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cristianrocharoa.bsky.social

@cristianrocharoa.bsky.social
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EMBL Events @events.embl.org · 25/09/2026
Join #EMBOinsitu if you want to identify the biological questions that can currently be addressed through in situ structural biology and explore future opportunities and challenges for the field 🔬 Reminder to submit your abstract by 3 Nov! s.embl.org/iss27-01-bl
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pilarcossio.bsky.social @pilarcossio.bsky.social · 30/09/2026
*Job alert*: Postdoc position at the Flatiron Institute to work on biophysical inference and cryo-EM. ❄️ 🔬Applications are welcome! apply.interfolio.com/193799
apply.interfolio.com
Apply - Interfolio {{$ctrl.$state.data.pageTitle}} - Apply - Interfolio
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Giovanni D’Angelo @giodang.bsky.social · 23/09/2026
#lipidtime: It's a lipid universe. Today in Nature we publish the Lipid Brain Atlas, the first map of membrane lipid composition across the entire mouse brain, a layer of organisation that cell-type and transcript maps had left out. #lipidomics #neuroscience #BrainAtlas
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Martin Pacesa @martinpacesa.bsky.social · 21/09/2026
ʙɪɴᴅᴄʀᴀꜰᴛ2 is out, and we're not waiting for the paper. The full code drops today, free for academic and industry use. We're releasing it early so you can start designing right now, and bring its full power to the current Adaptyv competition. github.com/PacesaLab/Bi...
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Pedro Beltrao @pedrobeltrao.bsky.social · 18/09/2026
Anthropic has used Claude to optimise structure prediction and design code to improve speed and memory efficiency. 2-3X speed improvements on AF3, 5X on OF3, 5X on BindCraft low memory modes to model large assemblies. All released as open source www.anthropic.com/research/cla...
anthropic.com
How Claude is uplifting biomolecular modeling
Anthropic is an AI safety and research company that's working to build reliable, interpretable, and steerable AI systems.
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bioRxivpreprint @biorxivpreprint.bsky.social · 13/09/2026
A new class of lipid transfer proteins is required for the recycling of lipids from the P. falciparum digestive vacuole www.biorxiv.org/content/10.64898/20…
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chipotlab.bsky.social @chipotlab.bsky.social · 10/09/2026
No predefined reaction coordinate. No mechanistic guesswork. No massive sampling campaign. Gen-COMPAS reconstructs biomolecular transition pathways from endpoint structures alone. Protein folding, allostery, membrane transport. Now in Nature. @nature.com @springernature.com
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Leonie Anton @leonieanton.bsky.social · 03/09/2026
I am excited to share that I will start my group @embl.org in Grenoble in February 2027, where we will investigate host-pathogen interactions using in situ cryo electron microscopy🦠❄️🔬! I am recruiting PhD students through the current open call of the EMBL PhD Program: www.embl.org/about/info/e...
embl.org
Anton Group – Cellular structural biology of host-pathogen interactions
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mareikejordan.bsky.social @mareikejordan.bsky.social · 04/09/2026
Check out our preprint on the structural mechanisms of how LEM2 and ESCRTs seal the nuclear envelope. Awesome collaboration with @karenpalacior.bsky.social who brought my structures to life 💃🔬❄️🌀 @hummerlab.bsky.social www.biorxiv.org/content/10.6...
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Journal of Cell Biology @jcb.org · 04/09/2026
Any1 is a #phospholipid scramblase involved in #endosome biogenesis. From Jieqiong Gao, @labvanni.bsky.social, Christian Ungermann and colleagues: rupress.org/jcb/article/... 📕 From our #Lipid and #Membrane collection: rupress.org/jcb/collecti... #EMBOLipidCode
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Kutay lab @kutaylab.bsky.social · 09/08/2026
We are excited by the publication of our work on Torsin1A, its interaction partner CLCC1, and their role in membrane fusion during NPC biogenesis! A fantastic collaboration with @jagannathan-lab.bsky.social @labvanni.bsky.social @gautamdey.bsky.social and the Korkhov and Antonin labs!
cell.com
The dystonia-associated Torsin1A sustains CLCC1 function in membrane fusion of the nuclear envelope for NPC biogenesis
Maslennikova et al. identify the ER membrane protein CLCC1 as an interaction partner of the dystonia-linked AAA+ ATPase Torsin1A. Torsin1A sustains the function of CLCC1, which is proposed to facilitate fusion of the nuclear envelope during NPC biogenesis by forming an oligomer that promotes lipid bilayer approach and remodeling.
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Carl Zimmer @carlzimmer.com · 01/07/2026
Meet SpudCell, a synthetic cell made from lifeless ingredients that feeds, grows, divides, and experiences selection. If it doesn't have all the hallmarks of life, it has a lot! Here's my story. Gift link: nyti.ms/4vCbTih
A series of images of a dividing synthetic cell
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André Nadler @nadlerlab.bsky.social · 29/07/2026
Lipids build the membranes of all cells, but identifying their precise functions is extremely challenging. Here’s our attempt to change that: How to find and understand lipid-protein interactions, by Katelyn Cook & company. www.biorxiv.org/content/10.6...
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bioRxiv Biophysics @biorxiv-biophys.bsky.social · 17/07/2026
Coarse-grained simulations of long intrinsically disordered proteins: a benchmark of Martini 3 force-fields www.biorxiv.org/content/10.64898/20…
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Ashutosh Kumar @mudgal17.bsky.social · 10/07/2026
Our work on identifying membrane fusion mechanism prior to NPC assembly is now out in peer reviewed form at @cp-molcell.bsky.social Have a look if you are interested in NPC biogenesis and membrane fusion.
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Veijo Salo @veijosalo.bsky.social · 23/06/2026
How does a cell remodel the ER membrane into a lipid droplet? Excited to share our new bioRxiv preprint, where we find that regulated opening of the seipin ring defines a functional ER–lipid droplet interface — and identify SMLR1 as a regulator of this transition. www.biorxiv.org/content/10.6...
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 12/06/2026
This amazing work by @danialv.bsky.social and Bodan Hu is now out in peer-reviewed form at @cp-cell.bsky.social with a lot of new simulations! Check it out if interested in lipid transport!
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 21/05/2026
Happy to share our latest work on bridge lipid transfer proteins, by PhD student @yarasayed1.bsky.social. A great collaboration with @ungermannlab.bsky.social @arnemoeller.bsky.social and Reggiori lab!
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Journal of Cell Biology @jcb.org · 07/05/2026
Covill-Cooke, Hirashima, Kawano, Endo, Kornmann (@ox.ac.uk) and colleagues find that the ERMES #lipid-transporting complex, long-thought to be an obligate heterotetramer, can be replaced by only one component: mitochondrially tethered Mmm1. rupress.org/jcb/article/... #Organelles #Mitochondria
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Journal of Cell Biology @jcb.org · 23/04/2026
@laylanassar.bsky.social & @shawnferguson.bsky.social @yaleschoolofmed.bsky.social discuss Kim et al.’s study (doi.org/10.1083/jcb....) showing that TMEM63A protects #lysosomes from rupture by acting as a pressure relief valve when membrane tension rises. rupress.org/jcb/article/...
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 07/04/2026
Happy to share our latest work where @Jennifersapia.bsky.social teamed up with @veijosalo.bsky.social and Xuewu Sui from @tamu.bsky.social to combine simulations and experiments to investigate DGAT1-dependent triglyceride synthesis, revealing more roles for DAG than previously known….(1/3)
biorxiv.org
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BehavEcolPapers @behavecolpapers.bsky.social · 29/03/2026
ICYMI: A bridge-like lipid transfer protein is critical for generation of invasive stages in malaria parasites @natcomms.nature.com
dlvr.it
A bridge-like lipid transfer protein is critical for generation of invasive stages in malaria parasites
Nature Communications, Published online: 28 March 2026; doi:10.1038/s41467-026-70887-1Organelle biogenesis in the rapidly growing malaria parasite requires extensive membrane genesis and remodeling. Here a mechanism to directly supply lipids from the ER to the inner membrane complex (IMC), a de novo formed organelle needed for progeny formation, is shown.
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Florian Fröhlich @flofroehlich.bsky.social · 16/02/2026
New preprint from the lab together with @labvanni.bsky.social. We looked what happens to ER generated free very long chain fatty acids.. VLCFAs are partionig into lipid droplets and are extracted from the hydrophobic core by Fat1. www.biorxiv.org/content/bior...
bsky.app
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 30/01/2026
Please share!!! I am looking for a postdoctoral researcher to join us. Focus will be on exciting collaborative projects on lipids and membrane biology, pushing the boundaries of in silico "reconstitutions". Previous experience with molecular dynamics simulations of biological systems a strong plus!
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pilarcossio.bsky.social @pilarcossio.bsky.social · 24/01/2026
I finally made my webpage, check it out: pilarcossio.org
pilarcossio.org
Dr. Pilar Cossio - Research Scientist
Senior Research Scientist at Flatiron Institute. Research in computational biology and biophysics.
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 12/01/2026
Happy to finally share the amazing results of our long-term collaboration with Karin Reinisch’s lab on how bridge lipid-transfer proteins (BLTPs) cooperate with partner proteins to orchestrate lipid delivery. A quick thread (1/7) www.biorxiv.org/content/10.6...
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c0nc0rdance @c0nc0rdance.bsky.social · 17/12/2025
“A process which led from the amoeba to man appeared to the philosophers to be obviously a progress - though whether the amoeba would agree with this opinion is not known" - Bertrand Russell, 1976. Time-lapse video of Vampyrella lateritia eating Spirogyra algae from Science Source/Oliver Skibbe. 🦠
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 26/11/2025
Thrilled to share that the work from @cristianrocharoa.bsky.social, identifying TMEM170 proteins as lipid scramblases that associate with bridge lipid transporters, is now out in @natsmb.nature.com Unexpectedly, the scrambling pathway does not "feed" directly into the BLTP cavity... rdcu.be/eRSst
rdcu.be
TMEM170 proteins are lipid scramblases associated with bridge-type lipid transporters BLTP1/Csf1
Nature Structural & Molecular Biology - Rocha-Roa et al. identify TMEM170 proteins as endoplasmic reticulum lipid scramblases that partner with bridge-like lipid transfer proteins BLTP1/Csf1...
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Abdou Rachid Thiam @abdourachidthiam.bsky.social · 17/11/2025
Thrilled to share our latest work showing that the bridge lipid transport protein ATG2A transfers diacylglycerol (DAG), and some TAG/PA, from the ER to LDs, thereby recruiting DGAT2 to drive local TAG synthesis, promoting LD expansion while protecting ER membranes. www.nature.com/articles/s41...
nature.com
ATG2A-mediated DAG transfer recruits DGAT2 for lipid droplet growth - Nature Structural & Molecular Biology
Elhan et al. show that ATG2A acts with DGAT2, the enzyme producing triacylglycerol (TAG), in lipid droplet growth. By delivering diacylglycerol to lipid droplets, ATG2A not only fuels TAG production b...
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Gioele La Manno @gioelelamanno.bsky.social · 16/10/2025
🧠 The Lipid #Brain Atlas is out now! If you think #lipids are boring and membranes are all the same, prepare to be surprised. Led by @lucafusarbassini.bsky.social with Giovanni D'Angelo's lab, we mapped membrane lipids in the mouse brain at high resolution. www.biorxiv.org/cgi/content/...
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 13/10/2025
Thanks to @snsf.ch, we are hiring two PhD students to investigate frontier topics in lipid biology using a combination of MD simulations and experiments. Preferred starting date: ASAP. Fribourg - and Switzerland - are quite nice, for both work and private life! Please spread the word!
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bioRxiv Biophysics @biorxiv-biophys.bsky.social · 03/08/2025
The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins. www.biorxiv.org/content/10.1101/202…
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Vanni Lab at UNIFR, Switzerland @labvanni.bsky.social · 23/07/2025
Happy to share the latest work from the lab, led by @mudgal17.bsky.social‬, in collaboration with the Weis lab @ethzurich.bsky.social. How do nuclear membranes fuse during NPC assembly? We answer this question in our latest work, where we identify a new mechanism for membrane fusion… (1/13)
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Melanie McDowell @melaniemcdowell.bsky.social · 12/07/2025
Proud to share our first lab pre-print: “SND3 is the membrane insertase within a fungal multipass translocon” where @tzujingyang.bsky.social solved the structure of a ribosome-associated SND3-translocon complex involved in ER membrane protein insertion ➡️ doi.org/10.1101/2025...
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