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Raphaël P. B. Jacquat
@bjacquat
Biophysicist curious to discover new thinks. I enjoy to draw and simplify problems in order to share my small knowledges.
ID: 1269619351973498886
07-06-2020 13:17:04
34 Tweet
88 Followers
118 Following
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📢 Finally out now: Our paper describing DigitISA, a platform for direct digital sensing of protein biomarkers in solution 🧪 (incl. antibodies, amyloid aggregates & condensates). KnowlesLab Cambridge Cambridge Chemistry Take a look: 👇nature.com/articles/s4146…
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Great to see our paper on DigitISA - a #microfluidic platform for direct detection of protein-based biomarkers - published in Nature Communications nature.com/articles/s4146… DigitISA allows detecting markers that have remained challenging with surface-based immunoassays, such as amyloid
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Check out the new DigitISA assay for sensing biomolecular complexes in solution! Well done Georg Krainer Kadi-Liis Saar Tim Welsh Magda Czekalska Raphaël P. B. Jacquat and colleagues from Owens, Alberti and Klenerman groups! nature.com/articles/s4146…
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📃 Our latest work is out! Sizing of single proteins using nanofluidics. 🧪 Great collaboration with Raphaël P. B. Jacquat and many others KnowlesLab Cambridge Cambridge Chemistry & in collaboration with #baumberglab,KeyserLab & Laser Analytics Group (Kaminski Lab) pubs.acs.org/doi/10.1021/ac…
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Appointed tenure at ETH Zurich. I'm grateful to my inspiring mentors, current and former group members, colleagues and collaborators, for all the support, dedication and contributions along the way. Looking forward to the new exciting projects in front of us!
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🔓 #OpenAccess + Most Read in the past 30 days: "Single-Molecule Sizing through Nanocavity Confinement" by Raphaël P. B. Jacquat, Georg Krainer, Peter, Babar, Vanderpoorten, Xu, Welsh, Kaminski, Keyser, Baumberg, & Knowles go.acs.org/48Z
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New PostDoc position! Join the vibrant LIAC team (LIAC at EPFL) for a project on “ML for Direct Air Capture Materials”. Develop models to accelerate the discovery of new CO2 adsorbents together with excellent experimental collaborators (LFIM - Wendy L. Queen)! RT appreciated. #ML4Sus
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RT appreciated. #ML4Sus New PostDoc position! Join the vibrant LIAC team (<a href="/SchwallerGroup/">LIAC at EPFL</a>) for a project on “ML for Direct Air Capture Materials”. Develop models to accelerate the discovery of new CO2 adsorbents together with excellent experimental collaborators (<a href="/lfim_epfl/">LFIM - Wendy L. Queen</a>)!
RT appreciated. #ML4Sus"
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Review: Amyloid formation as a protein phase transition By Thomas Michaels, Daoyuan Qian, Andela Saric, Michele Vendruscolo, Sara Linse & KnowlesLab Cambridge rdcu.be/dfzMr
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By <a href="/MichaelsLabETH/">Thomas Michaels</a>, <a href="/DaoyuanQian219/">Daoyuan Qian</a>, <a href="/SaricLab/">Andela Saric</a>, <a href="/mvendruscolo14/">Michele Vendruscolo</a>, Sara Linse & <a href="/KnowlesLabCamb/">KnowlesLab Cambridge</a>
rdcu.be/dfzMr Review: Amyloid formation as a protein phase transition
By <a href="/MichaelsLabETH/">Thomas Michaels</a>, <a href="/DaoyuanQian219/">Daoyuan Qian</a>, <a href="/SaricLab/">Andela Saric</a>, <a href="/mvendruscolo14/">Michele Vendruscolo</a>, Sara Linse & <a href="/KnowlesLabCamb/">KnowlesLab Cambridge</a>
rdcu.be/dfzMr"
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Very excited to finally see this out Nature Chemistry! The interface of hnRNPA1 LCD condensates promotes the transition to amyloids. Thanks to everyone involved for their important contributions! Paolo Arosio D-CHAB ETH Zurich nature.com/articles/s4155…
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We had the chance to present our work at the United Nations's Science, Techonology, and Innovation forum. Thank you to everyone who has supported us along the way 😊, and a special thanks to Engineering for Change for enabling us to present alongside the other selected innovators.
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Excited by the possibility of proteins being able to generate distinct pH microenvironments without needing mebrane enclosure, active transporters or energy input! KnowlesLab Cambridge
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Very excited to share our work in Nature Communications! We show that a-synuclein oligomers and fibrils form by secondary nucleation on existing fibril surfaces nature.com/articles/s4146…
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