Hofmann_Lab (@labhofmann) 's Twitter Profile
Hofmann_Lab

@labhofmann

Research group at the University of Cologne

ID: 1282701583948681226

calendar_today13-07-2020 15:41:26

54 Tweet

165 Followers

110 Following

Hofmann_Lab (@labhofmann) 's Twitter Profile Photo

In our new preprint, we show that a Chlamydia-like bacterium (Simkania) has a deubiquitinase repertoire similar to that of Legionella, but using very different DUB classes for the same linkage specificities (e.g. M1, K6). #ubiquitin Universität zu Köln researchsquare.com/article/rs-264…

Donghyuk Shin (@donghyuk_shin_) 's Twitter Profile Photo

🎉 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! 🤩

Biochemical Society (@biochemsoc) 's Twitter Profile Photo

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

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 (@labhofmann) 's Twitter Profile Photo

Our new manuscript on Burkholderia TssM is on bioRxiv. TssM is an interesting bacterial USP-type dubiquitinase effector, which lacks the so-called 'Fingers' Region used by other USPs for #ubiquitin recognition. Our structures show how TssM does the trick biorxiv.org/content/10.110…

Hofmann_Lab (@labhofmann) 's Twitter Profile Photo

Out now in NatComms: A Chlamydia-like bacterium with a deubiquitinase repertoire similar to Legionella, but using new DUB classes for the same linkage specificities (e.g. M1, K6). #ubiquitin Universität zu Köln Cologne Crystallisation facility doi.org/10.1038/s41467…

Hofmann_Lab (@labhofmann) 's Twitter Profile Photo

Now published: We analyzed the structure of the Burkholderia effector TssM with and without ubiquitin. TssM is a divergent member of the USP-type deubiquinases and can recognize #ubiquitin despite the lack of the 'fingers' domain. life-science-alliance.org/content/7/2/e2…

Hofmann_Lab (@labhofmann) 's Twitter Profile Photo

Two PhD positions in our research group! If you are interested to study the molecular mechanisms of necroptotic and pyroptotic cell death - and their relationship to plant cell death, do apply!

Hofmann_Lab (@labhofmann) 's Twitter Profile Photo

N4BP1 functions as a dimerization-dependent linear #ubiquitin reader which regulates TNF signalling nature.com/articles/s4142…

Malte Gersch (@maltegersch) 's Twitter Profile Photo

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)

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 (@labhofmann) 's Twitter Profile Photo

After a long time in the making, our study on bacterial clippases is finally available as a preprint biorxiv.org/content/10.110… These are really fascinating enzymes, for which there will be a ton of applications in studying the #ubiquitin system

Jane Dudley (@jane_dudley_lab) 's Twitter Profile Photo

Endlessly fascinating and exciting conference with great discussions #EMBOubiquitin24 ! Can’t wait to get back to the lab with some new ideas…

Endlessly fascinating and exciting conference with great discussions #EMBOubiquitin24 ! Can’t wait to get back to the lab with some new ideas…
Ole Schmöker (@oleschmoeker) 's Twitter Profile Photo

New Lammers Lab paper out now in Nature Communications!🥳 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/s4146…

Malte Gersch (@maltegersch) 's Twitter Profile Photo

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 Nature Chemical Biology. Congratulations Kim, Kai, and all authors! nature.com/articles/s4158…

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 <a href="/nchembio/">Nature Chemical Biology</a>. Congratulations Kim, Kai, and all authors! nature.com/articles/s4158…
Hofmann_Lab (@labhofmann) 's Twitter Profile Photo

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.

Hofmann_Lab (@labhofmann) 's Twitter Profile Photo

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.