Our paper on bacterial clippases is now out in @MolecularCell. These really interesting enzymes can make deconjugation of #ubiquitin irreversible. Thanks to @UniCologne and @C2fBiochemistry for support.
https://t.co/78lxodHhQa
Proud to share The E3-ome
A true collaborative effort to unify the human E3 ligase landscape, and create a shared foundation for the field
#Ubiquitin#E3Ligases@WEHI_research
https://t.co/yK0jtcCp7P
I am deeply saddened learning that my scientific hero Amos Bairoch has recently passed away. He will be remembered as the mastermind behind the SwissProt and many other endeavours in protein bioinformatics. There is a tribute web page at https://t.co/ku46u3iQVG
For all #ubiquitin aficionados out there: Our new study, where we used an #alphafold based screen and found a new class of plant-specific DUBs, which cleave K63 chains and interfere with endocytosis at the plasma membrane. https://t.co/274nqCYDeO
New Parkinson’s disease paper:
Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of USP30 and a framework for DUB ligandability - published by @MalteGersch group @maxplanckpress in @Nature Struct. & Mol. Biol.
https://t.co/VoRJybRUUI
Excited to share that our work on Parkinson's target USP30 has been published in Nature Structural & Molecular Biology! By combining DUB-domains onto USP30, we for the first time achieved crystallization with a small molecule (NK036) without Nanobodies! https://t.co/Pt2hy4WbqT
Our paper on bacterial clippases is now out in @MolecularCell. These really interesting enzymes can make deconjugation of #ubiquitin irreversible. Thanks to @UniCologne and @C2fBiochemistry for support.
https://t.co/78lxodHhQa
Congratulations, great paper! But what makes you think that this is a CARD and not just any death-fold domain? pyrin and DEDs can also activate caspases and invertebrates use all kinds of death-fold domains for that purpose! I don't think this one really should be called CARD.
We previously showed that bacteria encode the pore-forming protein gasdermin and that it defends against phage infection
https://t.co/bnIAyYlqQK
BUT the mechanism by which the gasdermin system defends bacteria against phage remained unknown.
Great paper, but sorry, this is *not* a CARD domain! It is a 6-helix death fold domain for sure, but there in no evidence provided that it belongs to the CARD subfamily. It might have (convergently?) acquired a similar function as mammalian caspase-associated CARDs. Just saying.
Our paper out @Nature: CARD domains mediate anti-phage defense in bacterial gasdermin systems
CARDs are essential for caspase recruitment in inflammasome activation. We now find them in bacterial immune systems
Congrats @TanaWein! Thanks Kranzusch lab!
https://t.co/yWUj5ZMjjO
Very excited to share that our manuscript on the "Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53" was published today at Nature Chemical Biology @nchembio. Congratulations Kim, Kai, and all authors! https://t.co/YTV5td5koG
New Lammers Lab paper out now in @NatureComms!🥳
We reveal high functional diversity within bacterial deac(et)ylases by systematic functional/structural characterization.
This is Leonies PhD project and I’m grateful to have contributed to this great work.
https://t.co/UbAY45Hl5H