Out @MolecularCell from Schulman group @StJudeResearch & @MPI_Biochem: E3 Ub ligase CRL2-KHLDC2 uses a kinetic mechanism and auto-inhibitory self-assembly to avoid targeting non-substrate proteins with degron-like sequence.
https://t.co/IFlQjMJaFr
Work from @LabHalic with @StefanCanzar now @NAR_Open.
Using genome-wide approaches to dissect the pathways that lead to #heterochromatin silencing, they unveil a new mechanism — decreased transcription efficiency, in a pathway that requires CCR4–NOT.
https://t.co/nRR4ybxcQS
Work from @TheBlanchardLab and @WilsonLab2 combines #smFRET and #cryoEM to reveal the mechanism of action of antimicrobial peptide argyrin: ArgB binds EF-G on ribosome and inhibits conformational changes required for translocation and EF-G dissociation.
https://t.co/er1HgfIqhK
Our new manuscript on LRRK2 activation with @zhu_hanwen Francesca and Dario @ASAP@LRRK2_central. We reveal a novel LRRK2 kinase activation mechanism via spatial regulation and protein non-symmetric tetramerization (dimer of asymmetric dimers). See animation (credit @NormanLuo5)
New work from @TheBlanchardLab and the Javitch group reveals new insights into beta-arrestin activation and interaction with GPCR, using the power of #smFRET, now out @CellCellPress, congratulations!
Check out the work here:
https://t.co/90hyisFrbv
Now out @NatureChemistry: work from @TanjaMittag lab in collaboration with @PappulabWashU deciphers the rules in the stickers-and-spacers model that govern phase separation by prion-like low-complexity domains.
https://t.co/SSDtPnVE2t
Out in @CD_AACR: by integrating biophysics, cellular imaging and transcriptomics, Kriwacki, Mullighan & colleagues demonstrate the role of LLPS in leukemogenesis by NUP98 fusion oncoproteins and identify the specific molecular interactions involved.
https://t.co/w7GQVRXZeR
Hi-res ssNMR illuminates structures of antifungal AmB “sponges” consisting of asymmetric head-to-tail homodimers staggered in a clathrate-like lattice with large void volumes similar to the size of sterols. @TarasPogorelov@nmrfam@Illinois_Alma@UWMadison https://t.co/B8oaGwGEXj
Today with @emblebi we’re expanding the #AlphaFold Protein Structure Database to cover UniProtKB/Swiss-Prot (of @uniprot). This includes key proteins of interest that have been manually curated by experts & will more than double the database size to >800k! https://t.co/vtBGmTClG8
More sodium-solute symporters @Nature, now from Lei Chen @PKU1898: #cryoEM structure of human SGLT2 in complex with auxiliary membrane protein MAP17 and inhibitor empagliflozin (used to treat type 2 diabetes).
https://t.co/gqNKqd0NcK
From Feng lab @StanfordMed and @LabSkiniotis:
#cryoEM of 2 human Na+/solute symporters —
SGLT1 (Na+/glucose, apo) and SMCT1 (Na+/monocarboxylates, with substrate) —
provide a trove of functional insights on these important transporters. Out in @nature
https://t.co/PvwJhhRBmW
Looking back at an exciting year: In this month’s editorial, we highlight some of our favorite research of 2021, including Covid-19 treatments, Nobel prizes, AlphaFold and more. Check it out here: https://t.co/9dUQziAtF2
Nature is looking for an editor with expertise in biochemistry, molecular biology and/or structural biology. Check it out, it closes on Dec 15!
https://t.co/wRbfGDlvSd