__as_n_ Kinas_s

We aim to understand kinase biology in order to cure human diseases.

[Miratul Muqit @miratul_neuro]

Delighted to share our new study on the mechanism of #PINK1 activation at the #TOM complex. Led by Wale @waleraimi & Hina @mrcppu @UoDLifeSciences in collaboration with @ruferbus & Sebastian Mathea @ASAP_Research Karim Labib @naranson @TDDeego
https://t.co/dC0skcQaG3

[Miratul Muqit @miratul_neuro]

Out Now! Our new preprint of mechanism of #PINK1 activation at TOM complex. Led by Wale @waleraimi & Hina @mrcppu Fantastic collaboration with @ruferbus Sebastian Mathea @ASAP_Research Karim Labib @naranson @TDDeego. #OpenScience click here https://t.co/i8sKK0Ydu9

[Eva Karasmanis @eva_karasmanis]

Another collaborative effort comes together! The Knapp lab creates DARPins targeting LRRK2-one of them is not only a great tool for cryoEM (go @aleschziner lab!), but also disrupts LRRK2 filament formation on microtubules and acts as an allosteric LRRK2 kinase inhibitor in cells

[Robert Fagiewicz @RFagiewicz]

The more European part of our ASAP Team! Thank you @ASAP_Research #CRNLondon2023

@aleschziner @ChasingKinases

[Samara Reck-Peterson @SamReckPeterson]

The LRRK2 kinase is a major drug target for Parkinson’s Disease (PD). These structures visualize different types of kinase inhibitors binding to wildtype and PD mutant versions of LRRK2. Important advance for PD research by our @ASAP_research team.

[__as_n_ Kinas_s @ChasingKinases]

Wow - beautiful summary movie - thank you - always a pleasure working with you!

@Goetheuni @thesgconline @chatterjeedeep

[Andres Leschziner @aleschziner]

We report the first #cryoEM structures of #LRRK2 bound to type-1 and type-2 kinase inhibitors. Great team effort to advance Parkinson’s Disease therapeutics research! #StefanKnapp @ChasingKinases @Marta_Sanz3 @acvillagransu @DedererVerena @ASAP_Research https://t.co/KrKzPbzRVb

[Ivan Đikić @iDikic2]

many thx to Hückmann-Foundation for the support of Visiting Professorships scheme and strengthening research areas of @Goetheuni @IBC2_GU @MPIbp
@RMU_EMTHERA
#ResearchClusterSCALE

[Jeanne Bark @marc_herb]

@aleschziner @biorxivpreprint
Structure of LRRK1 and mechanisms of autoinhibition and activation https://t.co/P5IcWJAQJn

[PROXIDRUGS @proxidrugs]

Amazing progress presented at the #PROXIDRUGS annual meeting. Fantstastic to see our #Cluster4Future being so productive within its first year!🥳
@BMBF_Bund #Clusters4Future #Zukunftscluster

[Biochemical Journal @Biochem_Journal]

📢 New research study from Professor Dario R Alessi and colleagues @mrcppu: Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding. #OpenAccess https://t.co/XW1JAGsQ28

[Kevan Shokat @kevansf]

Two drugs are better than one—blocking drug action in the periphery while maintaining CNS pharmacology (mTOR, Lrrk2 and Her2). #Glioblastoma @bignerdzzy and https://t.co/TfDaZ3irEB @UCSFCancer @HHMINEWS @UCB_Chemistry @MichaelJFoxOrg https://t.co/6BSAn3Jyh1

[Aligning Science Across Parkinson’s @ASAP_Research]

Join UC San Diego professor @aleschziner for this month's @LRRK2_central seminar.

🖋️Register today: https://t.co/aBLd3HDptS

[Ingo Hartung @HartungIngo]

One year ago we received the funding approval for our ProxiDrugs consortium. Academic and industrial partners from the Rhein-Main-Necker region are now studying various innovative ideas in the field of proximity-inducing drugs. We are now looking for a scientific project manager.

[Natalia Jura @JuraLab_UCSF]

In collaboration with the Verba lab and @KroganLab, we present the first structure of a fascinating PEAK3 pseudokinase, captured in complex with 14-3-3, and propose a mechanism by which 14-3-3 regulates PEAK3 signaling. https://t.co/RMtcyPt4uf

[Mohit @mohitasya]

My visa application is stuck with UK immigration for 55 days.Paid email (£2.74/email) queries result in generic responses,paid phone calls get disconnected abruptly without giving a solution.Need to travel to Cavtat next week and need my passport! Nightmare!!!#UKVISADELAY #UKVisa

[__as_n_ Kinas_s @ChasingKinases]

Solving the LRRK jigsaw piece by piece:

Protein kinase C switches on the LRRK1 kinase - simply by phosphorylation.
https://t.co/jcIlcFzMp0

@biochem_journal @asadm96 @chatterjeedeep

[Trends in Biochemical Sciences @TrendsBiochem]

Check out the Review "#Roc, the G-domain of the Parkinson’s disease-associated protein #LRRK2" by Quyen Hoang and colleagues @IUMedSchool.

#GTPase #kinase #allostery #conformationalchange #model #therapeutics

https://t.co/Z3eMiuP6q0

[LRRK2 Central @LRRK2_central]

Inspiring fireside chat about the future of #LRRK2 research at the Biennial International LRRK2 Meeting #BiochemEvent

[LRRK2 Central @LRRK2_central]

Excited to announce preprint from Alessi & Knapp labs describing new kinase activated by PKC isoforms through an unexpected mechanism: https://t.co/PuWHWDUJBN ​#LRRK2 #LRRK1 #PKC @ASAP_Research @LRRK2_central

[__as_n_ Kinas_s @ChasingKinases]

Long-awaited resource!

A global atlas of substrate specificities for the human serine/threonine kinome https://t.co/duEaIjtFfc