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X-WR-CALDESC:Events for SFB 1551
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DTSTART:20240101T000000
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BEGIN:VEVENT
DTSTART;TZID=UTC:20251009T103000
DTEND;TZID=UTC:20251009T113000
DTSTAMP:20251008T081955Z
CREATED:20250314T135708Z
LAST-MODIFIED:20251008T081955Z
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SUMMARY:SFB 1551 Seminar Series Event - Prof. Dr. Thomas Speck
DESCRIPTION:Methods talk by Prof. Dr. Thomas Speck\, Theoretical Physics Department\, Stuttgart University \nMore is different: Statistical physics of structure formation \nHow can we even dare to model complex phenomena like cellular processes in biology? I will introduce the philosophy of statistical physics to approach this question through minimal models and I will illustrate the key concepts for the case of phase separation. I will then sketch the current challenges of non-equilibrium and many-component systems and how we tackle those.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-prof-dr-thomas-speck/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
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BEGIN:VEVENT
DTSTART;TZID=UTC:20251023T103000
DTEND;TZID=UTC:20251023T113000
DTSTAMP:20251017T130455Z
CREATED:20250314T135838Z
LAST-MODIFIED:20251017T130455Z
UID:10000098-1761215400-1761219000@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Prof. Dr. Petra Beli
DESCRIPTION:Methods talk by Prof. Dr. Petra Beli\, Institute of Molecular Biology (IMB) \nQuantitative proteomics for investigations of protein-protein interactions and phosphorylation \nIn this methods talk\, I will provide an overview of mass spectrometry based proteomics approaches for analyzing protein-protein interactions and posttranslational modifications. I will focus on new proximity-based methods for analyzing transient and low affinity interactions that are also applicable for the analysis of phase-separated membraneless compartments. In addition\, I will give an overview into the quantitative analysis of posttranslational interactions with a focus on global and targeted analysis of protein phosphorylation.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-prof-dr-petra-beli/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
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BEGIN:VEVENT
DTSTART;VALUE=DATE:20251027
DTEND;VALUE=DATE:20251101
DTSTAMP:20250925T084138Z
CREATED:20250925T083027Z
LAST-MODIFIED:20250925T084138Z
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SUMMARY:SFB 1551 Advanced Microscopy Techniques to study (Bio)polymer Dynamics Workshop 2025
DESCRIPTION:Content is protected.
URL:https://crc1551.com/our-event/sfb-1551-quantitative-microscopy-for-biopolymers-workshop-2025/
LOCATION:Microscopy & Histology Core Facility (MHCF) – IMB\, Ackermannweg 4\, Mainz\, 55128\, Germany
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BEGIN:VEVENT
DTSTART;TZID=UTC:20251031T103000
DTEND;TZID=UTC:20251031T113000
DTSTAMP:20251008T145514Z
CREATED:20250217T092318Z
LAST-MODIFIED:20251008T145514Z
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SUMMARY:SFB 1551 Seminar Series Event - Prof. Dr. Dorothee Staiger
DESCRIPTION:Partners in time – the RNA interactome of plant RNA-binding proteins \nRNA-based regulation plays a key role in plant responses to endogenous cues and environmental stimuli. To provide insights into in vivo RNA-protein interactions shaping the transcriptome\, we improved our previous protocol for individual nucleotide resolution crosslinking and immunoprecipitation and\, in collaboration with Kathi Zarnack\, established a bioinformatics pipeline to evaluate iCLIP-seq data (plant iCLIP2). We comprehensively profiled the binding landscape of Arabidopsis thaliana glycine-rich RNA binding protein 7 implicated in different steps of RNA processing and function. In the compendium of target transcripts\, we delineated motifs preferentially associated with binding sites. Orthogonal transcriptomic data obtained from loss-of function mutants and plants overexpressing the RNA binding proteins provided insights into the mode of action how AtGRP7 affects its target transcripts. In particular\, in collaboration with Martin Crespi we pursue the idea that long noncoding RNAs interacting with AtGRP7 and the splicing regulator NSRa serve as regulators of alternative splicing. In turn\, we developed single mRNA interactome capture and identified ALBA4\, a protein interacting with m6A readers\, as an AtGRP7 interactor. Collectively\, our data begin to shed light on the organisation of networks in posttranscriptional regulation in Arabidopsis.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-prof-dr-dorothee-staiger/
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