Niels Schneberger

I am thrilled to share that I was selected for an @embo.org Postdoctoral Fellowship. Soon, I will join the lab of @mfwhite2.bsky.social to study prokaryotic immune mechanisms. Super exciting!

YouTube video by Exzellenzcluster ImmunoSensation Spot on Science, Episode#12, Sophie Binder / Self-regulation of protease CalpL by nuclease activity

🎬 Episode 12 of #SpotOnScience is out!

In this episode, Sophie Binder from the group of Gregor Hagelücken introduces her work "The SAVED domain of the type III CRISPR protease CalpL is a ring nuclease".

Check out the episode here: www.youtube.com/watch?v=cDTs...

#science #research #immunology

It was a pleasure to present my #TRAP #transporter work at this year's #BFB annual meeting.

CARD domains mediate anti-phage defence in bacterial gasdermin systems - Nature Caspase recruitment domains (CARDs) are present in defence systems that protect bacteria against phage, where the bacterial CARD domain is essential for protease-mediated activation of bacterial gasdermins that promote cell death.

Nature research paper: CARD domains mediate anti-phage defence in bacterial gasdermin systems

https://go.nature.com/3CvoD3W

Out today @ Science: TIR signaling activates caspase-like immunity in bacteria

We report a new immune signaling molecule: N7-cADPR. Produced by phage-induced TIRs and activates a defensive bacterial caspase

Congrats Francois Rousset, Ilya Osterman and coauthors!

www.science.org/doi/10.1126/...

Showing how the genes relevant to diseases can be identified more easily (clockwise from top left): Alexander Hoch, Katja Blumenstock, Marius Jentzsch, Caroline Fandrey und Prof. Jonathan Schmid-Burgk. - Copyright Felix Heyder / University Hospital Bonn

Colored nuclei reveal cellular key genes
The identification of genes involved in diseases is one of the major challenges of biomedical research. Researchers at the University of Bonn and the University Hospital Bonn (UKB) have developed a metho...
weiterlesen

BBSRC NWD: Structural Proteomics to spatially resolve interactions with mechanosensitive synaptic scaffold proteins at University of Liverpool on FindAPhD.com PhD Project - BBSRC NWD: Structural Proteomics to spatially resolve interactions with mechanosensitive synaptic scaffold proteins at University of Liverpool, listed on FindAPhD.com

*Fully funded PhD position available in the lab*

We will use structural proteomics to map the mechanosensitive interactions of talin in dendritic spines and how they change during long term potentiation.

Please share, and email for details :)

www.findaphd.com/phds/project...

Atomic structures of biological molecules have never been so available and ubiquitous, but this raises questions as to how they are made appropriately accessible for optimal use t.co/RTx2WLxR0W

Safer, nonradioactive staining alternatives for electron microscopy are introduced, simplifying sample preparation, reducing costs and making structural biology more accessible to researchers globally #NegativeStaining #ElectronMicroscopy doi.org/10.1107/S205...

GitHub - martinpacesa/BindCraft: User friendly and accurate binder design pipeline User friendly and accurate binder design pipeline. Contribute to martinpacesa/BindCraft development by creating an account on GitHub.

The link to the github and colab notebook remains unchaged, we now however include a link to the design models and sequences which you can download here:
github.com/martinpacesa...
doi.org/10.5281/zeno...

Registration now open for the EMBO Workshop: Immune System of Bacteria !!!!

www.sisb2025.conferences-pasteur.org/home

Joins us in Institut Pasteur, Paris, April 8-10th.

Substrate translocation and inhibition in human dicarboxylate transporter NaDC3 - Nature Structural & Molecular Biology The authors show cryo-electron microscopy structures of the human high-affinity sodium–dicarboxylate cotransporter, responsible for dicarboxylate import into the cell, in complex with various substrat...

Amazing work capturing NaDC3 in multiple states and with various substrates/inhibitors!

Congrats Yan Li, Da-Neng Wang, Joe Mindell, and Bill Rice!!

www.nature.com/articles/s41...

#CASP16 results are in! Template-based VFold seems to be lead method for nucleic acid structure prediction! AlphaFold2 and 3 still seem to be best methods for protein monomer and complex prediction.

A new class of binding protein-dependent solute transporter exemplified by the TAXI-GltS system from Bordetella pertussis Tripartite ATP-dependent periplasmic (TRAP) transporters are widespread in prokaryotes, but absent in eukaryotes, and facilitate the uptake of a wide variety of substrates. TRAP transporters are compo...

I’m very excitement to share a preprint of some very recent work from our lab on our continuing odyssey into the very interesting world of TAXI TRAP transporters.
tinyurl.com/4a7fra4x
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A tuneable minimal cell membrane reveals that two lipid species suffice for life Nature Communications - All cells are encapsulated by a membrane of complex lipidic composition, and understanding the roles of different lipids in membrane function is experimentally challenging...

All cells are encapsulated by a membrane of complex lipidic composition, right?

Not anymore! @JamesSaenz.bsky.social et al. show that a ‘minimal’ bacterial cell only needs 2 lipid species

#microNatComms #Microbiology #CellBiology #lipids

Read the paper:
www.nature.com/artic...

Congratulations to @philipphendricks.bsky.social for winning the #PosterPrize at this year's #ClusterScienceDays.
Way to go Jimbo!

Allosteric substrate release by a sialic acid TRAP transporter substrate binding protein - Communications Biology Biophysical and structural characterization of the TRAP transporter SBP SiaP in complex with a nanobody provides insights into an allosteric mechanism of inhibition.

We identified a #VHH antibody that allosterically inhibits sialic acid binding by the #TRAP transporter #SBP VcSiaP.
Thanks to the team including: @philipphendricks.bsky.social @scbinder.bsky.social @gavinhthomas.bsky.social @gha14.bsky.social
Read the full story here:

doi.org/10.1038/s420...