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Latest posts tagged with #ScienceInProgress on Bluesky

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Posts tagged #ScienceInProgress

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These microbial "artworks" by the Intermag Team in petri dishes are a glimpse into the creative side of our scientific daily life. With best wishes for 2026! 🌟
#Intermag #SpinFert #ScienceInProgress #Microbiology #R&D

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Their futures are bright and we cannot wait to see the meaningful impacts they will make as they develop in their careers. #UndergradResearch #ABRCMS25 #ScienceInProgress

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We are delighted to highlight the exceptional achievements of our undergraduate students, who showcased their outstanding research at the conference with 5 posters and 1 oral presentation. #UndergradResearch #ABRCMS25 #ScienceInProgress

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The Hamburg narwhale with 2 tusks.

The Hamburg narwhale with 2 tusks.

New study @ecol-evol.bsky.social: Our historic two-tusked #narwhal (ZMH-S-10192) isn’t a female after all - it’s male. DNA & isotope analyses corrected a 340-year assumption. Science is always evolving. → t1p.de/4psy6

©UHH,_RRZ_MCC,_Mentz#11D7_bearb_BB

#ScienceInProgress #CollectionsMatter

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🍂 Autumn break — but not for everyone at #KMEB 🍂

While some of our colleagues are enjoying a well-earned holiday this week, many of our researchers are still at work. The halls may be a little quieter, but the dedication to science never really takes a break📚🔬

#ResearchLife #ScienceInProgress

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Science is not about saying something is right but that it has not proven to be wrong yet. #ScienceNotCertainty
#AlwaysTesting
#ScienceInProgress

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LAB CHRONICLE #17
-Weekly Report-

No usable data.
But I learned how to pour a drop with style.

#LeidenfrostEffect #ScienceInProgress #HoldTheLine #NoDataNoCry #SchrödingerData #DataScience

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🎬Filming days for GlaCerHub!
We're capturing labs, equipment, and the amazing people behind the project – CEITEC BUT + FunGlass.
Stay tuned for a video showing GlaCerHub as a true European hub of excellence in glass & ceramics!
#GlaCerHub #Research #HorizonEurope #Glass #Ceramics #ScienceInProgress

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We're excited to be at #SIPS2025 in Budapest! Let's connect, exchange ideas, and advance better science in the field of cognitive control in children.
@improvingpsych.org #OpenScience #PsychTwitter #Reproducibility #SIPS2025 #ScienceInProgress

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Time to catch up on everything the lab’s been up to these past few weeks...and trust us, it’s been BUSY! 🧪💥
From late-night flow cytometry sessions to exciting conferences and new data from our EV studies, here’s a little peek behind the scenes… 👀👇
#LabLife #ScienceInProgress #CancerResearch

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RetiGene, a comprehensive gene atlas for inherited retinal diseases (IRDs) Inherited retinal diseases (IRDs) are rare disorders, typically presenting as Mendelian traits, that result in stationary or progressive visual impairment. They are characterized by extensive genetic ...

Our new manuscript has just been posted as a preprint on bioRxiv. You can read the full story here www.biorxiv.org/content/10.1...

#retigene #IRDs #bioRxiv #Preprint #ResearchLife #ScienceInProgress #OpenScience

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Last 12 hours of our beamtime at PETRA III! ⏳ Making the most of every photon and every scan. Let’s finish strong and squeeze out all the data we can! 💪✨ #Beamtime #PETRAIII #ScienceInProgress

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Structures and mechanism of condensation in non-ribosomal peptide synthesis | Nature Non-ribosomal peptide synthetases (NRPSs) are megaenzymes responsible for the biosynthesis of many clinically important natural products, from early modern medicines (penicillin, bacitracin) to current blockbuster drugs (cubicin, vancomycin) and newly approved therapeutics (rezafungin)1,2. The key chemical step in these biosyntheses is amide bond formation between aminoacyl building blocks, catalysed by the condensation (C) domain3. There has been much debate over the mechanism of this reaction3–12. NRPS condensation has been difficult to fully characterize because it is one of many successive reactions in the NRPS synthetic cycle and because the canonical substrates are each attached transiently as thioesters to mobile carrier domains, which are often both contained in the same very flexible protein as the C domain. Here we have produced a dimodular NRPS protein in two parts, modified each with appropriate non-hydrolysable substrate analogues13,14, assembled the two parts with protein

Discover the structural insights into NRPSs! Unravel how C domains catalyze amide bond formation, crucial for drugs like penicillin and vancomycin. #ScienceInProgress PMID:39662504, Nature 2025, @Nature https://doi.org/10.1038/s41586-024-08417-6 #Medsky #Pharmsky #RNA #ASHG #ESHG 🧪

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