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1. Characteristics, management, and outcomes of patients with infectious encephalitis requiring intensive care: A prospective multicentre observational study

Author

Abgrall, Sophie, Argaud, Laurent, Argemi, Xavier, Baille, Guillaume, Baldolli, Aurélie, Benghanem, Sarah, Bertrand, Kevin, Biberon, Julien, Biron, Charlotte, Fourcade, Geneviève Blanchet, Blot, Mathieu, Bothelo-Nevers, Elisabeth, Bourdain, Frédéric, Boutoille, David, Brasme, Hélène, Bruel, Cédric, Bruneel, Fabrice, Buzele, Rodolphe, Canet, Emmanuel, Canoui, Etienne, Casenave, Philippe, Castan, Bernard, Cazanave, Charles, Cazorla, Céline, Chavanet, Pascal, Chirouze, Catherine, Chroboczek, Tomasz, Courjon, Johan, Da Silva, Daniel, De Broucker, Thomas, De La Blanchardiere, Arnaud, De Montmollin, Etienne, Denes, Eric, Deschanvres, Colin, Dinh, Aurélien, Epaulard, Olivier, Fillatre, Pierre, Forestier, Emmanuel, Fraisse, Thibaut, Gaborit, Benjamin, Gagneux-Brunon, Amandine, Gaillard, Nicolas, Galbois, Arnaud, Godement, Mathieu, Goehringer, François, Goubin, Pascale, Gravier, Simon, Greigert, Valentin, Gueit, Isabelle, Guimard, Thomas, Henry, Carole, Hentzien, Maxime, Jaquet, Pierre, Jomier, Fanny, Jurici, Snejana, Kerneis, Solen, Le Bras, Morgane, Le Marechal, Marion, Le Moal, Gwenael, Le Turnier, Paul, Lecompte, Anne-Sophie, Lecomte, Raphael, Lejeune, Stéphanie, Lescure, François-Xavier, Lesieur, Olivier, Lesprit, Philippe, Louis, Guillaume, Mahieu, Rafael, Makinson, Alain, Marc, Guillaume, Maria, Alexandre, Marin, Nathalie, Martin-Blondel, Guillaume, Martinot, Martin, Mas, Alexandre, Mateu, Philippe, Matt, Morgan, Maulin, Laurence, Mechai, Frédéric, Mutez, Eugénie, Orain, Jérémie, Pachart, Anne, Pansu, Nathalie, Patrat-Delon, Solene, Pavese, Patricia, Pelerin, Hélène, Pelonde-Erimée, Véronique, Pierre, Isabelle, Piet, Emilie, Ponscarme, Diane, Psimaras, Dimitri, Puges, Mathilde, Reignier, Jean, Istin, Mathilde Reveillon, Rheims, Sylvain, Richard-Mornas, Aurélie, Roubeau, Vincent, Ruch, Yvon, Runge, Isabelle, Savini, Hélène, Sonneville, Romain, Stahl, Jean Paul, Tattevin, Pierre, Turmel, Jean-Marie, Tyvaert, Louise, Vareil, Marc-Olivier, Vidal-Roux, Magali, Vitrat, Virginie, Wang, Adrien, Wille, Heidi, Zuber, Mathieu, Almoyna-Martinez, Laurent, Herrmann, Jean-Louis, Honnorat, Jérome, Mailles, Alexandra, Morand, Patrice, Roblot, France, and Stahl, Jean-Paul

Published
2023
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2. Clinical and Epidemiologic Characteristics and Therapeutic Management of Patients with Vibrio Infections, Bay of Biscay, France, 2001-2019

Author

Hoefler, Florence, Pouget-Abadie, Xavier, Roncato-Saberan, Mariam, Lemarie, Romain, Takoudju, Eve-Marie, Raffi, Francois, Corvec, Stephane, Le Bras, Morgane, Cazanave, Charles, Lehours, Philippe, Guimard, Thomas, and Allix-Beguec, Caroline

Subjects
Bay of Biscay -- Health aspects, Statistics, Diagnosis, Care and treatment, Health aspects, Vibrio infections -- Statistics -- Care and treatment -- Diagnosis
Abstract

Some opportunistic pathogens associated with marine environments are already known but until now have caused rare infectious diseases. Among those pathogens are Vibrio spp. other than the well-known V. cholerae [...]

Published
2022
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3. Evaluation of the safety and efficacy of XAV-19 in patients with COVID-19-induced moderate pneumonia: study protocol for a randomized, double-blinded, placebo-controlled phase 2 (2a and 2b) trial

Author

Gaborit, Benjamin, Vanhove, Bernard, Vibet, Marie-Anne, Le Thuaut, Aurélie, Lacombe, Karine, Dubee, Vincent, Ader, Florence, Ferre, Virginie, Vicaut, Eric, Orain, Jéremie, Le Bras, Morgane, Omnes, Anne, Berly, Laetitia, Jobert, Alexandra, Morineau-Le Houssine, Pascale, Botturi, Karine, Josien, Régis, Flet, Laurent, Degauque, Nicolas, Brouard, Sophie, Duvaux, Odile, Poinas, Alexandra, and Raffi, François

Published
2021
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6. Characteristics, management, and outcomes of patients with infectious encephalitis requiring intensive care: A prospective multicentre observational study

Author

Fillatre, Pierre, primary, Mailles, Alexandra, additional, Stahl, Jean Paul, additional, Tattevin, Pierre, additional, Abgrall, Sophie, additional, Argaud, Laurent, additional, Argemi, Xavier, additional, Baille, Guillaume, additional, Baldolli, Aurélie, additional, Benghanem, Sarah, additional, Bertrand, Kevin, additional, Biberon, Julien, additional, Biron, Charlotte, additional, Fourcade, Geneviève Blanchet, additional, Blot, Mathieu, additional, Bothelo-Nevers, Elisabeth, additional, Bourdain, Frédéric, additional, Boutoille, David, additional, Brasme, Hélène, additional, Bruel, Cédric, additional, Bruneel, Fabrice, additional, Buzele, Rodolphe, additional, Canet, Emmanuel, additional, Canoui, Etienne, additional, Casenave, Philippe, additional, Castan, Bernard, additional, Cazanave, Charles, additional, Cazorla, Céline, additional, Chavanet, Pascal, additional, Chirouze, Catherine, additional, Chroboczek, Tomasz, additional, Courjon, Johan, additional, Da Silva, Daniel, additional, De Broucker, Thomas, additional, De La Blanchardiere, Arnaud, additional, De Montmollin, Etienne, additional, Denes, Eric, additional, Deschanvres, Colin, additional, Dinh, Aurélien, additional, Epaulard, Olivier, additional, Fillatre, Pierre, additional, Forestier, Emmanuel, additional, Fraisse, Thibaut, additional, Gaborit, Benjamin, additional, Gagneux-Brunon, Amandine, additional, Gaillard, Nicolas, additional, Galbois, Arnaud, additional, Godement, Mathieu, additional, Goehringer, François, additional, Goubin, Pascale, additional, Gravier, Simon, additional, Greigert, Valentin, additional, Gueit, Isabelle, additional, Guimard, Thomas, additional, Henry, Carole, additional, Hentzien, Maxime, additional, Jaquet, Pierre, additional, Jomier, Fanny, additional, Jurici, Snejana, additional, Kerneis, Solen, additional, Le Bras, Morgane, additional, Le Marechal, Marion, additional, Le Moal, Gwenael, additional, Le Turnier, Paul, additional, Lecompte, Anne-Sophie, additional, Lecomte, Raphael, additional, Lejeune, Stéphanie, additional, Lescure, François-Xavier, additional, Lesieur, Olivier, additional, Lesprit, Philippe, additional, Louis, Guillaume, additional, Mahieu, Rafael, additional, Makinson, Alain, additional, Marc, Guillaume, additional, Maria, Alexandre, additional, Marin, Nathalie, additional, Martin-Blondel, Guillaume, additional, Martinot, Martin, additional, Mas, Alexandre, additional, Mateu, Philippe, additional, Matt, Morgan, additional, Maulin, Laurence, additional, Mechai, Frédéric, additional, Mutez, Eugénie, additional, Orain, Jérémie, additional, Pachart, Anne, additional, Pansu, Nathalie, additional, Patrat-Delon, Solene, additional, Pavese, Patricia, additional, Pelerin, Hélène, additional, Pelonde-Erimée, Véronique, additional, Pierre, Isabelle, additional, Piet, Emilie, additional, Ponscarme, Diane, additional, Psimaras, Dimitri, additional, Puges, Mathilde, additional, Reignier, Jean, additional, Istin, Mathilde Reveillon, additional, Rheims, Sylvain, additional, Richard-Mornas, Aurélie, additional, Roubeau, Vincent, additional, Ruch, Yvon, additional, Runge, Isabelle, additional, Savini, Hélène, additional, Sonneville, Romain, additional, Turmel, Jean-Marie, additional, Tyvaert, Louise, additional, Vareil, Marc-Olivier, additional, Vidal-Roux, Magali, additional, Vitrat, Virginie, additional, Wang, Adrien, additional, Wille, Heidi, additional, Zuber, Mathieu, additional, Almoyna-Martinez, Laurent, additional, Herrmann, Jean-Louis, additional, Honnorat, Jérome, additional, Morand, Patrice, additional, Roblot, France, additional, and Stahl, Jean-Paul, additional

Published
2023
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10. Supplementary Figures S1 & S2 from Chemosensitization by Knockdown of Adenine Nucleotide Translocase-2

Author

Le Bras, Morgane, primary, Borgne-Sanchez, Annie, primary, Touat, Zahia, primary, El Dein, Ossama Sharaf, primary, Deniaud, Aurélien, primary, Maillier, Evelyne, primary, Lecellier, Gael, primary, Rebouillat, Dominique, primary, Lemaire, Christophe, primary, Kroemer, Guido, primary, Jacotot, Etienne, primary, and Brenner, Catherine, primary

Published
2023
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11. Data from Chemosensitization by Knockdown of Adenine Nucleotide Translocase-2

Author

Le Bras, Morgane, primary, Borgne-Sanchez, Annie, primary, Touat, Zahia, primary, El Dein, Ossama Sharaf, primary, Deniaud, Aurélien, primary, Maillier, Evelyne, primary, Lecellier, Gael, primary, Rebouillat, Dominique, primary, Lemaire, Christophe, primary, Kroemer, Guido, primary, Jacotot, Etienne, primary, and Brenner, Catherine, primary

Published
2023
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16. Corrigendum: The NFAT3/RERG complex in luminal breast cancers is required to inhibit cell invasion and may be correlated with an absence of axillary lymph nodes colonization

Author

Coillard, Lucie, primary, Guaddachi, Frédéric, additional, Ralu, Maëlle, additional, Brabencova, Eva, additional, Garbar, Christian, additional, Bensussan, Armand, additional, Le Bras, Morgane, additional, Lehmann-Che, Jacqueline, additional, and Jauliac, Sébastien, additional

Published
2022
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21. Cytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA

Author

Poncet, Delphine, Pauleau, Anne-Laure, Szabadkai, Gyorgy, Vozza, Angelo, Scholz, Sebastian R., Le Bras, Morgane, Briere, Jean-Jacques, Jalil, Abdelali, Le Moigne, Ronan, Brenner, Catherine, Hahn, Gabriele, Wittig, Ilka, Schagger, Hermann, Lemaire, Christophe, Bianchi, Katiuscia, Souquere, Sylvie, Pierron, Gerard, Rustin, Pierre, Goldmacher, Victor S., Rizzuto, Rosario, Palmieri, Ferdinando, and Kroemer, Guido

Subjects
Apoptosis -- Research, Bacterial proteins -- Research, Cytomegaloviruses -- Genetic aspects, Biological sciences
Abstract

Replication of human cytomegalovirus (CMV) requires the expression of the viral mitochondrialocalized inhibitor of apoptosis (vMIA). vMIA inhibits apoptosis by recruiting Bax to mitochondria, resulting in its neutralization. We show that vMIA decreases cell size, reduces actin polymerization, and induces cell rounding. As compared with vMIA-expressing CMV, vMIA-deficient CMV, which replicates in fibroblasts expressing the adenoviral apoptosis suppressor E1B19K, induces less cytopathic effects. These vMIA effects can be separated from its cell death-inhibitory function because vMIA modulates cellular morphology in Bax-deficient cells. Expression of vMIA coincided with a reduction in the cellular adenosine triphosphate (ATP) level, vMIA selectively inhibited one component of the ATP synthasome, namely, the mitochondrial phosphate carrier. Exposure of cells to inhibitors of oxidative phosphorylation produced similar effects, such as an ATP level reduced by 30%, smaller cell size, and deficient actin polymerization. Similarly, knockdown of the phosphate carrier reduced cell size. Our data suggest that the cytopathic effect of CMV can be explained by vMIA effects on mitochondrial bioenergetics.

Published
2006

24. Higher risk of death among MEN1 patients with mutations in the JunD interacting domain: a Groupe d’étude des Tumeurs Endocrines (GTE) cohort study

Author

Thevenon, Julien, Bourredjem, Abderrahmane, Faivre, Laurence, Cardot-Bauters, Catherine, Calender, Alain, Murat, Arnaud, Giraud, Sophie, Niccoli, Patricia, Odou, Marie-Françoise, Borson-Chazot, Françoise, Barlier, Anne, Lombard-Bohas, Catherine, Clauser, Eric, Tabarin, Antoine, Parfait, Béatrice, Chabre, Olivier, Castermans, Emilie, Beckers, Albert, Ruszniewski, Philippe, Le Bras, Morgane, Delemer, Brigitte, Bouchard, Philippe, Guilhem, Isabelle, Rohmer, Vincent, Goichot, Bernard, Caron, Philippe, Baudin, Eric, Chanson, Philippe, Groussin, Lionel, Du Boullay, Hélène, Weryha, Georges, Lecomte, Pierre, Penfornis, Alfred, Bihan, Hélène, Archambeaud, Françoise, Kerlan, Véronique, Duron, Françoise, Kuhn, Jean-Marc, Vergès, Bruno, Rodier, Michel, Renard, Michel, Sadoul, Jean-Louis, Binquet, Christine, and Goudet, Pierre

Published
2013
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27. hnRNP H/F drive RNA G-quadruplex-mediated translation linked to genomic instability and therapy resistance in glioblastoma

Author

Herviou, Pauline, Le Bras, Morgane, Dumas, Leïla, Hieblot, Corinne, Gilhodes, Julia, Cioci, Gianluca, Hugnot, Jean-Philippe, Ameadan, Alfred, Guillonneau, François, Dassi, Erik, Cammas, Anne, Millevoi, Stefania, Centre de Physiopathologie Toulouse Purpan (CPTP), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d’Excellence ‘TOUCAN’ [Toulouse], Institut Universitaire du Cancer de Toulouse - Oncopole (IUCT Oncopole - UMR 1037), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM), Toulouse Biotechnology Institute (TBI), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut des Neurosciences de Montpellier (INM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Plateforme protéomique 3P5 [Institut Cochin] (3P5), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), University of Trento [Trento], FEDER through the 'Operational Programme for Competitiveness Factors and employment 2007-2013', Région Ile-de-France, INSERM, Universite Toulouse III -Paul Sabatier, CNRS, LNCC (Ligue Nationale Contre le Cancer), Fondation ARC pour la Recherche sur le Cancer, Région Occitanie, MENRT, Emergence Canceropole GSO, ANR-11-LABX-0016,IGO,Immunothérapies Grand Ouest(2011), ANR-17-CE12-0017,G4ome,Perspective sur le G4ome ARN : caractérisation exhaustive de la traduction dépendante des G-quadruplexes contrôlée par des protéines de liaison à l'ARN(2017), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), CHU Toulouse [Toulouse]-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut des Neurosciences de Montpellier - Déficits sensoriels et moteurs (INM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Astruc, Suzette, Laboratoires d'excellence - Immunothérapies Grand Ouest - - IGO2011 - ANR-11-LABX-0016 - LABX - VALID, Perspective sur le G4ome ARN : caractérisation exhaustive de la traduction dépendante des G-quadruplexes contrôlée par des protéines de liaison à l'ARN - - G4ome2017 - ANR-17-CE12-0017 - AAPG2017 - VALID, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Institut National des Sciences Appliquées (INSA)-Université Fédérale Toulouse Midi-Pyrénées-Institut National des Sciences Appliquées (INSA)-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)

Subjects
[SDV.MHEP] Life Sciences [q-bio]/Human health and pathology, Heterogeneous-Nuclear Ribonucleoprotein Group F-H, Brain Neoplasms, Science, [SDV]Life Sciences [q-bio], RNA-binding proteins, [SDV.CAN]Life Sciences [q-bio]/Cancer, Article, Genomic Instability, [SDV] Life Sciences [q-bio], DEAD-box RNA Helicases, G-Quadruplexes, [SDV.CAN] Life Sciences [q-bio]/Cancer, Gene Expression Regulation, Cell Line, Tumor, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Humans, lcsh:Q, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Messenger, lcsh:Science, Glioblastoma, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract

RNA G-quadruplexes (RG4s) are four-stranded structures known to control mRNA translation of cancer relevant genes. RG4 formation is pervasive in vitro but not in cellulo, indicating the existence of poorly characterized molecular machinery that remodels RG4s and maintains them unfolded. Here, we performed a quantitative proteomic screen to identify cytosolic proteins that interact with a canonical RG4 in its folded and unfolded conformation. Our results identified hnRNP H/F as important components of the cytoplasmic machinery modulating the structural integrity of RG4s, revealed their function in RG4-mediated translation and uncovered the underlying molecular mechanism impacting the cellular stress response linked to the outcome of glioblastoma., RNA G-quadruplexes (RG4s) have been functionally linked to cancer gene expression. Here, Herviou, Le Bras et al. have identified the protein machinery modulating RG4s and reveal the role and mechanism of hnRNP H/F and DHX36 in RG4-mediated translational regulation affecting cancer treatment in glioblastoma.

Published
2019
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28. Specific TP53 mutation pattern in radiation-induced sarcomas

Author

Gonin-Laurent, Nathalie, Gibaud, Anne, Huygue, Mathilde, Lefèvre, Sandrine H., Le Bras, Morgane, Chauveinc, Laurent, Sastre-Garau, Xavier, Doz, François, Lumbroso, Livia, Chevillard, Sylvie, and Malfoy, Bernard

Published
2006

30. Rôle des protéines de liaison à l'ARN hnRNP H et hnRNP F dans les régulations traductionnelles dans les glioblastomes

Author

Le Bras, Morgane and Le Bras, Morgane

Abstract

Le glioblastome multiforme (GBM) est une tumeur cérébrale extrêmement agressive associée à un mauvais pronostic. C'est pourquoi, il apparaît nécessaire d'identifier les mécanismes moléculaires participant au développement des GBM ainsi qu'à leurs résistances aux traitements afin de développer de nouvelles approches thérapeutiques. Récemment, il a été montré que les régulations traductionnelles jouent un rôle fondamental dans les propriétés agressives du GBM. Les protéines de liaison à l'ARN (RBP) sont des acteurs majeurs de ces régulations dont l'expression/activité est altérée dans les GBM. Les RBP hnRNP HF (HF) font partie des RBP les plus surexprimées dans les GBM et leur contribution dans la régulation traductionnelle des GBM n'a encore jamais été investiguée. Nous avons émis l'hypothèse que hnRNP H et hnRNP F soient au centre d'un réseau de régulations post-transcriptionnelles impactant la machinerie traductionnelle qui contrôle le développement tumoral et la résistance aux traitements des GBM. Nos résultats montrent qu'HF régulent la prolifération et la réponse aux traitements car leur perte d'expression (i) diminue la prolifération des GBM (modèle cellulaire, sphéroïde et xénogreffes in vivo), (ii) active les voies de réponse aux dommages à l'ADN et (iii) sensibilise les cellules de GBM aux irradiations. De plus, nous avons identifié un nouveau rôle pour HF en tant que régulateurs de la traduction. En effet, nos données montrent que les hnRNP HF contrôlent la traduction d'un ensemble d'ARNm en régulant l'expression et l'activité de facteurs d'initiation ainsi qu'en collaborant avec des ARN hélicases partenaires en ciblant des ARNm impliqués dans des processus reliés au développement tumoral et la résistance aux traitements possédant des structures secondaires G-quadruplexe dans leurs 5'UTR. Les données que nous avons générées suggèrent que hnRNP H et hnRNP F sont des régulateurs traductionnels essentiels au développement tumoral et à la résistance aux traitem, Glioblastoma multiforme (GBM) is one of the most aggressive brain tumors with poor prognosis. Understanding the molecular mechanisms involved in the development and resistance to treatments of gliomas could improve treatment efficiency. Recently, it has been demonstrated that translational regulations play a key role in the GBM aggressivity. RNA binding proteins (RBP) are major regulators of these processes and have altered expression / activity in GBM. The RBP hnRNP H and hnRNP F (HF) are among the most overexpressed RBP in GBM and their role in GBM translational regulation has never been investigated yet. We hypothesize that HF are at the core of a post-transcriptional regulation network which impacts the translational machinery that controls GBM tumor development and resistance to treatment. We have demonstrated that hnRNP H and hnRNP F regulate proliferation and response to treatment because their depletion (i) decreases the GBM proliferation (cell line model, spheroid and in vivo xenografts), (ii) activates the DNA damage response pathways and (iii) sensitizes the GBM cells to irradiation. We have identified HF as new regulators of GBM translation. Indeed, our data show that hnRNP H and hnRNP F control mRNA translation by regulating expression/activity of initiation factors and in collaboration with RNA helicases by targeting mRNA involved in oncogenic processes and containing secondary structures called G-quadruplex in their 5'UTR. The data that we have generated suggest that HF are essential translational regulators involved in tumor development and resistance to treatment in GBM.

Published
2018

32. hnRNP A1-mediated translational regulation of the G quadruplex-containing RON receptor tyrosine kinase mRNA linked to tumor progression

Author

Cammas, Anne, primary, Lacroix-Triki, Magali, additional, Pierredon, Sandra, additional, Le Bras, Morgane, additional, Iacovoni, Jason S., additional, Teulade-Fichou, Marie-Paule, additional, Favre, Gilles, additional, Roché, Henri, additional, Filleron, Thomas, additional, Millevoi, Stefania, additional, and Vagner, Stéphan, additional

Published
2016
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33. Corrigendum to “The fourth isoform of the adenine nucleotide translocator inhibits mitochondrial apoptosis in cancer cells” [Int. J. Biochem. Cell Biol. 42 (2010) 623–629]

Author

Gallerne, Cindy, primary, Touat, Zahia, additional, Chen, Zhi Xiong, additional, Martel, Cécile, additional, Mayola, Eleonore, additional, el dein, Ossama Sharaf, additional, Buron, Nelly, additional, Le Bras, Morgane, additional, Jacotot, Etienne, additional, Borgne-Sanchez, Annie, additional, Lemoine, Antoinette, additional, Lemaire, Christophe, additional, Pervaiz, Shazib, additional, and Brenner, Catherine, additional

Published
2014
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40. Chemosensitization by Knockdown of Adenine Nucleotide Translocase-2

Author

Le Bras, Morgane, primary, Borgne-Sanchez, Annie, additional, Touat, Zahia, additional, El Dein, Ossama Sharaf, additional, Deniaud, Aurélien, additional, Maillier, Evelyne, additional, Lecellier, Gael, additional, Rebouillat, Dominique, additional, Lemaire, Christophe, additional, Kroemer, Guido, additional, Jacotot, Etienne, additional, and Brenner, Catherine, additional

Published
2006
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41. Ant2

Author

Le Bras, Morgane, primary, Deniaud, Aurelien, additional, Lecellier, Gael, additional, Kroemer, Guido, additional, and Brenner, Catherine, additional

Published
2005
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42. Ant1

Author

Deniaud, Aurelien, primary, Le Bras, Morgane, additional, Lecellier, Gael, additional, Brenner, Catherine, additional, and Kroemer, Guido, additional

Published
2005
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43. Additional file 1 of Evaluation of the safety and efficacy of XAV-19 in patients with COVID-19-induced moderate pneumonia: study protocol for a randomized, double-blinded, placebo-controlled phase 2 (2a and 2b) trial

Author

Gaborit, Benjamin, Vanhove, Bernard, Vibet, Marie-Anne, Le Thuaut, Aurélie, Lacombe, Karine, Dubee, Vincent, Ader, Florence, Ferre, Virginie, Vicaut, Eric, Orain, Jéremie, Le Bras, Morgane, Omnes, Anne, Berly, Laetitia, Jobert, Alexandra, Morineau-Le Houssine, Pascale, Botturi, Karine, Josien, Régis, Flet, Laurent, Degauque, Nicolas, Brouard, Sophie, Duvaux, Odile, Poinas, Alexandra, and Raffi, François

Subjects
Data_FILES, 3. Good health
Abstract

Additional file 1.

44. Additional file 1 of Evaluation of the safety and efficacy of XAV-19 in patients with COVID-19-induced moderate pneumonia: study protocol for a randomized, double-blinded, placebo-controlled phase 2 (2a and 2b) trial

Author

Gaborit, Benjamin, Vanhove, Bernard, Vibet, Marie-Anne, Le Thuaut, Aurélie, Lacombe, Karine, Dubee, Vincent, Ader, Florence, Ferre, Virginie, Vicaut, Eric, Orain, Jéremie, Le Bras, Morgane, Omnes, Anne, Berly, Laetitia, Jobert, Alexandra, Morineau-Le Houssine, Pascale, Botturi, Karine, Josien, Régis, Flet, Laurent, Degauque, Nicolas, Brouard, Sophie, Duvaux, Odile, Poinas, Alexandra, and Raffi, François

Subjects
Data_FILES, 3. Good health
Abstract

Additional file 1.

45. The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies.

Author

de Thé H, Le Bras M, and Lallemand-Breitenbach V

Subjects
Animals, Humans, Leukemia, Promyelocytic, Acute metabolism, Mice, Oncogene Proteins, Fusion metabolism, Oxidative Stress drug effects, Oxidative Stress physiology, Receptors, Retinoic Acid metabolism, Retinoic Acid Receptor alpha, Small Ubiquitin-Related Modifier Proteins metabolism, Antineoplastic Agents therapeutic use, Arsenic therapeutic use, Leukemia, Promyelocytic, Acute drug therapy, Tretinoin therapeutic use
Abstract

Acute promyelocytic leukemia (APL) is driven by a chromosomal translocation whose product, the PML/retinoic acid (RA) receptor α (RARA) fusion protein, affects both nuclear receptor signaling and PML body assembly. Dissection of APL pathogenesis has led to the rediscovery of PML bodies and revealed their role in cell senescence, disease pathogenesis, and responsiveness to treatment. APL is remarkable because of the fortuitous identification of two clinically effective therapies, RA and arsenic, both of which degrade PML/RARA oncoprotein and, together, cure APL. Analysis of arsenic-induced PML or PML/RARA degradation has implicated oxidative stress in the biogenesis of nuclear bodies and SUMO in their degradation.

Published
2012
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46. [RXR, a key member of the oncogenic complex in acute promyelocytic leukemia].

Author

Halftermeyer J, Le Bras M, and De Thé H

Subjects
Animals, Cell Transformation, Neoplastic metabolism, Humans, Models, Biological, Multiprotein Complexes genetics, Multiprotein Complexes metabolism, Multiprotein Complexes physiology, Oncogene Proteins, Fusion genetics, Oncogene Proteins, Fusion metabolism, Oncogene Proteins, Fusion physiology, Oncogenes genetics, Oncogenes physiology, Protein Binding, Receptors, Retinoic Acid genetics, Receptors, Retinoic Acid metabolism, Receptors, Retinoic Acid physiology, Retinoid X Receptors genetics, Retinoid X Receptors metabolism, Cell Transformation, Neoplastic genetics, Leukemia, Promyelocytic, Acute genetics, Retinoid X Receptors physiology
Abstract

Acute promyelocytic leukaemia (APL) is induced by fusion proteins always implying the retinoic acid receptor RARa. Although PML-RARa and other fusion oncoproteins are able to bind DNA as homodimers, in vivo they are always found in association with the nuclear receptor RXRa (Retinoid X Receptor). Thus, RXRa is an essential cofactor of the fusion protein for the transformation. Actually, RXRa contributes to several aspects of in vivo -transformation: RARa fusion:RXRa hetero-oligomeric complexes bind DNA with a much greater affinity than RARa fusion homodimers. Besides, PML-RARa:RXRa recognizes an enlarged repertoire of DNA binding sites. Thus the association between fusion proteins and RXRa regulates more genes than the homodimer alone. Titration of RXRa by the fusion protein may also play a role in the transformation process, as well as post-translational modifications of RXRa in the complex. Finally, RXRa is required for rexinoid-induced APL differentiation. Thus, RXRa is a key member of the oncogenic complex., (© 2011 médecine/sciences – Inserm / SRMS.)

Published
2011
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47. Small ubiquitin-related modifier paralogs are indispensable but functionally redundant during early development of zebrafish.

Author

Yuan H, Zhou J, Deng M, Liu X, Le Bras M, de The H, Chen SJ, Chen Z, Liu TX, and Zhu J

Subjects
Amino Acid Sequence, Animals, Animals, Genetically Modified, Cells, Cultured, Embryo, Nonmammalian, Gene Expression Profiling, Gene Expression Regulation, Developmental, Genetic Complementation Test, Humans, Molecular Sequence Data, Oligonucleotide Array Sequence Analysis, Protein Processing, Post-Translational genetics, Sequence Homology, Small Ubiquitin-Related Modifier Proteins genetics, Small Ubiquitin-Related Modifier Proteins metabolism, Zebrafish metabolism, Embryonic Development genetics, Small Ubiquitin-Related Modifier Proteins physiology, Zebrafish embryology, Zebrafish genetics
Abstract

The Small ubiquitin-related modifier (SUMO) conjugation to a variety of proteins regulates diverse cellular processes, including transcription, cell cycle regulation and maintenance of genome integrity. To investigate in vivo biological function of SUMO paralogs, we inactivated them in the early development of zebrafish. While zebrafish embryos deficient for all three SUMO paralogs, as Ubc9-deficient ones, displayed severe defects, loss of individual SUMO paralog was compatible with a normal development. SUMO-deficient embryos can be rescued by a single human or zebrafish SUMO. While key structural basic lysine residues and N-terminal unstructured stretch of SUMO are critical for in vivo rescue, the consensus K11 sumoylation site of SUMO2 is dispensable, implying that chain formation on this potential site is unessential for normal development. Inactivation of all three SUMOs triggered p53-dependent apoptosis and further inactivation of p53 restored normal zebrafish development. Interestingly, we also demonstrate that the dominant negative truncated form of p53, Delta113p53, significantly blunts SUMO depletion-induced p53 activity in vivo. Taken together, our results suggest that SUMO paralogs are indispensable, but redundant, in the early development of zebrafish.

Published
2010
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48. The modulation of inter-organelle cross-talk to control apoptosis.

Author

Le Bras M, Rouy I, and Brenner C

Subjects
Animals, Apoptosis Inducing Factor metabolism, Apoptosis Regulatory Proteins metabolism, Caspases metabolism, Endoplasmic Reticulum metabolism, Humans, Mitochondrial Proteins metabolism, NF-kappa B metabolism, Proto-Oncogene Proteins c-bcl-2 metabolism, Receptors, Cytoplasmic and Nuclear metabolism, Tumor Suppressor Protein p53 metabolism, bcl-X Protein metabolism, Apoptosis physiology, Organelles metabolism, Tumor Suppressor Proteins metabolism
Abstract

Mitochondria fulfill a wide array of functions dedicated to the energetic metabolism as well as the control of cell death. These functions imply that mitochondria can be activated by a variety of signals and can integrate them to trigger a process called mitochondrial membrane permeabilization (MMP), which induces the ultimate events of apoptosis. MMP consists in a sudden increase in the permeability of mitochondrial membrane that results in the release of critical proapoptotic intermembrane space effectors into the cytosol such as cytochrome c, apoptosis-inducing factor (AIF), Smac/Diablo, Endo G, and pro-caspases. In many models of apoptosis, mitochondrial translocation of proteins and/or lipids concomitantly with alterations of the intracellular milieu has been shown to activate MMP. This applies to tumor suppressors of the Bax/Bcl-2 family (Bax, Bad, Bid, Bim), several protein kinases (Akt, ASK1, hexokinase), p53, NF-kappaB, and nuclear orphan receptors such as TR3/Nur77. After mitochondrial membrane association, these proteins target constitutive mitochondrial proteins including the permeability transition pore complex (PTPC), Bcl-X(L), HSP70, and/or the lipid interphase. Subsequently, they switch their vital function into a lethal function to promote membrane permeabilization and protein release. In this review, we will describe some general rules of inter-organelle cross-talk activating MMP and will review selected examples of pro-apoptotic protein translocation. Finally, we will propose new pharmacological strategies to modulate this process in a therapeutic perspective.

Published
2006
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