47 results on '"Bost, Frederic"'
Search Results
2. Nanoblades allow high-level genome editing in murine and human organoids
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Tiroille, Victor, Krug, Adrien, Bokobza, Emma, Kahi, Michel, Bulcaen, Mattijs, Ensinck, Marjolein M., Geurts, Maarten H., Hendriks, Delilah, Vermeulen, François, Larbret, Frédéric, Gutierrez-Guerrero, Alejandra, Chen, Yu, Van Zundert, Indra, Rocha, Susana, Rios, Anne C., Medaer, Louise, Gijsbers, Rik, Mangeot, Philippe E., Clevers, Hans, Carlon, Marianne S., Bost, Frédéric, and Verhoeyen, Els
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- 2023
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3. TAXOMET: A French Prospective Multicentric Randomized Phase II Study of Docetaxel Plus Metformin Versus Docetaxel Plus Placebo in Metastatic Castration-Resistant Prostate Cancer
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Pujalte Martin, Marc, Borchiellini, Delphine, Thamphya, Brice, Guillot, Aline, Paoli, Jean-Baptiste, Besson, Dominique, Hilgers, Werner, Priou, Frank, El Kouri, Claude, Hoch, Benjamin, Deville, Jean-Laurent, Schiappa, Renaud, Cheli, Sandrine, Milano, Gérard, Tanti, Jean-François, Bost, Frédéric, and Ferrero, Jean-Marc
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- 2021
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4. Metformin: A metabolic disruptor and anti-diabetic drug to target human leukemia
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Rosilio, Célia, Ben-Sahra, Issam, Bost, Frédéric, and Peyron, Jean-François
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- 2014
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5. Nanoblades allow high-level genome editing in organoids
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Tirolle, Victor, primary, Krug, Adrien, additional, Bokobza, Emma, additional, Bulcaen, Mattijs, additional, Ensinck, Marjolein M., additional, Geurts, Maarten H., additional, Hendriks, Delilah, additional, Vermeulen, François, additional, Larbret, Frédéric, additional, Gutierrez-Guerrero, Alejandra, additional, Medaer, Louise, additional, Gijsbers, Rik, additional, Mangeot, Philippe E., additional, Clevers, Hans, additional, Carlon, Marianne S., additional, Bost, Frederic, additional, and Verhoeyen, Els, additional
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- 2022
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6. The metabolic perturbators metformin, phenformin and AICAR interfere with the growth and survival of murine PTEN-deficient T cell lymphomas and human T-ALL/T-LL cancer cells
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Rosilio, Célia, Lounnas, Nadia, Nebout, Marielle, Imbert, Véronique, Hagenbeek, Thijs, Spits, Hergen, Asnafi, Vahid, Pontier-Bres, Rodolphe, Reverso, Julie, Michiels, Jean-François, Ben Sahra, Issam, Bost, Fréderic, and Peyron, Jean-François
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- 2013
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7. VDAC1: a structural interface between primary cilia and metabolism?
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Rovini, Amandine, primary, Guo, Yingbo, additional, Fabbri, Lucilla, additional, Cunha-De Padua, Monique Meyenberg, additional, Bost, Frederic, additional, and Mazure, Nathalie M., additional
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- 2022
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8. Apelin and APJ regulation in adipose tissue and skeletal muscle of type 2 diabetic mice and humans
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Dray, Cedric, Debard, Cyrille, Jager, Jennifer, Disse, Emmanuel, Daviaud, Daniele, Martin, Pascal, Attane, Camille, Wanecq, Estelle, Guigne, Charlotte, Bost, Frederic, Tanti, Jean-Francois, Laville, Martine, Vidal, Hubert, Valet, Philippe, and Castan-Laurell, Isabelle
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Insulin resistance -- Research ,Type 2 diabetes -- Research ,Adipose tissues -- Research ,Biological sciences - Abstract
Apelin, an adipocyte-secreted factor upregulated by insulin, is increased in adipose tissue (AT) and plasma with obesity. Apelin was recently identified as a new player in the control of glucose homeostasis. However, the regulation of apelin and APJ (apelin receptor) expression in skeletal muscle in relation to insulin resistance or type 2 diabetes is not known. Thus we studied apelin and APJ expression in AT and muscle in different mice models of obesity and in type 2 diabetic patients. In insulin-resistant high-fat (HF)-fed mice, apelin and APJ expression were increased in AT compared with control. This was not the case in AT of highly insulin-resistant db/db mice. In skeletal muscle, apelin expression was similar in control and HF-fed mice and decreased in db/db mice. APJ expression was decreased in both HF-fed and db/db mice. Control subjects and type 2 diabetic patients were subjected to a hyperinsulinemic-euglycemic clamp, and tissues biopsies were obtained before and at the end of the clamp. There was no significant difference in basal apelin and APJ expression in AT and muscle between control and diabetic patients. However, apelin plasma levels were significantly increased in diabetic patients. During the clamp, hyperinsulinemia increased apelin and APJ expression in AT of control but not in diabetic subjects. In muscle, only APJ mRNA levels were increased in control but also in diabetic patients. Taken together, these data show that apelin and APJ expression in mice and humans is regulated in a tissue-dependent manner and according to the severity of insulin resistance. insulin resistance; adipokine; insulin doi: 10.1152/ajpendo.00598.2009.
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- 2010
9. UBTD1 regulates ceramide balance and endolysosomal positioning to coordinate EGFR signaling
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Torrino, Stéphanie, primary, Tiroille, Victor, additional, Dolfi, Bastien, additional, Dufies, Maeva, additional, Hinault, Charlotte, additional, Bonesso, Laurent, additional, Dagnino, Sonia, additional, Uhler, Jennifer, additional, Irondelle, Marie, additional, Gay, Anne-sophie, additional, Fleuriot, Lucile, additional, Debayle, Delphine, additional, Lacas-Gervais, Sandra, additional, Cormont, Mireille, additional, Bertero, Thomas, additional, Bost, Frederic, additional, Gilleron, Jerome, additional, and Clavel, Stephan, additional
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- 2021
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10. Author response: UBTD1 regulates ceramide balance and endolysosomal positioning to coordinate EGFR signaling
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Torrino, Stéphanie, primary, Tiroille, Victor, additional, Dolfi, Bastien, additional, Dufies, Maeva, additional, Hinault, Charlotte, additional, Bonesso, Laurent, additional, Dagnino, Sonia, additional, Uhler, Jennifer, additional, Irondelle, Marie, additional, Gay, Anne-sophie, additional, Fleuriot, Lucile, additional, Debayle, Delphine, additional, Lacas-Gervais, Sandra, additional, Cormont, Mireille, additional, Bertero, Thomas, additional, Bost, Frederic, additional, Gilleron, Jerome, additional, and Clavel, Stephan, additional
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- 2021
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11. Hypoxia decreases insulin signaling pathways in adipocytes
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Regazzetti, Claire, Peraldi, Pascal, Gremeaux, Thierry, Najem-Lendom, Rosanna, Ben-Sahra, Issam, Cormont, Mireille, Bost, Frederic, Le Marchand-Brustel, Yannick, Tanti, Jean-Francois, and Giorgetti-Peraldi, Sophie
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Insulin -- Receptors ,Hypoxia -- Complications and side effects -- Physiological aspects ,Fat cells -- Chemical properties -- Physiological aspects ,Health ,Chemical properties ,Complications and side effects ,Physiological aspects - Abstract
OBJECTIVE--Obesity is characterized by an overgrowth of adipose tissue that leads to the formation of hypoxic areas within this tissue. We investigated whether this phenomenon could be responsible for insulin resistance by studying the effect of hypoxia on the insulin signaling pathway in adipocytes. RESEARCH DESIGN AND METHODS--The hypoxic signaling pathway was modulated in adipocytes from human and murine origins through incubation under hypoxic conditions (1% [O.sub.2]) or modulation of hypoxia-inducible factor (HIF) expression. Insulin signaling was monitored through the phosphorylation state of several key partners of the pathway and glucose transport. RESULTS--In both human and murine adipocytes, hypoxia inhibits insulin signaling as revealed by a decrease in the phosphorylation of insulin receptor. In 3T3-L1 adipocytes, this inhibition of insulin receptor phosphorylation is followed by a decrease in the phosphorylation state of protein kinase B and AS160, as well as an inhibition of glucose transport in response to insulin. These processes were reversible under normoxic conditions. The mechanism of inhibition seems independent of protein tyrosine phosphatase activities. Overexpression of HIF-1α or -2α or activation of HIF transcription factor with Co[Cl.sub.2] mimicked the effect of hypoxia on insulin signaling, whereas downregulation of HIF-1α and -2α by small interfering RNA inhibited it. CONCLUSIONS--We have demonstrated that hypoxia creates a state of insulin resistance in adipocytes that is dependent upon HIF transcription factor expression. Hypoxia could be envisioned as a new mechanism that participates in insulin resistance in adipose tissue of obese patients., Obesity results from an imbalance between energy intake and energy expenditure. Abdominal obesity and adipose tissue dysfunction are major risk factors for chronic diseases, such as insulin resistance, type 2 [...]
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- 2009
12. The metabolic modulator PGC-1α in cancer
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Bost, Frederic, Kaminski, Lisa, and Inserm U1065, Centre Méditerranéen de Médecine Moléculaire
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mitochondria ,breast cancer ,PGC1 alpha ,pancreatic cancer ,melanoma ,[SDV.CAN]Life Sciences [q-bio]/Cancer ,Review Article ,[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] ,prostate cancer ,metabolism - Abstract
International audience; The peroxisome proliferator-activated receptor gamma coactivator 1 alpha (PGC-1α) is a central modulator of cell metabolism. It regulates mitochondrial biogenesis and oxidative metabolism. Modifications and adaptations in cellular metabolism are hallmarks of cancer cells, thus, it is not surprising that PGC-1α plays a role in cancer. Several recent articles have shown that PGC-1α expression is altered in tumors and metastasis in relation to modifications in cellular metabolism. The potential uses of PGC-1α as a therapeutic target and a biomarker of the advanced form of cancer will be summarized in this review.
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- 2019
13. Inhibition of p38MAPK increases adipogenesis from embryonic to adult stages
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Aouadi, Myriam, Laurent, Kathiane, Prot, Matthieu, Marchand-Brustel, Yannick Le, Binetruy, Bernard, and Bost, Frederic
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Mitogens -- Research -- Health aspects ,Adipose tissues -- Health aspects -- Research ,Protein kinases -- Research -- Health aspects ,Health ,Research ,Health aspects - Abstract
Formation of new adipocytes from precursor cells contributes to adipose tissue expansion and obesity. In this study, we asked whether p38 mitogen-activated protein kinase (MAPK) pathway regulates normal and pathological adipogenesis. In both dietary and genetically (ob/ob) obese mice, adipose tissues displayed a marked decrease in p38MAPK activity compared with the same tissues from lean mice. Furthermore, p38MAPK activity was significantly higher in preadipocytes than in adipocytes, suggesting that p38MAPK activity decreases during adipocyte differentiation. In agreement with an inhibitory role of p38MAPK in this process, we found that in vitro inhibition of p38MAPK, with the specific inhibitor PD169316, increased the expression of adipocyte markers in several cellular models, from embryonic to adult stages. Importantly, the expression of adipocyte markers was higher in p38MAPKa knockout cells than in their wild-type counterparts. Phosphorylation of C/EBPβ, which enhances its transcriptional activity, is increased after p38MAPK inhibition. Finally, either inhibition or disruption of p38MAPK increased peroxisome proliferator-activated receptor (PPAR)γ expression and transactivation. Rescue of p38MAPK in knockout cells reduced PPARγ activity to the low basal level of wild-type cells. We demonstrate here, by using multipronged approaches involving p38 chemical inhibitor and p38MAPKα knockout cells, that p38MAPK plays a negative role in adipogenesis via inhibition of C/EBPβ and PPARγ transcriptional activities., Intracellular mitogen-activated protein kinase (MAPK) signaling pathways play a pivotal role in many essential cellular processes, such as proliferation, inflammation, and differentiation. The MAPK family comprises three groups: extracellular signal-regulated [...]
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- 2006
14. The extracellular signal--regulated kinase isoform ERK1 is specifically required for in vitro and in vivo adipogenesis
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Bost, Frederic, Aouadi, Myriam, Caron, Leslie, Even, Patrick, Belmonte, Nathalie, Prot, Matthieu, Dani, Christian, Hofman, Paul, Pages, Gilles, Pouyssegur, Jacques, Le Marchard-Brustel, Yannick, and Binetruy, Bernard
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Obesity -- Case studies -- Risk factors ,Risk factors (Health) -- Case studies ,Cardiovascular diseases -- Risk factors -- Case studies ,Health ,Case studies ,Risk factors - Abstract
Hyperplasia of adipose tissue is critical for the development of obesity, but molecular mechanisms governing normal or pathological recruitment of new adipocytes remain unclear. The extracellular signal-regulated kinase (ERK) pathway plays a pivotal role in many essential cellular functions, such as proliferation and differentiation. Using ERK[1.sup.-/-] mice, we investigated the role of this isoform in adipose tissue development. Mice lacking ERK1 have decreased adiposity and fewer adipocytes than wild-type animals. Furthermore, ERK[1.sub.-/-] mice challenged with high-fat diet are resistant to obesity, are protected from insulin resistance, and have a higher postprandial metabolic rate. To get insights into cellular mechanisms implicated in reduced adiposity in ERK[1.sup.-/-] animals, we analyzed adipocyte differentiation in ERK1-/- cells. Compared with wild-type control cells, mouse embryo fibroblasts and cultures of adult preadipocytes isolated from ERK[1.sup.-/-] adult animals exhibit impaired adipogenesis. An inhibitor of the ERK pathway does not affect the residual adipogenesis of the ERK[1.sup.-/-] cells, suggesting that ERK2 is not implicated in adipocyte differentiation. Our results clearly link ERK1 to the regulation of adipocyte differentiation, adiposity, and high-fat diet-induced obesity. This suggests that a therapeutic approach of obesity targeting specifically the ERK1 isoform and not ERK2 would be of particular interest., Obesity represents a major health hazard and is a high-risk factor for type 2 diabetes and cardiovascular diseases. One of the main functions of adipocytes is to store surplus calories [...]
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- 2005
15. TAXOMET: A French prospective multicenter randomized controlled phase II study comparing docetaxel plus metformin versus docetaxel plus placebo in mCRPC.
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Pujalte Martin, MARC, primary, Borchiellini, Delphine, additional, Viotti, Julien, additional, Guillot, Aline, additional, Paoli, Jean Baptiste, additional, Besson, Dominique, additional, Hilgers, Werner, additional, El Kouri, Claude, additional, Cavaglione, Gerard, additional, Priou, Frank, additional, Lharidon, Tifenn, additional, Largillier, Remy, additional, Deville, Jean-Laurent, additional, Hoch, Benjamin, additional, Schiappa, Renaud, additional, Tanti, Jean François, additional, Bost, Frederic, additional, and Ferrero, Jean-Marc, additional
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- 2019
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16. Low doses of persistent organic pollutants (PFOA and PCB153) increase the tumor aggressiveness of hormone-dependent cancer cells
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Charazac, Aurelie, primary, Hinault, Charlotte, additional, Bost, Frederic, additional, Clavel, Stephan, additional, and Chevalier, Nicolas, additional
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- 2019
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17. An Adaptative Threshold Operator Taking Shape into Account: Application to Mitochondrial Network Segmentation
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Giulietti, Kevin, primary, Lavisse, Guillaume, additional, Charazac, Aurelie, additional, Clavel, Stephan, additional, Bost, Frederic, additional, and Descombes, Xavier, additional
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- 2019
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18. The energy disruptor metformin targets mitochondrial integrity via modification of calcium flux in cancer cells
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Loubiere, Camille, Clavel, Stephan, Gilleron, Jerome, Harisseh, Rania, Fauconnier, Jeremy, Ben-Sahra, Issam, Kaminski, Lisa, Laurent, Kathiane, Herkenne, Stephanie, Lacas-Gervais, Sandra, Ambrosetti, Damien, Alcor, Damien, Rocchi, Stephane, Cormont, Mireille, Michiels, Jean-François, Mari, Bernard, Mazure, Nathalie M., Scorrano, Luca, Lacampagne, Alain, Gharib, Abdallah, Tanti, Jean-François, Bost, Frederic, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Cardiovasculaire, métabolisme, diabétologie et nutrition (CarMeN), Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Hospices Civils de Lyon (HCL), Physiologie & médecine expérimentale du Cœur et des Muscles [U 1046] (PhyMedExp), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Northwestern University Chicago, Universita degli Studi di Padova, Dulbecco Telethon Institute, Telethon Foundation, Centre Commun de Microscopie Appliquée (CCMA), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA), Hôpital Pasteur [Nice] (CHU), Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut de signalisation, biologie du développement et cancer (ISBDC), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National de la Recherche Agronomique (INRA), Northwestern University [Chicago, Ill. USA], COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Université Côte d'Azur (UCA), ITMO-Cancer, foundation ARC, French Ministry of Research, Conseil General Alpes-Maritimes (Appel a projets santé), Region PACA (Appel a projets plateforme), and French Government (National Research Agency, ANR) through the 'Investments for the Future' LABEX SIGNALIFE [ANR-11-LABX-0028-01]
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endocrine system diseases ,Science ,[SDV]Life Sciences [q-bio] ,Endoplasmic Reticulum ,biogenèse mitochondriale ,Mitochondrial Membrane Transport Proteins ,Models, Biological ,Article ,Mice ,stress ,membrane mitochondriale ,Cell Line, Tumor ,Animals ,Humans ,réticulum endoplasmique ,cellule cancereuse ,Cancer ,apoptose ,Organelle Biogenesis ,Multidisciplinary ,Mitochondrial Permeability Transition Pore ,digestive, oral, and skin physiology ,nutritional and metabolic diseases ,flux de calcium ,Endoplasmic Reticulum Stress ,Metformin ,metformine ,Mitochondria ,Medicine ,Calcium ,Energy Metabolism ,Mitochondrial Swelling - Abstract
International audience; Mitochondrial integrity is critical for the regulation of cellular energy and apoptosis. Metformin is an energy disruptor targeting complex I of the respiratory chain. We demonstrate that metformin induces endoplasmic reticulum (ER) stress, calcium release from the ER and subsequent uptake of calcium into the mitochondria, thus leading to mitochondrial swelling. Metformin triggers the disorganization of the cristae and inner mitochondrial membrane in several cancer cells and tumors. Mechanistically, these alterations were found to be due to calcium entry into the mitochondria, because the swelling induced by metformin was reversed by the inhibition of mitochondrial calcium uniporter (MCU). We also demonstrated that metformin inhibits the opening of mPTP and induces mitochondrial biogenesis. Altogether, the inhibition of mPTP and the increase in mitochondrial biogenesis may account for the poor pro-apoptotic effect of metformin in cancer cells. Maintaining mitochondrial structural integrity is essential for cells to produce energy, overcome environmental stresses such as nutrient deprivation and hypoxia and respond to genotoxic agents, including chemotherapy. Consequently, the disruption of mitochondrial metabolism sensitizes cells to apoptosis and opens new therapeutic avenues in cancer treatment. Metformin is a biguanide and a widely prescribed anti-diabetic agent, but it is also a metabolic disruptor that specifically targets the metabolism of cancer cells 1. Several reports have shown that this drug inhibits cancer cell growth and has antitumoral effects 2, 3. Biguanides inhibit the activity of the mito-chondrial respiratory chain complex I, thus leading to energetic stress due to the decrease in ATP synthesis 4-6. Decreased intracellular ATP leads to the activation of the energy sensitive kinase AMP-activated protein kinase (AMPK) and the inhibition of mechanistic target of rapamycin (mTORC1), which regulates cell growth and cell proliferation and is frequently hyperactivated in tumors. Despite the well-characterized effects of biguanides on the respiratory chain, their effects on the mitochondrial ultrastructure are poorly understood.
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- 2017
19. Quantitative image based analysis of endocrine disruptor effects on mitochondria morphology-function in prostate cancer cells
- Author
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Charazac, Aurelie, primary, Deconde, Le Butor Celia, additional, Gueye, Mamadou, additional, Gilleron, Jerome, additional, Giulietti, Kevin, additional, Fenichel, Patrick, additional, Descombes, Xavier, additional, Bost, Frederic, additional, Clavel, Stephan, additional, and Chevalier, Nicolas, additional
- Published
- 2017
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20. Guidelines for the use and interpretation of assays for monitoring autophagy.
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Luxembourg Centre for Systems Biomedicine (LCSB): Clinical & Experimental Neuroscience (Krüger Group) [research center], Klionsky, Daniel J., Abdalla, Fabio C., Abeliovich, Hagai, Abraham, Robert T., Acevedo-Arozena, Abraham, Adeli, Khosrow, Agholme, Lotta, Agnello, Maria, Agostinis, Patrizia, Aguirre-Ghiso, Julio A., Ahn, Hyung Jun, Ait-Mohamed, Ouardia, Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akira, Shizuo, Al-Younes, Hesham M., Al-Zeer, Munir A., Albert, Matthew L., Albin, Roger L., Alegre-Abarrategui, Javier, Aleo, Maria Francesca, Alirezaei, Mehrdad, Almasan, Alexandru, Almonte-Becerril, Maylin, Amano, Atsuo, Amaravadi, Ravi, Amarnath, Shoba, Amer, Amal O., Andrieu-Abadie, Nathalie, Anantharam, Vellareddy, Ann, David K., Anoopkumar-Dukie, Shailendra, Aoki, Hiroshi, Apostolova, Nadezda, Arancia, Giuseppe, Aris, John P., Asanuma, Katsuhiko, Asare, Nana Y. O., Ashida, Hisashi, Askanas, Valerie, Askew, David S., Auberger, Patrick, Baba, Misuzu, Backues, Steven K., Baehrecke, Eric H., Bahr, Ben A., Bai, Xue-Yuan, Bailly, Yannick, Baiocchi, Robert, Baldini, Giulia, Balduini, Walter, Ballabio, Andrea, Bamber, Bruce A., Bampton, Edward T. W., Banhegyi, Gabor, Bartholomew, Clinton R., Bassham, Diane C., Bast, Robert C. Jr, Batoko, Henri, Bay, Boon-Huat, Beau, Isabelle, Bechet, Daniel M., Begley, Thomas J., Behl, Christian, Behrends, Christian, Bekri, Soumeya, Bellaire, Bryan, Bendall, Linda J., Benetti, Luca, Berliocchi, Laura, Bernardi, Henri, Bernassola, Francesca, Besteiro, Sebastien, Bhatia-Kissova, Ingrid, Bi, Xiaoning, Biard-Piechaczyk, Martine, Blum, Janice S., Boise, Lawrence H., Bonaldo, Paolo, Boone, David L., Bornhauser, Beat C., Bortoluci, Karina R., Bossis, Ioannis, Bost, Frederic, Bourquin, Jean-Pierre, Boya, Patricia, Boyer-Guittaut, Michael, Bozhkov, Peter V., Brady, Nathan R., Brancolini, Claudio, Brech, Andreas, Brenman, Jay E., Brennand, Ana, Bresnick, Emery H., Brest, Patrick, Bridges, Dave, Bristol, Molly L., Brookes, Paul S., Brown, Eric J., Brumell, John H., Brunetti-Pierri, Nicola, Brunk, Ulf T., Bulman, Dennis E., Bultman, Scott J., Bultynck, Geert, Burbulla, Lena F., Bursch, Wilfried, Butchar, Jonathan P., Buzgariu, Wanda, Bydlowski, Sergio P., Cadwell, Ken, Cahova, Monika, Cai, Dongsheng, Cai, Jiyang, Cai, Qian, Calabretta, Bruno, Calvo-Garrido, Javier, Camougrand, Nadine, Campanella, Michelangelo, Campos-Salinas, Jenny, Candi, Eleonora, Cao, Lizhi, Caplan, Allan B., Carding, Simon R., Cardoso, Sandra M., Carew, Jennifer S., Carlin, Cathleen R., Carmignac, Virginie, Carneiro, Leticia A. M., Carra, Serena, Caruso, Rosario A., Casari, Giorgio, Casas, Caty, Castino, Roberta, Cebollero, Eduardo, Cecconi, Francesco, Celli, Jean, Chaachouay, Hassan, Chae, Han-Jung, Chai, Chee-Yin, Chan, David C., Chan, Edmond Y., Chang, Raymond Chuen-Chung, Che, Chi-Ming, Chen, Ching-Chow, Chen, Guang-Chao, Chen, Guo-Qiang, Chen, Min, Chen, Quan, Chen, Steve S.-L., Chen, Wenli, Chen, Xihui, Chen, Xiangmei, Chen, Xiequn, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Zhixiang, Cheng, Alan, Cheng, Christopher H. K., Cheng, Yan, Cheong, Heesun, Cheong, Jae-Ho, Cherry, Sara, Chess-Williams, Russ, Cheung, Zelda H., Chevet, Eric, Chiang, Hui-Ling, Chiarelli, Roberto, Chiba, Tomoki, Chin, Lih-Shen, Chiou, Shih-Hwa, Chisari, Francis V., Cho, Chi Hin, Cho, Dong-Hyung, Choi, Augustine M. K., Choi, Dooseok, Choi, Kyeong Sook, Choi, Mary E., Chouaib, Salem, Choubey, Divaker, Choubey, Vinay, Chu, Charleen T., Chuang, Tsung-Hsien, Chueh, Sheau-Huei, Chun, Taehoon, Chwae, Yong-Joon, Chye, Mee-Len, Ciarcia, Roberto, Ciriolo, Maria R., Clague, Michael J., Clark, Robert S. B., Clarke, Peter G. H., Clarke, Robert, Codogno, Patrice, Coller, Hilary A., Colombo, Maria I., Comincini, Sergio, Condello, Maria, Condorelli, Fabrizio, Cookson, Mark R., Coombs, Graham H., Coppens, Isabelle, Corbalan, Ramon, Cossart, Pascale, Costelli, Paola, Costes, Safia, Coto-Montes, Ana, Couve, Eduardo, Coxon, Fraser P., Cregg, James M., Crespo, Jose L., Cronje, Marianne J., Cuervo, Ana Maria, Cullen, Joseph J., Czaja, Mark J., D'Amelio, Marcello, Darfeuille-Michaud, Arlette, Davids, Lester M., Davies, Faith E., De Felici, Massimo, de Groot, John F., de Haan, Cornelis A. M., De Martino, Luisa, De Milito, Angelo, De Tata, Vincenzo, Debnath, Jayanta, Degterev, Alexei, Dehay, Benjamin, Delbridge, Lea M. D., Demarchi, Francesca, Deng, Yi Zhen, Dengjel, Jorn, Dent, Paul, Denton, Donna, Deretic, Vojo, Desai, Shyamal D., Devenish, Rodney J., Di Gioacchino, Mario, Di Paolo, Gilbert, Di Pietro, Chiara, Diaz-Araya, Guillermo, Diaz-Laviada, Ines, Diaz-Meco, Maria T., Diaz-Nido, Javier, Dikic, Ivan, Dinesh-Kumar, Savithramma P., Ding, Wen-Xing, Distelhorst, Clark W., Diwan, Abhinav, Djavaheri-Mergny, Mojgan, Dokudovskaya, Svetlana, Dong, Zheng, Dorsey, Frank C., Dosenko, Victor, Dowling, James J., Doxsey, Stephen, Dreux, Marlene, Drew, Mark E., Duan, Qiuhong, Duchosal, Michel A., Duff, Karen, Dugail, Isabelle, Durbeej, Madeleine, Duszenko, Michael, Edelstein, Charles L., Edinger, Aimee L., Egea, Gustavo, Eichinger, Ludwig, Eissa, N. 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W., Jones, Nicola L., Joseph, Bertrand, Joseph, Suresh K., Joubert, Annie M., Juhasz, Gabor, Juillerat-Jeanneret, Lucienne, Jung, Chang Hwa, Jung, Yong-Keun, Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kadowaki, Motoni, Kagedal, Katarina, Kamada, Yoshiaki, Kaminskyy, Vitaliy O., Kampinga, Harm H., Kanamori, Hiromitsu, Kang, Chanhee, Kang, Khong Bee, Kang, Kwang Il, Kang, Rui, Kang, Yoon-A., Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanno, Haruo, Kanthasamy, Anumantha G., Kanthasamy, Arthi, Karantza, Vassiliki, Kaushal, Gur P., Kaushik, Susmita, Kawazoe, Yoshinori, Ke, Po-Yuan, Kehrl, John H., Kelekar, Ameeta, Kerkhoff, Claus, Kessel, David H., Khalil, Hany, Kiel, Jan A. K. 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Javier, Olsen, Laura J., Olsson, Stefan, Opota, Onya, Osborne, Timothy F., Ostrander, Gary K., Otsu, Kinya, Ou, Jing-Hsiung James, Ouimet, Mireille, Overholtzer, Michael, Ozpolat, Bulent, Paganetti, Paolo, Pagnini, Ugo, Pallet, Nicolas, Palmer, Glen E., Palumbo, Camilla, Pan, Tianhong, Panaretakis, Theocharis, Pandey, Udai Bhan, Papackova, Zuzana, Papassideri, Issidora, Paris, Irmgard, Park, Junsoo, Park, Ohkmae K., Parys, Jan B., Parzych, Katherine R., Patschan, Susann, Patterson, Cam, Pattingre, Sophie, Pawelek, John M., Peng, Jianxin, Perlmutter, David H., Perrotta, Ida, Perry, George, Pervaiz, Shazib, Peter, Matthias, Peters, Godefridus J., Petersen, Morten, Petrovski, Goran, Phang, James M., Piacentini, Mauro, Pierre, Philippe, Pierrefite-Carle, Valerie, Pierron, Gerard, Pinkas-Kramarski, Ronit, Piras, Antonio, Piri, Natik, Platanias, Leonidas C., Poggeler, Stefanie, Poirot, Marc, Poletti, Angelo, Pous, Christian, Pozuelo-Rubio, Mercedes, Praetorius-Ibba, Mette, Prasad, Anil, Prescott, Mark, Priault, Muriel, Produit-Zengaffinen, Nathalie, Progulske-Fox, Ann, Proikas-Cezanne, Tassula, Przedborski, Serge, Przyklenk, Karin, Puertollano, Rosa, Puyal, Julien, Qian, Shu-Bing, Qin, Liang, Qin, Zheng-Hong, Quaggin, Susan E., Raben, Nina, Rabinowich, Hannah, Rabkin, Simon W., Rahman, Irfan, Rami, Abdelhaq, Ramm, Georg, Randall, Glenn, Randow, Felix, Rao, V. 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V., Scharl, Michael, Schatzl, Hermann M., Scheper, Wiep, Schiaffino, Stefano, Schneider, Claudio, Schneider, Marion E., Schneider-Stock, Regine, Schoenlein, Patricia V., Schorderet, Daniel F., Schuller, Christoph, Schwartz, Gary K., Scorrano, Luca, Sealy, Linda, Seglen, Per O., Segura-Aguilar, Juan, Seiliez, Iban, Seleverstov, Oleksandr, Sell, Christian, Seo, Jong Bok, Separovic, Duska, Setaluri, Vijayasaradhi, Setoguchi, Takao, Settembre, Carmine, Shacka, John J., Shanmugam, Mala, Shapiro, Irving M., Shaulian, Eitan, Shaw, Reuben J., Shelhamer, James H., Shen, Han-Ming, Shen, Wei-Chiang, Sheng, Zu-Hang, Shi, Yang, Shibuya, Kenichi, Shidoji, Yoshihiro, Shieh, Jeng-Jer, Shih, Chwen-Ming, Shimada, Yohta, Shimizu, Shigeomi, Shintani, Takahiro, Shirihai, Orian S., Shore, Gordon C., Sibirny, Andriy A., Sidhu, Stan B., Sikorska, Beata, Silva-Zacarin, Elaine C. M., Simmons, Alison, Simon, Annabella, Simon, Hans-Uwe, Simone, Cristiano, Simonsen, Anne, Sinclair, David A., Singh, Rajat, Sinha, Debasish, Sinicrope, Frank A., Sirko, Agnieszka, Siu, Parco M., Sivridis, Efthimios, Skop, Vojtech, Skulachev, Vladimir P., Slack, Ruth S., Smaili, Soraya S., Smith, Duncan R., Soengas, Maria S., Soldati, Thierry, Song, Xueqin, Sood, Anil K., Soong, Tuck Wah, Sotgia, Federica, Spector, Stephen A., Spies, Claudia D., Springer, Wolfdieter, Srinivasula, Srinivasa M., Stefanis, Leonidas, Steffan, Joan S., Stendel, Ruediger, Stenmark, Harald, Stephanou, Anastasis, Stern, Stephan T., Sternberg, Cinthya, Stork, Bjorn, Stralfors, Peter, Subauste, Carlos S., Sui, Xinbing, Sulzer, David, Sun, Jiaren, Sun, Shi-Yong, Sun, Zhi-Jun, Sung, Joseph J. 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Paul, Terada, Lance S., Terman, Alexei, Tettamanti, Gianluca, Thevissen, Karin, Thompson, Craig B., Thorburn, Andrew, Thumm, Michael, Tian, Fengfeng, Tian, Yuan, Tocchini-Valentini, Glauco, Tolkovsky, Aviva M., Tomino, Yasuhiko, Tonges, Lars, Tooze, Sharon A., Tournier, Cathy, Tower, John, Towns, Roberto, Trajkovic, Vladimir, Travassos, Leonardo H., Tsai, Ting-Fen, Tschan, Mario P., Tsubata, Takeshi, Tsung, Allan, Turk, Boris, Turner, Lorianne S., Tyagi, Suresh C., Uchiyama, Yasuo, Ueno, Takashi, Umekawa, Midori, Umemiya-Shirafuji, Rika, Unni, Vivek K., Vaccaro, Maria I., Valente, Enza Maria, Van den Berghe, Greet, van der Klei, Ida J., van Doorn, Wouter, van Dyk, Linda F., van Egmond, Marjolein, van Grunsven, Leo A., Vandenabeele, Peter, Vandenberghe, Wim P., Vanhorebeek, Ilse, Vaquero, Eva C., Velasco, Guillermo, Vellai, Tibor, Vicencio, Jose Miguel, Vierstra, Richard D., Vila, Miquel, Vindis, Cecile, Viola, Giampietro, Viscomi, Maria Teresa, Voitsekhovskaja, Olga V., von Haefen, Clarissa, Votruba, Marcela, Wada, Keiji, Wade-Martins, Richard, Walker, Cheryl L., Walsh, Craig M., Walter, Jochen, Wan, Xiang-Bo, Wang, Aimin, Wang, Chenguang, Wang, Dawei, Wang, Fan, Wang, Fen, Wang, Guanghui, Wang, Haichao, Wang, Hong-Gang, Wang, Horng-Dar, Wang, Jin, Wang, Ke, Wang, Mei, Wang, Richard C., Wang, Xinglong, Wang, Xuejun, Wang, Ying-Jan, Wang, Yipeng, Wang, Zhen, Wang, Zhigang Charles, Wang, Zhinong, Wansink, Derick G., Ward, Diane M., Watada, Hirotaka, Waters, Sarah L., Webster, Paul, Wei, Lixin, Weihl, Conrad C., Weiss, William A., Welford, Scott M., Wen, Long-Ping, Whitehouse, Caroline A., Whitton, J. 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K., Wyttenbach, Andreas, Xavier, Ramnik J., Xi, Zhijun, Xia, Pu, Xiao, Gengfu, Xie, Zhiping, Xie, Zhonglin, Xu, Da-Zhi, Xu, Jianzhen, Xu, Liang, Xu, Xiaolei, Yamamoto, Ai, Yamamoto, Akitsugu, Yamashina, Shunhei, Yamashita, Michiaki, Yan, Xianghua, Yanagida, Mitsuhiro, Yang, Dun-Sheng, Yang, Elizabeth, Yang, Jin-Ming, Yang, Shi Yu, Yang, Wannian, Yang, Wei Yuan, Yang, Zhifen, Yao, Meng-Chao, Yao, Tso-Pang, Yeganeh, Behzad, Yen, Wei-Lien, Yin, Jia-Jing, Yin, Xiao-Ming, Yoo, Ook-Joon, Yoon, Gyesoon, Yoon, Seung-Yong, Yorimitsu, Tomohiro, Yoshikawa, Yuko, Yoshimori, Tamotsu, Yoshimoto, Kohki, You, Ho Jin, Youle, Richard J., Younes, Anas, Yu, Li, Yu, Long, Yu, Seong-Woon, Yu, Wai Haung, Yuan, Zhi-Min, Yue, Zhenyu, Yun, Cheol-Heui, Yuzaki, Michisuke, Zabirnyk, Olga, Silva-Zacarin, Elaine, Zacks, David, Zacksenhaus, Eldad, Zaffaroni, Nadia, Zakeri, Zahra, Zeh, Herbert J. Rd, Zeitlin, Scott O., Zhang, Hong, Zhang, Hui-Ling, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Lin, Zhang, Long, Zhang, Ming-Yong, Zhang, Xu Dong, Zhao, Mantong, Zhao, Yi-Fang, Zhao, Ying, Zhao, Zhizhuang J., Zheng, Xiaoxiang, Zhivotovsky, Boris, Zhong, Qing, Zhou, Cong-Zhao, Zhu, Changlian, Zhu, Wei-Guo, Zhu, Xiao-Feng, Zhu, Xiongwei, Zhu, Yuangang, Zoladek, Teresa, Zong, Wei-Xing, Zorzano, Antonio, Zschocke, Jurgen, Zuckerbraun, Brian, Luxembourg Centre for Systems Biomedicine (LCSB): Clinical & Experimental Neuroscience (Krüger Group) [research center], Klionsky, Daniel J., Abdalla, Fabio C., Abeliovich, Hagai, Abraham, Robert T., Acevedo-Arozena, Abraham, Adeli, Khosrow, Agholme, Lotta, Agnello, Maria, Agostinis, Patrizia, Aguirre-Ghiso, Julio A., Ahn, Hyung Jun, Ait-Mohamed, Ouardia, Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akira, Shizuo, Al-Younes, Hesham M., Al-Zeer, Munir A., Albert, Matthew L., Albin, Roger L., Alegre-Abarrategui, Javier, Aleo, Maria Francesca, Alirezaei, Mehrdad, Almasan, Alexandru, Almonte-Becerril, Maylin, Amano, Atsuo, Amaravadi, Ravi, Amarnath, Shoba, Amer, Amal O., Andrieu-Abadie, Nathalie, Anantharam, Vellareddy, Ann, David K., Anoopkumar-Dukie, Shailendra, Aoki, Hiroshi, Apostolova, Nadezda, Arancia, Giuseppe, Aris, John P., Asanuma, Katsuhiko, Asare, Nana Y. O., Ashida, Hisashi, Askanas, Valerie, Askew, David S., Auberger, Patrick, Baba, Misuzu, Backues, Steven K., Baehrecke, Eric H., Bahr, Ben A., Bai, Xue-Yuan, Bailly, Yannick, Baiocchi, Robert, Baldini, Giulia, Balduini, Walter, Ballabio, Andrea, Bamber, Bruce A., Bampton, Edward T. W., Banhegyi, Gabor, Bartholomew, Clinton R., Bassham, Diane C., Bast, Robert C. Jr, Batoko, Henri, Bay, Boon-Huat, Beau, Isabelle, Bechet, Daniel M., Begley, Thomas J., Behl, Christian, Behrends, Christian, Bekri, Soumeya, Bellaire, Bryan, Bendall, Linda J., Benetti, Luca, Berliocchi, Laura, Bernardi, Henri, Bernassola, Francesca, Besteiro, Sebastien, Bhatia-Kissova, Ingrid, Bi, Xiaoning, Biard-Piechaczyk, Martine, Blum, Janice S., Boise, Lawrence H., Bonaldo, Paolo, Boone, David L., Bornhauser, Beat C., Bortoluci, Karina R., Bossis, Ioannis, Bost, Frederic, Bourquin, Jean-Pierre, Boya, Patricia, Boyer-Guittaut, Michael, Bozhkov, Peter V., Brady, Nathan R., Brancolini, Claudio, Brech, Andreas, Brenman, Jay E., Brennand, Ana, Bresnick, Emery H., Brest, Patrick, Bridges, Dave, Bristol, Molly L., Brookes, Paul S., Brown, Eric J., Brumell, John H., Brunetti-Pierri, Nicola, Brunk, Ulf T., Bulman, Dennis E., Bultman, Scott J., Bultynck, Geert, Burbulla, Lena F., Bursch, Wilfried, Butchar, Jonathan P., Buzgariu, Wanda, Bydlowski, Sergio P., Cadwell, Ken, Cahova, Monika, Cai, Dongsheng, Cai, Jiyang, Cai, Qian, Calabretta, Bruno, Calvo-Garrido, Javier, Camougrand, Nadine, Campanella, Michelangelo, Campos-Salinas, Jenny, Candi, Eleonora, Cao, Lizhi, Caplan, Allan B., Carding, Simon R., Cardoso, Sandra M., Carew, Jennifer S., Carlin, Cathleen R., Carmignac, Virginie, Carneiro, Leticia A. M., Carra, Serena, Caruso, Rosario A., Casari, Giorgio, Casas, Caty, Castino, Roberta, Cebollero, Eduardo, Cecconi, Francesco, Celli, Jean, Chaachouay, Hassan, Chae, Han-Jung, Chai, Chee-Yin, Chan, David C., Chan, Edmond Y., Chang, Raymond Chuen-Chung, Che, Chi-Ming, Chen, Ching-Chow, Chen, Guang-Chao, Chen, Guo-Qiang, Chen, Min, Chen, Quan, Chen, Steve S.-L., Chen, Wenli, Chen, Xihui, Chen, Xiangmei, Chen, Xiequn, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Zhixiang, Cheng, Alan, Cheng, Christopher H. K., Cheng, Yan, Cheong, Heesun, Cheong, Jae-Ho, Cherry, Sara, Chess-Williams, Russ, Cheung, Zelda H., Chevet, Eric, Chiang, Hui-Ling, Chiarelli, Roberto, Chiba, Tomoki, Chin, Lih-Shen, Chiou, Shih-Hwa, Chisari, Francis V., Cho, Chi Hin, Cho, Dong-Hyung, Choi, Augustine M. K., Choi, Dooseok, Choi, Kyeong Sook, Choi, Mary E., Chouaib, Salem, Choubey, Divaker, Choubey, Vinay, Chu, Charleen T., Chuang, Tsung-Hsien, Chueh, Sheau-Huei, Chun, Taehoon, Chwae, Yong-Joon, Chye, Mee-Len, Ciarcia, Roberto, Ciriolo, Maria R., Clague, Michael J., Clark, Robert S. B., Clarke, Peter G. H., Clarke, Robert, Codogno, Patrice, Coller, Hilary A., Colombo, Maria I., Comincini, Sergio, Condello, Maria, Condorelli, Fabrizio, Cookson, Mark R., Coombs, Graham H., Coppens, Isabelle, Corbalan, Ramon, Cossart, Pascale, Costelli, Paola, Costes, Safia, Coto-Montes, Ana, Couve, Eduardo, Coxon, Fraser P., Cregg, James M., Crespo, Jose L., Cronje, Marianne J., Cuervo, Ana Maria, Cullen, Joseph J., Czaja, Mark J., D'Amelio, Marcello, Darfeuille-Michaud, Arlette, Davids, Lester M., Davies, Faith E., De Felici, Massimo, de Groot, John F., de Haan, Cornelis A. M., De Martino, Luisa, De Milito, Angelo, De Tata, Vincenzo, Debnath, Jayanta, Degterev, Alexei, Dehay, Benjamin, Delbridge, Lea M. D., Demarchi, Francesca, Deng, Yi Zhen, Dengjel, Jorn, Dent, Paul, Denton, Donna, Deretic, Vojo, Desai, Shyamal D., Devenish, Rodney J., Di Gioacchino, Mario, Di Paolo, Gilbert, Di Pietro, Chiara, Diaz-Araya, Guillermo, Diaz-Laviada, Ines, Diaz-Meco, Maria T., Diaz-Nido, Javier, Dikic, Ivan, Dinesh-Kumar, Savithramma P., Ding, Wen-Xing, Distelhorst, Clark W., Diwan, Abhinav, Djavaheri-Mergny, Mojgan, Dokudovskaya, Svetlana, Dong, Zheng, Dorsey, Frank C., Dosenko, Victor, Dowling, James J., Doxsey, Stephen, Dreux, Marlene, Drew, Mark E., Duan, Qiuhong, Duchosal, Michel A., Duff, Karen, Dugail, Isabelle, Durbeej, Madeleine, Duszenko, Michael, Edelstein, Charles L., Edinger, Aimee L., Egea, Gustavo, Eichinger, Ludwig, Eissa, N. Tony, Ekmekcioglu, Suhendan, El-Deiry, Wafik S., Elazar, Zvulun, Elgendy, Mohamed, Ellerby, Lisa M., Eng, Kai Er, Engelbrecht, Anna-Mart, Engelender, Simone, Erenpreisa, Jekaterina, Escalante, Ricardo, Esclatine, Audrey, Eskelinen, Eeva-Liisa, Espert, Lucile, Espina, Virginia, Fan, Huizhou, Fan, Jia, Fan, Qi-Wen, Fan, Zhen, Fang, Shengyun, Fang, Yongqi, Fanto, Manolis, Fanzani, Alessandro, Farkas, Thomas, Farre, Jean-Claude, Faure, Mathias, Fechheimer, Marcus, Feng, Carl G., Feng, Jian, Feng, Qili, Feng, Youji, Fesus, Laszlo, Feuer, Ralph, Figueiredo-Pereira, Maria E., Fimia, Gian Maria, Fingar, Diane C., Finkbeiner, Steven, Finkel, Toren, Finley, Kim D., Fiorito, Filomena, Fisher, Edward A., Fisher, Paul B., Flajolet, Marc, Florez-McClure, Maria L., Florio, Salvatore, Fon, Edward A., Fornai, Francesco, Fortunato, Franco, Fotedar, Rati, Fowler, Daniel H., Fox, Howard S., Franco, Rodrigo, Frankel, Lisa B., Fransen, Marc, Fuentes, Jose M., Fueyo, Juan, Fujii, Jun, Fujisaki, Kozo, Fujita, Eriko, Fukuda, Mitsunori, Furukawa, Ruth H., Gaestel, Matthias, Gailly, Philippe, Gajewska, Malgorzata, Galliot, Brigitte, Galy, Vincent, Ganesh, Subramaniam, Ganetzky, Barry, Ganley, Ian G., Gao, Fen-Biao, Gao, George F., Gao, Jinming, Garcia, Lorena, Garcia-Manero, Guillermo, Garcia-Marcos, Mikel, Garmyn, Marjan, Gartel, Andrei L., Gatti, Evelina, Gautel, Mathias, Gawriluk, Thomas R., Gegg, Matthew E., Geng, Jiefei, Germain, Marc, Gestwicki, Jason E., Gewirtz, David A., Ghavami, Saeid, Ghosh, Pradipta, Giammarioli, Anna M., Giatromanolaki, Alexandra N., Gibson, Spencer B., Gilkerson, Robert W., Ginger, Michael L., Ginsberg, Henry N., Golab, Jakub, Goligorsky, Michael S., Golstein, Pierre, Gomez-Manzano, Candelaria, Goncu, Ebru, Gongora, Celine, Gonzalez, Claudio D., Gonzalez, Ramon, Gonzalez-Estevez, Cristina, Gonzalez-Polo, Rosa Ana, Gonzalez-Rey, Elena, Gorbunov, Nikolai V., Gorski, Sharon, Goruppi, Sandro, Gottlieb, Roberta A., Gozuacik, Devrim, Granato, Giovanna Elvira, Grant, Gary D., Green, Kim N., Gregorc, Ales, Gros, Frederic, Grose, Charles, Grunt, Thomas W., Gual, Philippe, Guan, Jun-Lin, Guan, Kun-Liang, Guichard, Sylvie M., Gukovskaya, Anna S., Gukovsky, Ilya, Gunst, Jan, Gustafsson, Asa B., Halayko, Andrew J., Hale, Amber N., Halonen, Sandra K., Hamasaki, Maho, Han, Feng, Han, Ting, Hancock, Michael K., Hansen, Malene, Harada, Hisashi, Harada, Masaru, Hardt, Stefan E., Harper, J. 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W., Jones, Nicola L., Joseph, Bertrand, Joseph, Suresh K., Joubert, Annie M., Juhasz, Gabor, Juillerat-Jeanneret, Lucienne, Jung, Chang Hwa, Jung, Yong-Keun, Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kadowaki, Motoni, Kagedal, Katarina, Kamada, Yoshiaki, Kaminskyy, Vitaliy O., Kampinga, Harm H., Kanamori, Hiromitsu, Kang, Chanhee, Kang, Khong Bee, Kang, Kwang Il, Kang, Rui, Kang, Yoon-A., Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanno, Haruo, Kanthasamy, Anumantha G., Kanthasamy, Arthi, Karantza, Vassiliki, Kaushal, Gur P., Kaushik, Susmita, Kawazoe, Yoshinori, Ke, Po-Yuan, Kehrl, John H., Kelekar, Ameeta, Kerkhoff, Claus, Kessel, David H., Khalil, Hany, Kiel, Jan A. K. W., Kiger, Amy A., Kihara, Akio, Kim, Deok Ryong, Kim, Do-Hyung, Kim, Dong-Hou, Kim, Eun-Kyoung, Kim, Hyung-Ryong, Kim, Jae-Sung, Kim, Jeong Hun, Kim, Jin Cheon, Kim, John K., Kim, Peter K., Kim, Seong Who, Kim, Yong-Sun, Kim, Yonghyun, Kimchi, Adi, Kimmelman, Alec C., King, Jason S., Kinsella, Timothy J., Kirkin, Vladimir, Kirshenbaum, Lorrie A., Kitamoto, Katsuhiko, Kitazato, Kaio, Klein, Ludger, Klimecki, Walter T., Klucken, Jochen, Knecht, Erwin, Ko, Ben C. B., Koch, Jan C., Koga, Hiroshi, Koh, Jae-Young, Koh, Young Ho, Koike, Masato, Komatsu, Masaaki, Kominami, Eiki, Kong, Hee Jeong, Kong, Wei-Jia, Korolchuk, Viktor I., Kotake, Yaichiro, Koukourakis, Michael I., Kouri Flores, Juan B., Kovacs, Attila L., Kraft, Claudine, Krainc, Dimitri, Kramer, Helmut, Kretz-Remy, Carole, Krichevsky, Anna M., Kroemer, Guido, Krüger, Rejko, Krut, Oleg, Ktistakis, Nicholas T., Kuan, Chia-Yi, Kucharczyk, Roza, Kumar, Ashok, Kumar, Raj, Kumar, Sharad, Kundu, Mondira, Kung, Hsing-Jien, Kurz, Tino, Kwon, Ho Jeong, La Spada, Albert R., Lafont, Frank, Lamark, Trond, Landry, Jacques, Lane, Jon D., Lapaquette, Pierre, Laporte, Jocelyn F., Laszlo, Lajos, Lavandero, Sergio, Lavoie, Josee N., Layfield, Robert, Lazo, Pedro A., Le, Weidong, Le Cam, Laurent, Ledbetter, Daniel J., Lee, Alvin J. X., Lee, Byung-Wan, Lee, Gyun Min, Lee, Jongdae, Lee, Ju-Hyun, Lee, Michael, Lee, Myung-Shik, Lee, Sug Hyung, Leeuwenburgh, Christiaan, Legembre, Patrick, Legouis, Renaud, Lehmann, Michael, Lei, Huan-Yao, Lei, Qun-Ying, Leib, David A., Leiro, Jose, Lemasters, John J., Lemoine, Antoinette, Lesniak, Maciej S., Lev, Dina, Levenson, Victor V., Levine, Beth, Levy, Efrat, Li, Faqiang, Li, Jun-Lin, Li, Lian, Li, Sheng, Li, Weijie, Li, Xue-Jun, Li, Yan-Bo, Li, Yi-Ping, Liang, Chengyu, Liang, Qiangrong, Liao, Yung-Feng, Liberski, Pawel P., Lieberman, Andrew, Lim, Hyunjung J., Lim, Kah-Leong, Lim, Kyu, Lin, Chiou-Feng, Lin, Fu-Cheng, Lin, Jian, Lin, Jiandie D., Lin, Kui, Lin, Wan-Wan, Lin, Weei-Chin, Lin, Yi-Ling, Linden, Rafael, Lingor, Paul, Lippincott-Schwartz, Jennifer, Lisanti, Michael P., Liton, Paloma B., Liu, Bo, Liu, Chun-Feng, Liu, Kaiyu, Liu, Leyuan, Liu, Qiong A., Liu, Wei, Liu, Young-Chau, Liu, Yule, Lockshin, Richard A., Lok, Chun-Nam, Lonial, Sagar, Loos, Benjamin, Lopez-Berestein, Gabriel, Lopez-Otin, Carlos, Lossi, Laura, Lotze, Michael T., Low, Peter, Lu, Binfeng, Lu, Bingwei, Lu, Bo, Lu, Zhen, Luciano, Frederic, Lukacs, Nicholas W., Lund, Anders H., Lynch-Day, Melinda A., Ma, Yong, Macian, Fernando, MacKeigan, Jeff P., Macleod, Kay F., Madeo, Frank, Maiuri, Luigi, Maiuri, Maria Chiara, Malagoli, Davide, Malicdan, May Christine V., Malorni, Walter, Man, Na, Mandelkow, Eva-Maria, Manon, Stephen, Manov, Irena, Mao, Kai, Mao, Xiang, Mao, Zixu, Marambaud, Philippe, Marazziti, Daniela, Marcel, Yves L., Marchbank, Katie, Marchetti, Piero, Marciniak, Stefan J., Marcondes, Mateus, Mardi, Mohsen, Marfe, Gabriella, Marino, Guillermo, Markaki, Maria, Marten, Mark R., Martin, Seamus J., Martinand-Mari, Camille, Martinet, Wim, Martinez-Vicente, Marta, Masini, Matilde, Matarrese, Paola, Matsuo, Saburo, Matteoni, Raffaele, Mayer, Andreas, Mazure, Nathalie M., McConkey, David J., McConnell, Melanie J., McDermott, Catherine, McDonald, Christine, McInerney, Gerald M., McKenna, Sharon L., McLaughlin, Bethann, McLean, Pamela J., McMaster, Christopher R., McQuibban, G. 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M., Simmons, Alison, Simon, Annabella, Simon, Hans-Uwe, Simone, Cristiano, Simonsen, Anne, Sinclair, David A., Singh, Rajat, Sinha, Debasish, Sinicrope, Frank A., Sirko, Agnieszka, Siu, Parco M., Sivridis, Efthimios, Skop, Vojtech, Skulachev, Vladimir P., Slack, Ruth S., Smaili, Soraya S., Smith, Duncan R., Soengas, Maria S., Soldati, Thierry, Song, Xueqin, Sood, Anil K., Soong, Tuck Wah, Sotgia, Federica, Spector, Stephen A., Spies, Claudia D., Springer, Wolfdieter, Srinivasula, Srinivasa M., Stefanis, Leonidas, Steffan, Joan S., Stendel, Ruediger, Stenmark, Harald, Stephanou, Anastasis, Stern, Stephan T., Sternberg, Cinthya, Stork, Bjorn, Stralfors, Peter, Subauste, Carlos S., Sui, Xinbing, Sulzer, David, Sun, Jiaren, Sun, Shi-Yong, Sun, Zhi-Jun, Sung, Joseph J. Y., Suzuki, Kuninori, Suzuki, Toshihiko, Swanson, Michele S., Swanton, Charles, Sweeney, Sean T., Sy, Lai-King, Szabadkai, Gyorgy, Tabas, Ira, Taegtmeyer, Heinrich, Tafani, Marco, Takacs-Vellai, Krisztina, Takano, Yoshitaka, Takegawa, Kaoru, Takemura, Genzou, Takeshita, Fumihiko, Talbot, Nicholas J., Tan, Kevin S. W., Tanaka, Keiji, Tanaka, Kozo, Tang, Daolin, Tang, Dingzhong, Tanida, Isei, Tannous, Bakhos A., Tavernarakis, Nektarios, Taylor, Graham S., Taylor, Gregory A., Taylor, J. Paul, Terada, Lance S., Terman, Alexei, Tettamanti, Gianluca, Thevissen, Karin, Thompson, Craig B., Thorburn, Andrew, Thumm, Michael, Tian, Fengfeng, Tian, Yuan, Tocchini-Valentini, Glauco, Tolkovsky, Aviva M., Tomino, Yasuhiko, Tonges, Lars, Tooze, Sharon A., Tournier, Cathy, Tower, John, Towns, Roberto, Trajkovic, Vladimir, Travassos, Leonardo H., Tsai, Ting-Fen, Tschan, Mario P., Tsubata, Takeshi, Tsung, Allan, Turk, Boris, Turner, Lorianne S., Tyagi, Suresh C., Uchiyama, Yasuo, Ueno, Takashi, Umekawa, Midori, Umemiya-Shirafuji, Rika, Unni, Vivek K., Vaccaro, Maria I., Valente, Enza Maria, Van den Berghe, Greet, van der Klei, Ida J., van Doorn, Wouter, van Dyk, Linda F., van Egmond, Marjolein, van Grunsven, Leo A., Vandenabeele, Peter, Vandenberghe, Wim P., Vanhorebeek, Ilse, Vaquero, Eva C., Velasco, Guillermo, Vellai, Tibor, Vicencio, Jose Miguel, Vierstra, Richard D., Vila, Miquel, Vindis, Cecile, Viola, Giampietro, Viscomi, Maria Teresa, Voitsekhovskaja, Olga V., von Haefen, Clarissa, Votruba, Marcela, Wada, Keiji, Wade-Martins, Richard, Walker, Cheryl L., Walsh, Craig M., Walter, Jochen, Wan, Xiang-Bo, Wang, Aimin, Wang, Chenguang, Wang, Dawei, Wang, Fan, Wang, Fen, Wang, Guanghui, Wang, Haichao, Wang, Hong-Gang, Wang, Horng-Dar, Wang, Jin, Wang, Ke, Wang, Mei, Wang, Richard C., Wang, Xinglong, Wang, Xuejun, Wang, Ying-Jan, Wang, Yipeng, Wang, Zhen, Wang, Zhigang Charles, Wang, Zhinong, Wansink, Derick G., Ward, Diane M., Watada, Hirotaka, Waters, Sarah L., Webster, Paul, Wei, Lixin, Weihl, Conrad C., Weiss, William A., Welford, Scott M., Wen, Long-Ping, Whitehouse, Caroline A., Whitton, J. Lindsay, Whitworth, Alexander J., Wileman, Tom, Wiley, John W., Wilkinson, Simon, Willbold, Dieter, Williams, Roger L., Williamson, Peter R., Wouters, Bradly G., Wu, Chenghan, Wu, Dao-Cheng, Wu, William K. K., Wyttenbach, Andreas, Xavier, Ramnik J., Xi, Zhijun, Xia, Pu, Xiao, Gengfu, Xie, Zhiping, Xie, Zhonglin, Xu, Da-Zhi, Xu, Jianzhen, Xu, Liang, Xu, Xiaolei, Yamamoto, Ai, Yamamoto, Akitsugu, Yamashina, Shunhei, Yamashita, Michiaki, Yan, Xianghua, Yanagida, Mitsuhiro, Yang, Dun-Sheng, Yang, Elizabeth, Yang, Jin-Ming, Yang, Shi Yu, Yang, Wannian, Yang, Wei Yuan, Yang, Zhifen, Yao, Meng-Chao, Yao, Tso-Pang, Yeganeh, Behzad, Yen, Wei-Lien, Yin, Jia-Jing, Yin, Xiao-Ming, Yoo, Ook-Joon, Yoon, Gyesoon, Yoon, Seung-Yong, Yorimitsu, Tomohiro, Yoshikawa, Yuko, Yoshimori, Tamotsu, Yoshimoto, Kohki, You, Ho Jin, Youle, Richard J., Younes, Anas, Yu, Li, Yu, Long, Yu, Seong-Woon, Yu, Wai Haung, Yuan, Zhi-Min, Yue, Zhenyu, Yun, Cheol-Heui, Yuzaki, Michisuke, Zabirnyk, Olga, Silva-Zacarin, Elaine, Zacks, David, Zacksenhaus, Eldad, Zaffaroni, Nadia, Zakeri, Zahra, Zeh, Herbert J. Rd, Zeitlin, Scott O., Zhang, Hong, Zhang, Hui-Ling, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Lin, Zhang, Long, Zhang, Ming-Yong, Zhang, Xu Dong, Zhao, Mantong, Zhao, Yi-Fang, Zhao, Ying, Zhao, Zhizhuang J., Zheng, Xiaoxiang, Zhivotovsky, Boris, Zhong, Qing, Zhou, Cong-Zhao, Zhu, Changlian, Zhu, Wei-Guo, Zhu, Xiao-Feng, Zhu, Xiongwei, Zhu, Yuangang, Zoladek, Teresa, Zong, Wei-Xing, Zorzano, Antonio, Zschocke, Jurgen, and Zuckerbraun, Brian
- Abstract
In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes. A key point that needs to be emphasized is that there is a difference between measurements that monitor the numbers or volume of autophagic elements (e.g., autophagosomes or autolysosomes) at any stage of the autophagic process vs. those that measure flux through the autophagy pathway (i.e., the complete process); thus, a block in macroautophagy that results in autophagosome accumulation needs to be differentiated from stimuli that result in increased autophagic activity, defined as increased autophagy induction coupled with increased delivery to, and degradation within, lysosomes (in most higher eukaryotes and some protists such as Dictyostelium) or the vacuole (in plants and fungi). In other words, it is especially important that investigators new to the field understand that the appearance of more autophagosomes does not necessarily equate with more autophagy. In fact, in many cases, autophagosomes accumulate because of a block in trafficking to lysosomes without a concomitant change in autophagosome biogenesis, whereas an increase in autolysosomes may reflect a reduction in degradative activity. Here, we present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused o
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- 2012
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21. THE RESULTS OF TREATMENT OF CONGENITAL DISLOCATION OF THE HIP IN INFANCY
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Bost, Frederic C., Hagey, Helen, Schottstaedt, Edwin R., and Larsen, Loren J.
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- 1948
22. COMPLETE MUSCLE TRANSPOSITION
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Schottstaedt, E. R., Larsen, Loren J., and Bost, Frederic C.
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- 1955
23. Experiences with Lengthening of the Femur over an Intramedullary Rod
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Bost, Frederic C. and Larsen, Loren J.
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- 1956
24. The Surgical Reconstruction of the Upper Extremity Paralyzed by Poliomyelitis
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SCHOTTSTAEDT, EDWIN R., LARSEN, LOREN J., and BOST, FREDERIC C.
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- 1958
25. Quo Vadis Orthopaedia Americana: Editorial
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BOST, FREDERIC C.
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- 1958
26. Plantar Dissection: An Operation to Release the Soft Tissues in Recurrent or Recalcitrant Talipes Equinovarus
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Bost, Frederic C., Schottstaedt, Edwin R., and Larsen, Loren J.
- Published
- 1960
27. THE EVALUATION OF CORTICAL AND CANCELLOUS BONE AS GRAFTING MATERIAL: A Clinical and Experimental Study
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ABBOTT, LEROY C., SCHOTTSTAEDT, EDWIN R., SAUNDERS, JOHN B. DE C. M., and BOST, FREDERIC C.
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- 1947
28. INJURIES TO THE LIGAMENTS OF THE KNEE JOINT
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Abbott, LeRoy C., Saunders, John B. deC. M., Bost, Frederic C., and Anderson, Carl E.
- Published
- 1944
29. THE PATHOLOGICAL CHANGES IN RECURRENT DISLOCATION OF THE SHOULDER: A Report of Bankartʼs Operative Procedure
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Bost, Frederic C. and Inman, Verne T.
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- 1942
30. ARTHRODESIS OF THE WRIST WITH THE USE OF GRAFTS OF CANCELLOUS BONE
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Abbott, Leroy C., Saunders, John B. Dec. M., and Bost, Frederic C.
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- 1942
31. Perthes Lesion (A Variant of the Bankart Lesion)
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Wischer, Thorsten K., primary, Bredella, Miriam A., additional, Genant, Harry K., additional, Stoller, David W., additional, Bost, Frederic W., additional, and Tirman, Phillip F. J., additional
- Published
- 2002
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- View/download PDF
32. Inter-alpha-trypsin inhibitor proteoglycan family. A group of proteins binding and stabilizing the extracellular matrix
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Bost, Frederic, primary, Diarra-Mehrpour, Maryam, additional, and Martin, Jean-Pierre, additional
- Published
- 1998
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33. A PRACTICAL APPROACH TO IMAGING OF THE SHOULDER WITH EMPHASIS ON MR IMAGING
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Tirman, Phillip F.J., primary, Steinbach, Lynne S., additional, Belzer, John P., additional, and Bost, Frederic W., additional
- Published
- 1997
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34. Frequency and prognostic evaluation of 3p21-22 allelic losses in non-small-cell lung cancer
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Thiberville, Luc, primary, Bourguignon, Jeannette, additional, Metayer, Josette, additional, Bost, Frederic, additional, Diarra-Mehrpour, Maryam, additional, Bignon, Jean, additional, Lam, Stephen, additional, Martin, Jean-Pierre, additional, and Nouvet, Georges, additional
- Published
- 1995
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35. Isolation and characterization of the human inter-alpha-trypsin inhibitor heavy-chain H1 gene
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BOST, Frederic, primary, BOURGUIGNON, Jeannette, additional, MARTIN, Jean-Pierre, additional, SESBOUE, Richard, additional, THIBERVILLE, Luc, additional, and DIARRA-MEHRPOUR, Maryam, additional
- Published
- 1993
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36. YAP1 modulation of primary cilia‐mediated ciliogenesis in 2D and 3D prostate cancer models.
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Guo, Yingbo, Dupart, Mathilde, Irondelle, Marie, Peraldi, Pascal, Bost, Frederic, and Mazure, Nathalie M.
- Subjects
- *
GENETIC models , *CILIA & ciliary motion , *PROSTATE cancer , *CELL lines , *PROSTATE - Abstract
The primary cilium, a non‐motile organelle present in most human cells, plays a crucial role in detecting microenvironmental changes and regulating intracellular signaling. Its dysfunction is linked to various diseases, including cancer. We explored the role of ciliated cells in prostate cancer by using Gefitinib and Jasplakinolide compounds to induce ciliated cells in both normal and tumor‐like prostate cell lines. We assessed GLI1 and IFT20 expression and investigated YAP1 protein's role, which is implicated in primary cilium regulation. Finally, we examined these compounds in 3D cell models, aiming to simulate in vivo conditions. Our study highlights YAP1 as a potential target for novel genetic models to understand the primary cilium's role in mediating resistance to anticancer treatments. [ABSTRACT FROM AUTHOR]
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- 2024
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37. Pediatrics—Epitomes of Progress: Treatment of Metatarsus Adductus in Infants
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Bost, Frederic W.
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Important Advances in Clinical Medicine - Published
- 1982
38. The Importance of the Emergency Treatment of Compound Fractures*
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Bost, Frederic C.
- Subjects
Original Articles - Published
- 1938
39. Multiple congenital dislocations associated with characteristics facial abnormality
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Larsen, Loren J., primary, Schottstaedt, Edwin R., additional, and Bost, Frederic C., additional
- Published
- 1950
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40. Plantar Dissection
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Bost, Frederic C., primary, Schottstaedt, Edwin R., additional, and Larsen, Loren J., additional
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- 1960
- Full Text
- View/download PDF
41. ROLE OF THE ORTHOPEDIC SURGEON IN TREATMENT OF CEREBRAL PALSY
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Bost, Frederic C., primary
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- 1956
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42. ROLE OF THE ORTHOPEDIC SURGEON IN TREATMENT OF CEREBRAL PALSY
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Bost, Frederic C., Ashley, R. Kirklin, and Kelley, Warren J.
- Abstract
• Integration of the services of specialists in the professions of medicine, education, and sociology has resulted in greatly improved care for the patient suffering from cerebral palsy. Within the medical team there must also be a balance among the specialties represented. Proper use must be made of exercise and training, of restraint and support by braces, and of surgical operations.Analysis of several hundred operations on such patients showed that well-planned surgery contributed to the correction of deformities and to the improvement of muscle function and skill. One qualified person should be responsible for the integration of the efforts of the members of the team, in which both the physiatrist and the orthopedic surgeon are qualified to make important contributions.
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- 1956
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43. The Effect of Spine Fusion on Respiratory Function in Duchenne Muscular Dystrophy.
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Miller, Robert G., Filler-Katz, Amy, Dao, Hung, Keroes, Amanda, Chalmers, Antonia, Holman, David, and Bost, Frederic
- Published
- 1989
44. The metabolic modulator PGC-1α in cancer.
- Author
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Bost F and Kaminski L
- Abstract
The peroxisome proliferator-activated receptor gamma coactivator 1 alpha (PGC-1α) is a central modulator of cell metabolism. It regulates mitochondrial biogenesis and oxidative metabolism. Modifications and adaptations in cellular metabolism are hallmarks of cancer cells, thus, it is not surprising that PGC-1α plays a role in cancer. Several recent articles have shown that PGC-1α expression is altered in tumors and metastasis in relation to modifications in cellular metabolism. The potential uses of PGC-1α as a therapeutic target and a biomarker of the advanced form of cancer will be summarized in this review., Competing Interests: None.
- Published
- 2019
45. The energy disruptor metformin targets mitochondrial integrity via modification of calcium flux in cancer cells.
- Author
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Loubiere C, Clavel S, Gilleron J, Harisseh R, Fauconnier J, Ben-Sahra I, Kaminski L, Laurent K, Herkenne S, Lacas-Gervais S, Ambrosetti D, Alcor D, Rocchi S, Cormont M, Michiels JF, Mari B, Mazure NM, Scorrano L, Lacampagne A, Gharib A, Tanti JF, and Bost F
- Subjects
- Animals, Cell Line, Tumor, Endoplasmic Reticulum drug effects, Endoplasmic Reticulum metabolism, Endoplasmic Reticulum Stress drug effects, Humans, Mice, Mitochondria drug effects, Mitochondria ultrastructure, Mitochondrial Membrane Transport Proteins metabolism, Mitochondrial Permeability Transition Pore, Mitochondrial Swelling drug effects, Models, Biological, Organelle Biogenesis, Calcium metabolism, Energy Metabolism drug effects, Metformin pharmacology, Mitochondria metabolism
- Abstract
Mitochondrial integrity is critical for the regulation of cellular energy and apoptosis. Metformin is an energy disruptor targeting complex I of the respiratory chain. We demonstrate that metformin induces endoplasmic reticulum (ER) stress, calcium release from the ER and subsequent uptake of calcium into the mitochondria, thus leading to mitochondrial swelling. Metformin triggers the disorganization of the cristae and inner mitochondrial membrane in several cancer cells and tumors. Mechanistically, these alterations were found to be due to calcium entry into the mitochondria, because the swelling induced by metformin was reversed by the inhibition of mitochondrial calcium uniporter (MCU). We also demonstrated that metformin inhibits the opening of mPTP and induces mitochondrial biogenesis. Altogether, the inhibition of mPTP and the increase in mitochondrial biogenesis may account for the poor pro-apoptotic effect of metformin in cancer cells.
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- 2017
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46. Informatics for neglected diseases collaborations.
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Bost F, Jacobs RT, and Kowalczyk P
- Subjects
- Computer Communication Networks, Database Management Systems, Humans, International Cooperation, Internationality, Internet, Public-Private Sector Partnerships organization & administration, Software, Communicable Diseases drug therapy, Cooperative Behavior, Drug Discovery methods, Medical Informatics methods, Tropical Medicine instrumentation, Tropical Medicine methods
- Abstract
Many different public and private organizations from across the globe are collaborating on neglected diseases drug-discovery and development projects with the aim of identifying a cure for tropical infectious diseases. These neglected diseases collaborations require a global, secure, multi-organization data-management solution, combined with a platform that facilitates communication and supports collaborative work. This review discusses the solutions offered by 'Software as a Service' (SaaS) web-based platforms, despite notable challenges, and the evolution of these platforms required to foster efficient virtual research efforts by geographically dispersed scientists.
- Published
- 2010
47. Perthes lesion (a variant of the Bankart lesion): MR imaging and MR arthrographic findings with surgical correlation.
- Author
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Wischer TK, Bredella MA, Genant HK, Stoller DW, Bost FW, and Tirman PF
- Subjects
- Adolescent, Adult, Arthroscopy, Female, Humans, Male, Middle Aged, Periosteum pathology, Periosteum surgery, Scapula pathology, Scapula surgery, Sensitivity and Specificity, Shoulder Dislocation diagnosis, Shoulder Dislocation pathology, Shoulder Dislocation surgery, Shoulder Joint pathology, Shoulder Joint surgery, Arthrography, Magnetic Resonance Imaging, Periosteum injuries, Scapula injuries, Shoulder Injuries
- Abstract
Objective: The aim of this study was to evaluate the use of MR imaging in the characterization of the Perthes lesion by correlating MR findings with findings at arthroscopy., Conclusion: The use of a combination of axial and abduction-external rotation position sequences on MR images can be helpful in the diagnosis of a Perthes lesion. A fluid-filled joint with capsular distension, caused by either a large amount of effusion or MR arthrography, was found to be helpful in outlining Perthes lesions. Adding the abduction-external rotation position to the protocol in patients in whom Perthes lesion is suspected will increase diagnostic accuracy and may reveal a Perthes lesion not visible on axial images, as was the case in 50% of the patients in our series.
- Published
- 2002
- Full Text
- View/download PDF
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