April 29-30 or even better, sign up now: lnkd.in/eEQmaCYT
It takes place at Van Swieten Hall, 1090 Vienna & is organized by the SFB Targeted Protein Degradation (incl. numerous research groups at Vienna BioCenter)
@sfb-tpd-vienna.bsky.social
We‘re looking for a motivated Master student to join our team!
Do you want to optogenetically control metabolic activity to see how metabolism affects patterning and morphogenesis? 💡🧫🧬🔬
Then please apply!
#optogenetics #metabolism #devbio #hESCs
Please RT. Thank you!🙏
Please spread the word: the Structural Studies Division @mrclmb.bsky.social is looking for a new tenure-track, independent group leader with an exciting plan in any area of Structural (Molecular & Cell) biology, in discovery biology and/or methods development. 🥳
mrc.tal.net/vx/mobile-0/...
Our paper is out in @natcomms.nature.com! APOBEC3s drive mutagenesis in cancer. We uncover a novel pathway keeping them in check. The key is APOBEC3 binding of cellular RNAs, which simultaneously controls their nuclear localization and shields them from degradation.
Read it here: rdcu.be/e4qaa
This work was spearheaded by @hannabrunner.bsky.social and was again a great collaboration with @johanneszuber.bsky.social. It features a saturation mutagenesis screen, a cryo structure of the import complex and in-vitro reconstitution of the process
In the nucleus the importins are released and Akirin2 is degraded by the proteasome itself.
It shows how the proteasome is bound by Akirin2 in the cytoplasm. This then recruits the importin IPO9 and further Akirin2 dimers. All Akirin2 protomers will then bind canonical importins, leading to clustering of importins on the proteasome surface enableing the transition through he nuclear pore.
The video shows how how the proteasome binds Akirin2 dimers in the cytoplasm. These recruit the importin IPO9 as well as the further Akirin2 dimers. Each Akirin2 dimer will also bind canonical importins leading to importin clustering. This in turn enables the passage through the nuclear pore
Nuclear transport of the proteasome!
And a new paper from the lab. A follow up to a previous study in which we elucidate the mechanism of the nuclear transport. Read the full story: www.nature.com/articles/s41...
A near-complete map of human cytosolic degrons and their relevance for disease
We measured degron potency of >200,000 30-residue tiles from >5,000 human proteins, and trained a model to predict degrons from sequence
Led by @vvouts.bsky.social in @rhp-lab.bsky.social
doi.org/10.1126/scia...
Great story from our neighbours at the university of Vienna. We are that we could contribute to this.
Please share!
My group at @zmbp-tuebingen.bsky.social is offering a post-doctoral position (4 years). We look for a structural biologist with experience in Cryo-EM/Cryo-ET to investigate the mechanisms of host invasion by pathogenic fungi. Deadline February 28th!
uni-tuebingen.de/universitaet...
Thank you Ahmad
Check out our new paper in @natcomms.nature.com .com where we used #cryoEM together with biochemical and mutational analyses investigated the cotranslational protein folding by Ssb in yeast.
Publication: doi.org/10.1038/s41467-025-67685-6
Check below for the cryoEM centric feed. 👇
Formation & function of #MembranelessOrganelles! #CryoET structures of #proteasome storage granules inside cells!
Read our paper @cp-cell.bsky.social!
❕Publication: doi.org/10.1016/j.ce...
❕Press Release: www.biochem.mpg.de/en/pressroom
@uoftmedicine.bsky.social
@erc.europa.eu #UPSmeetMet
New work from our Haselbach lab with collaborators captures ribosomes 𝘮𝘪𝘥-𝘣𝘶𝘪𝘭𝘥 and reveals a flexible, modular strategy behind their assembly, rather than a strict assembly line.
Published in _Nucleic Acids Research _👉 https://doi.org/10.1093/nar/gkag036