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4. Co-creating Artificial Intelligence: Designing and Enhancing Democratic AI Solutions Through Citizen Science

Author

Annelies Duerinckx, Carina Veeckman, Karen Verstraelen, Neena Singh, Jef Van Laer, Michiel Vaes, Charlotte Vandooren, and Pieter Duysburgh

Subjects
citizen science, artificial intelligence, co-creation, crowdsourcing, education, democratization, Science
Abstract

Although artificial intelligence (AI) is omnipresent in our everyday lives, the level of awareness and knowledge among the general population remains mixed. The lack of understanding is particularly prevalent among older adults, and people with a low education and income. To bridge this knowledge gap and to empower individuals to become informed AI users, further outreach and awareness raising is necessary. This article presents a case study in Flanders (Belgium), called the amai! program (Flemish slang for “oh my!”). The program invites participants to voice their ideas or societal problems they wish to solve through AI and to be involved in the development of citizen-driven research projects. Using a citizen science (CS) approach, ideas are collected through a centralized platform and eventually realized through an open project call with partners from industry, civil society, and research institutions. As a result, 988 ideas have been submitted through the program’s platform and 14 are being realized in the domains of mobility, climate, health, and work. Here, we outline a phase-based approach for setting up citizen-driven research projects, as well as lessons learned on how to sensitize and activate citizens. Guidelines are also provided on how to involve participants to become aware and learn about science and technology, especially those with no prior knowledge or interest. Overall, this case study demonstrates how AI innovation and governance can be democratized through citizen participation and can build capacities in a fun and accessible way.

Published
2024
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6. Protection of stromal cell-derived factor-1 SDF-1/CXCL12 against proteases yields improved skin wound healing

Author

Rafaela Vaz Sousa Pereira, Mostafa EzEldeen, Estefania Ugarte-Berzal, Jennifer Vandooren, Erik Martens, Mieke Gouwy, Eva Ganseman, Jo Van Damme, Patrick Matthys, Jan Jeroen Vranckx, Paul Proost, and Ghislain Opdenakker

Subjects
SDF-1, CXCL12, proteolysis, chemokine, COAM, wound healing, Immunologic diseases. Allergy, RC581-607
Abstract

SDF-1/CXCL12 is a unique chemotactic factor with multiple functions on various types of precursor cells, all carrying the cognate receptor CXCR4. Whereas individual biological functions of SDF-1/CXCL12 have been well documented, practical applications in medicine are insufficiently studied. This is explained by the complex multifunctional biology of SDF-1 with systemic and local effects, critical dependence of SDF-1 activity on aminoterminal proteolytic processing and limited knowledge of applicable modulators of its activity. We here present new insights into modulation of SDF-1 activity in vitro and in vivo by a macromolecular compound, chlorite-oxidized oxyamylose (COAM). COAM prevented the proteolytic inactivation of SDF-1 by two inflammation-associated proteases: matrix metalloproteinase-9/MMP-9 and dipeptidylpeptidase IV/DPPIV/CD26. The inhibition of proteolytic inactivation was functionally measured by receptor-mediated effects, including intracellular calcium mobilization, ERK1/2 phosphorylation, receptor internalization and chemotaxis of CXCR4-positive cells. Protection of SDF-1/CXCL12 against proteolysis was dependent on electrostatic COAM-SDF-1 interactions. By in vivo experiments in mice, we showed that the combination of COAM with SDF-1 delivered through physiological fibrin hydrogel had beneficial effect for the healing of skin wounds. Collectively, we show that COAM protects SDF-1 from proteolytic inactivation, maintaining SDF-1 biological activities. Thus, protection from proteolysis by COAM represents a therapeutic strategy to prolong SDF-1 bioavailability for wound healing applications.

Published
2024
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7. Etelcalcetide use During Maintenance Hemodialysis and Incidence of Parathyroidectomy After Kidney Transplantation

Author

Decleire, Pierre-Yves, Rommelaere, Marie, Guillen, Miguel-Ange, Buysschaert, Benoit, Vanderperren, Bénédicte, Cuvelier, Charles, Georges, Benoît, Papakrivopoulou, Eugenia, Braun, Claude, Gillerot, Gaëlle, Lengelé, Jean-Philippe, Reginster, François, Leroy, Philippe, Vandooren, Ann-Karolien, Madhoun, Philippe, Delaey, Philippe, Devresse, Arnaud, Morelle, Johann, Faitatzidou, Danai, Iriarte, Miren, Kanaan, Nada, Buemi, Antoine, Mourad, Michel, Darius, Tom, Goffin, Eric, Jadoul, Michel, and Labriola, Laura

Published
2024
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9. Monolithic Complementary Field Effect Transistors (CFET) Demonstrated using Middle Dielectric Isolation and Stacked Contacts.

Author

Steven Demuynck, Victor Vega-Gonzalez, C. Toledo de Carvalho Cavalcante, L. Petersen Barbosa Lima, K. Stiers, C. Sheng, A. Vandooren, M. Hosseini, X. Zhou, Hans Mertens, Thomas Chiarella, Jürgen Bömmels, Roger Loo, E. Rosseel, Clement Porret, Y. Shimura, A. Akula, G. Mannaert, S. Choudhury, V. Brissonneau, E. Dupuy, T. Sarkar, Nathali Franchina-Vergel, A. Peter, Nicolas Jourdan 0002, J. P. Soulie, Kevin Vandersmissen, F. Sebaai, P. Puttarame Gowda, K. Lai, A. Mingardi, S. Sumar Sarkar, K. D'Have, B. T. Chan, A. Sepulveda Marquez, R. Langer, I. Gyo Koo, E. Altamirano Sanchez, Katia Devriendt, P. Rincon Delgadillo, F. Lazzarino, Jérôme Mitard, J. Geypen, E. Grieten, D. Batuk, Y.-F. Chen, F. Verbeek, F. Holsteyns, S. Subramanian, N. Horiguchi, and S. Biesemans

Published
2024
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10. Chlorite-Oxidized Oxyamylose (COAM) Has Antibacterial Activity and Positively Affects Skin Wound Healing

Author

Pereira RVS, Ugarte-Berzal E, Vandooren J, Nylander K, Martens E, Van Mellaert L, Van Damme J, Vranckx JJ, Matthys P, Alamäe T, Phillipson M, Visnapuu T, and Opdenakker G

Subjects
antimicrobial, wound healing, neutrophils, macrophages, amylose derivative, staphylococcus, Pathology, RB1-214, Therapeutics. Pharmacology, RM1-950
Abstract

Rafaela Vaz Sousa Pereira,1 Estefania Ugarte-Berzal,1 Jennifer Vandooren,1 Karin Nylander,2 Erik Martens,1 Lieve Van Mellaert,1 Jo Van Damme,1 Jan Jeroen Vranckx,3 Patrick Matthys,1 Tiina Alamäe,4 Mia Phillipson,2 Triinu Visnapuu,4 Ghislain Opdenakker1 1Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, KU Leuven, Leuven, Belgium; 2Department of Medical Cell Biology, Division of Integrative Physiology, Uppsala University, Uppsala, Sweden; 3Department of Development & Regeneration & Department of Plastic & Reconstructive Surgery, University Hospitals Leuven and KU Leuven, Leuven, Belgium; 4Department of Genetics, Institute of Molecular and Cell Biology, University of Tartu, Tartu, EstoniaCorrespondence: Ghislain Opdenakker, Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, KU Leuven, Herestraat 49 Box 1044, Leuven, 3000, Belgium, Tel +32 16 37 9020, Fax +32 16 33 3026, Email ghislain.opdenakker@kuleuven.bePurpose: To verify the antibacterial and immunomodulatory effects of the amylose derivative – chlorite-oxidized oxyamylose (COAM) – in a skin wound setting.Methods: In vitro antibacterial effects of COAM against opportunistic bacterial pathogens common to skin wounds, including Staphylococcus aureus and methicillin-resistant Staphylococcus aureus (MRSA), were determined by cultivation methods. The effects of COAM on myeloid cell infiltration into full thickness skin wounds were investigated in wild-type and in transgenic CX3CR1-GFP mice.Results: On the basis of in vitro experiments, an antibacterial effect of COAM against Staphylococcus species including MRSA was confirmed. The minimum inhibitory concentration of COAM was determined as 2000 μg/mL against these bacterial strains. Control full thickness skin wounds yielded maximal neutrophil influxes and no additive effect on neutrophil influx was observed following topical COAM-treatment. However, COAM administration increased local CX3CR1 macrophage counts at days 3 and 4 and induced a trend towards better wound healing.Conclusion: Aside from its known broad antiviral impact, COAM possesses in vitro antibacterial effects specifically against Gram-positive opportunistic pathogens of the skin and modulates in vivo macrophage contents in mouse skin wounds.Keywords: antimicrobial, wound healing, neutrophils, macrophages, amylose derivative, Staphylococcus

Published
2022

11. HIV protease inhibitors Nelfinavir and Lopinavir/Ritonavir markedly improve lung pathology in SARS-CoV-2-infected Syrian hamsters despite lack of an antiviral effect

Author

Foo, Caroline S., Abdelnabi, Rana, Kaptein, Suzanne J.F., Zhang, Xin, ter Horst, Sebastiaan, Mols, Raf, Delang, Leen, Rocha-Pereira, Joana, Coelmont, Lotte, Leyssen, Pieter, Dallmeier, Kai, Vergote, Valentijn, Heylen, Elisabeth, Vangeel, Laura, Chatterjee, Arnab K., Annaert, Pieter P., Augustijns, Patrick F., De Jonghe, Steven, Jochmans, Dirk, Gouwy, Mieke, Cambier, Seppe, Vandooren, Jennifer, Proost, Paul, van Laer, Christine, Weynand, Birgit, and Neyts, Johan

Published
2022
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12. Combining a Drug and a Nutraceutical: A New Cocrystal of Praziquantel and Curcumin

Author

Camila Caro Garrido, Marie Vandooren, Koen Robeyns, Damien P. Debecker, Patricia Luis, and Tom Leyssens

Subjects
praziquantel, curcumin, nutraceutical, coformer, cocrystal solvate, cocrystal, Crystallography, QD901-999
Abstract

This study explores the co-crystallization between the drug praziquantel (PZQ) and the nutraceutical curcumin (CU). The investigation revealed two novel solid forms: a cocrystal solvate with ethyl acetate and a non-solvated cocrystal. This novel drug–nutraceutical cocrystal is a praziquantel–curcumin (2:1) cocrystal. The cocrystal solvate has ethyl acetate molecules occupying the voids with minimal interactions within the crystal lattice. The application of heat treatment induces solvent removal and prompts the transition to the non-solvated cocrystal, as highlighted by variable-temperature X-ray powder diffraction (VT-XRPD). Thermal analyses demonstrate the stability of the cocrystal solvate up to approximately 100 °C, beyond which it transforms into the non-solvated phase, which eventually melts at 130 °C.

Published
2024
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14. Physiological fibrin hydrogel modulates immune cells and molecules and accelerates mouse skin wound healing

Author

Rafaela Vaz Sousa Pereira, Mostafa EzEldeen, Estefania Ugarte-Berzal, Erik Martens, Bert Malengier-Devlies, Jennifer Vandooren, Jan Jeroen Vranckx, Patrick Matthys, and Ghislain Opdenakker

Subjects
wound healing, fibrin, leukocytes, macrophages, inflammation, hydrogel, Immunologic diseases. Allergy, RC581-607
Abstract

IntroductionWound healing is a complex process to restore homeostasis after injury and insufficient skin wound healing is a considerable problem in medicine. Whereas many attempts of regenerative medicine have been made for wound healing with growth factors and cell therapies, simple pharmacological and immunological studies are lagging behind. We investigated how fibrin hydrogels modulate immune cells and molecules in skin wound healing in mice.MethodsPhysiological fibrin hydrogels (3.5 mg/mL fibrinogen) were generated, biophysically analyzed for stiffness and protein contents and were structurally studied by scanning electron microscopy. Physiological fibrin hydrogels were applied to full thickness skin wounds and, after 3 days, cells and molecules in wound tissues were analyzed. Leukocytes, endothelial cells, fibroblasts and keratinocytes were explored with the use of Flow Cytometry, whereas cytokines and matrix metalloproteinases were analyzed with the use of qPCR, ELISAs and zymography. Skin wound healing was analyzed microscopically at day 3, macroscopically followed daily during repair in mice and compared with commercially available fibrin sealant Tisseel.ResultsExogenous fibrin at physiological concentrations decreased neutrophil and increased non-classical Ly6Clow monocyte and resolutive macrophage (CD206+ and CX3CR1+) populations, at day 3 after injury. Fibrin hydrogel reduced the expression of pro-inflammatory cytokines and increased IL-10 levels. In line with these findings, gelatinase B/MMP-9 was decreased, whereas gelatinase A/MMP-2 levels remained unaltered. Frequencies of dermal endothelial cells, fibroblasts and keratinocytes were increased and keratinocyte migration was enhanced by fibrin hydrogel. Importantly, physiological fibrin accelerated the healing of skin wounds in contrast to the highly concentrated fibrin sealant Tisseel, which delayed wound repair and possessed a higher fiber density.ConclusionCollectively, we show that adding a tailored fibrin hydrogel scaffold to a wound bed positively influences the healing process, modulating leukocyte populations and inflammatory responses towards a faster wound repair.

Published
2023
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18. ‘What about the coffee break?’ Designing virtual conference spaces for conviviality

Author

Michelle Bastian, Emil Henrik Flatø, Lisa Baraitser, Helge Jordheim, Laura Salisbury, and Thom vanDooren

Subjects
climate change, flying less, online conferences, time studies, virtual meetings, Environmental sciences, GE1-350, Geography (General), G1-922
Abstract

Abstract Geography, like many other disciplines, is reckoning with the carbon intensity of its practices and rethinking how activities such as annual meetings are held. The Climate Action Task Force of the American Association of Geographers (AAG), for example, was set up in 2019 and seeks to transform the annual conference in light of environmental justice concerns. Mirroring shifts in geographic practice across the globe, these efforts point to a need to understand how new opportunities for knowledge production, such as online events, can operate effectively. In this paper, we offer suggestions for best practice in virtual spaces arising from our Material Life of Time conference held in March 2021, a two‐day global event that ran synchronously across 15 time zones. Given concerns about lack of opportunities for informal exchanges at virtual conferences, or the ‘coffee break problem’, we designed the event to focus particularly on opportunities for conviviality. This was accomplished through a focus on three key design issues: the spatial, the temporal, and the social. We review previous work on the benefits and drawbacks of synchronous and asynchronous online conference methods and the kinds of geographic communities they might support. We then describe our design approach and reflect on its effectiveness via a variety of feedback materials. We show that our design enabled high delegate satisfaction, a sense of conviviality, and strong connections with new colleagues. However, we also discuss the problems with attendance levels and external commitments that hampered shared time together. We thus call for collective efforts to support the ‘event time’ of online meetings, rather than expectations to fit them around everyday tasks. Even so, our results suggest that synchronous online events need not result in geographical exclusions linked to time‐zone differences, and we outline further recommendations for reworking the spacetimes of the conference.

Published
2022
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19. Low incidence of SARS-CoV-2, risk factors of mortality and the course of illness in the French national cohort of dialysis patients

Author

Abbassi, Abdelhamid, Debure, Alain, Guerraoui, Abdallah, Benmoussa, Abdelatif, Hamani, Abdelaziz, Ziane, Abdelaziz, Nefti, Abdelhamid, Hadj, Abdelkader, El Amari, Abderrahim, Ghazali, Abderrahmane, Abd El Fatah Mohamed, Abo Bakr, Laradi, Achour, Ben Ahmed, Adel, Sahar, Adel, Pillet, Adele, Lacraz, Adeline, Moinat, Adnan, Massoumi, Afshin, Pardon, Agathe, Beaudoin, Agnes Caillette, Debout, Agnes Chapelet, Mariot, Agnes, Rachi, Ahmed, Afiani, Aida, Boula, Aime Remy, Jalaby, Al, Cremault, Alain, Fournier, Alain, Jeanson, Alain, Lyon, Alain, Nony, Alain, Robert, Alain, Slingeneyer, Alain, Labatide, Alanor Agnes, Sartorius, Albane Brodin, Bensman, Albert, Fournier, Albert, Ranlin, Alex, Sandor, Alex Vido, Colombo, Alexandra, Duhem, Alexandra, Stancu, Alexandra, Dufay, Alexandre, Dumoulin, Alexandre, Ebel, Alexandre, Klein, Alexandre, Martin, Alexandre, Mouneimne, Alexandre, Seidowsky, Alexandre, De Martin, Alfio, Zannier, Alfredo, Aizel, Ali, Hafi, Ali, Diddaoui, Ali Zineddine, Heyani, Alim, Mocanu, Alina, Preda, Alina, Hafi, Aline, Talaszka, Aline, Duquesne, Alyette, Amaouche, Amar, Ghemmour, Amel, Simon, Amelie, Skalli, Amina, Boukadida, Amine, Ragab Eid, Amr Ekhlas, Fedorca, Ana, Baillet, Anabelle, Poyet, Anais, Giorgita, Ancuta Bouffandeau, Ratsimbazafy, Anderson, Pruna, Andre, Argiles, Angel, Testa, Angelo, Vandooren, Ann Karolien, Jolivot, Anne, Labadens, Anne Kolko, Lataste, Anne, Maisin, Anne, Paris, Anne, Sechet, Anne, Wuillai, Anne, Heng, Anne Elisabeth, Josse, Anne Gaelle, Querard, Anne Helene, Reboux, Anne Helene, Adra, Anne Laure, Faller, Anne Laure, Leclerc, Anne Laure, Poitou, Anne Laure, Manucci, Annie Lahoche, Jacquet, Antoine, Pommereau, Antoine, Thierry, Antoine, Adem, Arezki, Chapelet, Arielle, Del Bello, Arnaud, Delezire, Arnaud, Garnier, Arnaud, Guerard, Arnaud, Klisnick, Arnaud, Lionet, Arnaud, Roccabianca, Arnaud, Stolz, Arnaud, Capdeville, Arthur, Allal, Asma, Alrifai, Assem, Diarrassouba, Assetou, Djema, Assia, Carre, Assia Ferhat, Dubrasquet, Astrid Godron, Elmrabet, Atman Haddj, Jegado, Audrey, Thomas, Aurelia Bertholet, Salandre, Aurelie Davourie, Pajot, Aurelie, Lorthioir, Aurelien, Tiple, Aurelien, Sury, Aurore, Abokasem, Ayman, Sarraj, Ayman, Henaoui, Bachir, Chaghouri, Baher, Wehbe, Bassem, Ball, Beatrice, Viron, Beatrice, Issad, Belkassem, Corne, Benedicte Hodemon, Janbon, Benedicte, Deroure, Benjamin, Savenkoff, Benjamin, Jonon, Benoit, Vendrely, Benoit, Djelaleddine, Benyakoub, Ohry, Bernard, Painchart, Bernard, Strullu, Bernard, Temperville, Bernard, Ebikili, Bertin, Hacq, Bertrand, Morel, Bertrand, Aoun, Bilal, Muniz, Blanca, Chlih, Bouchra, Amara, Brahim, Mayor, Brice, Gilson, Brigitte, Llanas, Brigitte, Zins, Brigitte, Bourgeon, Bruno, Coevoet, Bruno, Guery, Bruno, Legallicier, Bruno, Paris, Bruno, Ranchin, Bruno, Seigneuric, Bruno, Dita, Camelia Ghiciuc, Prelipcean, Camelia, Hottelart, Carine Achard, Diet, Carine, Frangie, Carlos, Vela, Carlos, Muresan, Carmina, Deprele, Carole, Araujo, Caroline, Bidault, Caroline, Creput, Caroline, Delclaux, Caroline, Du Halgouet, Caroline, Favennec, Caroline, Freguin, Caroline, Vercel, Caroline Gourraud, Mesguen, Caroline, Obama, Caroline Ndomo, Poitou, Caroline, Dirhold, Caroline Preissig, Roubiou, Caroline, Albert, Catherine, Bessin, Catherine, De Marion Gaja, Catherine, Godart, Catherine, Lasseur, Catherine, Leocardi, Catherine, Lumbroso, Catherine, Melander, Catherine, Michel, Catherine, Maurouard, Catherine Quere, Rouannet, Catherine, Taddei, Catherine, Verove, Cathy, Guiraud, Cecile, Tafelin, Cecile, Baron, Cecile Turc, Formet, Cedric, Pinier, Cedric, De Ste Foy, Celia Lessore, Granolleras, Celine, Bennini, Chaouki, Cartou, Charles, Chazot, Charles, Jouzel, Charlotte, Badid, Cherif, Roubicek, Christa, Viaud, Christel, Verrier, Christelle, Chuet, Christian, Combe, Christian, Dabot, Christian, Duvic, Christian, Emond, Christian, Lagarde, Christian, Lamotte, Christian, Pain, Christian, Mousson, Christiane, Lorriaux, Christie, Beauchamp, Christine, Fumeron, Christine, Le Gurun, Christine, Leroy, Christine, Pietrement, Christine, Richer, Christine, Bouaka, Christophe, Charasse, Christophe, Goupy, Christophe, Ridel, Christophe, Castrale, Cindy, Detourne, Cindy, Francois, Clair, Presne, Claire, Trivin, Claire, Von Kotze, Clarissa, Bernard, Claude, Bonniol, Claude, Desvergnes, Claude, Raharivelina, Claude, Nistor, Claudia, Gueret, Claudine, Lloret, Claudine, Saltiel, Claudine, Rosati, Clelia, Rabate, Clementine, Stanescu, Corina, Ferrandini, Corinne, Guibergia, Corinne, Lemoine, Corinne, Passeron, Corinne, Kahil, Cynthia, Garrouste, Cyril, Van, Cyril Vo, Jolimoy, Cyrille, Kesraoui, Dalila, Jolly, Damien, Thibaudin, Damien, Teboulle, Dan, Daubresse, Daniel, Louvet, Daniel, Rasamimanantsoa, Daniel, Toledano, Daniel, Babici, Daniela, David, Daniela, Dincu, Daniela, Bruno, Danielle, May, Delia, Haussaire, Delphine, Viprey, Delphine Henriet, Bugnon, Denis, Fouque, Denis, Morin, Denis, Nour, Derradji, Mahmoud, Diab Mohamed, Cristescu, Diana Istrati, Aguilera, Didier, Coste, Didier, Hamel, Didier, Le Chapois, Didier, Testou, Didier, Erbilgin, Dilaver, Dahmane, Djamal, Quang, Doan Bui, Bertrand, Dominique, Besnier, Dominique, Blanchier, Dominique, Briffa, Dominique, Caux, Dominique, Durand, Dominique, Fleury, Dominique, Guerrot, Dominique, Hestin, Dominique, Jaubert, Dominique, Joly, Dominique, Lombart, Dominique, Pagniez, Dominique, Pierre, Dominique, Schohn, Dominique, Ikonga, Donatien, Visanica, Dorina, Bazin, Dorothee, Boury, Edouard, Maksour, Edouard, Agbonon, Ekoue, Harrami, Elarbi, Marcu, Elena, Tudorache, Elena, Caniot, Elisabeth, Semjen, Elisabeth, Tomkiewicz, Elisabeth, Scheidt, Elise, Gaboriau, Elke, Lamouroux, Elodie, Guiard, Elsa, Passos, Elsa Martin, Nsembani, Emerson, Fache, Emilie, Kalbacher, Emilie, Pambrun, Emilie, Pincon, Emilie, Launay, Emma Allain, Baron, Emmanuel, Dupuis, Emmanuel, Villar, Emmanuel, Charlin, Emmanuelle, Hecquet, Emmanuelle, Kohler, Emmanuelle, Laurain, Emmanuelle, Rosier, Emmanuelle, Figueroa, Enrique, Azoulay, Eric, Canivet, Eric, Daugas, Eric, Gauthier, Eric, Laruelle, Eric, Le Guen, Eric, Legrand, Eric, Moumas, Eric, Postec, Eric, Prinz, Eric, Renaudineau, Eric, Desport, Estelle, Sutra, Estelle Ricard, Berard, Etienne, Ged, Etienne, Robin, Etienne, Vilaine, Eve, Bargas, Evelyne, Namara, Evelyne Mac, Combarnous, François, Yazbeck, Fatima, Gerard, Fabien, Metivier, Fabien, Parazols, Fabien, Soulis, Fabien, Garnier, Fabrice, Messaoudene, Fadhila Pech, Haidar, Fadi, Boullenger, Fanny, Lepeytre, Fanny, Leroy, Fanny, Frejate, Fares, Bellahsene, Farid, Bellhasene, Farid, Saidani, Farid, Toure, Fatouma, Kriaa, Faycal, Nemmar, Fazia, Vetromile, Fernando, Chalmin, Florence, Lucats, Florence, Sens, Florence, Villemain, Florence, Plasse, Florent, Lebhour, Fouad, Schillinger, Francis, Berge, Franck, Bourdon, Franck, Bridoux, Franck, Reynaud, Franck, Babinet, Francois, Basse, Francois, Chantrel, Francois, Clair, Francois, Coulomb, Francois, De Cornelissen, Francois, Glowacki, Francois, Marchal, Francois, Maurice, Francois, Nobili, Francois, Pourreau, Francois, Provot, Francois, Amani, Francois Roux, Broux, Francoise, Bulte, Francoise, Heibel, Francoise, Leonetti, Francoise, Schott, Francoise Moussion, Le Roy, Frank, Besson, Frederic, Lavainne, Frederic, Tollis, Frederic, Bocquentin, Frederique, Meeus, Frederique, Vecina, Frederique, Von Ey, Friederike, Balit, Gabriel, Choukroun, Gabriel, Gruget, Gabriel, Huchard, Gabriel, Golea, Gabriella, Duneau, Gabrielle, Lefrancois, Gaelle, Pelle, Gaelle, Lebrun, Gaetan, Dumont, Genevieve, Brillet, Georges, Deschenes, Georges, Mourad, Georges, Stamatakis, Georges, Cazajous, Geraldine, D'ythurbide, Geraldine, Wiart, Geraldine Robitaille, Cardon, Gerard, Champion, Gerard, Deschodt, Gerard, Mangenot, Gerard, Motte, Gerard, Schortgen, Gerard, Boulahia, Ghada, Maakaroun, Ghassan, Michel, Ghylene Bourdat, Zanetta, Gilbert, Hufnagel, Gilles, Messier, Gilles, Piccoli, Giorgina, Desvergnes, Gregoire Couvrat, Bobrie, Guillaume, Bonnard, Guillaume, Clement, Guillaume, Jean, Guillaume, Queffeulou, Guillaume, Seret, Guillaume, Vernin, Guillaume, Delavaud, Guy, Lambrey, Guy, Rostoker, Guy, Poussard, Gwenaelle, Kesler, Gwenaelle Roussey, Leon, H., Aboubekr, Habib, Boulechfar, Hacene, Sekhri, Hacene, Hebibi, Hadia, Benalia, Hadjira, Fessi, Hafed, Atchia, Hafsabhai, Bittar, Haiat, Maiza, Hakim, Mazouz, Hakim, El Ali, Hamid, Bougrida, Hammouche, Van Der Pijl, Hans, Lokmane, Hassan, Izzedine, Hassane, Adda, Hassen, De Preneuf, Helene, Leray, Helene, Philippot, Helene, Boulanger, Henri, Merault, Henri, Renaud, Henri, Bonarek, Herve, Maheut, Herve, Nzeyimana, Hilaire, Mehama, Hocine, Zaidi, Hocine, Weclawiak, Hugo, Flodrops, Hugues, Karaaslan, Huseyin, Haskour, Ibrahim, Belhadj, Ihssen, Almoubarak, Imad, Haddad, Imad, Castellano, Ines, Ferrandiz, Ines, Daniliuc, Ioana, Darie, Ioana, Enache, Ioana, Prunescu, Ionut, Djiconkpode, Irenee, Shahapuni, Irina, Bouchoule, Isabelle, Devriendt, Isabelle, Kazes, Isabelle, Kolb, Isabelle, Landru, Isabelle, Poli, Isabelle, Rey, Isabelle, Segalen, Isabelle, Selcer, Isabelle, Vernier, Isabelle, Vrillon, Isabelle, Guenifi, Ismahane, Gheerbrandt, J. Dominique, Potier, Jacky, Becart, Jacques, Cledes, Jacques, Ducros, Jacques, Duvic, Jacques, Fourcade, Jacques, Gaultier, Jacques, Jurine, Jacques, Lebleu, Jacques, Ollier, Jacques, Charles, Jacques Ibsen, Yazji, Jamal, Mansour, Janette, Arnautou, Jean, Brocard, Jean, Carolfi, Jean, Montoriol, Jean, Gouin, Jean Baptiste, Palcoux, Jean Bernard, Bendini, Jean Christophe, Aldigier, Jean Claude, Alphonse, Jean Claude, Delbet, Jean Daniel, Bonne, Jean Francois, Cantin, Jean Francois, De Fremont, Jean Francois, Dessassis, Jean Francois, Subra, Jean Francois, Valentin, Jean Francois, Verdier, Jean Francois, Dion, Jean Jacques, Haultier, Jean Jacques, Montseny, Jean Jacques, Bacri, Jean Louis, Bouchet, Jean Louis, Mahe, Jean Luc, Chalopin, Jean Marc, Gabriel, Jean Marc, Hurot, Jean Marc, Lanau, Jean Marc, Batho, Jean Marie, Coulibaly, Jean Marie, Hardin, Jean Michel, Marc, Jean Michel, Poux, Jean Michel, Rebibou, Jean Michel, Tivollier, Jean Michel, Ottavioli, Jean Noel, Faucon, Jean Paul, Imiela, Jean Paul, Jaulin, Jean Paul, Masselot, Jean Paul, Ortiz, Jean Paul, Bourdenx, Jean Philippe, Devaux, Jean Philippe, Hammelin, Jean Philippe, Rivory, Jean Pierre, Wauquier, Jean Pierre, Larue, Jean Rene, Mondain, Jean Rene, Borde, Jean Sebastien, Virot, Jean Simon, Bosc, Jean Yves, Achiche, Jedjiga, Parasote, Jennifer, Diolez, Jeremie, Harambat, Jerome, Potier, Jerome, Sampol, Jerome, Mustel, Jihad, Lefevre, Jean Jacques, Maurizi, Jocelyne, Gamberoni, Joel, Claudeon, Joelle, Terzic, Joelle, Rogol, Joffrey, Sayegh, Johnny, Cardozo, Jorge, Brasseur, Jose, Guiserix, Jose, Barsumau, Joseph, Albaret, Julie, Beaume, Julie, Attias, Julie Sohier, Dehay, Julien, Hogan, Julien, Journet, Julien, Ott, Julien, Baleynaud, Juliette, Bacchetta, Justine, Faucher, Justine, Yousfi, Kamel, Dardim, Karim, Clabault, Karine, Moreau, Karine, Thomas, Kedna, Sirajedine, Khaled, Chedid, Khalil, El Kaeoui, Khalil, El Karoui, Khalil, Bouachi, Khedidja, Hue, Kheira, El Nasser, Khuzama, Akposso, Kodso, Kunz, Kristian, Bijak, Krzysztof, Kihal, Lilia, Rasoloarijaona, L., Harbouche, Laid, Bencheikh, Larbi, Lamriben, Larbie, Hanafi, Latifa, Parvez, Laura Braun, Champion, Laure, Croze, Laure, Eprinchard, Laure, Patrier, Laure, Nicolet, Laurence, Vrigneaud, Laurence, Duflot, Laurent, Mackaya, Leandre, Chenine, Leila, Odry, Leon, Tamiji, Lili Taghipour, Bouzar, Lilia Antri, Nga Messi, Liliane Ngango, Le Mouellic, Lionel, Mandart, Lise, Weis, Lise, Pouteau, Lise Marie, Georgieva, Lora, Vitanova, Lorita, Chalabi, Lotfi, Delvallez, Luc, Frimat, Luc, Fromentin, Luc, Marty, Luc, Monjot, Luc, Spataru, Luciana, Bessenay, Lucie, Boissinot, Lucie, Wajsbrot, Lucie, Rakoff, Lucien, Lebourg, Ludivine, Perez, Lydie, Lafage, Lyliane, Azzouz, Lynda, Dumoulin, Madeleine, Ouziala, Messaoud, Joseph, Maan, Brahimi, Mabrouk, Fat, Maeva Wong, Fort, Magalie, Nakhla, Magued, Abtahi, Mahdi, Albadawy, Mahen, Alouach, Mahmoud, Mezghani, Mahmoud, Daroux, Maite, Boukelmoune, Maklouf, Dhib, Malek, Touam, Malik, Dubau, Malina, Balde, Mamadou, Khoa, Man Nguyen, Ismer, Manfred, Mehdi, Manolie, Laforet, Manon, Bouiller, Marc, Eugene, Marc, Fila, Marc, Hazzan, Marc, Kribs, Marc, Ladriere, Marc, Lebot, Marc, Padilla, Marc, Souid, Marc, Marraoui, Marcel, Burbach, Maren, Manescu, Maria, Noguera Gonzalez, Maria Eugenia, Revenco, Mariana, Terrasse, Marianne, Essi, Marie, Macher, Marie Alice, Nogier, Marie Beatrice, Cazin, Marie Cecile, Schweitzer Camoin, Marie Christine, Thouret, Marie Christine, Hannaert, Marie Claude, Servel, Marie France, Chabannier, Marie Helene, Coudert Krier, Marie Jeanne, Catoliquot, Marie Noelle, Guillodo, Marie Paule, Gavard, Marie Sophie, Vairon Codaccioni, Marie Xaviere, Rabec, Marina, Freist, Marine, Gauthier, Marion, Lemaire, Marion, Mehrenberger, Marion, Venot, Marion, Pongas, Marios, Diant, Marlene Beaubrun, Levannier, Martial, Bertaux, Martine, Jablonski, Mathieu, Sacquepee, Mathieu, Dargelos, Mathilde, Lemoine, Mathilde, Tamain, Mathilde, Monge, Matthieu, Reberolle, Matthieu, Cousin, Maud, Francois, Maud, Baron, Maurice, Hoffmann, Maxime, Ingwiller, Maxime, Touzot, Maxime, Mohajer, Mederick, Maaz, Mehadji, Hanoy, Melanie, Marroc, Melanie, Cuny, Melodie, Van Der Straaten, Menno, Serveaux, Mf., Basteri, Michel, Chong, Michel Fen, Hecht, Michel, Massad, Michel, Normand, Michel, Olmer, Michel, Tolani, Michel, Tsimaratos, Michel, Hemery, Michele, Kessler, Michele, Esposito, Miguel, Shenouda, Milad, Kareche, Mimi, Khalili, Mina, Diaconita, Mirella, Rifard, Mohamad Khair, Aladib, Mohamed, Belmouaz, Mohamed, Brahim, Mohamed, Diouani, Mohamed, Cherif, Mohamed Fodil, Jamali, Mohamed, Maghlaoua, Mohamed, Meddeb, Mohamed, Ramdane, Mohamed, Rifaat, Mohamed, Islam, Mohamed Sharifull, Abbade, Mohamed Adnan, Amrandi, Mokhtar, Chawki, Mokhtar, Ciobotaru, Monica, Indrieis, Monica, Chanas, Monique, Hoarau, Monique, Tomeh, Monzer, Bellou, Moufida, Bouzernidj, Mouloud, Ammor, Mounia, Guergour, Mounir, Benzakour, Mountassir, Hachicha, Mourad, Coulibaly, Moussa, Smati, Mustafa, Al Morabiti, Mustapha, Amirou, Mustapha, Isnard, Myriam, Pastural, Myriam, Pujo, Myriam, Boumendjel, Nourredine, Majbri, Nabil, Goumri, Nabila, Mingat, Nadege, Bassilios, Nader, Kerkeni, Nadia, Sedrati, Nadia, Soltani, Nadia, Maroun, Nadine, Neyrat, Nadine, Luang, Nahn, El Esper, Najeh, Ammar, Naji, Ghali, Nasredine, Hamdini, Nasser, Noel, Natacha, Potelune, Natacha, Maisonneuve, Nathalie, Pertuiset, Nathalie, Raynal, Nathalie, Vittoz, Nathalie, Terki, Nazim, Castin, Nelly, Nankeu, Nestor, Bouvier, Nicolas, Keller, Nicolas, Legros, Nicolas, Peters, Nicolas, Quirin, Nicolas, Lefrancois, Nicole, Monnier, Nicole, Rance, Nicole, Bruckmann, Niels, Mertens, Noel, Lorcy, Nolwenn, Gilbert, Olivia, Coldefy, Olivier, Drouineau, Olivier, Dunand, Olivier, Fritz, Olivier, Imhoff, Olivier, Kourilsky, Olivier, Lavelle, Olivier, Moranne, Olivier, Papin, Olivier, Roques, Olivier, Le Maner, Ophelie, Benbrahim, Oussamah Fikri, Erina Torres, Pablo Antonio, Urena Torres, Pablo Antonio, Malvezzi, Paolo, Bindi, Pascal, Cluzel, Pascal, Fontanier, Pascal, Wheatley, Pascal, Depraetre, Pascale, Dubosq, Pascale, Halin, Pascale, Sebahoun, Pascale, Siohan, Pascale, Testevuide, Pascale, Deteix, Patrice, Nolen, Patrice, Hue, Patricia, Lemarchand, Patricia, Donnadieu, Patrick, Fievet, Patrick, Fohrer, Patrick, Francais, Patrick, Giraud, Patrick, Hallonet, Patrick, Henri, Patrick, Michaut, Patrick, Niaudet, Patrick, Pauly, Patrick, Thomas, Patrick, Deleaval, Patrik, Finielz, Paul, Stroumza, Paul, Yverneau, Paule Hardy, Caillard, Pauline, Palacin, Pedro, Aubertin, Perrine, Attias, Philippe, Brunet, Philippe, Chauveau, Philippe, Coindre, Philippe, Coste, Philippe, Dubot, Philippe, Fournier, Philippe, Hiernaux, Philippe, Jousset, Philippe, Yue Wah, Philippe Lan, Lang, Philippe, Le Cacheux, Philippe, Dupont, Philippe Martin, Michel, Philippe, Mirgaine, Philippe, Moriniere, Philippe, Nicoud, Philippe, Rieu, Philippe, Rousseau, Philippe, Sporer, Philippe, Thorel, Philippe, Vanhille, Philippe, Vigeral, Philippe, Zaoui, Philippe, Bataille, Pierre, Brignon, Pierre, Filipozzi, Pierre, Housset, Pierre, Peyronnet, Pierre, Ramperez, Pierre, Vautrin, Pierre, Michel, Pierre Alexandre, Westeel, Pierre Francois, Carron, Pierre Louis, Durand, Pierre Yves, Parent, Pierrot, Seniuta, Piotr, Kuentz, François, Fraoui, Rabah, Tetaz, Rachel, Amaria, Rachid, Bourouma, Rachid, Djeffal, Rachid, Nebbad, Rachida, Allal, Radia, Dimulescu, Radu, Boustani, Rafaat, Mesbah, Rafik, Makdassi, Raifat, Diab, Raji, Puslenghea, Raluca, Roura, Raoul, Khayat, Rateb, Azar, Raymond, Frayssinet, Raymond, Monkam, Regine, Boulahrouz, Rehouni, Boudet, Remi, Demontis, Renato, Gansey, Renaud, Cuvelier, Rene, Schmitt, Renee, Noordally, Reschad, Binaut, Reynald, Latif, Rezkallah, Dufresne, Richard, Montagnac, Richard, Reade, Richard, Genin, Robert, Novo, Robert, Fickl, Rocsana, Dufresne, Roger, Magnol, Roger, Issautier, Roland, Mortelette, Romain, Delaval, Ronan, Lohro, Ronan, M'barga, Roseline, Beau, S., Dupuis, Clémentine, Vidil, Marie Jacques, Hacini, Sabria, Dahmoune, Said, Lekhal, Saliha, Sakso, Salima Ahriz, Saksi, Salima, Citarda, Salvatore, Boubenider, Samir, Kassis, Samuel, Verhille, Sandra, Genestier, Sandrine, Muller, Sandrine, Krid, Saoussen, Richter, Sarah, Delbes, Sebastien, Mailliez, Sebastien, Veillon, Sebastien, Nony, Sébastien, Benarbia, Seddick, Beaudreuil, Severine, Benyaghla, Sidi Ali, Duquennoy, Simon, Baluta, Simona, Boncila, Simona, Mzoughi, Sonia, Ribal, Sonia, Acamer, Sophie, Chauvet, Sophie, Girerd, Sophie, Ozenne, Sophie, Parahy, Sophie, Duval, Sophie Rubens, Taque, Sophie, Menouer, Soraya, Chargui, Soumaya, Bataille, Stanislas, Barbier, Stephane, Billion, Stephane, Roueff, Stephane, Torner, Stephane, Martin, Stephane Jean, Coupel, Stephanie, Cloarec, Sylvie, Lavaud, Sylvie, Leou, Sylvie, Chatelet, T., Onesta, Tania, Benhabib, Tassadit, Bensalem, Tayeb, Dimulescu, Theodora, Sawadogo, Theophile, Hitze, Thibault Dolley, Baranger, Thierry, Boudemaghe, Thierry, Hannedouche, Thierry, Krummel, Thierry, Lobbedez, Thierry, Milcent, Thierry, Dervaux, Thomas, Guincestre, Thomas, Kofman, Thomas, Raphael, Thomas, Sadreux, Thomas, Ulinski, Tim, Roger, Tiphaine Guyon, Serrato, Tomas, Kofman, Tomek, Wong, Tony, Boubia, Toufik, Gbindoun, Ubald Assogba, Khuzaie, Usama, Caudwell, Valerie, Chatelet, Valerie, Crougneau, Valerie, De Precigout, Valerie, Drouillat, Valerie, Galantine, Valerie, Hugot, Valerie Granveau, Leroy, Valerie, Boubia, Veronique, Falque, Veronique, Fournier, Veronique, Queron, Veronique, Viviani, Veronique, Gueuttin, Victor, Panescu, Victor, Calonge, Victorio Menoyo, Nguyen, Viet, Allot, Vincent, Delattre, Vincent, Leduc, Vincent, Pradier, Vincent, Aglae, Violaine Emal, Badulescu, Viorica, Molina, Virginia, Besson, Virginie, Chaigne, Virginie, Jaber, Waddah, Boudi, Wael, El Haggan, Wael, Guillon, Wen Qin, Aneni, Wided Tabbi, Hanf, William, Kohn, Wladimir, Bellenfant, Xavier, Gaudry, Xavier Moreau, Delmas, Yahsou, Knefati, Yannick, Saingra, Yannick, Tirolien, Yannick, Mann, Youssef, Brunak, Yvan, Dimitrov, Yves, Doussy, Yves, Tanter, Yves, Benabid, Zaid, Soltani, Zaara, Boukerroucha, Zacharia, Takla, Zafer, Ramanantsialonina, Zana, Dickson, Zara, Tubail, Zead, Pour, Zoe Koochaki, Boukhalfa, Zohra, Jacquot, Zohra, Couchoud, Cécile, Bayer, Florian, Ayav, Carole, Béchade, Clémence, Chantrel, François, Galland, Roula, Hourmant, Maryvonne, and Mercadal, Lucile

Published
2020
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21. Demonstration of 3D sequential FD-SOI on CMOS FinFET stacking featuring low temperature Si layer transfer and top tier device fabrication with tier interconnections.

Author

A. Vandooren, N. Parihar, Jacopo Franco, Roger Loo, Hiroaki Arimura, R. Rodriguez, F. Sebaai, S. Iacovo, Kevin Vandersmissen, W. Li, G. Mannaert, D. Radisic, E. Rosseel, Andriy Hikavyy, Anne Jourdain, O. Mourey, G. Gaudin, Shay Reboh, L. Le Van-Jodin, Guillaume Besnard, C. Roda Neve, Bich-Yen Nguyen, Iuliana P. Radu, E. Dentoni Litta, and N. Horiguchi

Published
2022
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23. Atypical response to bacterial coinfection and persistent neutrophilic bronchoalveolar inflammation distinguish critical COVID-19 from influenza

Author

Seppe Cambier, Mieke Metzemaekers, Ana Carolina de Carvalho, Amber Nooyens, Cato Jacobs, Lore Vanderbeke, Bert Malengier-Devlies, Mieke Gouwy, Elisabeth Heylen, Philippe Meersseman, Greet Hermans, Els Wauters, Alexander Wilmer, the CONTAGIOUS Consortium, Dominique Schols, Patrick Matthys, Ghislain Opdenakker, Rafael Elias Marques, Joost Wauters, Jennifer Vandooren, and Paul Proost

Subjects
COVID-19, Immunology, Medicine
Abstract

Neutrophils are recognized as important circulating effector cells in the pathophysiology of severe coronavirus disease 2019 (COVID-19). However, their role within the inflamed lungs is incompletely understood. Here, we collected bronchoalveolar lavage (BAL) fluids and parallel blood samples of critically ill COVID-19 patients requiring invasive mechanical ventilation and compared BAL fluid parameters with those of mechanically ventilated patients with influenza, as a non–COVID-19 viral pneumonia cohort. Compared with those of patients with influenza, BAL fluids of patients with COVID-19 contained increased numbers of hyperactivated degranulating neutrophils and elevated concentrations of the cytokines IL-1β, IL-1RA, IL-17A, TNF-α, and G-CSF; the chemokines CCL7, CXCL1, CXCL8, CXCL11, and CXCL12α; and the protease inhibitors elafin, secretory leukocyte protease inhibitor, and tissue inhibitor of metalloproteinases 1. In contrast, α-1 antitrypsin levels and net proteolytic activity were comparable in COVID-19 and influenza BAL fluids. During antibiotic treatment for bacterial coinfections, increased BAL fluid levels of several activating and chemotactic factors for monocytes, lymphocytes, and NK cells were detected in patients with COVID-19 whereas concentrations tended to decrease in patients with influenza, highlighting the persistent immunological response to coinfections in COVID-19. Finally, the high proteolytic activity in COVID-19 lungs suggests considering protease inhibitors as a treatment option.

Published
2022
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24. Alpha-2-Macroglobulin in Inflammation, Immunity and Infections

Author

Jennifer Vandooren and Yoshifumi Itoh

Subjects
alpha-2-macroglobulin, proteolysis, inflammation, immunity, infections, macrophages, Immunologic diseases. Allergy, RC581-607
Abstract

Alpha-2-macroglobulin is an extracellular macromolecule mainly known for its role as a broad-spectrum protease inhibitor. By presenting itself as an optimal substrate for endopeptidases of all catalytic types, alpha-2-macroglobulin lures active proteases into its molecular cage and subsequently ‘flags’ their complex for elimination. In addition to its role as a regulator of extracellular proteolysis, alpha-2-macroglobulin also has other functions such as switching proteolysis towards small substrates, facilitating cell migration and the binding of cytokines, growth factors and damaged extracellular proteins. These functions appear particularly important in the context of immune-cell function. In this review manuscript, we provide an overview of all functions of alpha-2-macroglobulin and place these in the context of inflammation, immunity and infections.

Published
2021
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25. Proteoform Analysis of Matrix Metalloproteinase-9/Gelatinase B and Discovery of Its Citrullination in Rheumatoid Arthritis Synovial Fluids

Author

Bernard Grillet, Karen Yu, Estefania Ugarte-Berzal, Rik Janssens, Rafaela Vaz Sousa Pereira, Lise Boon, Erik Martens, Nele Berghmans, Isabelle Ronsse, Ilse Van Aelst, Pierre Fiten, René Conings, Jennifer Vandooren, Patrick Verschueren, Jo Van Damme, Paul Proost, and Ghislain Opdenakker

Subjects
matrix metalloproteinase, arthritis, proteoform, proteolysis, citrullination, synovial fluid, Immunologic diseases. Allergy, RC581-607
Abstract

ObjectivesTo explore posttranslational modifications (PTMs), including proteolytic activation, multimerization, complex formation and citrullination of gelatinases, in particular of gelatinase B/MMP-9, and to detect in gelatin-Sepharose affinity-purified synovial fluids, the presence of specific MMP proteoforms in relation to arthritis.MethodsLatent, activated, complexed and truncated gelatinase-A/MMP-2 and gelatinase B/MMP-9 proteoforms were detected with the use of zymography analysis to compare specific levels, with substrate conversion assays, to test net proteolytic activities and by Western blot analysis to decipher truncation variants. Citrullination was detected with enhanced sensitivity, by the use of a new monoclonal antibody against modified citrullines.ResultsAll MMP-9 and MMP-2 proteoforms were identified in archival synovial fluids with the use of zymography analysis and the levels of MMP-9 versus MMP-2 were studied in various arthritic diseases, including rheumatoid arthritis (RA). Secondly, we resolved misinterpretations of MMP-9 levels versus proteolytic activities. Thirdly, a citrullinated, truncated proteoform of MMP-9 was discovered in archival RA synovial fluid samples and its presence was corroborated as citrullinated hemopexin-less MMP-9 in a small prospective RA sample cohort.ConclusionSynovial fluids from rheumatoid arthritis contain high levels of MMP-9, including its truncated and citrullinated proteoform. The combination of MMP-9 as analyte and its PTM by citrullination could be of clinical interest, especially in the field of arthritic diseases.

Published
2021
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27. Protection of stromal cell-derived factor-1 SDF-1/CXCL12 against proteases yields improved skin wound healing.

Author

Sousa Pereira, Rafaela Vaz, EzEldeen, Mostafa, Ugarte-Berzal, Estefania, Vandooren, Jennifer, Martens, Erik, Gouwy, Mieke, Ganseman, Eva, Van Damme, Jo, Matthys, Patrick, Vranckx, Jan Jeroen, Proost, Paul, and Opdenakker, Ghislain

Subjects
STROMAL cell-derived factor 1, CHEMOTACTIC factors, CXCR4 receptors, INTRACELLULAR calcium, WOUND healing, FIBRIN
Abstract

SDF-1/CXCL12 is a unique chemotactic factor with multiple functions on various types of precursor cells, all carrying the cognate receptor CXCR4. Whereas individual biological functions of SDF-1/CXCL12 have been well documented, practical applications in medicine are insufficiently studied. This is explained by the complex multifunctional biology of SDF-1 with systemic and local effects, critical dependence of SDF-1 activity on aminoterminal proteolytic processing and limited knowledge of applicable modulators of its activity. We here present new insights into modulation of SDF-1 activity in vitro and in vivo by a macromolecular compound, chlorite-oxidized oxyamylose (COAM). COAM prevented the proteolytic inactivation of SDF-1 by two inflammationassociated proteases: matrix met a lloproteinase-9/MMP-9 and dipeptidylpeptidase IV/DPPIV/CD26. The inhibition of proteolytic inactivation was functionally measured by receptor-mediated effects, including intracellular calcium mobilization, ERK1/2 phosphorylation, receptor internalization and chemotaxis of CXCR4-positive cells. Protection of SDF-1/CXCL12 against proteolysis was dependent on electrostatic COAM-SDF-1 interactions. By in vivo experiments in mice, we showed that the combination of COAM with SDF-1 delivered through physiological fibrin hydrogel had beneficial effect for the healing of skin wounds. Collectively, we show that COAM protects SDF-1 from proteolytic inactivation, maintaining SDF-1 biological activities. Thus, protection from proteolysis by COAM represents a therapeutic strategy to prolong SDF-1 bioavailability for wound healing applications. [ABSTRACT FROM AUTHOR]

Published
2024
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28. 3D Stacked Devices and MOL Innovations for Post-Nanosheet CMOS Scaling

Author

Horiguchi, N., primary, Mertens, H., additional, Chiarella, T., additional, Demuynck, S., additional, Vega-Gonzalez, V., additional, Vandooren, A., additional, Veloso, A., additional, Bardon, M. Garcia, additional, Sisto, G., additional, Gupta, A., additional, Tokei, Z., additional, Biesemans, S., additional, and Ryckaert, J., additional

Published
2023
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30. Internal Disulfide Bonding and Glycosylation of Interleukin-7 Protect Against Proteolytic Inactivation by Neutrophil Metalloproteinases and Serine Proteases

Author

Jennifer Vandooren, Rafaela Vaz Sousa Pereira, Estefania Ugarte-Berzal, Vasily Rybakin, Sam Noppen, Melissa R. Stas, Eline Bernaerts, Eva Ganseman, Mieke Metzemaekers, Dominique Schols, Paul Proost, and Ghislain Opdenakker

Subjects
IL-7, matrix metalloproteinase-9, proteolysis, signal transduction, proliferation, neutrophils, Immunologic diseases. Allergy, RC581-607
Abstract

Interleukin 7 (IL-7) is a cell growth factor with a central role in normal T cell development, survival and differentiation. The lack of IL-7–IL-7 receptor(R)-mediated signaling compromises lymphoid development, whereas increased signaling activity contributes to the development of chronic inflammation, cancer and autoimmunity. Gain-of-function alterations of the IL-7R and the signaling through Janus kinases (JAKs) and signal transducers and activators of transcription (STATs) are enriched in T cell acute lymphoblastic leukemia (T-ALL) and autocrine production of IL-7 by T-ALL cells is involved in the phenotypes of leukemic initiation and oncogenic spreading. Several IL-7-associated pathologies are also characterized by increased presence of matrix metalloproteinase-9 (MMP-9), due to neutrophil degranulation and its regulated production by other cell types. Since proteases secreted by neutrophils are known to modulate the activity of many cytokines, we investigated the interactions between IL-7, MMP-9 and several other neutrophil-derived proteases. We demonstrated that MMP-9 efficiently cleaved human IL-7 in the exposed loop between the α-helices C and D and that this process is delayed by IL-7 N-linked glycosylation. Functionally, the proteolytic cleavage of IL-7 did not influence IL-7Rα binding and internalization nor the direct pro-proliferative effects of IL-7 on a T-ALL cell line (HPB-ALL) or in primary CD8+ human peripheral blood mononuclear cells. A comparable effect was observed for the neutrophil serine proteases neutrophil elastase, proteinase 3 and combinations of neutrophil proteases. Hence, glycosylation and disulfide bonding as two posttranslational modifications influence IL-7 bioavailability in the human species: glycosylation protects against proteolysis, whereas internal cysteine bridging under physiological redox state keeps the IL-7 conformations as active proteoforms. Finally, we showed that mouse IL-7 does not contain the protease-sensitive loop and, consequently, was not cleaved by MMP-9. With the latter finding we discovered differences in IL-7 biology between the human and mouse species.

Published
2021
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32. Sequential 3D: Key integration challenges and opportunities for advanced semiconductor scaling.

Author

A. Vandooren, Liesbeth Witters, Jacopo Franco, Arindam Mallik, Bertrand Parvais, Z. Wu, Amey Walke, V. Deshpande, E. Rosseel, Andriy Hikavyy, W. Li, L. Peng, Nouredine Rassoul, Geraldine Jamieson, Fumihiro Inoue, G. Verbinnen, Katia Devriendt, Lieve Teugels, N. Heylen, E. Vecchio, T. Zheng, Niamh Waldron, Vincent De Heyn, Dan Mocuta, and Nadine Collaert

Published
2018
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33. Study on the economic and technical evolution of the scientific publication markets in Europe [The EU scientific publishing study]

Author

Vandooren, Francoise

Subjects
JH. Digital preservation., E. Publishing and legal issues., BG. Information dissemination and diffusion.
Abstract

Dissemination and access to research results is a pillar in the development of the ERA. Current public debate reveals worries about the current conditions of access and dissemination of scientific publications. The study launched by EC DG Research seeks to identify measures at European level which could help improve the conditions governing access to and the exchange, dissemination and archiving of scientific publications. Its aim is to lead to positive actions, taking into account all actors/stakeholders.

Published
2005

34. From ELISA to Immunosorbent Tandem Mass Spectrometry Proteoform Analysis: The Example of CXCL8/Interleukin-8

Author

Mieke Metzemaekers, Sara Abouelasrar Salama, Jennifer Vandooren, Anneleen Mortier, Rik Janssens, Sofie Vandendriessche, Eva Ganseman, Erik Martens, Mieke Gouwy, Barbara Neerinckx, Patrick Verschueren, Lien De Somer, Carine Wouters, Sofie Struyf, Ghislain Opdenakker, Jo Van Damme, and Paul Proost

Subjects
chemokine, CXCL8, neutrophil, ELISA, proteolysis, posttranslational modification, Immunologic diseases. Allergy, RC581-607
Abstract

With ELISAs one detects the ensemble of immunoreactive molecules in biological samples. For biomolecules undergoing proteolysis for activation, potentiation or inhibition, other techniques are necessary to study biology. Here we develop methodology that combines immunosorbent sample preparation and nano-scale liquid chromatography—tandem mass spectrometry (nano-LC-MS/MS) for proteoform analysis (ISTAMPA) and apply this to the aglycosyl chemokine CXCL8. CXCL8, the most powerful human chemokine with neutrophil chemotactic and –activating properties, occurs in different NH2-terminal proteoforms due to its susceptibility to site-specific proteolytic modification. Specific proteoforms display up to 30-fold enhanced activity. The immunosorbent ion trap top-down mass spectrometry-based approach for proteoform analysis allows for simultaneous detection and quantification of full-length CXCL8(1-77), elongated CXCL8(-2-77) and all naturally occurring truncated CXCL8 forms in biological samples. For the first time we demonstrate site-specific proteolytic activation of CXCL8 in synovial fluids from patients with chronic joint inflammation and address the importance of sample collection and processing.

Published
2021
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35. Kinetics of peripheral blood neutrophils in severe coronavirus disease 2019

Author

Mieke Metzemaekers, Seppe Cambier, Marfa Blanter, Jennifer Vandooren, Ana Carolina deCarvalho, Bert Malengier‐Devlies, Lore Vanderbeke, Cato Jacobs, Sofie Coenen, Erik Martens, Noëmie Pörtner, Lotte Vanbrabant, Pierre Van Mol, Yannick Van Herck, Nathalie Van Aerde, Greet Hermans, Jan Gunst, Alexandre Borin, Bruna Toledo N Pereira, Arilson Bernardo dosSP Gomes, Stéfanie Primon Muraro, Gabriela Fabiano de Souza, Alessandro S Farias, José Luiz Proenca‐Modena, Marco Aurélio R Vinolo, the CONTAGIOUS Consortium, Pedro Elias Marques, Carine Wouters, Els Wauters, Sofie Struyf, Patrick Matthys, Ghislain Opdenakker, Rafael Elias Marques, Joost Wauters, Mieke Gouwy, and Paul Proost

Subjects
neutrophil, COVID‐19, chemokine, cytokine, protease, emergency myelopoiesis, Immunologic diseases. Allergy, RC581-607
Abstract

Abstract Objectives Emerging evidence of dysregulation of the myeloid cell compartment urges investigations on neutrophil characteristics in coronavirus disease 2019 (COVID‐19). We isolated neutrophils from the blood of COVID‐19 patients receiving general ward care and from patients hospitalised at intensive care units (ICUs) to explore the kinetics of circulating neutrophils and factors important for neutrophil migration and activation. Methods Multicolour flow cytometry was exploited for the analysis of neutrophil differentiation and activation markers. Multiplex and ELISA technologies were used for the quantification of protease, protease inhibitor, chemokine and cytokine concentrations in plasma. Neutrophil polarisation responses were evaluated microscopically. Gelatinolytic and metalloproteinase activity in plasma was determined using a fluorogenic substrate. Co‐culturing healthy donor neutrophils with severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) allowed us to investigate viral replication in neutrophils. Results Upon ICU admission, patients displayed high plasma concentrations of granulocyte–colony‐stimulating factor (G‐CSF) and the chemokine CXCL8, accompanied by emergency myelopoiesis as illustrated by high levels of circulating CD10−, immature neutrophils with reduced CXCR2 and C5aR expression. Neutrophil elastase and non‐metalloproteinase‐derived gelatinolytic activity were increased in plasma from ICU patients. Significantly higher levels of circulating tissue inhibitor of metalloproteinase 1 (TIMP‐1) in patients at ICU admission yielded decreased total MMP proteolytic activity in blood. COVID‐19 neutrophils were hyper‐responsive to CXCL8 and CXCL12 in shape change assays. Finally, SARS‐CoV‐2 failed to replicate inside human neutrophils. Conclusion Our study provides detailed insights into the kinetics of neutrophil phenotype and function in severe COVID‐19 patients, and supports the concept of an increased neutrophil activation state in the circulation.

Published
2021
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37. Beyond-Si materials and devices for more Moore and more than Moore applications.

Author

Nadine Collaert, AliReza Alian, Hiroaki Arimura, Geert Boccardi, Geert Eneman, Jacopo Franco, Tsvetan Ivanov, Dennis Lin, Jérôme Mitard, S. Ramesh, R. Rooyackers, Marc Schaekers, A. Sibaya-Hernandez, S. Sioncke, Quentin Smets, Abhitosh Vais, A. Vandooren, Anabela Veloso, Anne S. Verhulst, Devin Verreck, Niamh Waldron, Amey Walke, Liesbeth Witters, H. Yu, X. Zhou, and Aaron Voon-Yew Thean

Published
2016
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38. In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering

Author

Glorieux, Laura, primary, Vandooren, Laura, additional, Derclaye, Sylvie, additional, Pyr dit Ruys, Sébastien, additional, Oncina-Gil, Paloma, additional, Salowka, Anna, additional, Herinckx, Gaëtan, additional, Aajja, Elias, additional, Lemoine, Pascale, additional, Spourquet, Catherine, additional, Lefort, Hélène, additional, Henriet, Patrick, additional, Tyteca, Donatienne, additional, Spagnoli, Francesca M., additional, Alsteens, David, additional, Vertommen, Didier, additional, and Pierreux, Christophe E., additional

Published
2023
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39. Molybdenum Nitride as a Scalable and Thermally Stable pWFM for CFET

Author

Arimura, H., primary, Brus, S., additional, Franco, J., additional, Oniki, Y., additional, Vandooren, A., additional, Conard, T., additional, Chan, B.-T., additional, Kannan, B., additional, Samiee, M., additional, Li, W., additional, Deminskyi, P., additional, Shero, E., additional, Bakke, J., additional, Jourdan, N., additional, Verni, G. Alessio, additional, Maes, J. W., additional, Givens, M., additional, Ragnarsson, L.-Å., additional, Mitard, J., additional, Litta, E. Dentoni, additional, and Horiguchi, N., additional

Published
2023
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40. MMP-9/Gelatinase B Degrades Immune Complexes in Systemic Lupus Erythematosus

Author

Estefania Ugarte-Berzal, Lise Boon, Erik Martens, Vasily Rybakin, Daniel Blockmans, Jennifer Vandooren, Paul Proost, and Ghislain Opdenakker

Subjects
matrix metalloproteinase-9, immune complexes, immunoglobulins, systemic lupus erythematosus, drug-induced lupus erythematosus, Immunologic diseases. Allergy, RC581-607
Abstract

Systemic Lupus Erythematosus (SLE) is a common and devastating autoimmune disease, characterized by a dysregulated adaptive immune response against intracellular antigens, which involves both autoreactive T and B cells. In SLE, mainly intracellular autoantigens generate autoantibodies and these assemble into immune complexes and activate the classical pathway of the complement system enhancing inflammation. Matrix metalloproteinase-9 (MMP-9) levels have been investigated in the serum of SLE patients and in control subjects. On the basis of specific studies, it has been suggested to treat SLE patients with MMP inhibitors. However, some of these inhibitors induce SLE. Analysis of LPR−/−MMP-9−/− double knockout mice suggested that MMP-9 plays a protective role in autoantigen clearance in SLE, but the effects of MMP-9 on immune complexes remained elusive. Therefore, we studied the role of MMP-9 in the clearance of autoantigens, autoantibodies and immune complexes and demonstrated that the lack of MMP-9 increased the levels of immune complexes in plasma and local complement activation in spleen and kidney in the LPR−/− mouse model of SLE. In addition, we showed that MMP-9 dissolved immune complexes from plasma of lupus-prone LPR−/−/MMP-9−/− mice and from blood samples of SLE patients. Surprisingly, autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, were cleaved by MMP-9. We discovered Apolipoprotein-B 100 as a new substrate of MMP-9 by analyzing the degradation of immune complexes from human plasma samples. These data are relevant to understand lupus immunopathology and side-effects observed with the use of known drugs. Moreover, we caution against the use of MMP inhibitors for the treatment of SLE.

Published
2019
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44. In-Depth Analysis of the Pancreatic Extracellular Matrix during Development for Next-Generation Tissue Engineering

Author

Pierreux, Laura Glorieux, Laura Vandooren, Sylvie Derclaye, Sébastien Pyr dit Ruys, Paloma Oncina-Gil, Anna Salowka, Gaëtan Herinckx, Elias Aajja, Pascale Lemoine, Catherine Spourquet, Hélène Lefort, Patrick Henriet, Donatienne Tyteca, Francesca M. Spagnoli, David Alsteens, Didier Vertommen, and Christophe E.

Subjects
pancreas, extracellular matrix, development, decellularization, proteomics, atomic force microscopy
Abstract

The pancreas is a complex organ consisting of differentiated cells and extracellular matrix (ECM) organized adequately to enable its endocrine and exocrine functions. Although much is known about the intrinsic factors that control pancreas development, very few studies have focused on the microenvironment surrounding pancreatic cells. This environment is composed of various cells and ECM components, which play a critical role in maintaining tissue organization and homeostasis. In this study, we applied mass spectrometry to identify and quantify the ECM composition of the developing pancreas at the embryonic (E) day 14.5 and postnatal (P) day 1 stages. Our proteomic analysis identified 160 ECM proteins that displayed a dynamic expression profile with a shift in collagens and proteoglycans. Furthermore, we used atomic force microscopy to measure the biomechanical properties and found that the pancreatic ECM was soft (≤400 Pa) with no significant change during pancreas maturation. Lastly, we optimized a decellularization protocol for P1 pancreatic tissues, incorporating a preliminary crosslinking step, which effectively preserved the 3D organization of the ECM. The resulting ECM scaffold proved suitable for recellularization studies. Our findings provide insights into the composition and biomechanics of the pancreatic embryonic and perinatal ECM, offering a foundation for future studies investigating the dynamic interactions between the ECM and pancreatic cells.

Published
2023
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46. Oncostatin M-induced astrocytic tissue inhibitor of metalloproteinases-1 drives remyelination

Author

Jennifer Vandooren, Jack van Horssen, Ivo Lambrichts, Melissa Schepers, Chris Van den Haute, Ghislain Opdenakker, Helena Slaets, Wia Baron, Veerle Baekelandt, Niels Hellings, Tim Vanmierlo, Evelien Houben, Doryssa Hermans, Bieke Broux, Kris Janssens, Molecular cell biology and Immunology, Amsterdam Neuroscience - Neuroinfection & -inflammation, Molecular Neuroscience and Ageing Research (MOLAR), Vandooren, Jennifer/0000-0002-7157-3370, Lambrichts, Ivo/0000-0001-7520-0021, Opdenakker, Ghislain/0000-0003-1714-2294, HOUBEN, Evelien, JANSSENS, Kris, HERMANS, Doryssa, Vandooren, Jennifer, Van den Haute, Chris, SCHEPERS, Melissa, VANMIERLO, Tim, LAMBRICHTS, Ivo, VAN HORSSEN, Jack, Baekelandt, Veerle, OPDENAKKER, Ghislain, Baron, Wia, BROUX, Bieke, Slaets, Helena, HELLINGS, Niels, Psychiatrie & Neuropsychologie, and RS: MHeNs - R3 - Neuroscience

Subjects
Central Nervous System, EXPRESSION, Multiple Sclerosis, Central nervous system, oligodendrocyte precursor cells, Matrix metalloproteinase, UP-REGULATION, PROTECTS, Myelin, Mice, Downregulation and upregulation, OLIGODENDROCYTE PROGENITOR CELLS, medicine, Animals, Humans, Remyelination, Demyelinating Disorder, Myelin Sheath, Mice, Knockout, Multidisciplinary, Tissue Inhibitor of Metalloproteinase-1, biology, RECEPTOR, business.industry, Interleukin-6, LIF, Multiple sclerosis, CENTRAL-NERVOUS-SYSTEM, Oncostatin M, astrocytes, MULTIPLE-SCLEROSIS, MEDIATED DEMYELINATION, Biological Sciences, medicine.disease, Axons, Cell biology, medicine.anatomical_structure, remyelination, biology.protein, CNS, business, tissue inhibitor of metalloproteinases-1, Demyelinating Diseases, oncostatin M
Abstract

The brain's endogenous capacity to restore damaged myelin deteriorates during the course of demyelinating disorders. Currently, no treatment options are available to establish remyelination. Chronic demyelination leads to damaged axons and irreversible destruction of the central nervous system (CNS). We identified two promising therapeutic candidates which enhance remyelination: oncostatin M (OSM), a member of the interleukin-6 family, and downstream mediator tissue inhibitor of metalloproteinases-1 (TIMP-1). While remyelination was completely abrogated in OSMR beta knockout (KO) mice, OSM overexpression in the chronically demyelinated CNS established remyelination. Astrocytic TIMP-1 was demonstrated to play a pivotal role in OSM-mediated remyelination. Astrocyte-derived TIMP-1 drove differentiation of oligodendrocyte precursor cells into mature oligodendrocytes in vitro. In vivo, TIMP-1 deficiency completely abolished spontaneous remyelination, phenocopying OSMR beta KO mice. Finally, TIMP-1 was expressed by human astrocytes in demyelinated multiple sclerosis lesions, confirming the human value of our findings. Taken together, OSM and its downstream mediator TIMP-1 have the therapeutic potential to boost remyelination in demyelinating disorders. We thank Dr. Tom Struys, Katrien Wauterickx, and Joke Vanhoof for excellent technical assistance. This work was financially supported by grants from the Research Foundation of Flanders (FWO Vlaanderen, G04441N, G050617N, G0A5716N, and 1106817N), the Interuniversity Attraction Poles (IUAP-P7-39), the Belgian MS-Liga and the Charcot Foundation of Belgium, Methusalem NEURONET, the European FP7 project, HEALTH-F2-2011-278850 (INMiND), and Bijzonder Onderzoeksfonds (BOF)-UHasselt. Hellings, N (reprint author), Hasselt Univ, Biomed Res Inst, Dept Immunol, B-3590 Diepenbeek, Belgium. niels.hellings@uhasselt.be

Published
2020
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47. Combining a Drug and a Nutraceutical: A New Cocrystal of Praziquantel and Curcumin.

Author

Caro Garrido, Camila, Vandooren, Marie, Robeyns, Koen, Debecker, Damien P., Luis, Patricia, and Leyssens, Tom

Subjects
PRAZIQUANTEL, X-ray powder diffraction, CURCUMIN, ETHYL acetate, CRYSTAL lattices, HEAT treatment
Abstract

This study explores the co-crystallization between the drug praziquantel (PZQ) and the nutraceutical curcumin (CU). The investigation revealed two novel solid forms: a cocrystal solvate with ethyl acetate and a non-solvated cocrystal. This novel drug–nutraceutical cocrystal is a praziquantel–curcumin (2:1) cocrystal. The cocrystal solvate has ethyl acetate molecules occupying the voids with minimal interactions within the crystal lattice. The application of heat treatment induces solvent removal and prompts the transition to the non-solvated cocrystal, as highlighted by variable-temperature X-ray powder diffraction (VT-XRPD). Thermal analyses demonstrate the stability of the cocrystal solvate up to approximately 100 °C, beyond which it transforms into the non-solvated phase, which eventually melts at 130 °C. [ABSTRACT FROM AUTHOR]

Published
2024
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48. Co-creating Artificial Intelligence: Designing and Enhancing Democratic AI Solutions Through Citizen Science.

Author

Duerinckx, Annelies, Veeckman, Carina, Verstraelen, Karen, Singh, Neena, Van Laer, Jef, Vaes, Michiel, Vandooren, Charlotte, and Duysburgh, Pieter

Subjects
ARTIFICIAL intelligence, CONSCIOUSNESS raising, POLITICAL participation, RESEARCH & development projects, OLDER people
Abstract

Although artificial intelligence (AI) is omnipresent in our everyday lives, the level of awareness and knowledge among the general population remains mixed. The lack of understanding is particularly prevalent among older adults, and people with a low education and income. To bridge this knowledge gap and to empower individuals to become informed AI users, further outreach and awareness raising is necessary. This article presents a case study in Flanders (Belgium), called the amai! program (Flemish slang for "oh my!"). The program invites participants to voice their ideas or societal problems they wish to solve through AI and to be involved in the development of citizen-driven research projects. Using a citizen science (CS) approach, ideas are collected through a centralized platform and eventually realized through an open project call with partners from industry, civil society, and research institutions. As a result, 988 ideas have been submitted through the program's platform and 14 are being realized in the domains of mobility, climate, health, and work. Here, we outline a phase-based approach for setting up citizen-driven research projects, as well as lessons learned on how to sensitize and activate citizens. Guidelines are also provided on how to involve participants to become aware and learn about science and technology, especially those with no prior knowledge or interest. Overall, this case study demonstrates how AI innovation and governance can be democratized through citizen participation and can build capacities in a fun and accessible way. [ABSTRACT FROM AUTHOR]

Published
2024
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49. Cost analysis of device options and scaling boosters below the A14 technology node

Author

Mirabelli, Gioele, primary, Vandooren, Anne, additional, Roda Neve, Cesar, additional, Gonzalez, Victor Vega, additional, Mertens, Hans, additional, Farokhnejad, Anita, additional, Schuddinck, Pieter, additional, Murdoch, Gayle, additional, Salahuddin, Shairfe Muhammad, additional, Zografos, Odysseas, additional, Ragnarsson, Lars, additional, Weckx, Pieter, additional, Tokei, Zsolt, additional, Hellings, Geert, additional, and Ryckaert, Julien, additional

Published
2023
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50. Detection of bonding voids for 3D integration

Author

Chen, Cong, primary, Van Den Heuvel, Dieter, additional, Beggiato, Matteo, additional, Tunca Altintas, Bensu, additional, Moussa, Alain, additional, Vandooren, Anne, additional, Baudemprez, Bart, additional, Schöbitz, Michael, additional, Khaldi, Wassim, additional, Bogdanowicz, Janusz, additional, Beral, Christophe, additional, and Charley, Anne-Laure, additional

Published
2023
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