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<span style="font-size: 12pt; color: black;">Dear all,</span></p>
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<span style="font-size: 12pt; color: black;">This is a reminder for the upcoming <b>
AI4Biomed meetup.</b> </span></p>
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<span style="font-size: 12pt; color: black;"><b>Thursday October 30th 2025, 16:00h - 18:00h in NU-4A25</b></span></p>
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<span style="font-size: 12pt; color: black;">Join us to welcome our speakers <b>Evelina Tutucci</b> (Systems Biology lab) and
<b>Melissa Bärenfänger </b>(Chemistry and Pharmaceutical Sciences), and stay for drinks and networking afterwards!</span></p>
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<span style="font-size: 12pt; color: black;"> </span></p>
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<span style="font-size: 14pt; color: rgb(23, 78, 134);"><b><a class="OWAAutoLink" id="OWA022b6713-9911-a44c-db57-39965a3c08d9" style="margin-top: 0px; margin-bottom: 0px;" title="https://docs.google.com/forms/d/e/1FAIpQLSd_ZccBr7R1PkKrG0_NdwHteK16tp5eK-b9Lcpom5-XpZ8WgA/viewform?usp=header" href="https://docs.google.com/forms/d/e/1FAIpQLSd_ZccBr7R1PkKrG0_NdwHteK16tp5eK-b9Lcpom5-XpZ8WgA/viewform?usp=header">Please
register here.</a></b></span></p>
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<span style="font-size: 12pt; color: black;">Please forward the invitation to other group members who may be interested to hear more about AI for biomedicine. </span></p>
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<span style="font-size: 12pt; color: black;"> </span></p>
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<span style="font-size: 12pt; color: black;">We are looking forward to welcoming you soon!</span></p>
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<span style="font-size: 12pt; color: black;"> </span></p>
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<span style="font-size: 12pt; color: black;">If you are not yet on the mailing list for the AI4Biomed series, please contact
<b>a.sajan@vu.nl</b>.</span></p>
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<span style="font-size: 12pt; color: black;">Best wishes,</span></p>
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<span style="font-size: 12pt; color: black;">The Organizers</span></p>
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<span style="font-size: 12pt; color: black;">-----------------------------------------------------------------------------------------------------------------</span></p>
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<span style="font-size: 12pt; color: black;"><b>AI4 Biomed,Thursday October 30th 2025, 16:00h - 18:00h in NU-4A25 (NU Building on the VU Campus)</b></span></p>
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<span style="font-size: 12pt; color: black;"><b><i>Schedule</i></b></span></p>
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<span style="font-size: 12pt; color: black;"><b><i>16:00h - 16:30h:</i></b><i> </i></span><span style="font-size: 12pt; color: rgb(17, 85, 204);"><u><a style="color: rgb(17, 85, 204); margin: 0px;" data-auth="NotApplicable" data-linkindex="1" data-ogsc="" rel="noopener noreferrer" title="https://www.tutuccilab.com/home" class="OWAAutoLink" id="OWAd424965f-cf9a-61a4-b589-f52e82f31501" target="_blank" href="https://www.tutuccilab.com/home">Evelina Tutucci</a></u></span><span style="font-size: 12pt; color: black;"> -
“<b>Shapeshifting Fungi: How Spatial and Temporal Gene Expression Control Contribute to Fungal Success</b>”</span></p>
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<span style="font-size: 12pt; color: black;"><i>Across the fungal kingdom, species exhibit remarkable diversity in both lifestyle—ranging from single-celled to multicellular forms—and morphology, enabling their successful adaptation to diverse ecosystems. Fungi
can grow as simple, spherical single cells or develop into elongated, highly asymmetric structures that facilitate the organization of distinct subcellular compartments. To understand how fungi regulate their lifestyle choices and morphology, we develop imaging
technologies to analyze gene expression changes at the single-cell level. By visualizing and quantifying single mRNA molecules in both fixed (single-molecule RNA FISH) and living (MS2 system) fungal cells, we investigate how spatial and temporal gene expression
regulation contributes to fungal physiology. To identify both species-specific and conserved strategies, we study fungal differentiation across diverse species, including pathogenic (Candida albicans, Aspergillus fumigatus) and non-pathogenic (Arbuscular mycorrhizal
fungi, Saccharomyces cerevisiae, Aspergillus niger) fungi. Our findings reveal an unexpected level of spatial organization in gene expression, where the synthesis and localization of mRNAs within fungal structures contribute to growth and adaptation.</i></span></p>
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<span style="font-family: Aptos, sans-serif; font-size: 12pt; color: black;"><b><i>16:30h - 17:00h:
</i></b></span><span style="font-family: Aptos, sans-serif; font-size: 12pt; color: rgb(17, 85, 204);"><u><a style="color: rgb(17, 85, 204); margin: 0px;" data-auth="NotApplicable" data-linkindex="2" data-ogsc="" rel="noopener noreferrer" title="https://research.vu.nl/en/persons/melissa-baerenfaenger" class="OWAAutoLink" id="OWAcc078120-16ff-8757-e90c-18e3cbf8fce0" target="_blank" href="https://research.vu.nl/en/persons/melissa-baerenfaenger">Melissa
Bärenfänger</a></u></span><span style="font-family: Aptos, sans-serif; font-size: 12pt; color: black;"> -
<b>"</b></span><span style="font-family: Aptos, sans-serif; font-size: 11pt; color: rgb(0, 0, 0);"><b>Using Ion-mobility mass spectrometry to understand 2D and 3D structure of glycoproteins in human health and disease"</b></span></p>
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<span style="font-family: Aptos, sans-serif; font-size: 11pt; color: rgb(0, 0, 0); background-color: rgb(255, 255, 255);"><i>Protein glycosylation, the attachment of carbohydrates to proteins, plays a vital role in determining protein structure, stability,
and function. Distinct glycosylation patterns, for example in human antibodies, can directly modulate immune responses, promoting either inflammation or anti-inflammatory effects. Aberrant glycosylation has also been correlated with various diseases, including
cancer or Alzheimer’s disease. Despite these correlations, a major challenge remains in understanding how specific glycan modifications alter protein structure and therefore function.<br>
Our research employs ion mobility mass spectrometry (IM-MS) to bridge this gap by revealing both the chemical composition and conformational landscape of glycoproteins. Through advanced bottom-up glycoproteomics, we generate large datasets that provide comprehensive
views of glycosylation across single proteins and entire proteomes. On intact protein lever, the ion mobility dimension enables measurement of collision cross sections (CCS, Ų), offering direct insights into how glycans influence protein folding and three-dimensional
architecture.<br>
In this presentation, I will highlight our work on three glycoproteins: Clusterin (Alzheimer’s disease), β-2-glycoprotein 1 (antiphospholipid syndrome), and TDP-43 (ALS) to demonstrate how IM-MS can dissect glycosylation patterns and reveal protein conformation.</i></span></p>
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<span style="font-size: 12pt; color: black;"><b><i>17:00h - 18:00h:</i></b><i> Drinks and networking</i></span></p>
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<span style="font-size: 12pt; color: black;"><b>Organizing Team:</b></span></p>
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<span style="font-size: 12pt; color: black;">Daan Geerke</span></p>
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<span style="font-size: 12pt; color: black;">Jaap Heringa</span></p>
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<span style="font-size: 12pt; color: black;">Mark Hoogendoorn</span></p>
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<span style="font-size: 12pt; color: black;">Martijn Schut</span></p>
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<span style="font-size: 12pt; color: black;">Annette ten Teije</span></p>
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<span style="font-size: 12pt; color: black;">Bas Teusink</span></p>
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<span style="font-size: 12pt; color: black;">Bernd Brandt </span></p>
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<span style="font-size: 12pt; color: black;">Aneta Lisowska </span></p>
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<span style="font-size: 12pt; color: black;">Gustavo Jeuken</span></p>
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<span style="font-size: 12pt; color: black;">Halima Mouhib</span></p>
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<span style="font-size: 12pt; color: black;">Mifen Chen</span></p>
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<span style="font-size: 12pt; color: black;">Akshay Sajan</span></p>
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