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PhD student in F.U.Hartl group - MPI of Biochemistry | Molecular cell biology | Single particle tracking | Proteostasis | Chaperone mediated protein folding
Niko Dalheimer






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New from our lab @crick.ac.uk. Nascent proteins emerge from the human ribosome into a cytosol packed with hundreds of different molecular chaperones. Which chaperones recognise specific nascent chains, and what dictates their binding preferences? www.biorxiv.org/content/10.6...
Nature research paper: Single-molecule dynamics of the TRiC chaperonin system in vivo go.nature.com/4qZM3Cn
The new publication "Stages of biomolecular condensate formation in pro-β-carboxysome assembly" from the Manajit Hayer-Hartl team is out at Nature Plants! ❕ Publication: www.nature.com/articles/s41... #Rubisco #carboxysome #cyanobacteria
"Single-molecule dynamics of the #TRiC #chaperonin system in vivo" is out @nature.com. ❕Publication: www.nature.com/articles/s41... ❕Press Release: www.biochem.mpg.de/live-broadca... Authors: @rongqinxiaoxiao.bsky.social, @niko-dalheimer.bsky.social, @mamueller.bsky.social, F.-Ulrich Hartl
Our new paper's out: FidlTrack—structure-aware single-particle tracking benchmarks/boost SPT fidelity With it we resolve with sub-organelle res. e.g. BACE1 amyloidogenic APP cleavage #Alzheimers, ER exit events, map nanobody binding in realtime in ER/organelles 🔬🧠#SingleMolecule rdcu.be/e3Ris
All lights on protein folding 💡 Out @nature.com , @niko-dalheimer.bsky.social & @rongqinxiaoxiao.bsky.social from the Hartl lab at @maxplanck.de Institute of Biochemistry developed single-particle tracking in living cells to study the dynamics of co-translational protein folding #sciart #scicomm
Finally out in @Cellcellpress! Proteins with long IDRs are prone to misfolding during protein synthesis. This is prevented by mRNA 3′UTRs that act as mRNA-based IDR chaperones. www.cell.com/cell/fulltex...
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Single-particle tracking experiments in intact cells reveal dynamic co- and post-translational interactions of the TRiC–PFD chaperonin complex with client proteins during in vivo protein folding.
go.nature.com
Single-molecule dynamics of the TRiC chaperonin system in vivo - Nature
Highly conserved mRNA 3′ UTRs act as co-translational chaperones for intrinsically disordered regions (IDRs), preventing inter-domain misfolding and enabling biogenesis of fully active proteins.
www.cell.com
mRNA 3′ UTRs chaperone intrinsically disordered regions to control protein activity
David Balchin
Nature
Max Planck Institute of Biochemistry
Max Planck Institute of Biochemistry
Carboxysomes are cyanobacterial CO2-concentrating compartments with a proteinaceous shell. The elucidation of the role of the shell adaptor protein ApN in stepwise β-carboxysome assembly will aid the ...
www.nature.com
Stages of biomolecular condensate formation in pro-β-carboxysome assembly - Nature Plants
Avezov lab
Marzia Munafò
Christine Mayr