Hofmann_Lab retweeted
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
cell.com/cell/fulltext/S0092…
Hofmann_Lab retweeted
Measure protein deamidation by bacterial secreted proteins? Check out the recent NMR paper. Congratulations to @Rashmi_Agrata
doi.org/10.1002/mrc.70045
Hofmann_Lab retweeted
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.
nature.com/articles/s41594-0…
Hofmann_Lab retweeted
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! nature.com/articles/s41594-0…
Hofmann_Lab retweeted
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! nature.com/articles/s41589-0…
For all ubiquitin, deubiquitinase and chemical biology aficionados:
Here's a preprint from the lab introducing 2 new active DUBs in humans & a unique type of DUB activity one would miss with the widely used panels of free ubiquitin chains.
t.ly/GnRVv
Thread👇(1/10)
Hofmann_Lab retweeted
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.
nature.com/articles/s41467-0…
Hofmann_Lab retweeted
Endlessly fascinating and exciting conference with great discussions #EMBOubiquitin24 ! Can’t wait to get back to the lab with some new ideas…
Hofmann_Lab retweeted
Recent reports implicated USP53 mutations in a hereditary liver disorder in children.
We got interested in USP53 and its homologue USP54 as phylogenetically they are the most diverse USP DUB family members but according to uniprot are supposed to be catalytically inactive.(2/10)
Hofmann_Lab retweeted
DUBS 2023 will bring together leading academic researchers in the DUB/ULP area with their counterparts in biotech and pharma to initiate, and advance collaborative research. Register now and join us on 19-21 June: bit.ly/DUBS-2023
Hofmann_Lab retweeted
🎉 We made it! Our lab's first research paper is out! A big thank you to our collaborators Soung-Hun & Gerbrand, and a special shoutout to my students who made this happen from an empty lab! 🤩
Legionella, a pathogenic bacteria, hinder the host ubiquitin system with "Legionella OTU deubiquitinases (Lot DUBs)." This study unlocks their structure & molecular mechanism. @Donghyuk_Shin_ @yonsei_u life-science-alliance.org/co…
Hofmann_Lab retweeted
Come join us in Edinburgh for the 2023 @BiochemSoc meeting on DUBs! Exciting line up of speakers including @jnpruneda @hw1o9 @Morris_Lab_DSBs @komander_lab @werner_achim @LabHofmann @AnjaBremm @BuhrlageLab #ubiquitin #UBL
Registration now open: bit.ly/DUBS-2023
Hofmann_Lab retweeted
Just published! Our latest review, A Guide to UFMylation, delves into the latest research on the mechanisms & function of this enigmatic #ubiquitin like modifier in cellular homeostasis and human disease @DMillrine @joshuajk2007 @mrcppu
bit.ly/3XwJfxS
Hofmann_Lab retweeted
Announcing the 3rd edition of focussed meeting on DUB mechanisms & therapeutic opportunities Edinburgh 19-21 June, 2023. Exciting line up of speakers. Lots of talk slots for young researchers #ubiquitin #UBL #protease @BiochemSoc
More details coming soon bit.ly/3CZtDe1
Hofmann_Lab retweeted
We recently proposed a classification system for DUB inhibitors based on their mode of action in our review @MolecularCell Happy to see this nomenclature catching on!
Exciting new work from @hw1o9 reveals cool mechanism of a Type IV allosteric inhibitor
biorxiv.org/content/10.1101/…
Hofmann_Lab retweeted
We’ve posted our work on characterising Nsp3 from #SARS-Cov-2 @biorxivpreprint. We find extended Nsp3 is a more active protease compared to PLpro. We engineer nanobodies that bind to and inhibit Nsp3 which will be useful tools to dissect Nsp3 biology.biorxiv.org/content/10.1101/…























