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861 | 861 | "text": "Starting early next year, Jarek will begin a two-year research stay at Vilnius University 🇱🇹. There, he’ll:\n\n🔬 Study the impact of small molecules on amyloid polymorphism\n\n🧩 Apply the findings to expand the AmyloGraph database\n\n🤝 Collaborate closely with top researchers in the field\n\nThis project promises to push forward our understanding of amyloid structures and interactions and feed valuable insights into our growing infrastructure!\n\n\nWe’re incredibly proud of Jarek for this achievement and perseverance. From nearly missing out to scoring an amazing opportunity, this grant will open new doors for international collaboration and career development!" |
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866 | 866 | "title": "📢 New review article published in Protein Science!", |
867 | 867 | "section": "", |
868 | 868 | "text": "🎉 We’re excited to share that our review article, “Experimental methods for studying amyloid cross-interactions”, is now published and open access in Protein Science!\n🔗 You can read it here\n\n\n\n\nAleksandra Kalitnik, Anna Lassota, Oliwia Polańska, Marlena Gąsior-Głogowska, Monika Szefczyk, Agnieszka Barbach, Jarosław Chilimoniuk, Izabela Jęśkowiak-Kossakowska, Alicja W. Wojciechowska, Jakub W. Wojciechowski, Natalia Szulc, Małgorzata Kotulska and Michał Burdukiewicz.\n\n\n\n\nCross-interactions between amyloid proteins are a key factor in many diseases, from Alzheimer’s to prion diseases. Yet, capturing the full picture of these interactions remains a major experimental challenge.\nIn this comprehensive review, we:\n\n🔬 Survey the most widely used (in vitro) and in vivo methods to study amyloid cross-interactions\n\n💡 Discuss how each method contributes unique (but partial) insights, from aggregation kinetics to fibril morphology and hetero-aggregate composition\n\n📷 Highlight the complementarity of techniques such as:\n\nThioflavin T fluorescence\nAFM, Cryo-EM, immuno-TEM\nMass spectrometry & solid-state NMR\nCo-immunoprecipitation and super-resolution imaging\n\n\n📊 And we emphasize: no single method is enough, it’s only through hybrid strategies that we can start to decode the complexity of amyloid cross-interactions.\n\n\n\n\n\n“The only recommended approach is to combine indirect and direct evidence to create a more complete outlook of this process.”\n\nWhether you’re developing new tools, studying amyloid polymorphism or exploring proteinopathies, we hope this work helps chart the path toward better experimental designs and interpretations.\n\n🧠💪 Congrats to the whole team and special thanks to everyone who contributed ideas, figures and hard-won insights!" |
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873 | 873 | "title": "📢 New review article published in Protein Science!", |
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875 | 875 | "text": "Aleksandra Kalitnik, Anna Lassota, Oliwia Polańska, Marlena Gąsior-Głogowska, Monika Szefczyk, Agnieszka Barbach, Jarosław Chilimoniuk, Izabela Jęśkowiak-Kossakowska, Alicja W. Wojciechowska, Jakub W. Wojciechowski, Natalia Szulc, Małgorzata Kotulska and Michał Burdukiewicz." |
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880 | 880 | "title": "📢 New review article published in Protein Science!", |
881 | 881 | "section": "", |
882 | 882 | "text": "Cross-interactions between amyloid proteins are a key factor in many diseases, from Alzheimer’s to prion diseases. Yet, capturing the full picture of these interactions remains a major experimental challenge.\nIn this comprehensive review, we:\n\n🔬 Survey the most widely used (in vitro) and in vivo methods to study amyloid cross-interactions\n\n💡 Discuss how each method contributes unique (but partial) insights, from aggregation kinetics to fibril morphology and hetero-aggregate composition\n\n📷 Highlight the complementarity of techniques such as:\n\nThioflavin T fluorescence\nAFM, Cryo-EM, immuno-TEM\nMass spectrometry & solid-state NMR\nCo-immunoprecipitation and super-resolution imaging\n\n\n📊 And we emphasize: no single method is enough, it’s only through hybrid strategies that we can start to decode the complexity of amyloid cross-interactions." |
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887 | 887 | "title": "📢 New review article published in Protein Science!", |
888 | 888 | "section": "", |
889 | 889 | "text": "“The only recommended approach is to combine indirect and direct evidence to create a more complete outlook of this process.”\n\nWhether you’re developing new tools, studying amyloid polymorphism or exploring proteinopathies, we hope this work helps chart the path toward better experimental designs and interpretations.\n\n🧠💪 Congrats to the whole team and special thanks to everyone who contributed ideas, figures and hard-won insights!" |
|
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