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2. Understanding the Dosage-Dependent Role of Dicer1 in Thyroid Tumorigenesis.

Author

Rojo-Pardillo, María, Godefroid, Ludivine, Dom, Geneviève, Lefort, Anne, Libert, Frederick, Robaye, Bernard, and Maenhaut, Carine

Subjects
PATIENT experience, CELL motility, THYROID cancer, CELL cycle, PAPILLARY carcinoma
Abstract

Tumors originating from thyroid follicular cells are the most common endocrine tumors, with rising incidence. Despite a generally good prognosis, up to 20% of patients experience recurrence and persistence, highlighting the need to identify the underlying molecular mechanisms. Dicer1 has been found to be altered in papillary thyroid cancer (PTC). Studies suggest that Dicer1 functions as a haploinsufficient tumor suppressor gene: partial loss promotes tumorigenesis, while complete loss prevents it. To investigate the effects of partial or total Dicer1 loss in PTC in vitro, we generated stable Dicer1 (+/−) cell lines from TPC1 using CRISPR-Cas9, though no Dicer1 (−/−) lines could be produced. Therefore, siRNA against Dicer1 was transfected into Dicer1 (+/−) cell lines to further decrease its expression. Transcriptomic analysis revealed changes in proliferation and cell locomotion. BrdU staining indicated a slow-down of the cell cycle, with fewer cells in S phase and more in G0-G1-phase. Additionally, transwell assays showed decreased invasion and migration after Dicer1 knockdown by siRNA. Moreover, Dicer1 overexpression led to decreased proliferation, invasion, and increased apoptosis. Our findings deepen the understanding of Dicer1's role in thyroid cancer, demonstrating that both complete elimination and overexpression of Dicer1 inhibit thyroid oncogenesis, highlighting Dicer1 as a promising target for novel therapeutic strategies. [ABSTRACT FROM AUTHOR]

Published
2024
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3. Identification of cellular factors as novel epigenetic regulators of the Human Immunodeficiency Virus Type 1 (HIV-1) transcription

Author

Van Lint, Carine, Vanhamme, Luc, Marini, Anna Maria, Bellefroid, Eric, Robaye, Bernard, Renard, Patricia, Rohr, Olivier, Santangelo, Marion, Van Lint, Carine, Vanhamme, Luc, Marini, Anna Maria, Bellefroid, Eric, Robaye, Bernard, Renard, Patricia, Rohr, Olivier, and Santangelo, Marion

Abstract

Infection by the Human Immunodeficiency Virus type 1 (HIV-1) remains a major global public health issue. Despite effective antiretroviral therapy, HIV-1 persistence occurs in cellular reservoirs, necessitating continuous drug intake leading HIV-1 infection into a chronic disease. Therefore, an HIV cure requires either eliminating these viral reservoirs or achieving an deep blockade of HIV-1 transcription in the absence of treatment. Deciphering the underlying molecular mechanisms that drive HIV-1 into latency is critical for targeted HIV cure efforts.This Ph.D. thesis aims to enhance the knowledge on the molecular mechanisms of HIV-1 latency, specifically at epigenetic level. First, this work contributes to the discovery of a novel epigenetic actor of HIV-1 latency, known as UHRF1, in both infected T-lymphoid and myeloid cells. UHRF1 acts as a HIV-1 transcriptional repressor by modulating both DNA and histone methylation. In addition to DNA methylation, many evidence have highlighted DNA hydroxymethylation as a new epigenetic mark involved in cellular transcriptional regulation. This Ph.D. thesis demonstrated the presence of DNA hydroxymethylation along both the latent and the reactivated HIV-1 provirus. Finally, this work led to the discovery of another novel epigenetic actor of HIV-1 latency, known as KLF16. This cellular transcription factor regulates HIV-1 transcription by modulating both histone acetylation and methylation in both the infected T-lymphocytic cell line and the infected monocytic cell line. Altogether, our findings expand our understanding of the molecular mechanisms involved in HIV-1 transcriptional latency, specifically at epigenetic level. Moreover, the identification of novel HIV-1 regulators have unveiled new drug targets that could be critical in HIV-1 cure efforts., Doctorat en Sciences, info:eu-repo/semantics/nonPublished

Published
2024

4. Investigation du rôle fonctionnel des miR-204-3p et miR-204-5p dans la progression tumorale des cancers thyroïdiens papillaires

Author

Maenhaut, Carine, Dewachter, Laurence, Robaye, Bernard, Chamekh, Mostafa, Van Keymeulen, Alexandra, Burniat, Agnès, Journe, Fabrice, Dupuy, Corinne, Van Branteghem, Cindy, Maenhaut, Carine, Dewachter, Laurence, Robaye, Bernard, Chamekh, Mostafa, Van Keymeulen, Alexandra, Burniat, Agnès, Journe, Fabrice, Dupuy, Corinne, and Van Branteghem, Cindy

Abstract

Au cours de cette étude, le rôle des miR-204-5p et miR-204-3p dans la tumorigenèse thyroïdienne, en particulier dans les carcinomes papillaires de la thyroïde (PTC), a été exploré. Bien que les PTC soient généralement associés à un pronostic favorable, certains évoluent vers des formes plus agressives. La transformation maligne de la thyroïde en PTC, induite par des mutations oncogéniques dans la voie des MAPK, s'accompagne de changements significatifs dans l'expression des miARNs parmi lesquels les miR-204-5p et miR-204-3p ont été précédemment identifiés dans les PTC comme étant sous régulés et associés à l’agressivité. Afin d’évaluer leur rôle précis dans la progression tumorale des PTC, trois lignées thyroïdiennes humaines, qui ont perdu l’expression de ces deux miARNs, ont été transfectées de manière transitoire à l’aide d’un mimique spécifique du miR-204-5p et du miR-204-3p et des tests fonctionnels de migration/d’invasion, de prolifération, de croissance et d’apoptose ont été réalisés 72h après transfection. La caractérisation fonctionnelle de ces deux miARNs a révélé que ceux-ci agissaient en tant que suppresseur de tumeurs en inhibant l'invasion cellulaire. De nouvelles cibles du miR-204-5p ont alors pu être identifiées dont HMGA2, SNAI2, SOX4, TGFBR2, MMP14, ADAMTS9, et sont toutes étroitement associées à la transition épithélio-mésenchymateuse (TEM). La caractérisation approfondie de la fonction de ce miARN a révélé que celui-ci pourrait être inversement corrélé à l’agressivité tumorale en contrôlant le processus de différenciation cellulaire. Nous avons montré que l’inhibition de l’invasion et le maintien de la différenciation cellulaire par le miR-204-5p impliquait la liaison directe et la répression de HMGA2, régulé par la voie des MAPK. Nos résultats ont également mis en évidence que des modifications épigénétiques, en particulier la méthylation de l'ADN, étaient responsables de la sous expression du miR-204-5p dans les PTC. Ensuite, la pertinence clin, During this study, the role of miR-204-5p and miR-204-3p in thyroid tumorigenesis, particularly in papillary thyroid carcinomas (PTC), was investigated. While PTCs are generally associated with a favorable prognosis, some progress to more aggressive forms. The malignant transformation of the thyroid into PTC, induced by oncogenic mutations in the MAPK pathway, is accompanied by significant changes in the expression of miRNAs, among which miR-204-5p and miR-204-3p have been previously identified in PTCs as downregulated and associated with aggressiveness. To assess their precise role in the tumor progression of PTCs, three human thyroid cell lines, which had lost the expression of these two miRNAs, were transiently transfected with specific mimics of miR-204-5p and miR-204-3p. Functional tests for migration/invasion, proliferation, growth, and apoptosis were performed 72 hours after transfection. The functional characterization of these two miRNAs revealed that they acted as tumor suppressors by inhibiting cell invasion.Novel targets of miR-204-5p were identified, including HMGA2, SNAI2, SOX4, TGFBR2, MMP14, ADAMTS9, all closely associated with the epithelial-mesenchymal transition (EMT). In-depth characterization of miR-204-5p's function revealed its potential inverse correlation with tumor aggressiveness by controlling the process of cellular differentiation. We demonstrated that the inhibition of invasion and maintenance of cellular differentiation by miR-204-5p involved direct binding and repression of HMGA2, regulated by the MAPK pathway.Our results also highlighted that epigenetic modifications, particularly DNA methylation, were responsible for the underexpression of miR-204-5p in PTCs. Subsequently, the clinical relevance of our findings was evaluated in vivo. Correlation analyses in a murine PTC model and in human PTCs revealed a negative correlation between the expression of miR-204-5p and HMGA2, as well as between the expression of HMGA2 and various genes, Doctorat en Sciences biomédicales et pharmaceutiques (Médecine), info:eu-repo/semantics/nonPublished

Published
2024

5. Deciphering Prdm12 role from nociceptor development to pain perception

Author

Bellefroid, Eric, Vanhamme, Luc, Vanhollebeke, Benoît, Robaye, Bernard, Clotman, Frederic, Nady, Natalie, Dannawi, Maya, Bellefroid, Eric, Vanhamme, Luc, Vanhollebeke, Benoît, Robaye, Bernard, Clotman, Frederic, Nady, Natalie, and Dannawi, Maya

Abstract

The Prdm12 gene encodes the first transcriptional regulator that, once mutated, causes congenital insensitivity to pain (CIP) in humans. In recent years, epigenetic mechanisms have opened an avenue for the development of novel kind of analgesics. Work of our laboratory has shown that in mice, during development, Prdm12 is strongly expressed in somato-sensory ganglia where it is selectively transcribed in neurons from the nociceptive lineage, and that it remains expressed in mature neurons where it controls nociception. However, its mechanisms of action remain largely unknown. In my work, we have investigated the mechanisms behind Prdm12’s role in the specification of the nociceptive lineage in nervous system development. Results obtained have confirmed that Prdm12 is required for progenitor survival. They also revealed that it is required in developing somato-sensory neuron to repress an alternate viscero-sensory fate. Using a transgenic mouse line of Prdm12 overexpression in an inducible conditional manner, we showed that Prdm12 does not block Phox2b expression when ectopically expressed in visceral ganglia, revealing a context dependent repressive function. Previous work from the lab showed that the loss of Prdm12 in mature nociceptors of adult mice deregulates the expression of many nociceptive genes, and reduces their response to capsaicin. A hypersensitivity to formalin was also observed. To further approach the role of Prdm12 in nociception, we performed complementary Prdm12 gain of function experiments using AAV. The preliminary results obtained further suggest a role for Prdm12 in nociception., Doctorat en Sciences, info:eu-repo/semantics/nonPublished

Published
2024

11. Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: A potential carbamylation route involved in the formation of atherosclerotic plaques?

Author

Delporte, Cédric, Zouaoui Boudjeltia, Karim, Furtmüller, Paul G., Maki, Richard A., Dieu, Marc, Noyon, Caroline, Soudi, Monika, Dufour, Damien, Coremans, Catherine, Nuyens, Vincent, Reye, Florence, Rousseau, Alexandre, Raes, Martine, Moguilevsky, Nicole, Vanhaeverbeek, Michel, Ducobu, Jean, Nève, Jean, Robaye, Bernard, Vanhamme, Luc, Reynolds, Wanda F., Obinger, Christian, and Van Antwerpen, Pierre

Published
2018
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12. Thyroid-specific inactivation of KIF3A alters the TSH signaling pathway and leads to hypothyroidism

Author

D'Amico, Eva, Gayral, Stéphanie, Massart, Claude, Van Sande, Jacqueline, Reiter, Jeremy F, Dumont, Jacques E, Robaye, Bernard, and Schurmans, Stéphane

Subjects
Biomedical and Clinical Sciences, Clinical Sciences, Underpinning research, Aetiology, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Metabolic and endocrine, Animals, Hypothyroidism, Kinesins, Mice, Mice, Mutant Strains, PAX8 Transcription Factor, Paired Box Transcription Factors, Signal Transduction, Thyroid Gland, Thyrotropin, thyroid, hypothyroidism, genetically-modified mouse, Kif3a, molecular motor, kinesin 2, Kinesin, Veterinary Sciences, Paediatrics and Reproductive Medicine, Endocrinology & Metabolism, Clinical sciences
Abstract

Kinesins, including the kinesin 2/KIF3 molecular motor, play an important role in intracellular traffic and can deliver vesicles to distal axon terminals, to cilia, to nonpolarized cell surfaces or to epithelial cell basolateral membranes, thus taking part in the establishment of cellular polarity. We report here the consequences of kinesin 2 motor inactivation in the thyroid of 3-week-old Kif3a(Δ)(/flox) Pax8(Cre/)(+) mutant mice. Our results indicate first that 3-week-old Pax8(Cre/)(+) mice used in these experiments present minor thyroid functional defects resulting in a slight increase in circulating bioactive TSH and intracellular cAMP levels, sufficient to maintain blood thyroxine levels in the normal range. Second, Kif3a inactivation in thyrocytes markedly amplified the phenotype observed in Pax8(Cre/)(+) mice, resulting in altered TSH signaling upstream of the second messenger cAMP and mild hypothyroidism. Finally, our results in mouse embryonic fibroblasts indicate that Kif3a inactivation in the absence of any Pax8 gene alteration leads to altered G protein-coupled receptor plasma membrane expression, as shown for the β2 adrenergic receptor, and we suggest that a similar mechanism may explain the altered TSH signaling and mild hypothyroidism detected in Kif3a(Δ)(/flox) Pax8(Cre/)(+) mutant mice.

Published
2013

14. L'inhibition de Yes-associated protein et l'induction de la ferroptose, deux nouvelles pistes pour le traitement des tumeurs stromales gastro-intestinales

Author

Vanderwinden, Jean-Marie, Erneux, Christophe, Maenhaut, Carine, Robaye, Bernard, Van Laethem, Jean-Luc, Verset, Laurine, Emile, Jean-François, Feron, Olivier, Delvaux, Marine, Vanderwinden, Jean-Marie, Erneux, Christophe, Maenhaut, Carine, Robaye, Bernard, Van Laethem, Jean-Luc, Verset, Laurine, Emile, Jean-François, Feron, Olivier, and Delvaux, Marine

Abstract

Les tumeurs stromales gastro-intestinales (GIST) sont les sarcomes les plus fréquents du tube digestif et sont généralement associées à des mutations gain de fonction des gènes codant pour le récepteur tyrosine kinase (RTK) KIT ou PDGFRA. Le traitement des GIST localisés est la résection chirurgicale alors qu’en cas de GIST non résécables ou métastatiques, le traitement de première ligne est l’imatinib, un inhibiteur de tyrosine kinase (TKI). Malgré une bonne réponse initiale aux TKI, la plupart des GIST développent des résistances secondaires et continuent de progresser. Malheureusement, les autres TKI développés par la suite n’ont que des effets cliniques assez limités. La recherche de nouvelles cibles thérapeutiques est donc essentielle pour le traitement des GIST résistants dans l’optique de développer des multithérapies. Notre travail de thèse s’appuie sur une publication de notre laboratoire dans laquelle la protéine « Yes-associated protein » (YAP) était identifiée comme un acteur important pour la survie des cellules sensibles (GIST882) et résistantes (GIST48) à l’imatinib. En effet, l’inhibition pharmacologique de la protéine YAP par la verteporfin (VP) entrainait une forte diminution de la viabilité des cellules GIST882 et GIST48. Le laboratoire avait aussi montré une localisation nucléaire de la protéine YAP dans 71% des arrays de tissus humains de GIST, reflétant l’activité transcriptionnelle de YAP dans ces tissus. Cependant, le type de mort cellulaire induite par la verteporfin dans les cellules GIST restait inconnu. De récentes publications ont identifié des liens entre YAP et la ferroptose. La ferroptose est une nouvelle forme de mort cellulaire non apoptotique, résultant d’un déséquilibre entre les dommages oxydatifs, liés au fer et aux radicaux libres oxygénés (ROS, « reactive oxygen species »), et les défenses antioxydantes principalement assurées par l’axe glutathion (GSH) / glutathion peroxydase 4 (GPX4). L’induction de la ferroptose a émergé co, Doctorat en Sciences biomédicales et pharmaceutiques (Médecine), info:eu-repo/semantics/nonPublished

Published
2023

15. Étude du rôle de Prdm12 dans la nociception chez la souris adulte

Author

Bellefroid, Eric, Ris, Laurence, Vanhamme, Luc, Vanhollebeke, Benoît, Robaye, Bernard, Tafforeau, Lionel, Leroy, Baptiste, Moqrich, Aziz, Latragna, Aurore, Bellefroid, Eric, Ris, Laurence, Vanhamme, Luc, Vanhollebeke, Benoît, Robaye, Bernard, Tafforeau, Lionel, Leroy, Baptiste, Moqrich, Aziz, and Latragna, Aurore

Abstract

La douleur est un problème de santé publique majeur puisqu'elle touche 20 % de la population mondiale. Les traitements actuels procurent souvent un soulagement limité et sont associés à des effets secondaires. Il y a donc un besoin urgent de meilleurs traitements contre la douleur. La douleur résulte de l'activation d'un sous-ensemble de neurones somatosensoriels appelés nocicepteurs qui sont spécialisés pour détecter les stimuli potentiellement douloureux. Prdm12 est un régulateur épigénétique sélectivement exprimé dans les nocicepteurs dans le système nerveux en développement dont la mutation provoque une insensibilité congénitale à la douleur, une maladie génétique rare caractérisée par l'incapacité à ressentir la douleur. Au cours des années précédentes, notre laboratoire a montré que Prdm12 est nécessaire durant la neurogenèse sensorielle pour la génération du lignage nociceptif. L’expression de Prdm12 est maintenue dans les nocicepteurs matures suggérant un rôle fonctionnel potentiel chez l'adulte. Nos résultats ont montré que la perte de Prdm12 dans les nocicepteurs matures provoquait une dérégulation des gènes codant pour des récepteurs et des canaux ioniques impliqués dans la nociception, modifie l'excitabilité neuronale ainsi que les réponses comportementales à la formaline et à la capsaïcine. En conclusion, nos données ont montré que Prdm12 exerce également une influence sur le bon fonctionnement des nocicepteurs chez la souris adulte.Pain is a major health burden as it affects 20% of the worldwide population. Current therapies often provide limited relief and are associated with side effects. There is thus an urgent need for better analgesics. Pain results from the activation of a subset of somatosensory neurons called nociceptors that are specialized to detect potentially painful stimuli. Prdm12 is an epigenetic regulator selectively expressed in nociceptors in the developing peripheral nervous system whose mutation causes congenital insensitivity to pa, Doctorat en Sciences, info:eu-repo/semantics/nonPublished

Published
2023

18. Etude du rôle des macrophages dans les différenciations physiologiques et pathologiques des cellules souches mésenchymateuses en ostéoblastes

Author

Robaye, Bernard, Vanhamme, Luc, Oldenhove, Guillaume, Vanhollebeke, Benoît, Marini, Anna Maria, Jacquel, Arnaud, Veriter, Sophie V. S., Bonesso, Billy, Robaye, Bernard, Vanhamme, Luc, Oldenhove, Guillaume, Vanhollebeke, Benoît, Marini, Anna Maria, Jacquel, Arnaud, Veriter, Sophie V. S., and Bonesso, Billy

Abstract

In vivo, dans les conditions physiologiques, la capacité de minéralisation est exclusivement portée par les ostéoblastes et les ondotoblastes. La grande majorité des cellules composant un vertébré ne peut induire la formation de cristaux d’hydroxyapatite. Toutefois, certaines cellules non osseuses comme les cellules stromales mésenchymateuses (MSCs) et les cellules musculaires lisses vasculaires (VSMCs) ont la capacité d’adopter un phénotype ostéoblastogénique dans certains contextes pathologiques et font exception à cette règle. Le processus de minéralisation résulte d’une balance entre des facteurs pro et anti-ostéoblastogéniques. Il existe donc des mécanismes permettant de réguler négativement l’ostéoblastogenèse/la minéralisation dans les tissus « mous ». Ce projet de thèse est porté sur la compréhension de ces mécanismes et plus particulièrement sur le rôle des macrophages dans cette régulation. En effet, il a été précédemment démontré au niveau de la moelle osseuse qu’une population de macrophages, appelés OsteoMacs, facilite la différenciation des cellules stromales mésenchymateuses médulaires. De façon étonnante, au laboratoire, des résultats préliminaires nous ont menés à penser que les macrophages non médullaires participeraient à la régulation négative de la différenciation ostéoblastogénique des MSCs issues d’autres tissus représentés ici par les MSCs du tissu adipeux (ATMSCs) et les VSMCs.La première partie de ce travail de recherche a consisté en la caractérisation de l’effet inhibiteur des macrophages sur la différenciation ostéoblastogénique des ATMSCs et des VSMCs, ainsi qu’à l’identification des mécanismes moléculaires gouvernant cet effet inhibiteur des macrophages. Les résultats obtenus suggèrent que les macrophages exercent cet effet sur la différenciation de façon tardive. En effet, les macrophages produisent du TGFß stocké dans le milieu extracellulaire sous forme latente. Dans les étapes tardives de la différenciation ostéoblastogénique, les, Doctorat en Sciences, info:eu-repo/semantics/nonPublished

Published
2022

19. Molecular dissection of brain endothelial barrier function: a cross-species transcriptomic guided approach

Author

Vanhollebeke, Benoît, Robaye, Bernard, Bellefroid, Eric, Freitas Vale Germano, Raoul, Vanhollebeke, Benoît, Robaye, Bernard, Bellefroid, Eric, and Freitas Vale Germano, Raoul

Abstract

Molecular dissection of brain endothelial barrier function: a cross-species transcriptomic-guided approachThe vertebrate brain endothelium ensures central nervous system homeostasis and neuroprotection, by tight control of molecular and cellular transit across the blood-brain-barrier (BBB). However, knowledge on the molecular control of BBB function during development and maintenance remains fragmentary. Identification of novel players in BBB formation relies on transcriptomic analysis, but this approach proved to be limited for the effective selection of genes and pathways to functionally investigate. To meaningfully prioritize candidate regulatory genes, a cross-species comparative transcriptomic analysis was implemented of larval zebrafish with analogous mouse datasets, and human brain endothelial gene expression datasets, allowing the identification of a shared evolutionary conserved genetic blueprint of BBB enriched genes. Novel genetic tools were developed to streamline in vivo investigation of the functional impact of selected genes on BBB integrity. This work uncovered the conserved genetics of the vertebrate BBB, and opens avenues for functional BBB investigation., Dissection moléculaire de la fonction de la barrière endothéliale cérébrale :une approche inter-espèces guidée par la transcriptomiqueL'endothélium du cerveau des vertébrés assure l'homéostasie et la neuroprotection du système nerveux central, en contrôlant le transit des molécules et des cellules à travers la barrière hémato-encéphalique (BHE). Cependant, les connaissances sur le contrôle moléculaire de la fonction de la BHE au cours du développement et chez l’adulte, restent fragmentaires. L'identification de nouveaux acteurs dans la formation de la BHE repose sur l'analyse transcriptomique, mais cette approche s'est révélée limitée pour la sélection efficace des gènes et des voies pour l'investigation fonctionnelle. Afin de prioriser les gènes candidats, une analyse comparative du transcriptome de larves de poisson zèbre, des données analogues de la souris, et l'expression génique de l'endothélium du cerveau humain, a été mise en œuvre, permettant l'identification des gènes et de voies de signalisation enrichis au niveau de la BHE à travers l’évolution. Des nouveaux outils génétiques ont été développés pour permettre l'étude in vivo de l'impact fonctionnel des gènes sélectionnés sur l'intégrité de la BHE. Ces travaux ont dévoilé la génétique conservée de la BHE des vertébrés, et ouvrent des voies pour l'étude fonctionnelle de la BHE., Doctorat en Sciences, info:eu-repo/semantics/nonPublished

Published
2022

23. Targeting the P2Y13 Receptor Suppresses IL-33 and HMGB1 Release and Ameliorates Experimental Asthma

Author

Werder, Rhiannon B., primary, Ullah, Md Ashik, additional, Rahman, Muhammed Mahfuzur, additional, Simpson, Jennifer, additional, Lynch, Jason P., additional, Collinson, Natasha, additional, Rittchen, Sonja, additional, Rashid, Ridwan B., additional, Sikder, Md Al Amin, additional, Handoko, Herlina Y., additional, Curren, Bodie F., additional, Sebina, Ismail, additional, Hartel, Gunter, additional, Bissell, Alec, additional, Ngo, Sylvia, additional, Yarlagadda, Tejasri, additional, Hasnain, Sumaira Z., additional, Lu, Wenying, additional, Sohal, Sukhwinder S., additional, Martin, Megan, additional, Bowler, Simon, additional, Burr, Lucy D., additional, Martinez, Laurent O., additional, Robaye, Bernard, additional, Spann, Kirsten, additional, Ferreira, Manuel A. R., additional, and Phipps, Simon, additional

Published
2022
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28. Etude des propriétés d’échafaudage de la phosphoinositide 5-phosphatase SHIP2 et leur impact dans les remaniements membranaires

Author

Pirson, Isabelle, Erneux, Christophe, Langer, Ingrid, Delporte, Christine, Igoillo Esteve, Mariana, Robaye, Bernard, Bertrand, Luc, Rider, Mark H., Antoine, Mathieu, Pirson, Isabelle, Erneux, Christophe, Langer, Ingrid, Delporte, Christine, Igoillo Esteve, Mariana, Robaye, Bernard, Bertrand, Luc, Rider, Mark H., and Antoine, Mathieu

Abstract

La phosphoinositide phosphatase SHIP2 est une protéine capable de moduler le PI(3,4,5)P3, le PI(4,5)P2 et le PI(3,4)P2 qui sont des phosphoinositides importants lors des remaniements membranaires de la cellule. La régulation de la composition en phosphoinositides des membranes permettant l’assemblage de complexes protéiques est primordiale pour la génération de protrusions essentielles pour la migration et l’invasion cellulaire. D’autre part, SHIP2 possède des propriétés d’échafaudage permettant sa participation à plusieurs complexes multi-protéiques et à son ancrage à des localisations subcellulaires spécifiques. Plusieurs études ont montré que SHIP2 pouvait jouer un rôle dans le développement de certains cancers dont le cancer du sein. Au cours de ce travail, nous avons mis en évidence deux nouveaux partenaires de SHIP2 :IRSp53 et CIN85. Ces deux protéines participent respectivement à la formation d’invadopode et à l’endocytose. IRSp53 et CIN85 lient la même région C-terminale riche en prolines (PRR-II) de SHIP2, mais toutefois pas par les mêmes séquences. Cette région contient plusieurs motifs consensus permettant l’interaction de SHIP2 avec plusieurs autres partenaires connus comme l’intersectine, une protéine impliquée dans l’endocytose et Mena, un partenaire commun de SHIP2 et d’IRSp53 impliqué dans l’invasion cellulaire. Nous avons également montré que la mutation de la F1053 située dans la PRR-II de SHIP2 est, essentielle pour la liaison à l’intersectine, impliquée dans la stabilité de la liaison avec Mena et IRSp53 mais pas impliquée dans la liaison de CIN85. De plus, nous montrons qu’à la différence d’IRSp53 qui n’en possède qu’un, CIN85 possède trois domaines SH3 mais ne doit lier que deux motifs dans la PRR-II de SHIP2 afin d’assurer sa complète interaction.Dans les cellules dérivées du cancer du sein MDA-MB-231, nous avons montré que Mena n’est pas nécessaire pour l’interaction entre SHIP2 et IRSp53. Cependant, nous avons observé que l’absence de Mena d, Doctorat en Sciences biomédicales et pharmaceutiques (Médecine), info:eu-repo/semantics/nonPublished

Published
2021

29. Etude des rôles des récepteurs P2Y2 et P2Y6 dans la différenciation adipogénique et ostéoblastogénique des cellules stromales mésenchymateuses multipotentes dérivées du tissu adipeux inguinal murin

Author

Robaye, Bernard, Droogmans, Louis, Marini, Anna Maria, Vanhamme, Luc, Oldenhove, Guillaume, Kauffenstein, Gilles, Noël, Danièle DN, Kostov, Laura, Robaye, Bernard, Droogmans, Louis, Marini, Anna Maria, Vanhamme, Luc, Oldenhove, Guillaume, Kauffenstein, Gilles, Noël, Danièle DN, and Kostov, Laura

Abstract

Toutes les cellules de l’organisme relarguent de façon constitutive des nucléotides dans l’espace extracellulaire. Ces nucléotides extracellulaires agissent comme des molécules de signalisation, entre autres, via les récepteurs P2Y (P2YRs) qui sont des récepteurs couplés aux protéines G (GPCRs). Les P2YRs sont exprimés, pour la majorité, de façon ubiquitaire dans l’organisme. L’analyse phénotypique des lignées de souris knockout pour les P2YRs (P2YR-/-) a permis de confirmer l’importance de cette voie de communication dans différents processus physio/pathologiques. Au sein de notre laboratoire, grâce à l’utilisation de souris P2YR-/-, nous étudions depuis quelques années le rôle de ces récepteurs dans la biologie des cellules stromales mésenchymateuses multipotentes (MSCs). Ces cellules se caractérisent par une faible immunogénicité et surtout par la propriété de multipotence, i.e. capacité de se différencier en plusieurs types cellulaires (adipocytes, chondroblastes, ostéoblastes). Cette dernière propriété suscite l’intérêt de la médecine régénérative qui vise à exploiter la multipotence de ces cellules en thérapie cellulaire. Toutefois, leur utilisation à des fins thérapeutiques est encore limitée, notamment parce que les mécanismes régulateurs de ces processus de différenciation sont encore mal compris. Il est donc fondamental de continuer à étudier les voies de signalisation régulant les processus de différenciation de ces cellules pour leurs applications cliniques.Dans ce travail de recherche, nous avons investigué l’implication de la signalisation dépendant des P2YR dans le modèle expérimental des MSCs dérivées du tissu adipeux sous-cutané inguinal (ATMSCs) murin. D’abord, nous avons montré que parmi les 7 sous-types connus de récepteur P2Ys, les ATMSCs expriment le P2Y2R (récepteur à l’ATP et l’UTP) et le P2Y6R (récepteur à l’UDP) et que ces récepteurs sont fonctionnels. Par une approche combinant l’analyse quantitative de leur expression, l’effet de leur act, Doctorat en Sciences, info:eu-repo/semantics/nonPublished

Published
2021

30. Ntpdase1 modulates smooth muscle contraction in mice bladder by regulating nucleotide receptor activation distinctly in male and female

Author

Babou Kammoe, Romuald Brice, Kauffenstein, Gilles, Pelletier, Julien, Robaye, Bernard, Sévigny, Jean, Babou Kammoe, Romuald Brice, Kauffenstein, Gilles, Pelletier, Julien, Robaye, Bernard, and Sévigny, Jean

Abstract

Nucleotides released by smooth muscle cells (SMCs) and by innervating nerve terminals activate specific P2 receptors and modulate bladder contraction. We hypothesized that cell surface enzymes regulate SMC contraction in mice bladder by controlling the concentration of nucleotides. We showed by immunohistochemistry, enzymatic histochemistry, and biochemical activities that nucleoside triphosphate diphosphohydrolase-1 (NTPDase1) and ecto-5′-nucleotidase were the major ectonucleotidases expressed by SMCs in the bladder. RT-qPCR revealed that, among the nucleotide receptors, there was higher expression of P2X1, P2Y1, and P2Y6 receptors. Ex vivo, nucleotides induced a more potent contraction of bladder strips isolated from NTPDase1 deficient (Entpd1−/−) mice compared to wild type controls. The strongest responses were obtained with uridine 5′-triphosphate (UTP) and uridine 5′-diphosphate (UDP), suggesting the involvement of P2Y6 receptors, which was confirmed with P2ry6−/− bladder strips. Interestingly, this response was reduced in female bladders. Our results also suggest the participation of P2X1, P2Y2 and/or P2Y4, and P2Y12 in these contractions. A reduced response to the thromboxane analogue U46619 was also observed in wild type, Entpd1−/−, and P2ry6−/− female bladders showing another difference due to sex. In summary, NTPDase1 modulates the activation of nucleotide receptors in mouse bladder SMCs, and contractions induced by P2Y6 receptor activation were weaker in female bladders., SCOPUS: ar.j, info:eu-repo/semantics/published

Published
2021

31. NcoA-1

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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32. Nek5

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

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2012
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33. Nucleotide Receptor P2x

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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34. Neural Wiskott–Aldrich Syndrome Protein

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

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2012
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35. NCoA-2

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

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2012
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36. Nuclear Factor-Kappa-B

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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37. NR3C4 (Nuclear Receptor Subfamily 3, Group C, Member 4)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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38. N-Myristoyltransferase

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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39. NF-E2-Related Factor 2

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

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2012
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40. Nuclear Factor of Kappa Light Polypeptide Gene Enhancer in B-Cells Inhibitor, Zeta

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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41. NF-Kappa-B Inhibitor Zeta

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

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2012
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42. Nuclear Receptor Subfamily 1, Group I, Member 1 (NR1I1)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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43. NFAT1 (Nuclear Factor of Activated T-Cells 1, NFATp, NFAT Preexisting, NFATc2, NFAT Cytosolic 2)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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44. nrip1 (Nuclear Receptor-Interacting Protein 1)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

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2012
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45. Nucleotide Receptors

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

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2012
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46. NINAC (p174, p132)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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47. Net1 (Neuroepithelial Cell Transforming Gene 1 Protein)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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48. Nucleoside Triphosphate Diphosphohydrolase

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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49. NFAT2 (Nuclear Factor of Activated T-Cells 2, NFATc, NFAT Cytosolic, NFATc1, NFAT Cytosolic 1)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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50. NFAT3 (Nuclear Factor of Activated T-Cells 3, NFATc4, NFAT Cytosolic 4)

Author

Horstkorte, Rüdiger, primary, Büttner, Bettina, additional, Bork, Kaya, additional, Sahota, Navdeep, additional, Sabir, Sarah, additional, O’Regan, Laura, additional, Blot, Joelle, additional, Zalli, Detina, additional, Baxter, Joanne, additional, Barone, Giancarlo, additional, Fry, Andrew, additional, Frost, Jeffrey A., additional, Mizuno, Tooru, additional, Valdor, Rut, additional, Abe, Brian T., additional, Macian, Fernando, additional, Sanchez-Niño, Maria D., additional, Sanz, Ana B., additional, Izquierdo, Maria C., additional, Poveda, Jonay, additional, Ortiz, Alberto, additional, Yoo, Byong Kwon, additional, Yun, C. Chris, additional, Xu, Bin, additional, Gewe, Mesfin, additional, Finton, Kathryn, additional, Strong, Roland K., additional, McCarthy, Michael T., additional, O’Callaghan, Christopher A., additional, Sivori, Simona, additional, Kumar, Sujeet, additional, Selvakumar, Ponniah, additional, Dimmock, Jonathan R., additional, Sharma, Rajendra K., additional, Park, Gibeom, additional, Park, Woong-Yang, additional, Kim, Sang Geon, additional, Lee, Woo Hyung, additional, Kim, Young Woo, additional, Ho, Ping-Chih, additional, Wei, Li-Na, additional, Shen, Jian-Bing, additional, Liang, Bruce T., additional, Soto, Florentina, additional, Communi, Didier, additional, Robaye, Bernard, additional, Boeynaems, Jean Marie, additional, Park, Haein, additional, Dovas, Athanassios, additional, and Cox, Dianne, additional

Published
2012
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