292 results on '"Ait-Si-Ali, Slimane"'
Search Results
2. The cytoplasmic fraction of the histone lysine methyltransferase Setdb1 is essential for embryonic stem cells
- Author
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Rapone, Roberta, Del Maestro, Laurence, Bouyioukos, Costas, Albini, Sonia, Cruz-Tapias, Paola, Joliot, Véronique, Cosson, Bertrand, and Ait-Si-Ali, Slimane
- Published
- 2023
- Full Text
- View/download PDF
3. Metabolic imprint of an intracellular pathogen drives histone hypermethylation and tunes the host transcriptional response to infection
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Charendoff, Chloé I., primary, Louchez, Félix V., additional, Wu, Yongzheng, additional, Dolat, Lee, additional, Velasco, Guillaume, additional, Perrinet, Stéphanie, additional, Torres, Adrian Gabriel, additional, Blanchet, Laure, additional, Duchateau, Magalie, additional, Gianetto, Quentin Giai, additional, Matondo, Mariette, additional, Maestro, Laurence Del, additional, Ait-Si-Ali, Slimane, additional, Bonhomme, Frédéric, additional, Millot, Gaël A., additional, Ribas de Pouplana, Lluís, additional, Martinez, Elisabeth D., additional, Valdivia, Raphael H., additional, and Subtil, Agathe, additional
- Published
- 2024
- Full Text
- View/download PDF
4. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
- Author
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Klionsky, Daniel J, Abdelmohsen, Kotb, Abe, Akihisa, Abedin, Md Joynal, Abeliovich, Hagai, Acevedo Arozena, Abraham, Adachi, Hiroaki, Adams, Christopher M, Adams, Peter D, Adeli, Khosrow, Adhihetty, Peter J, Adler, Sharon G, Agam, Galila, Agarwal, Rajesh, Aghi, Manish K, Agnello, Maria, Agostinis, Patrizia, Aguilar, Patricia V, Aguirre-Ghiso, Julio, Airoldi, Edoardo M, Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akporiaye, Emmanuel T, Al-Rubeai, Mohamed, Albaiceta, Guillermo M, Albanese, Chris, Albani, Diego, Albert, Matthew L, Aldudo, Jesus, Algül, Hana, Alirezaei, Mehrdad, Alloza, Iraide, Almasan, Alexandru, Almonte-Beceril, Maylin, Alnemri, Emad S, Alonso, Covadonga, Altan-Bonnet, Nihal, Altieri, Dario C, Alvarez, Silvia, Alvarez-Erviti, Lydia, Alves, Sandro, Amadoro, Giuseppina, Amano, Atsuo, Amantini, Consuelo, Ambrosio, Santiago, Amelio, Ivano, Amer, Amal O, Amessou, Mohamed, Amon, Angelika, An, Zhenyi, Anania, Frank A, Andersen, Stig U, Andley, Usha P, Andreadi, Catherine K, Andrieu-Abadie, Nathalie, Anel, Alberto, Ann, David K, Anoopkumar-Dukie, Shailendra, Antonioli, Manuela, Aoki, Hiroshi, Apostolova, Nadezda, Aquila, Saveria, Aquilano, Katia, Araki, Koichi, Arama, Eli, Aranda, Agustin, Araya, Jun, Arcaro, Alexandre, Arias, Esperanza, Arimoto, Hirokazu, Ariosa, Aileen R, Armstrong, Jane L, Arnould, Thierry, Arsov, Ivica, Asanuma, Katsuhiko, Askanas, Valerie, Asselin, Eric, Atarashi, Ryuichiro, Atherton, Sally S, Atkin, Julie D, Attardi, Laura D, Auberger, Patrick, Auburger, Georg, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Avantaggiati, Maria Laura, Avrahami, Limor, Awale, Suresh, Azad, Neelam, Bachetti, Tiziana, Backer, Jonathan M, Bae, Dong-Hun, Bae, Jae-Sung, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric H, Baek, Seung-Hoon, Baghdiguian, Stephen, and Bagniewska-Zadworna, Agnieszka
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Biochemistry and Cell Biology ,Biological Sciences ,Animals ,Autophagy ,Biological Assay ,Computer Simulation ,Humans ,autolysosome ,autophagosome ,chaperone-mediated autophagy ,flux ,LC3 ,lysosome ,macroautophagy ,phagophore ,stress ,vacuole ,Biochemistry & Molecular Biology ,Biochemistry and cell biology - Published
- 2016
5. Guidelines for the use and interpretation of assays for monitoring autophagy.
- Author
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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 YO, 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 TW, Bánhegyi, Gábor, Bartholomew, Clinton R, Bassham, Diane C, Bast, Robert C, Batoko, Henri, Bay, Boon-Huat, Beau, Isabelle, Béchet, 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, Sébastien, 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, Frédéric, Bourquin, Jean-Pierre, Boya, Patricia, Boyer-Guittaut, Michaël, 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, and Brumell, John H
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Animals ,Humans ,Biological Assay ,Models ,Biological ,Autophagy ,Generic health relevance ,autolysosome ,autophagosome ,flux ,LC3 ,lysosome ,phagophore ,stress ,vacuole ,Biochemistry and Cell Biology ,Biochemistry & Molecular Biology - 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 on these processes. These guidelines are not meant to be a formulaic set of rules, because the appropriate assays depend in part on the question being asked and the system being used. In addition, we emphasize that no individual assay is guaranteed to be the most appropriate one in every situation, and we strongly recommend the use of multiple assays to monitor autophagy. In these guidelines, we consider these various methods of assessing autophagy and what information can, or cannot, be obtained from them. Finally, by discussing the merits and limits of particular autophagy assays, we hope to encourage technical innovation in the field.
- Published
- 2012
6. SETDB1 modulates the TGFβ response in Duchenne muscular dystrophy myotubes
- Author
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Granados, Alice, primary, Zamperoni, Maeva, additional, Rapone, Roberta, additional, Bouyioukos, Costas, additional, Del Maestro, Laurence, additional, Joliot, Véronique, additional, Albini, Sonia, additional, and Ait-Si-Ali, Slimane, additional
- Published
- 2023
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7. Acute conversion of patient-derived Duchenne muscular dystrophy iPSC into myotubes reveals constitutive and inducible over-activation of TGFβ-dependent pro-fibrotic signaling
- Author
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Caputo, Luca, Granados, Alice, Lenzi, Jessica, Rosa, Alessandro, Ait-Si-Ali, Slimane, Puri, Pier Lorenzo, and Albini, Sonia
- Published
- 2020
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8. Contributors
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Ait-Si-Ali, Slimane, primary, Albini, Sonia, additional, Atzmon, Gil, additional, Badylak, Stephen F., additional, Barnstable, C.J., additional, Biferali, Beatrice, additional, Caporale, Nicolò, additional, Chen, Zhaoyi, additional, Chiacchiera, Fulvio, additional, Coffman, James A., additional, D’Angelo, William, additional, Dean, Wendy, additional, Eriksson, Jonas, additional, Fernández, Agustín F., additional, Fraga, Mario F., additional, Guil, Sònia, additional, Gutman, Danielle, additional, Hadi, Nur Annies Abd, additional, Hanna, Courtney W., additional, Josipović, Nataša, additional, Julian, Lisa M., additional, Mai, Antonello, additional, Marelli, Luca, additional, McCarthy, Ryan L., additional, McLaughlin, Katy A., additional, Meehan, Richard R., additional, Mozzetta, Chiara, additional, Nicetto, Dario, additional, Oliveira-Mateos, Cristina, additional, Ottaviano, Raffaele, additional, Pagiatakis, Christina, additional, Palacios, Daniela, additional, Papait, Roberto, additional, Papantonis, Argyris, additional, Pennings, Sari, additional, Pérez, Raúl F., additional, Petchreing, Petchroi, additional, Pietrobon, Adam, additional, Popova, E.Y., additional, Revuelta, Ailsa, additional, Sánchez-Castillo, Anaís, additional, Santamarina, Pablo, additional, Serio, Simone, additional, Stanford, William L., additional, Stazi, Giulia, additional, Testa, Giuseppe, additional, Valente, Sergio, additional, Viscomi, Maria Teresa, additional, Zakharova, Vlada, additional, Zaret, Kenneth S., additional, and Zwergel, Clemens, additional
- Published
- 2019
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9. Histone Modifications
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Albini, Sonia, primary, Zakharova, Vlada, additional, and Ait-Si-Ali, Slimane, additional
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- 2019
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10. Protocol for differential analysis of Trim71-associated protein complexes in mouse embryonic stem cells by mass spectrometry using Perseus
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Cosson, Bertrand, Rapone, Roberta, Del Maestro, Laurence, and Ait-Si-Ali, Slimane
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- 2024
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11. H19 IncRNA controls gene expression of the Imprinted Gene Network by recruiting MBD1
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Monnier, Paul, Martinet, Clémence, Pontis, Julien, Stancheva, Irina, Ait-Si-Ali, Slimane, and Dandolo, Luisa
- Published
- 2013
12. Glucose controls co-translation of structurally related mRNAs via the mTOR and eIF2 pathways in human pancreatic beta cells
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Bulfoni, Manuel, primary, Bouyioukos, Costas, additional, Zakaria, Albatoul, additional, Nigon, Fabienne, additional, Rapone, Roberta, additional, Del Maestro, Laurence, additional, Ait-Si-Ali, Slimane, additional, Scharfmann, Raphaël, additional, and Cosson, Bertrand, additional
- Published
- 2022
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13. Histone acetylation and the control of the cell cycle
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Magnaghi-Jaulin, Laura, Ait-Si-Ali, Slimane, Harel-Bellan, Annick, Meijer, Laurent, editor, Jézéquel, Armelle, editor, and Ducommun, Bernard, editor
- Published
- 2000
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14. SETDB1 fuels the lung cancer phenotype by modulating epigenome, 3D genome organization and chromatin mechanical properties
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Zakharova, Vlada V, primary, Magnitov, Mikhail D, additional, Del Maestro, Laurence, additional, Ulianov, Sergey V, additional, Glentis, Alexandros, additional, Uyanik, Burhan, additional, Williart, Alice, additional, Karpukhina, Anna, additional, Demidov, Oleg, additional, Joliot, Veronique, additional, Vassetzky, Yegor S, additional, Mège, René-Marc, additional, Piel, Matthieu, additional, Razin, Sergey V, additional, and Ait-Si-Ali, Slimane, additional
- Published
- 2022
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15. Paramecium Polycomb repressive complex 2 physically interacts with the small RNA-binding PIWI protein to repress transposable elements
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Miró-Pina, Caridad, primary, Charmant, Olivia, additional, Kawaguchi, Takayuki, additional, Holoch, Daniel, additional, Michaud, Audrey, additional, Cohen, Isadora, additional, Humbert, Adeline, additional, Jaszczyszyn, Yan, additional, Chevreux, Guillaume, additional, Del Maestro, Laurence, additional, Ait-Si-Ali, Slimane, additional, Arnaiz, Olivier, additional, Margueron, Raphaël, additional, and Duharcourt, Sandra, additional
- Published
- 2022
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16. Tandem Affinity Purification Approach Coupled to Mass Spectrometry to Identify Post-translational Modifications of Histones Associated with Chromatin-Binding Proteins
- Author
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Beyer, Sophie, primary, Robin, Philippe, additional, and Ait-Si-Ali, Slimane, additional
- Published
- 2016
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- View/download PDF
17. A Bacterial Protein Targets the BAHD1 Chromatin Complex to Stimulate Type III Interferon Response
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Lebreton, Alice, Lakisic, Goran, Job, Viviana, Fritsch, Lauriane, Tham, To Nam, Camejo, Ana, Matteï, Pierre-Jean, Regnault, Beatrice, Nahori, Marie-Anne, Cabanes, Didier, Gautreau, Alexis, Ait-Si-Ali, Slimane, Dessen, Andréa, Cossart, Pascale, and Bierne, Hélène
- Published
- 2011
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18. Triplex-Forming Oligonucleotide-Orthophenanthroline Conjugates for Efficient Targeted Genome Modification
- Author
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Cannata, Fabio, Brunet, Erika, Perrouault, Loïc, Roig, Victoria, Ait-Si-Ali, Slimane, Asseline, Ulysse, Concordet, Jean-Paul, and Giovannangeli, Carine
- Published
- 2008
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19. Glucose controls co-translation of structurally related mRNAs via the mTOR and eIF2 pathways in human pancreatic beta cells
- Author
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Bulfoni, Manuel, primary, Bouyioukos, Costas, additional, Zakaria, Albatoul, additional, Nigon, Fabienne, additional, Rapone, Roberta, additional, Maestro, Laurence Del, additional, Ait-Si-Ali, Slimane, additional, Scharfmann, Raphaël, additional, and Cosson, Bertrand, additional
- Published
- 2021
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- View/download PDF
20. SETDB1 Fuels the Lung Cancer Phenotype by Modulating Epigenome, 3D Genome Organization and Chromatin Mechanical Properties
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Zakharova, Vlada V., primary, Magnitov, Mikhail D., additional, Del-Maestro, Laurence, additional, Ulianov, Sergey V., additional, Glentis, Alexandros, additional, Ulyanik, Burhan, additional, Williart, Alice, additional, Karpukhina, Anna, additional, Demidov, Oleg, additional, Joliot, Veronique, additional, Vassetzky, Yegor S., additional, Mège, René-Marc, additional, Piel, Matthieu, additional, Razin, Sergey V., additional, and Ait-Si-Ali, Slimane, additional
- Published
- 2021
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21. Paramecium Polycomb Repressive Complex 2 physically interacts with the small RNA binding PIWI protein to repress transposable elements
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Pina, Caridad Miró, primary, Kawaguchi, Takayuki, additional, Charmant, Olivia, additional, Michaud, Audrey, additional, Cohen, Isadora, additional, Humbert, Adeline, additional, Jaszczyszyn, Yan, additional, Del Maestro, Laurence, additional, Holoch, Daniel, additional, Ait-Si-Ali, Slimane, additional, Arnaiz, Olivier, additional, Margueron, Raphaël, additional, and Duharcourt, Sandra, additional
- Published
- 2021
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- View/download PDF
22. The histone methyltransferase SETDB1 is recurrently amplified in melanoma and accelerates its onset
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Ceol, Craig J., Houvras, Yariv, Jane-Valbuena, Judit, Bilodeau, Steve, Orlando, David A., Battisti, Valentine, Fritsch, Lauriane, Lin, William M., Hollmann, Travis J., Ferre, Fabrizio, Bourque, Caitlin, Burke, Christopher J., Turner, Laura, Uong, Audrey, Johnson, Laura A., Beroukhim, Rameen, Mermel, Craig H., Loda, Massimo, Ait-Si-Ali, Slimane, Garraway, Levi A., Young, Richard A., and Zon, Leonard I.
- Subjects
Gene expression -- Physiological aspects -- Research -- Genetic aspects ,Methyltransferases -- Physiological aspects -- Genetic aspects -- Research ,Melanoma -- Genetic aspects -- Risk factors -- Development and progression -- Research ,Environmental issues ,Science and technology ,Zoology and wildlife conservation - Abstract
The most common mutation in human melanoma, BRAF(V600E), activates the serine/threonine kinase BRAF and causes excessive activity in the mitogen-activated protein kinase pathway (1,2). BRAF(V600E) mutations are also present in benign melanocytic naevi (3), highlighting the importance of additional genetic alterations in the genesis of malignant tumours. Such changes include recurrent copy number variations that result in the amplification of oncogenes (4,5). For certain amplifications, the large number of genes in the interval has precluded an understanding of the cooperating oncogenic events. Here we have used a zebrafish melanoma model to test genes in a recurrently amplified region of chromosome 1 for the ability to cooperate with BRAF(V600E) and accelerate melanoma. SETDB1, an enzyme that methylates histone H3 on lysine 9 (H3K9), was found to accelerate melanoma formation significantly in zebrafish. Chromatin immunoprecipitation coupled with massively parallel DNA sequencing and gene expression analyses uncovered genes, including HOX genes, that are transcriptionally dysregulated in response to increased levels of SETDB1. Our studies establish SETDB1 as an oncogene in melanoma and underscore the role of chromatin factors in regulating tumorigenesis., To identify genes that promote melanoma, we focused on genomic regions that are subject to copy number amplification in human tumour samples. In a study of 101 cell lines and [...]
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- 2011
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23. PRMT5-mediated histone H4 arginine-3 symmetrical dimethylation marks chromatin at G + C-rich regions of the mouse genome
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Girardot, Michael, Hirasawa, Ryutaro, Kacem, Salim, Fritsch, Lauriane, Pontis, Julien, Kota, Satya K., Filipponi, Doria, Fabbrizio, Eric, Sardet, Claude, Lohmann, Felix, Kadam, Shilpa, Ait-Si-Ali, Slimane, and Feil, Robert
- Published
- 2014
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24. Additional file 5 of Acute conversion of patient-derived Duchenne muscular dystrophy iPSC into myotubes reveals constitutive and inducible over-activation of TGFβ-dependent pro-fibrotic signaling
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Caputo, Luca, Granados, Alice, Lenzi, Jessica, Rosa, Alessandro, Ait-Si-Ali, Slimane, Puri, Pier Lorenzo, and Albini, Sonia
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musculoskeletal system - Abstract
Additional file 5: Figure S5. Pro-fibrotic gene activation in differentiated human myoblasts following electrical pacing.
- Published
- 2020
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25. Additional file 1 of Acute conversion of patient-derived Duchenne muscular dystrophy iPSC into myotubes reveals constitutive and inducible over-activation of TGFβ-dependent pro-fibrotic signaling
- Author
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Caputo, Luca, Granados, Alice, Lenzi, Jessica, Rosa, Alessandro, Ait-Si-Ali, Slimane, Puri, Pier Lorenzo, and Albini, Sonia
- Abstract
Additional file 1: Figure S1. Myogenic potential of Control and DMD iPSC expressing inducible epB vectors for BAF60C and MyoD.
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- 2020
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26. Additional file 2 of Acute conversion of patient-derived Duchenne muscular dystrophy iPSC into myotubes reveals constitutive and inducible over-activation of TGFβ-dependent pro-fibrotic signaling
- Author
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Caputo, Luca, Granados, Alice, Lenzi, Jessica, Rosa, Alessandro, Ait-Si-Ali, Slimane, Puri, Pier Lorenzo, and Albini, Sonia
- Abstract
Additional file 2: Figure S2. Validation of the exacerbated TGFβ response in DMD iPSC ex45del- derived myotubes.
- Published
- 2020
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27. Acetylation is important for MyoD function in adult mice
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Duquet, Arnaud, Polesskaya, Anna, Cuvellier, Sylvain, Ait‐Si‐Ali, Slimane, Héry, Patrick, Pritchard, Linda L, Gerard, Matthieu, and Harel‐Bellan, Annick
- Published
- 2006
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28. Essential Cytoplasmic Role of the Histone Lysine Methyltransferase Setdb1 in Post-Transcriptional Regulation in Embryonic Stem Cells
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Rapone, Roberta, primary, Maestro, Laurence Del, additional, Bouyioukos, Costas, additional, Albini, Sonia, additional, Cruz-Tapias, Paola, additional, Joliot, Véronique, additional, Cosson, Bertrand, additional, and Ait-Si-Ali, Slimane, additional
- Published
- 2021
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29. A Suv39h‐dependent mechanism for silencing S‐phase genes in differentiating but not in cycling cells
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Ait‐Si‐Ali, Slimane, Guasconi, Valentina, Fritsch, Lauriane, Yahi, Hakima, Sekhri, Redha, Naguibneva, Irina, Robin, Philippe, Cabon, Florence, Polesskaya, Anna, and Harel‐Bellan, Annick
- Published
- 2004
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30. SPOC1 modulates DNA repair by regulating key determinants of chromatin compaction and DNA damage response
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Mund, Andreas, Schubert, Tobias, Staege, Hannah, Kinkley, Sarah, Reumann, Kerstin, Kriegs, Malte, Fritsch, Lauriane, Battisti, Valentine, Ait-Si-Ali, Slimane, Hoffbeck, Anne-Sophie, Soutoglou, Evi, and Will, Hans
- Published
- 2012
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31. Cell cycle‐dependent recruitment of HDAC‐1 correlates with deacetylation of histone H4 on an Rb–E2F target promoter
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Ferreira, Roger, Naguibneva, Irina, Mathieu, Marion, Ait‐Si‐Ali, Slimane, Robin, Philippe, Pritchard, Linda L, and Harel‐Bellan, Annick
- Published
- 2001
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32. The Rb/chromatin connection and epigenetic control: opinion
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Ferreira, Roger, Naguibneva, Irina, Pritchard, Linda L, Ait-Si-Ali, Slimane, and Harel-Bellan, Annick
- Published
- 2001
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33. CBP/p300 histone acetyl-transferase activity is important for the G1/S transition
- Author
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Ait-Si-Ali, Slimane, Polesskaya, Anna, Filleur, Stéphanie, Ferreira, Roger, Duquet, Arnaud, Robin, Philippe, Vervish, Arlette, Trouche, Didier, Cabon, Florence, and Harel-Bellan, Annick
- Published
- 2000
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34. The Wilms' tumor gene product represses the transcription of thrombospondin 1 in response to overexpression of c-Jun
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Dejong, Valérie, Degeorges, Armelle, Filleur, Stéphanie, Ait-Si-Ali, Slimane, Mettouchi, Amel, Bornstein, Paul, Binétruy, Bernard, and Cabon, Florence
- Published
- 1999
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35. SPOC1 modulates DNA repair by regulating key determinants of chromatin compaction and DNA damage response
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Mund, Andreas, primary, Schubert, Tobias, additional, Staege, Hannah, additional, Kinkley, Sarah, additional, Reumann, Kerstin, additional, Kriegs, Malte, additional, Fritsch, Lauriane, additional, Battisti, Valentine, additional, Ait-Si-Ali, Slimane, additional, Hoffbeck, Anne-Sophie, additional, Soutoglou, Evi, additional, and Will, Hans, additional
- Published
- 2020
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- View/download PDF
36. The histone acetyltransferase hMOF promotes vascular invasion in hepatocellular carcinoma
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Poté, Nicolas, primary, Cros, Jérôme, additional, Laouirem, Samira, additional, Raffenne, Jérôme, additional, Negrão, Magda, additional, Albuquerque, Miguel, additional, Bedossa, Pierre, additional, Godinho Ferreira, Miguel, additional, Ait Si Ali, Slimane, additional, Fior, Rita, additional, and Paradis, Valérie, additional
- Published
- 2020
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- View/download PDF
37. The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein
- Author
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Nicolas, Estelle, Ait-Si-Ali, Slimane, and Trouche, Didier
- Published
- 2001
38. Expression of the Major and Pro-Oncogenic H3K9 Lysine Methyltransferase SETDB1 in Non-Small Cell Lung Cancer
- Author
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Cruz-Tapias, Paola, primary, Zakharova, Vlada, additional, Perez-Fernandez, Oscar, additional, Mantilla, William, additional, Ramírez-Clavijo, Sandra, additional, and Ait-Si-Ali, Slimane, additional
- Published
- 2019
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- View/download PDF
39. Tandem Affinity Purification Approach Coupled to Mass Spectrometry to Identify Post-translational Modifications of Histones Associated with Chromatin-Binding Proteins
- Author
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Beyer, Sophie, Robin, Philippe, Ait-Si-Ali, Slimane, Centre épigénétique et destin cellulaire (EDC (UMR_7216)), and Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)
- Subjects
[SDV]Life Sciences [q-bio] ,ComputingMilieux_MISCELLANEOUS - Abstract
International audience
- Published
- 2017
40. Jmjd2c facilitates the assembly of essential enhancer-protein complexes at the onset of embryonic stem cell differentiation
- Author
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Tomaz, Rute, Harman, Jennifer, Karimlou, Donja, Weavers, Lauren, Fritsch, Lauriane, Bou-Kheir, Tony, Bell, Emma, del Valle Torres, Ignacio, Niakan, Kathy, Fisher, Cynthia, Joshi, Onkar, Stunnenberg, Hendrik, Curry, Edward, Ait-Si-Ali, Slimane, Jørgensen, Helle, Azuara, Véronique, Genesis Research Trust, Parkinson's UK, Biotechnology and Biological Sciences Research Council (BBSRC), Niakan, Kathy [0000-0003-1646-4734], Jorgensen, Helle [0000-0002-7909-2977], Apollo - University of Cambridge Repository, Centre épigénétique et destin cellulaire (EDC (UMR_7216)), and Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)
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Embryonic stem cells ,[SDV]Life Sciences [q-bio] ,MOUSE EMBRYOS ,Lineage specification ,9 METHYLTRANSFERASES G9A ,XEN CELLS ,Enhancers ,Jmjd2c (Kdm4c) ,GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries) ,Molecular Biology ,HISTONE H3 ,ComputingMilieux_MISCELLANEOUS ,reproductive and urinary physiology ,Jmjd2c/Kdm4c, enhancers, gene regulation, embryonic stem cells, epiblast stem cells, lineage specification ,Science & Technology ,VISCERAL ENDODERM ,DEMETHYLASE ACTIVITY ,11 Medical And Health Sciences ,06 Biological Sciences ,Gene regulation ,SELF-RENEWAL ,TRANSCRIPTION FACTORS ,CPG ISLANDS ,embryonic structures ,biological phenomena, cell phenomena, and immunity ,Life Sciences & Biomedicine ,Epiblast stem cells ,Developmental Biology ,GROUND-STATE PLURIPOTENCY - Abstract
Jmjd2 H3K9 demethylases cooperate in promoting mouse embryonic stem cell (ESC) identity. However, little is known about their importance at the exit of ESC pluripotency. Here, we reveal that Jmjd2c facilitates this process by stabilising the assembly of mediator-cohesin complexes at lineage-specific enhancers. Functionally, we show that Jmjd2c is required in ESCs to initiate appropriate gene expression programs upon somatic multi-lineage differentiation. In the absence of Jmjd2c, differentiation is stalled at an early post-implantation epiblast-like stage, while Jmjd2c-knockout ESCs remain capable of forming extra-embryonic endoderm derivatives. Dissection of the underlying molecular basis revealed that Jmjd2c is re-distributed to lineage-specific enhancers during ESC priming for differentiation. Interestingly, Jmjd2c-bound enhancers are co-occupied by the H3K9-methyltransferase G9a (also known as Ehmt2), independently of its H3K9-modifying activity. Loss of Jmjd2c abrogates G9a recruitment and further destabilises loading of the mediator and cohesin components Med1 and Smc1a at newly activated and poised enhancers in ESC-derived epiblast-like cells. These findings unveil Jmjd2c and G9a as novel enhancer-associated factors, and implicate Jmjd2c as a molecular scaffold for the assembly of essential enhancer-protein complexes with an impact on timely gene activation.
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- 2016
41. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
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Klionsky, Daniel J., Abdelmohsen, Kotb, Abe, Akihisa, Abedin, Md Joynal, Abeliovich, Hagai, Arozena, Abraham Acevedo, Adachi, Hiroaki, Adams, Christopher M., Adams, Peter D., Adeli, Khosrow, Adhihetty, Peter J., Adler, Sharon G., Agam, Galila, Agarwal, Rajesh, Aghi, Manish K., Agnello, Maria, Agostinis, Patrizia, Aguilar, Patricia V., Aguirre-Ghiso, Julio, Airoldi, Edoardo M., Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akporiaye, Emmanuel T., Al-Rubeai, Mohamed, Albaiceta, Guillermo M., Albanese, Chris, Albani, Diego, Albert, Matthew L., Aldudo, Jesus, Algül, Hana, Alirezaei, Mehrdad, Alloza, Iraide, Almasan, Alexandru, Almonte-Beceril, Maylin, Alnemri, Emad S., Alonso, Covadonga, Altan-Bonnet, Nihal, Altieri, Dario C., Alvarez, Silvia, Alvarez-Erviti, Lydia, Alves, Sandro, Amadoro, Giuseppina, Amano, Atsuo, Færgeman, Nils J., Guerra, Barbara, and Wang, Ying Jan
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Flux ,Autophagosome ,Chaperonemediated autophagy ,Stress ,Lysosome ,Autolysosome ,Macroautophagy ,LC3 ,Phagophore ,Vacuole ,Humans ,Animals ,Computer Simulation ,Autophagy/physiology ,Biological Assay/methods - Published
- 2016
42. Erratum to Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
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Klionsky, Daniel J., Abdelmohsen, Kotb, Abe, Akihisa, Abedin, Md Joynal, Abeliovich, Hagai, Arozena, Abraham Acevedo, Adachi, Hiroaki, Adams, Christopher M., Adams, Peter D., Adeli, Khosrow, Adhihetty, Peter J., Adler, Sharon G., Agam, Galila, Agarwal, Rajesh, Aghi, Manish K., Agnello, Maria, Agostinis, Patrizia, Aguilar, Patricia V., Aguirre-Ghiso, Julio, Airoldi, Edoardo M., Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akporiaye, Emmanuel T., Al-Rubeai, Mohamed, Albaiceta, Guillermo M., Albanese, Chris, Albani, Diego, Albert, Matthew L., Aldudo, Jesus, Algül, Hana, Alirezaei, Mehrdad, Alloza, Iraide, Almasan, Alexandru, Almonte-Beceril, Maylin, Alnemri, Emad S., Alonso, Covadonga, Altan-Bonnet, Nihal, Altieri, Dario C., Alvarez, Silvia, Alvarez-Erviti, Lydia, Alves, Sandro, Amadoro, Giuseppina, Amano, Atsuo, Amantini, Consuelo, Arnould, Thierry, Feron, Olivier, Hamer, Isabelle, Michiels, Carine, Wu, Min, and Zhang, Jing Pu
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- 2016
43. The histone variant mH2A1.1 interferes with transcription by down-regulating PARP-1 enzymatic activity
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Ait-Si-Ali, Slimane and Robin, Philippe
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Genetic regulation -- Research ,Histones -- Research ,Genetic research ,Biological sciences - Abstract
The promoters of the inducible human Hsp-70.1 and Hsp-70.2 genes, but not the constitutively expressed HSP-70.8 gene (HSC70), are shown to be very highly enriched in the histone variant macroH2A1.1 (mH2A1.1). A novel mechanism is described for control of Hsp-70.1 gene transcription through down-regulation of the activity of poly (ADP-ribose) polymerases (PARP)-1 by macroH2A (mH2A)1.1
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- 2006
44. Jmjd2c/Kdm4c facilitates the assembly of essential enhancer-protein complexes at the onset of embryonic stem cell differentiation
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Tomaz, Rute A., primary, Harman, Jennifer L., additional, Karimlou, Donja, additional, Weavers, Lauren, additional, Fritsch, Lauriane, additional, Bou-Kheir, Tony, additional, Bell, Emma, additional, Torres, Ignacio del Valle, additional, Niakan, Kathy K., additional, Fisher, Cynthia, additional, Joshi, Onkar, additional, Stunnenberg, Hendrik G., additional, Curry, Edward, additional, Ait-Si-Ali, Slimane, additional, Jørgensen, Helle F., additional, and Azuara, Véronique, additional
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- 2017
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45. Erratum: Roche, J. et al. Global Decrease of Histone H3K27 Acetylation in ZEB1-Induced Epithelial to Mesenchymal Transition in Lung Cancer Cells. Cancers, 2013, 5, 334–356
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Roche, Joëlle, primary, Nasarre, Patrick, additional, Gemmill, Robert, additional, Baldys, Aleksander, additional, Pontis, Julien, additional, Korch, Christopher, additional, Guilhot, Joëlle, additional, Ait-Si-Ali, Slimane, additional, and Drabkin, Harry, additional
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- 2016
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46. Guidelines for the use and interpretation of assays for monitoring autophagy:3rd edition
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Klionsky, Daniel J, Abdelmohsen, Kotb, Abe, Akihisa, Abedin, Md Joynal, Abeliovich, Hagai, Acevedo Arozena, Abraham, Adachi, Hiroaki, Adams, Christopher M, Adams, Peter D, Adeli, Khosrow, Adhihetty, Peter J, Adler, Sharon G, Agam, Galila, Agarwal, Rajesh, Aghi, Manish K, Agnello, Maria, Agostinis, Patrizia, Aguilar, Patricia V, Aguirre-Ghiso, Julio, Airoldi, Edoardo M, Ait-Si-Ali, Slimane, Akematsu, Takahiko, Akporiaye, Emmanuel T, Al-Rubeai, Mohamed, Albaiceta, Guillermo M, Albanese, Chris, Albani, Diego, Albert, Matthew L, Aldudo, Jesus, Algül, Hana, Alirezaei, Mehrdad, Alloza, Iraide, Almasan, Alexandru, Almonte-Beceril, Maylin, Alnemri, Emad S, Alonso, Covadonga, Altan-Bonnet, Nihal, Altieri, Dario C, Alvarez, Silvia, Alvarez-Erviti, Lydia, Alves, Sandro, Amadoro, Giuseppina, Amano, Atsuo, Amantini, Consuelo, Ambrosio, Santiago, Amelio, Ivano, Amer, Amal O, Amessou, Mohamed, Amon, Angelika, An, Zhenyi, Anania, Frank A, Andersen, Stig U, Andley, Usha P, Andreadi, Catherine K, Andrieu-Abadie, Nathalie, Anel, Alberto, Ann, David K, Anoopkumar-Dukie, Shailendra, Antonioli, Manuela, Aoki, Hiroshi, Apostolova, Nadezda, Aquila, Saveria, Aquilano, Katia, Araki, Koichi, Arama, Eli, Aranda, Agustin, Araya, Jun, Arcaro, Alexandre, Arias, Esperanza, Arimoto, Hirokazu, Ariosa, Aileen R, Armstrong, Jane L, Arnould, Thierry, Arsov, Ivica, Asanuma, Katsuhiko, Askanas, Valerie, Asselin, Eric, Atarashi, Ryuichiro, Atherton, Sally S, Atkin, Julie D, Attardi, Laura D, Auberger, Patrick, Auburger, Georg, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Avantaggiati, Maria Laura, Avrahami, Limor, Awale, Suresh, Azad, Neelam, Bachetti, Tiziana, Backer, Jonathan M, Bae, Dong-Hun, Bae, Jae-Sung, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric H, Baek, Seung-Hoon, Baghdiguian, Stephen, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xue-Yuan, Bailly, Yannick, Balaji, Kithiganahalli Narayanaswamy, Balduini, Walter, Ballabio, Andrea, Balzan, Rena, Banerjee, Rajkumar, Bánhegyi, Gábor, Bao, Haijun, Barbeau, Benoit, Barrachina, Maria D, Barreiro, Esther, Bartel, Bonnie, Bartolomé, Alberto, Bassham, Diane C, Bassi, Maria Teresa, Bast, Robert C, Basu, Alakananda, Batista, Maria Teresa, Batoko, Henri, Battino, Maurizio, Bauckman, Kyle, Baumgarner, Bradley L, Bayer, K Ulrich, Beale, Rupert, Beaulieu, Jean-François, Beck, George R, Becker, Christoph, Beckham, J David, Bédard, Pierre-André, Bednarski, Patrick J, Begley, Thomas J, Behl, Christian, Behrends, Christian, Behrens, Georg Mn, Behrns, Kevin E, Bejarano, Eloy, Belaid, Amine, Belleudi, Francesca, Bénard, Giovanni, Berchem, Guy, Bergamaschi, Daniele, Bergami, Matteo, Berkhout, Ben, Berliocchi, Laura, Bernard, Amélie, Bernard, Monique, Bernassola, Francesca, Bertolotti, Anne, Bess, Amanda S, Besteiro, Sébastien, Bettuzzi, Saverio, Bhalla, Savita, Bhattacharyya, Shalmoli, Bhutia, Sujit K, Biagosch, Caroline, Bianchi, Michele Wolfe, Biard-Piechaczyk, Martine, Billes, Viktor, Bincoletto, Claudia, Bingol, Baris, Bird, Sara W, Bitoun, Marc, Bjedov, Ivana, Blackstone, Craig, Blanc, Lionel, Blanco, Guillermo A, Blomhoff, Heidi Kiil, Boada-Romero, Emilio, Böckler, Stefan, Boes, Marianne, Boesze-Battaglia, Kathleen, Boise, Lawrence H, Bolino, Alessandra, Boman, Andrea, Bonaldo, Paolo, Bordi, Matteo, Bosch, Jürgen, Botana, Luis M, Botti, Joelle, Bou, German, Bouché, Marina, Bouchecareilh, Marion, Boucher, Marie-Josée, Boulton, Michael E, Bouret, Sebastien G, Boya, Patricia, Boyer-Guittaut, Michaël, Bozhkov, Peter V, Brady, Nathan, Braga, Vania Mm, Brancolini, Claudio, Braus, Gerhard H, Bravo-San Pedro, José M, Brennan, Lisa A, Bresnick, Emery H, Brest, Patrick, Bridges, Dave, Bringer, Marie-Agnès, Brini, Marisa, Brito, Glauber C, Brodin, Bertha, Brookes, Paul S, Brown, Eric J, Brown, Karen, Broxmeyer, Hal E, Bruhat, Alain, Brum, Patricia Chakur, Brumell, John H, Brunetti-Pierri, Nicola, Bryson-Richardson, Robert J, Buch, Shilpa, Buchan, Alastair M, Budak, Hikmet, Bulavin, Dmitry V, Bultman, Scott J, Bultynck, Geert, Bumbasirevic, Vladimir, Burelle, Yan, Burke, Robert E, Burmeister, Margit, Bütikofer, Peter, Caberlotto, Laura, Cadwell, Ken, Cahova, Monika, Cai, Dongsheng, Cai, Jingjing, Cai, Qian, Calatayud, Sara, Camougrand, Nadine, Campanella, Michelangelo, Campbell, Grant R, Campbell, Matthew, Campello, Silvia, Candau, Robin, Caniggia, Isabella, Cantoni, Lavinia, Cao, Lizhi, Caplan, Allan B, Caraglia, Michele, Cardinali, Claudio, Cardoso, Sandra Morais, Carew, Jennifer S, Carleton, Laura A, Carlin, Cathleen R, Carloni, Silvia, Carlsson, Sven R, Carmona-Gutierrez, Didac, Carneiro, Leticia Am, Carnevali, Oliana, Carra, Serena, Carrier, Alice, Carroll, Bernadette, Casas, Caty, Casas, Josefina, Cassinelli, Giuliana, Castets, Perrine, Castro-Obregon, Susana, Cavallini, Gabriella, Ceccherini, Isabella, Cecconi, Francesco, Cederbaum, Arthur I, Ceña, Valentín, Cenci, Simone, Cerella, Claudia, Cervia, Davide, Cetrullo, Silvia, Chaachouay, Hassan, Chae, Han-Jung, Chagin, Andrei S, Chai, Chee-Yin, Chakrabarti, Gopal, Chamilos, Georgios, Chan, Edmond Yw, Chan, Matthew Tv, Chandra, Dhyan, Chandra, Pallavi, Chang, Chih-Peng, Chang, Raymond Chuen-Chung, Chang, Ta Yuan, Chatham, John C, Chatterjee, Saurabh, Chauhan, Santosh, Che, Yongsheng, Cheetham, Michael E, Cheluvappa, Rajkumar, Chen, Chun-Jung, Chen, Gang, Chen, Guang-Chao, Chen, Guoqiang, Chen, Hongzhuan, Chen, Jeff W, Chen, Jian-Kang, Chen, Min, Chen, Mingzhou, Chen, Peiwen, Chen, Qi, Chen, Quan, Chen, Shang-Der, Chen, Si, Chen, Steve S-L, Chen, Wei-Jung, Chen, Wen Qiang, Chen, Wenli, Chen, Xiangmei, Chen, Yau-Hung, Chen, Ye-Guang, Chen, Yin, Chen, Yingyu, Chen, Yongshun, Chen, Yu-Jen, Chen, Yue-Qin, Chen, Yujie, Chen, Zhen, Chen, Zhong, Cheng, Alan, Cheng, Christopher Hk, Cheng, Hua, Cheong, Heesun, Cherry, Sara, Chesney, Jason, Cheung, Chun Hei Antonio, Chevet, Eric, Chi, Hsiang Cheng, Chi, Sung-Gil, Chiacchiera, Fulvio, Chiang, Hui-Ling, Chiarelli, Roberto, Chiariello, Mario, Chieppa, Marcello, Chin, Lih-Shen, Chiong, Mario, Chiu, Gigi Nc, Cho, Dong-Hyung, Cho, Ssang-Goo, Cho, William C, Cho, Yong-Yeon, Cho, Young-Seok, Choi, Augustine Mk, Choi, Eui-Ju, Choi, Eun-Kyoung, Choi, Jayoung, Choi, Mary E, Choi, Seung-Il, Chou, Tsui-Fen, Chouaib, Salem, Choubey, Divaker, Choubey, Vinay, Chow, Kuan-Chih, Chowdhury, Kamal, Chu, Charleen T, Chuang, Tsung-Hsien, Chun, Taehoon, Chung, Hyewon, Chung, Taijoon, Chung, Yuen-Li, Chwae, Yong-Joon, Cianfanelli, Valentina, Ciarcia, Roberto, Ciechomska, Iwona A, Ciriolo, Maria Rosa, Cirone, Mara, Claerhout, Sofie, Clague, Michael J, Clària, Joan, Clarke, Peter Gh, Clarke, Robert, Clementi, Emilio, Cleyrat, Cédric, Cnop, Miriam, Coccia, Eliana M, Cocco, Tiziana, Codogno, Patrice, Coers, Jörn, Cohen, Ezra Ew, Colecchia, David, Coletto, Luisa, Coll, Núria S, Colucci-Guyon, Emma, Comincini, Sergio, Condello, Maria, Cook, Katherine L, Coombs, Graham H, Cooper, Cynthia D, Cooper, J Mark, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corazzari, Marco, Corbalan, Ramon, Corcelle-Termeau, Elisabeth, Cordero, Mario D, Corral-Ramos, Cristina, Corti, Olga, Cossarizza, Andrea, Costelli, Paola, Costes, Safia, Cotman, Susan L, Coto-Montes, Ana, Cottet, Sandra, Couve, Eduardo, Covey, Lori R, Cowart, L Ashley, Cox, Jeffery S, Coxon, Fraser P, Coyne, Carolyn B, Cragg, Mark S, Craven, Rolf J, Crepaldi, Tiziana, Crespo, Jose L, Criollo, Alfredo, Crippa, Valeria, Cruz, Maria Teresa, Cuervo, Ana Maria, Cuezva, Jose M, Cui, Taixing, Cutillas, Pedro R, Czaja, Mark J, Czyzyk-Krzeska, Maria F, Dagda, Ruben K, Dahmen, Uta, Dai, Chunsun, Dai, Wenjie, Dai, Yun, Dalby, Kevin N, Dalla Valle, Luisa, Dalmasso, Guillaume, D'Amelio, Marcello, Damme, Markus, Darfeuille-Michaud, Arlette, Dargemont, Catherine, Darley-Usmar, Victor M, Dasarathy, Srinivasan, Dasgupta, Biplab, Dash, Srikanta, Dass, Crispin R, Davey, Hazel Marie, Davids, Lester M, Dávila, David, Davis, Roger J, Dawson, Ted M, Dawson, Valina L, Daza, Paula, de Belleroche, Jackie, de Figueiredo, Paul, de Figueiredo, Regina Celia Bressan Queiroz, de la Fuente, José, De Martino, Luisa, De Matteis, Antonella, De Meyer, Guido Ry, De Milito, Angelo, De Santi, Mauro, de Souza, Wanderley, De Tata, Vincenzo, De Zio, Daniela, Debnath, Jayanta, Dechant, Reinhard, Decuypere, Jean-Paul, Deegan, Shane, Dehay, Benjamin, Del Bello, Barbara, Del Re, Dominic P, Delage-Mourroux, Régis, Delbridge, Lea Md, Deldicque, Louise, Delorme-Axford, Elizabeth, Deng, Yizhen, Dengjel, Joern, Denizot, Melanie, Dent, Paul, Der, Channing J, Deretic, Vojo, Derrien, Benoît, Deutsch, Eric, Devarenne, Timothy P, Devenish, Rodney J, Di Bartolomeo, Sabrina, Di Daniele, Nicola, Di Domenico, Fabio, Di Nardo, Alessia, Di Paola, Simone, Di Pietro, Antonio, Di Renzo, Livia, DiAntonio, Aaron, Díaz-Araya, Guillermo, Díaz-Laviada, Ines, Diaz-Meco, Maria T, Diaz-Nido, Javier, Dickey, Chad A, Dickson, Robert C, Diederich, Marc, Digard, Paul, Dikic, Ivan, Dinesh-Kumar, Savithrama P, Ding, Chan, Ding, Wen-Xing, Ding, Zufeng, Dini, Luciana, Distler, Jörg Hw, Diwan, Abhinav, Djavaheri-Mergny, Mojgan, Dmytruk, Kostyantyn, Dobson, Renwick Cj, Doetsch, Volker, Dokladny, Karol, Dokudovskaya, Svetlana, Donadelli, Massimo, Dong, X Charlie, Dong, Xiaonan, Dong, Zheng, Donohue, Terrence M, Doran, Kelly S, D'Orazi, Gabriella, Dorn, Gerald W, Dosenko, Victor, Dridi, Sami, Drucker, Liat, Du, Jie, Du, Li-Lin, Du, Lihuan, du Toit, André, Dua, Priyamvada, Duan, Lei, Duann, Pu, Dubey, Vikash Kumar, Duchen, Michael R, Duchosal, Michel A, Duez, Helene, Dugail, Isabelle, Dumit, Verónica I, Duncan, Mara C, Dunlop, Elaine A, Dunn, William A, Dupont, Nicolas, Dupuis, Luc, Durán, Raúl V, Durcan, Thomas M, Duvezin-Caubet, Stéphane, Duvvuri, Umamaheswar, Eapen, Vinay, Ebrahimi-Fakhari, Darius, Echard, Arnaud, Eckhart, Leopold, Edelstein, Charles L, Edinger, Aimee L, Eichinger, Ludwig, Eisenberg, Tobias, Eisenberg-Lerner, Avital, Eissa, N Tony, El-Deiry, Wafik S, El-Khoury, Victoria, Elazar, Zvulun, Eldar-Finkelman, Hagit, Elliott, Chris Jh, Emanuele, Enzo, Emmenegger, Urban, Engedal, Nikolai, Engelbrecht, Anna-Mart, Engelender, Simone, Enserink, Jorrit M, Erdmann, Ralf, Erenpreisa, Jekaterina, Eri, Rajaraman, Eriksen, Jason L, Erman, Andreja, Escalante, Ricardo, Eskelinen, Eeva-Liisa, Espert, Lucile, Esteban-Martínez, Lorena, Evans, Thomas J, Fabri, Mario, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Færgeman, Nils J, Faggioni, Alberto, Fairlie, W Douglas, Fan, Chunhai, Fan, Daping, Fan, Jie, Fang, Shengyun, Fanto, Manolis, Fanzani, Alessandro, Farkas, Thomas, Faure, Mathias, Favier, Francois B, Fearnhead, Howard, Federici, Massimo, Fei, Erkang, Felizardo, Tania C, Feng, Hua, Feng, Yibin, Feng, Yuchen, Ferguson, Thomas A, Fernández, Álvaro F, Fernandez-Barrena, Maite G, Fernandez-Checa, Jose C, Fernández-López, Arsenio, Fernandez-Zapico, Martin E, Feron, Olivier, Ferraro, Elisabetta, Ferreira-Halder, Carmen Veríssima, Fesus, Laszlo, Feuer, Ralph, Fiesel, Fabienne C, Filippi-Chiela, Eduardo C, Filomeni, Giuseppe, Fimia, Gian Maria, Fingert, John H, Finkbeiner, Steven, Finkel, Toren, Fiorito, Filomena, Fisher, Paul B, Flajolet, Marc, Flamigni, Flavio, Florey, Oliver, Florio, Salvatore, Floto, R Andres, Folini, Marco, Follo, Carlo, Fon, Edward A, Fornai, Francesco, Fortunato, Franco, Fraldi, Alessandro, Franco, Rodrigo, Francois, Arnaud, François, Aurélie, Frankel, Lisa B, Fraser, Iain Dc, Frey, Norbert, Freyssenet, Damien G, Frezza, Christian, Friedman, Scott L, Frigo, Daniel E, Fu, Dongxu, Fuentes, José M, Fueyo, Juan, Fujitani, Yoshio, Fujiwara, Yuuki, Fujiya, Mikihiro, Fukuda, Mitsunori, Fulda, Simone, Fusco, Carmela, Gabryel, Bozena, Gaestel, Matthias, Gailly, Philippe, Gajewska, Malgorzata, Galadari, Sehamuddin, Galili, Gad, Galindo, Inmaculada, Galindo, Maria F, Galliciotti, Giovanna, Galluzzi, Lorenzo, Galluzzi, Luca, Galy, Vincent, Gammoh, Noor, Gandy, Sam, Ganesan, Anand K, Ganesan, Swamynathan, Ganley, Ian G, Gannagé, Monique, Gao, Fen-Biao, Gao, Feng, Gao, Jian-Xin, García Nannig, Lorena, García Véscovi, Eleonora, Garcia-Macía, Marina, Garcia-Ruiz, Carmen, Garg, Abhishek D, Garg, Pramod Kumar, Gargini, Ricardo, Gassen, Nils Christian, Gatica, Damián, Gatti, Evelina, Gavard, Julie, Gavathiotis, Evripidis, Ge, Liang, Ge, Pengfei, Ge, Shengfang, Gean, Po-Wu, Gelmetti, Vania, Genazzani, Armando A, Geng, Jiefei, Genschik, Pascal, Gerner, Lisa, Gestwicki, Jason E, Gewirtz, David A, Ghavami, Saeid, Ghigo, Eric, Ghosh, Debabrata, Giammarioli, Anna Maria, Giampieri, Francesca, Giampietri, Claudia, Giatromanolaki, Alexandra, Gibbings, Derrick J, Gibellini, Lara, Gibson, Spencer B, Ginet, Vanessa, Giordano, Antonio, Giorgini, Flaviano, Giovannetti, Elisa, Girardin, Stephen E, Gispert, Suzana, Giuliano, Sandy, Gladson, Candece L, Glavic, Alvaro, Gleave, Martin, Godefroy, Nelly, Gogal, Robert M, Gokulan, Kuppan, Goldman, Gustavo H, Goletti, Delia, Goligorsky, Michael S, Gomes, Aldrin V, Gomes, Ligia C, Gomez, Hernando, Gomez-Manzano, Candelaria, Gómez-Sánchez, Rubén, 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- 2016
47. Unambiguous demonstration of triple-helix-directed gene modification
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Barre, Francois-Xavier, Ait-Si-Ali, Slimane, Giovannangeli, Carine, Luis, Richard, Robin, Philippe, Pritchard, Linda L., Helene, Claude, and Harel-Bellan, Annick
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Nucleotides -- Analysis ,Nucleic acid probes -- Usage ,Science and technology - Abstract
Triple-helix-forming oligonucleotides (TFOs), which can potentially modify target genes irreversibly, represent promising tools for antiviral therapies. However, their effectiveness on endogenous genes has yet to be unambiguously demonstrated. To monitor endogenous gene modification by TFOs in a yeast model, we inactivated an auxotrophic marker gene by inserting target sequences of interest into its coding region. The genetically engineered yeast cells then were treated with psoralen-linked TFOs followed by UV irradiation, thus generating highly mutagenic covalent crosslinks at the target site whose repair could restore gene function; the number of revertants and spectrum of mutations generated were quantified. Results showed that a phosphoramidate TFO indeed reaches its target sequence, forms crosslinks, and generates mutations at the expected site via a triplex-mediated mechanism: (i) under identical conditions, no mutations were generated by the same TFO at two other loci in the target strain, nor in an isogenic control strain carrying a modified target sequence incapable of supporting triple-helix formation; (ii) for a given target sequence, whether the triplex was formed in vivo on an endogenous gene or in vitro on an exogenous plasmid, the nature of the mutations generated was identical, and consistent with the repair of a psoralen crosslink at the target site. Although the mutation efficiency was probably too low for therapeutic applications, our results confirm the validity of the triple-helix approach and provide a means of evaluating the effectiveness of new chemically modified TFOs and analogs. oligonucleotide | psoralen | HIV-1 polypurine tract
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- 2000
48. Erratum: Canonical Wnt signalling regulates nuclear export of Setdb1 during skeletal muscle terminal differentiation
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Beyer, Sophie, primary, Pontis, Julien, additional, Schirwis, Elija, additional, Battisti, Valentine, additional, Rudolf, Anja, additional, Le Grand, Fabien, additional, and Ait-Si-Ali, Slimane, additional
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- 2016
- Full Text
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49. Canonical Wnt signalling regulates nuclear export of Setdb1 during skeletal muscle terminal differentiation
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Beyer, Sophie, primary, Pontis, Julien, additional, Schirwis, Elija, additional, Battisti, Valentine, additional, Rudolf, Anja, additional, Le Grand, Fabien, additional, and Ait-Si-Ali, Slimane, additional
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- 2016
- Full Text
- View/download PDF
50. Unexpected Distinct Roles of the Related Histone H3 Lysine 9 Methyltransferases G9a and G9a-Like Protein in Myoblasts
- Author
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Battisti, Valentine, primary, Pontis, Julien, additional, Boyarchuk, Ekaterina, additional, Fritsch, Lauriane, additional, Robin, Philippe, additional, Ait-Si-Ali, Slimane, additional, and Joliot, Véronique, additional
- Published
- 2016
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