Happy to see our work on defining a dependency map of short linear motifs out. We use base editing screens to install more than 80000 mutations into SLiMs in more than 4000 proteins to determine their contribution to cell fitness. nature.com/articles/s41594-0…
Looking forward to a great line up of speakers at #CRISPRMED26 in Copenhagen: linkedin.com/pulse/crisprmed…
Come join us for some excellent science in the heart of Copenhagen - still places available
We are very excited to open the registration for the upcoming @EMBOevents on Chromosome Segregation and Aneuploidy in beautiful Stresa!!! You can find all the relevant info at meetings.embo.org/event/25-a…
Hope to see many of you in a few months!! 🧬🔬😍
#ChromoPloidy25
Dear colleagues, we have a postdoctoral opening financed by the ERC_AdG project INTETOOLS @ERC_Research. Retweets much appreciated !!!
see the link below for details 👇
candidate.hr-manager.net/App…
Deadline for applications 6-11-24
Our latest work from lab member jimmy Ly! This fundamentally changed the way we see mitosis. Massive rewiring of translational control. There is something for everyone and an amazing mechanism. Check it out.
Cells make variants of thousands of proteins. These variants are not produced indiscriminately, but rather through precise regulatory mechanisms that can meet rapidly changing needs of the cell. New work from @iaincheeseman's lab in @Nature: wi.mit.edu/news/elegant-swit…@MITBiology
We (@alexholehouse and @ProteinMagnus) started IDPSeminars in May 2020. It has been a wonderful platform to host an incredible array of international science. What began as a pandemic alternative to conferences has blossomed into a consistent and supportive community.
Just a few hours into the new year, and the first paper of the year involving our lab has been published🥳
Read about the substrate specificity of the B55 subunit of PP2A and its inhibitor we designed.
Great collaboration with @NilssonLabCph, @KettenbachLab and @torbenheick labs!
Using this inhibitor we find that it blocks the function of the NEXT complex, a complex involved in nuclear RNA quality control. Consistent with this we find that PP2A-B55 directly binds the RBM7 component of the complex.
An interesting observation for those interested in PP2A-B55 biology is that PME1, the enzyme that removes the C-terminal methyl group on the catalytic subunit causing inactivation of PP2A-B55, contains an N-terminal helix binding directly to B55.
Great work from the @duxin_lab - happy that we could make a contribution with base editing screen and some none froggy experiments:-)
nature.com/articles/s41594-0…
Would you see your name in this list of illustrious speakers?
Then we need your abstract before October 1st! We will close the abstract submission and select attendees for our wonderful meeting on biomolecular condensates on this date.
events.au.dk/biomolecular-co…
Have you ever wondered how many of the human SLiMs are required for cell viability? We mutated them all to find out in another extremely fun collaboration with the @NilssonLabCph group. The results are now on bioRxiv biorxiv.org/content/10.1101/…. Check it out!