🚨One probe. 🧪One assay. 👯Two answers. Our new fluorescent platform identifies prenylation inhibitors and reveals how they work, streamlining both screening and mechanistic studies! Full text here: www.tandfonline.com/doi/full/10.... @telavivuni.bsky.social #MedicinalChemistry #DrugDiscovery

A multipurpose probe for identification and mechanistic analysis of prenylation inhibitors

Protein prenylation is a critical post-translational modification that controls many cancer-related signalling pathways and represents an important therapeutic target currently lacking effective ph...

tandfonline.com

🚨One probe. 🧪One assay. 👯Two answers. Our new fluorescent platform identifies prenylation inhibitors and reveals how they work, streamlining both screening and mechanistic studies! Full text here: www.tandfonline.com/doi/full/10.... @telavivuni.bsky.social #MedicinalChemistry #DrugDiscovery

A multipurpose probe for identification and mechanistic analysis of prenylation inhibitors

Protein prenylation is a critical post-translational modification that controls many cancer-related signalling pathways and represents an important therapeutic target currently lacking effective ph...

tandfonline.com

Correct DOI here: doi.org/10.1002/pro....

Use of biomolecular emulator for characterizing flexible proteins by small‐angle x‐ray scattering

Flexible proteins populate heterogeneous conformational ensembles that are essential for their function. Small-angle x-ray scattering (SAXS) is widely used to study protein structure in solution and ...

doi.org

Excited to share our new paper in @proteinsociety.bsky.social 🎉 We combine #BioEmu and SAXS ensemble optimization to characterize protein conformational heterogeneity, bridging AI-generated ensembles and experimental data. doi.org/10.1002/pro.70… #SAXS #MachineLearning

Excited to share our new paper in @proteinsociety.bsky.social 🎉 We combine #BioEmu and SAXS ensemble optimization to characterize protein conformational heterogeneity, bridging AI-generated ensembles and experimental data. doi.org/10.1002/pro.70… #SAXS #MachineLearning

Hi!

Proud of this collaboration - our third paper on cisPT! Loved this one the most: a beautiful mix of high-res, low-res, and computational approaches. Grateful for this long-standing, truly fruitful team effort. Congrats to everyone!

HaitinLab@haitinlab.bsky.social · 8mo ago

🚨It's finally out!🥂 | A few years after solving the structure of human cis-PT, we now tackle its dynamics in @NatureComms , revealing that a conserved interfacial loop serves as an allosteric hub, communicating with the active site to regulate catalysis. rdcu.be/eShjl

🚨It's finally out!🥂 | A few years after solving the structure of human cis-PT, we now tackle its dynamics in @NatureComms , revealing that a conserved interfacial loop serves as an allosteric hub, communicating with the active site to regulate catalysis. rdcu.be/eShjl

Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex

Nature Communications - This study shows how the NgBR subunit controls the activity of human cis-prenyltransferase, a key enzyme for protein glycosylation. Combined experimental and computational...

rdcu.be

A huge Thank You to all the collaborators who contributed to this fun project: Udi Qimron, @haitinlab.bsky.social, @bursteinlab.bsky.social, and congrats to the first author @tridibmahata.bsky.social ! An open question remains - where will this be published? 😏

two men are sitting next to each other and one of them is saying teamwork

ALT: two men are sitting next to each other and one of them is saying teamwork

media.tenor.com

Great collaboration (as always)! And very funny story how HDX and native MS complement each other and reveal details about ions, substrates and mutations. We enjoyed this ride!

HaitinLab@haitinlab.bsky.social · last yr.

Excited to share our new paper in @febsj.bsky.social! 🎉 We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation 🔗 doi.org/10.1111/febs... @peterslab1.bsky.social

Excited to share our new paper in @febsj.bsky.social! 🎉 We show how a #MYELOMA-linked GGPPS mutation tweaks hexamerization, substrate binding and product inhibition, revealing an unexpected layer of protein prenylation regulation 🔗 doi.org/10.1111/febs... @peterslab1.bsky.social

FEBS Press

Geranylgeranyl diphosphate synthase (GGPPS) plays a key role in multiple myeloma biology. Using crystallography, mass spectrometry, and fluorescence spectroscopy, this study shows that a somatic mult...

doi.org

HaitinLab@haitinlab.bsky.social · 2y ago

🚨New preprint alert! Wonder how a cancer-associated mutation in GGPPS impacts hexameric stoichiometry, substrate affinity, and product inhibition? Our results shed light on a novel regulatory mechanism in protein prenylation bit.ly/3ZR7w47 #MultipleMyeloma

How does a cytoplasmic enzyme make a membrane product? 🤔🧬 We found that a hydrophobic residue cluster helps the human cis-prenyltransferase feed its product into the ER membrane! MD simulations + fluorescence = mechanistic insight 👇 🔗https://doi.org/10.1002/pro.70167

But your results are 🔥 as usual!

elmo from sesame street is standing in front of a wall of flames

ALT: elmo from sesame street is standing in front of a wall of flames

media.tenor.com

peterslab (BIOCEV,CZ)@peterslab1.bsky.social · last yr.

This was literally cool work. ❄️ We locked ourselves in the cold room to slow down the HDX and catch even the fastest dynamics. Bonus: It turns out you can manually capture a 2-second exchange reproducibly (next time we set up the quench flow!).

Whenever we get a bioRxiv alert, we'are always curious to see what it brings. This time, the timing couldn’t have been better - a very pleasant surprise! 😄 biorxiv.org/content/10.1... www.biorxiv.org/content/10.1...

💃🕺Happy to share a team effort to uncover the molecular "dance" behind human cis-prenyltransferase regulation!🔬🧬 @peterslab1.bsky.social @AlbGiacomello #Biochemistry #StructuralBiology @TAUMedFaculty @of_sagol biorxiv.org/content/10.1...

Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex

Human cis-prenyltransferase (hcis-PT) synthesizes long-chain isoprenoids essential for N-linked protein glycosylation. This heteromeric complex comprises the catalytic subunit DHDDS and the regulatory...

biorxiv.org

🥳

ChemRxiv Bot@chemrxivbot.bsky.social · 2y ago

Identifying and Quantifying Membrane Interactions of the Protein Human cis-Prenyltransferase Authors: Duncan Boren, Shiri Kredi, Ekaterina Positselskaya, Moshe Giladi, Yoni Haitin, Josh Vermaas DOI: 10.26434/chemrxiv-2024-3gh6x

🚨New preprint alert! Wonder how a cancer-associated mutation in GGPPS impacts hexameric stoichiometry, substrate affinity, and product inhibition? Our results shed light on a novel regulatory mechanism in protein prenylation bit.ly/3ZR7w47 #MultipleMyeloma

A somatic multiple myeloma mutation unravels a mechanism of oligomerization-mediated product inhibition in GGPPS

Protein prenylation regulates the cellular localization of small GTPases and is pivotal for multiple myeloma (MM) pathology. Geranylgeranyl diphosphate synthase (GGPPS), synthesizing a prenylation moi...

bit.ly

1/ How do animals integrate different forms of learning? Our @eyalrozenfeld.bsky.social new study in Science Advances shows that active mechanisms prevent the co-formation of competing memories. Here’s what we found! 🧵👇 science.org/doi/10.1126/...

Long overlooked but significant! This is the post-Cys specificity in post-proline cleaving enzymes like AnPEP or neprosin. Good work Zuza and the team!🎉🔥 pubs.acs.org/doi/10.1021/... (illustration IG:kuba_draws_science)

Hi!