Search

Your search keyword '"Romain Baer"' showing total 14 results
Start Over Author "Romain Baer"
14 results on '"Romain Baer"'

1. Pancreatic cancer intrinsic PI3Kα activity accelerates metastasis and rewires macrophage component

Author

Benoit Thibault, Fernanda Ramos‐Delgado, Elvire Pons‐Tostivint, Nicole Therville, Celia Cintas, Silvia Arcucci, Stephanie Cassant‐Sourdy, Gabriela Reyes‐Castellanos, Marie Tosolini, Amelie V Villard, Coralie Cayron, Romain Baer, Justine Bertrand‐Michel, Delphine Pagan, Dina Ferreira Da Mota, Hongkai Yan, Chiara Falcomatà, Fabrice Muscari, Barbara Bournet, Jean‐Pierre Delord, Ezra Aksoy, Alice Carrier, Pierre Cordelier, Dieter Saur, Celine Basset, and Julie Guillermet‐Guibert

Subjects
pancreatic cancer, phosphoinositide, PI3K isoforms, targeted therapy, tumour‐stroma dialog, Medicine (General), R5-920, Genetics, QH426-470
Abstract

Abstract Pancreatic ductal adenocarcinoma (PDAC) patients frequently suffer from undetected micro‐metastatic disease. This clinical situation would greatly benefit from additional investigation. Therefore, we set out to identify key signalling events that drive metastatic evolution from the pancreas. We searched for a gene signature that discriminate localised PDAC from confirmed metastatic PDAC and devised a preclinical protocol using circulating cell‐free DNA (cfDNA) as an early biomarker of micro‐metastatic disease to validate the identification of key signalling events. An unbiased approach identified, amongst actionable markers of disease progression, the PI3K pathway and a distinctive PI3Kα activation signature as predictive of PDAC aggressiveness and prognosis. Pharmacological or tumour‐restricted genetic PI3Kα‐selective inhibition prevented macro‐metastatic evolution by hindering tumoural cell migratory behaviour independently of genetic alterations. We found that PI3Kα inhibition altered the quantity and the species composition of the produced lipid second messenger PIP3, with a selective decrease of C36:2 PI‐3,4,5‐P3. Tumoural PI3Kα inactivation prevented the accumulation of pro‐tumoural CD206‐positive macrophages in the tumour‐adjacent tissue. Tumour cell‐intrinsic PI3Kα promotes pro‐metastatic features that could be pharmacologically targeted to delay macro‐metastatic evolution.

Published
2021
Full Text
View/download PDF

2. Retail CBDC purposes and risk transfers to the central bank

Author

Romain Baeriswyl, Samuel Reynard, and Alexandre Swoboda

Subjects
Central bank digital currency (CBDC), Fractional-reserve banking, Gresham’s law, Medium of exchange, Statistics, HA1-4737, Economics as a science, HB71-74
Abstract

Abstract The issuance of retail central bank digital currency (CBDC) involves a transfer of risk from commercial banks to the central bank. Mechanisms that limit the transfer of risk, such as an unattractive interest rate, a quantity ceiling or the non-convertibility of cash and reserves into CBDC, are likely to discourage the use of CBDC as a medium of exchange and thus defeat the purpose of issuing CBDC.

Published
2024
Full Text
View/download PDF

3. eIF4A inhibition circumvents uncontrolled DNA replication mediated by 4E-BP1 loss in pancreatic cancer

Author

Romain Baer, Laia Masvidal-Sanz, Sauyeun Shin, Julie Guillermet-Guibert, Manon Strehaiano, Yoshinori Tsukumo, Corinne Bousquet, Nahum Sonenberg, Ola Larsson, Stéphane Pyronnet, Nicolas Guilbaud, Yvan Martineau, Jean-Sébastien Hoffmann, Théo Goullet de Rugy, Frédéric Marion, David Müller, Christine Jean, and Rémi Samain

Subjects
DNA Replication, 0301 basic medicine, DNA damage, DNA repair, Cell Cycle Proteins, Mice, 03 medical and health sciences, 0302 clinical medicine, Cell Line, Tumor, Protein biosynthesis, Animals, Humans, PI3K/AKT/mTOR pathway, Adaptor Proteins, Signal Transducing, Acinar cell proliferation, Messenger RNA, Chemistry, TOR Serine-Threonine Kinases, DNA replication, Translation (biology), General Medicine, Pancreatic Neoplasms, 030104 developmental biology, Protein Biosynthesis, 030220 oncology & carcinogenesis, Eukaryotic Initiation Factor-4A, Cancer research, Research Article, Carcinoma, Pancreatic Ductal
Abstract

Pancreatic ductal adenocarcinoma (PDAC) relies on hyperactivated protein synthesis. Consistently, human and mouse PDAC lose expression of the translational repressor and mTOR target 4E-BP1. Using genome-wide polysome profiling, we here explore mRNAs whose translational efficiencies depend on the mTOR/4E-BP1 axis in pancreatic cancer cells. We identified a functional enrichment for mRNAs encoding DNA replication and repair proteins, including RRM2 and CDC6. Consequently, 4E-BP1 depletion favors DNA repair and renders DNA replication insensitive to mTOR inhibitors, in correlation with a sustained protein expression of CDC6 and RRM2, which is inversely correlated with 4E-BP1 expression in PDAC patient samples. DNA damage and pancreatic lesions induced by an experimental pancreatitis model uncover that 4E-BP1/2-deleted mice display an increased acinar cell proliferation and a better recovery than WT animals. Targeting translation, independently of 4E-BP1 status, using eIF4A RNA helicase inhibitors (silvestrol derivatives) selectively modulates translation and limits CDC6 expression and DNA replication, leading to reduced PDAC tumor growth. In summary, 4E-BP1 expression loss during PDAC development induces selective changes in translation of mRNA encoding DNA replication and repair protein. Importantly, targeting protein synthesis by eIF4A inhibitors circumvents PDAC resistance to mTOR inhibition.

Published
2019
Full Text
View/download PDF

4. Abstract B19: New tools to study the role of RAS/CRAF interaction in RAS-driven lung cancer

Author

Miriam Molina-Arcas, David C. Hancock, Julian Downward, Ian Rosewell, and Romain Baer

Subjects
MAPK/ERK pathway, Cancer Research, Mutation, Cell growth, Kinase, Effector, Cancer, Biology, medicine.disease, medicine.disease_cause, Oncology, medicine, Cancer research, Lung cancer, Molecular Biology, Binding domain
Abstract

The RAF/MAPK pathway is a major RAS effector pathway implicated in RAS oncogenic properties, regulating a diversity of cellular processes. As RAF kinases (A-, B-, CRAF) are thought to be attractive therapeutic targets for RAS-driven cancers, pan-RAF inhibitors are currently under development. However, preclinical studies focusing on targeting only the CRAF kinase by genetic inactivation revealed effective inhibition of tumor development without inducing significant systemic toxicities in a model of KRAS-driven lung tumor initiation. Recently, Sanclemente et al. further demonstrated that the complete ablation of CRAF in established advanced lung tumors (KrasG12V/Trp53) triggers sustainable tumor regression. Although this approach validates CRAF as a powerful therapeutic target for KRAS-driven lung cancer, specific CRAF inhibitors are not available yet. It was described more than 20 years ago that RAS GTPases strongly interact with CRAF kinase through its Ras Binding domain. This interaction is required to activate CRAF. Many efforts are being made to try to disrupt this interaction with small compounds, but currently none of those drugs are potent enough for further testing in vivo. Surprisingly, this therapeutic approach has never been proven to be efficient in vivo. Using CRISPR/Cas9 technology, we engineered a new mouse model in which the Ras binding domain of CRAF is constitutively mutated to completely abolish its interaction with RAS GTPases (CRAFR89L). We also engineered two murine lung cancer cell lines (KrasG12D/Trp53) that are heterozygous for this mutation (CRAFR89L/KO). Preliminary data confirm that CRAF interaction with RAS is minimally involved in 2D cell proliferation, as well as KRAS-driven MAPK pathway activation, but important for anchorage-independent cell growth. Citation Format: Romain Baer, Ian Rosewell, David Hancock, Miriam Molina-Arcas, Julian Downward. New tools to study the role of RAS/CRAF interaction in RAS-driven lung cancer [abstract]. In: Proceedings of the AACR Special Conference on Targeting RAS-Driven Cancers; 2018 Dec 9-12; San Diego, CA. Philadelphia (PA): AACR; Mol Cancer Res 2020;18(5_Suppl):Abstract nr B19.

Published
2020
Full Text
View/download PDF

5. Pancreatic preneoplastic lesions plasma signatures and biomarkers based on proteome profiling of mouse models

Author

Jérémy Nigri, Richard Tomasini, Frédéric Lopez, Frédéric Pont, Talal Al Saati, Aïcha El-Mrani, Pierre Cordelier, Julie Guillermet-Guibert, Véronique Gigoux, Marlène Dufresne, Laetitia Ligat, Romain Baer, Nathalie Saint-Laurent, Sébastien Déjean, Surfaces Cellulaires et Signalisation chez les Végétaux (SCSV), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Institut de médecine moléculaire de Rangueil (I2MR), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Biologie et Pathologie Digestive, Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR 31 Louis Bugnard (IFR 31), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Service d'anatomie et cytologie pathologiques [Purpan], Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Hôpital Purpan [Toulouse], CHU Toulouse [Toulouse], Centre de Recherche en Cancérologie de Marseille (CRCM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), Institut de Mathématiques de Toulouse UMR5219 (IMT), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse 1 Capitole (UT1)-Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Centre de Recherches en Cancérologie de Toulouse (CRCT), 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), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT)-Université de Toulouse (UT)- Institut Fédératif de Recherche Bio-médicale Institution (IFR150)-Institut National de la Santé et de la Recherche Médicale (INSERM), IFR 31 Louis Bugnard (IFR 31), 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)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), 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)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service Anatomie et cytologie pathologiques [CHU Toulouse], Pôle Biologie [CHU Toulouse], Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse), Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Toulouse Capitole (UT Capitole), Université de Toulouse (UT)-Université de Toulouse (UT)-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 Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), 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), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Toulouse [Toulouse]-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-Université Toulouse 1 Capitole (UT1), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)

Subjects
Cancer Research, Pathology, medicine.medical_specialty, Proteome, endocrine system diseases, Colorectal cancer, pancreatic cancer, Protein Array Analysis, Pancreatic Intraepithelial Neoplasia, Mice, 03 medical and health sciences, Prostate cancer, proteomics, 0302 clinical medicine, [MATH.MATH-ST]Mathematics [math]/Statistics [math.ST], Biomarkers, Tumor, Animals, Medicine, Molecular Diagnostics, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, business.industry, Carcinoma in situ, ITIH, complement C3, medicine.disease, genetically engineered mouse model, Neoplasm Proteins, 3. Good health, Pancreatic Neoplasms, Disease Models, Animal, medicine.anatomical_structure, Oncology, 030220 oncology & carcinogenesis, Cancer cell, biomarker, PanIN, Peptides, business, Pancreas, Liver cancer, Precancerous Conditions, Carcinoma in Situ, alpha-2-macroglobulin, Carcinoma, Pancreatic Ductal
Abstract

Background: Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal malignancies with a mortality that is almost identical to incidence. Because early detected PDAC is potentially curable, blood-based biomarkers that could detect currently developing neoplasia would improve patient survival and management. PDAC develops from pancreatic intraepithelial neoplasia (PanIN) lesions, graded from low grade (PanIN1) to high grade (PanIN3). We made the hypothesis that specific proteomic signatures from each precancerous stage exist and are detectable in plasma. Methods: We explored the peptide profiles of microdissected PanIN cells and of plasma samples corresponding to the different PanIN grade from genetically engineered mouse models of PDAC using capillary electrophoresis coupled to mass spectrometry (CE-MS) and Chip-MS/MS. Results: We successfully characterised differential peptides profiles from PanIN microdissected cells. We found that plasma from tumor-bearing mice and age-matched controls exhibit discriminative peptide signatures. We also determined plasma peptide signatures corresponding to low- and high-grade precancerous step present in the mice pancreas using the two mass spectrometry technologies. Importantly, we identified biomarkers specific of PanIN3. Conclusions: We demonstrate that benign and advanced PanIN lesions display distinct plasma peptide patterns. This strongly supports the perspectives of developing a non-invasive screening test for prediction and early detection of PDAC.

Published
2015
Full Text
View/download PDF

6. Pancreatic cell plasticity and cancer initiation induced by oncogenic Kras is completely dependent on wild-type PI 3-kinase p110α

Author

Romain Baer, Stéphane Pyronnet, Bettina Couderc, Julie Guillermet-Guibert, Stéphanie Cassant-Sourdy, Nina Schönhuber, Laetitia Planque, Bart Vanhaesebroeck, Marlène Dufresne, Hubert Lulka, Barbara Garmy-Susini, Dieter Saur, Célia Cintas, and Corinne Bousquet

Subjects
Biology, P110α, medicine.disease_cause, Cell morphology, Animals, Genetically Modified, Proto-Oncogene Proteins p21(ras), Mice, Genetics, medicine, Animals, Humans, Gene Silencing, PI3K/AKT/mTOR pathway, Cell Proliferation, Transdifferentiation, Epithelial Cells, Actin cytoskeleton, digestive system diseases, Class Ia Phosphatidylinositol 3-Kinase, Pancreatic Neoplasms, medicine.anatomical_structure, Mutation, Cancer research, KRAS, Carcinogenesis, Pancreas, Carcinoma, Pancreatic Ductal, Signal Transduction, Research Paper, Developmental Biology
Abstract

Increased PI 3-kinase (PI3K) signaling in pancreatic ductal adenocarcinoma (PDAC) correlates with poor prognosis, but the role of class I PI3K isoforms during its induction remains unclear. Using genetically engineered mice and pharmacological isoform-selective inhibitors, we found that the p110α PI3K isoform is a major signaling enzyme for PDAC development induced by a combination of genetic and nongenetic factors. Inactivation of this single isoform blocked the irreversible transition of exocrine acinar cells into pancreatic preneoplastic ductal lesions by oncogenic Kras and/or pancreatic injury. Hitting the other ubiquitous isoform, p110β, did not prevent preneoplastic lesion initiation. p110α signaling through small GTPase Rho and actin cytoskeleton controls the reprogramming of acinar cells and regulates cell morphology in vivo and in vitro. Finally, p110α was necessary for pancreatic ductal cancers to arise from Kras-induced preneoplastic lesions by increasing epithelial cell proliferation in the context of mutated p53. Here we identify an in vivo context in which p110α cellular output differs depending on the epithelial transformation stage and demonstrate that the PI3K p110α is required for PDAC induced by oncogenic Kras, the key driver mutation of PDAC. These data are critical for a better understanding of the development of this lethal disease that is currently without efficient treatment.

Published
2014
Full Text
View/download PDF

7. Sequential or concomitant application of PI3K isoform signal targeted therapies enhances cell death by preventing their cross-redundancy in pancreatic ductal adenocarcinoma

Author

Thibaut Douché, Dantes Zahra, Barbara Garmy-Susini, Julie Guillermet-Guibert, Nicole Therville, Célia Cintas, Céline Basset, Max Reichert, and Romain Baer

Subjects
Oncology, Gene isoform, medicine.medical_specialty, Programmed cell death, Pancreatic ductal adenocarcinoma, Hepatology, business.industry, Endocrinology, Diabetes and Metabolism, Gastroenterology, Concomitant, Internal medicine, medicine, Redundancy (engineering), business, PI3K/AKT/mTOR pathway
Published
2017
Full Text
View/download PDF

8. Implication of PI3K/Akt pathway in pancreatic cancer: When PI3K isoforms matter?

Author

Julie Guillermet-Guibert, Romain Baer, Célia Cintas, and Nicole Therville

Subjects
Cancer Research, Cancer, Biology, Bioinformatics, medicine.disease, Malignancy, medicine.disease_cause, Hedgehog signaling pathway, Clinical trial, Pancreatic Neoplasms, Phosphatidylinositol 3-Kinases, Pancreatic cancer, Immunology, Genetics, medicine, Molecular Medicine, Adenocarcinoma, Animals, Humans, Protein Isoforms, Carcinogenesis, Molecular Biology, Proto-Oncogene Proteins c-akt, PI3K/AKT/mTOR pathway, Signal Transduction
Abstract

Pancreatic cancer belongs to the incurable family of solid cancers. Despite of a recent better understanding its molecular biology, and an increased number of clinical trials, there is still a lack for innovative targeted therapies to fight this deadly malignancy. PI3K/Akt signalling is one of the most commonly deregulated signalling pathways in cancer, which explains the massive attention from many pharmaceutical companies over the ten past years on these signalling molecules. The already developed small molecule inhibitors are currently under clinical trial in various cancer types. Class I PI3Ks have 4 isoforms for which the role in physiology starts to be well described in the literature. Data are more unclear for their differential involvement in oncogenesis. In this review, we will discuss about the cognitive and therapeutic potential of targeting this signalling pathway and in particular Class I PI3K isoforms for pancreatic cancer treatment. Isoform-specificity of PI3K inhibitors are currently designed to achieve the same goal as pan-PI3K inhibitors but without potential adverse effects. We will discuss if such strategy is relevant in pancreatic adenocarcinoma.

Published
2015

9. The phosphoinositide-3-kinase PI3Kalpha inhibition protects from exocrine pancreatic cell susceptibility to cancer in chronic pancreatitis

Author

Céline Basset, Célia Cintas, Marlène Dufresne, Julie Guillermet-Guibert, Anne Couvelard, Romain Baer, and Nicole Therville

Subjects
Phosphoinositide 3-kinase, Hepatology, biology, business.industry, Endocrinology, Diabetes and Metabolism, Cell, Gastroenterology, Cancer, medicine.disease, medicine.anatomical_structure, medicine, biology.protein, Cancer research, Pancreatitis, business
Published
2017
Full Text
View/download PDF

10. Loss of 4E-BP1-mediated translational control favors DNA replication in pancreatic cancer

Author

Yoshinori Tsukumo, Sauyeun Shin, David Müller, Stéphanie Cassant-Sourdy, Laia Masvidal-Sanz, Romain Baer, Julie Guillermet-Guibert, Théo Goullet de Rugy, Yvan Martineau, Ola Larsson, Stéphane Pyronnet, Christine Jean, Fanny Grimal, Nahum Sonenberg, Rémi Saamin, Corinne Bousquet, Jean-Sébastien Hoffmann, and Hervé Avet-Loiseau

Subjects
Genetics, Hepatology, business.industry, Endocrinology, Diabetes and Metabolism, Pancreatic cancer, Gastroenterology, medicine, DNA replication, Cancer research, medicine.disease, business
Published
2017
Full Text
View/download PDF

11. The non-mutated PI3Kalpha is a master signaling enzyme for pancreatic cancerogenesis

Author

Barbara Garmy-Susini, Stéphanie Cassant-Sourdy, Bart Vanhaesebroeck, Stéphane Pyronnet, Célia Cintas, Marlène Dufresne, Hubert Lulka, Julie Guillermet-Guibert, Nina Schönhuber, Laetitia Planque, Mounira Chalabi, Romain Baer, Corinne Bousquet, and Dieter Saur

Subjects
chemistry.chemical_classification, Enzyme, Hepatology, chemistry, business.industry, Endocrinology, Diabetes and Metabolism, Gastroenterology, Cancer research, Medicine, business
Published
2014
Full Text
View/download PDF

12. Translational regulation of exocrine cell function and survival by ATF4-dependent expression of 4E-BP1

Author

Stéphane Pyronnet, Yvan Martineau, Daniel DiRenzo, David Müller, Romain Baer, Charline Lasfargues, Julie Guillermet-Guibert, Stephen F. Konieczny, Nahum Sonenberg, Arkady Khoutorsky, David A. Hess, and Corinne Bousquet

Subjects
Hepatology, Expression (architecture), business.industry, Endocrinology, Diabetes and Metabolism, Exocrine cell, Translational regulation, ATF4, Gastroenterology, Medicine, business, Function (biology), Cell biology
Published
2015
Full Text
View/download PDF

13. Increase in PI3K signalling mimics mutated-Kras induction of pancreatic cancer

Author

Stéphane Pyronnet, Romain Baer, and Julie Guillermet-Guibert

Subjects
Oncology, medicine.medical_specialty, TNF Receptor-Associated Factor 3, Hepatology, business.industry, Gastroenterology, Protein Serine-Threonine Kinases, medicine.disease, medicine.disease_cause, Pancreatic Neoplasms, Phosphatidylinositol 3-Kinases, Signalling, Proto-Oncogene Proteins, Pancreatic cancer, Internal medicine, ras Proteins, medicine, Cancer research, Animals, Humans, KRAS, business, Gene, PI3K/AKT/mTOR pathway
Published
2013
Full Text
View/download PDF

14. The isoform of PI3K p110alpha is necessary for oncogenic Kras-driven initiation of pancreatic cancerogenesis

Author

Romain Baer, Mounira Chalabi, Bart Vanhaeseboreck, Stéphanie Cassant-Sourdy, Laetitia Planque, Marlene Dufresnes, Julie Guillermet-Guibert, Hubert Lulka, Corinne Bousquet, and Stéphane Pyronnet

Subjects
Gene isoform, Hepatology, business.industry, Endocrinology, Diabetes and Metabolism, Gastroenterology, medicine, Cancer research, KRAS, medicine.disease_cause, business, PI3K/AKT/mTOR pathway
Published
2013
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results