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41 results on '"Ouararhni, Khalid"'

2. Leveraging wastewater surveillance for managing the spread of SARS-CoV-2 and concerned pathogens during FIFA World Cup Qatar 2022

Author

El-Malah, Shimaa S., Saththasivam, Jayaprakash, K, Arun K., Abdul Jabbar, Khadeeja, Gomez, Tricia A., Wahib, Sara, Lawler, Jenny, Tang, Patrick, Mirza, Faheem, Al-Hail, Hamad, Ouararhni, Khalid, Abdul Azis, Thasni K., Abu Raddad, Laith Jamal, Chemaitelly, Hiam S., Abu Halaweh, Hussein A., Khalife, Sara, Bertollini, Roberto, and Mahmoud, Khaled A.

Published
2024
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5. Uncovering a neurological protein signature for severe COVID-19

Author

El-Agnaf, Omar, Bensmail, Ilham, Al-Nesf, Maryam A.Y., Flynn, James, Taylor, Mark, Majbour, Nour K., Abdi, Ilham Y., Vaikath, Nishant N., Farooq, Abdulaziz, Vemulapalli, Praveen B., Schmidt, Frank, Ouararhni, Khalid, Al-Siddiqi, Heba H., Arredouani, Abdelilah, Wijten, Patrick, Al-Maadheed, Mohammed, Mohamed-Ali, Vidya, Decock, Julie, and Abdesselem, Houari B.

Published
2023
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6. Prognostic tools and candidate drugs based on plasma proteomics of patients with severe COVID-19 complications

Author

Al-Nesf, Maryam A. Y., Abdesselem, Houari B., Bensmail, Ilham, Ibrahim, Shahd, Saeed, Walaa A. H., Mohammed, Sara S. I., Razok, Almurtada, Alhussain, Hashim, Aly, Reham M. A., Al Maslamani, Muna, Ouararhni, Khalid, Khatib, Mohamad Y., Hssain, Ali Ait, Omrani, Ali S., Al-Kaabi, Saad, Al Khal, Abdullatif, Al-Thani, Asmaa A., Samsam, Waseem, Farooq, Abdulaziz, Al-Suwaidi, Jassim, Al-Maadheed, Mohammed, Al-Siddiqi, Heba H., Butler, Alexandra E., Decock, Julie V., Mohamed-Ali, Vidya, and Al-Ejeh, Fares

Published
2022
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11. Dual role of histone variant H3.3B in spermatogenesis: positive regulation of piRNA transcription and implication in X-chromosome inactivation

Author

Fontaine, Emeline, primary, Papin, Christophe, additional, Martinez, Guillaume, additional, Le Gras, Stéphanie, additional, Nahed, Roland Abi, additional, Héry, Patrick, additional, Buchou, Thierry, additional, Ouararhni, Khalid, additional, Favier, Bertrand, additional, Gautier, Thierry, additional, Sabir, Jamal S M, additional, Gerard, Matthieu, additional, Bednar, Jan, additional, Arnoult, Christophe, additional, Dimitrov, Stefan, additional, and Hamiche, Ali, additional

Published
2022
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15. ANP32E is a histone chaperone that removes H2A.Z from chromatin

Author

Obri, Arnaud, Ouararhni, Khalid, Papin, Christophe, Diebold, Marie-Laure, Padmanabhan, Kiran, Marek, Martin, Stoll, Isabelle, Roy, Ludovic, Reilly, Patrick T., Mak, Tak W., Dimitrov, Stefan, Romier, Christophe, and Hamiche, Ali

Subjects
Chromatin -- Physiological aspects, Histones -- Physiological aspects, Molecular chaperones -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

H2A.Z is an essential histone variant implicated in the regulation of key nuclear events. However, the metazoan chaperones responsible for H2A.Z deposition and its removal from chromatin remain unknown. Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone. We show that ANP32E is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). The 1.48 Å resolution crystal structure of the complex formed between the ANP32E-ZID and the H2A.Z/H2B dimer and biochemical data support an underlying molecular mechanism for H2A.Z/H2B eviction from the nucleosome and its stabilization by ANP32E through a specific extension of the H2A.Z carboxy-terminal [alpha]-helix. Finally, analysis of H2A.Z localization in ANP32E.sup.-/- cells by chromatin immunoprecipitation followed by sequencing shows genome-wide enrichment, redistribution and accumulation of H2A.Z at specific chromatin control regions, in particular at enhancers and insulators. Human protein ANP32E is a histone chaperone that promotes removal of H2A.Z from chromatin. Chaperoning a histone variant The histone H2A.Z is a variant of histone H2A, one of the canonical histones present in the chromatin of eukaryotic cells. H2A.Z has important functions in transcription and other nuclear processes. Here, Ali Hamiche and colleagues identify the human protein ANP32E as an H2A.Z chaperone capable of promoting the removal of H2A.Z from chromatin. Biochemical and structural data indicate the molecular basis for H2A.Z recognition and eviction by ANP32E, and genome-wide mapping analyses reveal how ANP32E regulates H2A.Z occupancy at important regulatory regions of the genome., Author(s): Arnaud Obri [sup.1] , Khalid Ouararhni [sup.1] , Christophe Papin [sup.1] , Marie-Laure Diebold [sup.2] , Kiran Padmanabhan [sup.3] , Martin Marek [sup.2] , Isabelle Stoll [sup.1] , Ludovic [...]

Published
2014
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16. Age, Disease Severity and Ethnicity Influence Humoral Responses in a Multi-Ethnic COVID-19 Cohort

Author

Smith, Muneerah, primary, Abdesselem, Houari B., additional, Mullins, Michelle, additional, Tan, Ti-Myen, additional, Nel, Andrew J. M., additional, Al-Nesf, Maryam A. Y., additional, Bensmail, Ilham, additional, Majbour, Nour K., additional, Vaikath, Nishant N., additional, Naik, Adviti, additional, Ouararhni, Khalid, additional, Mohamed-Ali, Vidya, additional, Al-Maadheed, Mohammed, additional, Schell, Darien T., additional, Baros-Steyl, Seanantha S., additional, Anuar, Nur D., additional, Ismail, Nur H., additional, Morris, Priscilla E., additional, Mamat, Raja N. R., additional, Rosli, Nurul S. M., additional, Anwar, Arif, additional, Ellan, Kavithambigai, additional, Zain, Rozainanee M., additional, Burgers, Wendy A., additional, Mayne, Elizabeth S., additional, El-Agnaf, Omar M. A., additional, and Blackburn, Jonathan M., additional

Published
2021
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17. Robust prognostic signatures derived from proteomic panel profiling of plasma from patients with severe COVID-19 complications

Author

Al-Nesf, Maryam, primary, Abdesselem, Houari, additional, Bensmail, Ilham, additional, Ibrahim, Shahd, additional, Saeed, Walaa, additional, Mohammed, Sara, additional, Razok, Almurtada, additional, Alhussain, Hashim, additional, Aly, Reham, additional, Maslamani, Muna Al, additional, Ouararhni, Khalid, additional, Khatib, Mohamad, additional, Hssain, Ali Ait, additional, Omrani, Ali, additional, Al-Kaabi, Saad, additional, Khal, Abdullatif Al, additional, Althani, Asma, additional, Samsam, Waseem, additional, Farooq, Abdulaziz, additional, Al-Suwaidi, Jassim, additional, Al-Maadheedh, Mohammed, additional, Al-Siddiqi, Heba, additional, Butler, Alexandra, additional, Decock, Julie, additional, Mohamed-Ali, Vidya, additional, and Al-Ejeh, Fares, additional

Published
2021
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18. The H2A.J histone variant contributes to Interferon-Stimulated Gene expression in senescence by its weak interaction with H1 and the derepression of repeated DNA sequences

Author

Mangelinck, Adele, primary, Coudereau, Clement, additional, Courbeyrette, Regis, additional, Ouararhni, Khalid, additional, Hamiche, Ali, additional, Redon, Christophe E., additional, Bonner, William M., additional, Van Dijk, Erwin, additional, Derbois, Celine, additional, Olaso, Robert, additional, Deleuze, Jean-Francois, additional, Fenaille, Francois, additional, Ruebe, Claudia E., additional, Thuret, Jean-Yves, additional, and MANN, Carl, additional

Published
2020
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19. Transcriptomic Profiling of Tumor-Infiltrating CD4+TIM-3+ T Cells Reveals Their Suppressive, Exhausted, and Metastatic Characteristics in Colorectal Cancer Patients

Author

Sasidharan Nair, Varun, primary, M Toor, Salman, additional, Z Taha, Rowaida, additional, Ahmed, Ayman A, additional, Kurer, Mohamed A, additional, Murshed, Khaled, additional, Soofi, Madiha E, additional, Ouararhni, Khalid, additional, M. Alajez, Nehad, additional, Abu Nada, Mohamed, additional, and Elkord, Eyad, additional

Published
2020
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22. Thymoquinone challenges UHRF1 to commit auto-ubiquitination: a key event for apoptosis induction in cancer cells

Author

Ibrahim, Abdulkhaleg, primary, Alhosin, Mahmoud, additional, Papin, Christophe, additional, Ouararhni, Khalid, additional, Omran, Ziad, additional, Zamzami, Mazin A., additional, Al-Malki, Abdulrahman Labeed, additional, Choudhry, Hani, additional, Mély, Yves, additional, Hamiche, Ali, additional, Mousli, Marc, additional, and Bronner, Christian, additional

Published
2018
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25. H1–nucleosome interactions and their functional implications

Author

Sharma, Abhishek Bharadwaj, Van Dyck, Eric, Razvi, Syed Shoeb, Hasan, Mohammed Nihal, Hassan, Mohammed, Moselhy, Said Salama, Abualnaja, Khalid Omer, Kumosani, Taha Abduallah, Halwani, Majed, Asami, Tadao, Shukla, Manu, Soueidan, Lama, Noirclerc-Savoye, Marjolaine, Le Roy, Aline, Omran, Ziad, Zamzami, Mazin, Al-Malki, Abdulrahman Labeed, Choudhry, Hani, Andronov, Leonid, Michalon, Jonathan, Orlov, Igor, Vonesch, Jean-Luc, Klaholz, Bruno, Richert, Ludovic, Ashraf, Waseem, Alhosin, Mahmoud, Zaayter, Liliyana, Ahmad, Tanveer, Mély, Yves, Mousli, Marc, Garcia-Saez, Isabel, Cutter, Amber, Reymer, Anna, Syed, Sajad, Tonchev, Ognyan, Crucifix, Corinne, Lavery, Richard, Hayes, Jeffrey, Petosa, Carlo, Ibrahim, Abdulkhaleg, Gras, Stéphanie Le, VELT, Amandine, Jost, Bernard, Bronner, Christian, Fromental-Ramain, Catherine, Ramain, Philippe, Ors, Aysegul, Favier, Bertrand, Dalkara, Defne, Ozturk, Mehmet, Naidenov, Mladen, Ramos, Lorrie, Shuaib, Muhammad, Syed, Sajad Hussain, Lone, Imtiaz Nizar, Boopathi, Ramachandran, Fontaine, Emeline, Papai, Gabor, Tachiwana, Hiroaki, Gautier, Thierry, Skoufias, Dimitrios, Padmanabhan, Kiran, Kurumizaka, Hitoshi, Schultz, Patrick, Charles Richard, John Lalith, Shukla, Manu Shubhdarshan, Menoni, Hervé, Lone, Imtiaz Nisar, Roulland, Yohan, Ben Simon, Elsa, Kundu, Tapas, Angelov, Dimitar, Latrick, Chrysa, Marek, Martin, Ouararhni, Khalid, Papin, Christophe, Stoll, Isabelle, Ignatyeva, Maria, Obri, Arnaud, Ennifar, Eric, Romier, Christophe, Bednar, Jan, Hamiche, Ali, Dimitrov, Stefan, Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire de Biologie Moléculaire de la Cellule (LBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Institut de biologie structurale (IBS - UMR 5075 ), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Louis Pasteur - Strasbourg I, Fonctions et dysfonctions épithéliales - UFC (EA 4267) (FDE), Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Laboratoire de Bioimagerie et Pathologies (UMR 7021), Université de Strasbourg (UNISTRA), Laboratoire de Biophotonique et Pharmacologie - UMR 7213 (LBP), Réseau nanophotonique et optique, Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Bioimagerie et Pathologies (LBP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institute for advanced biosciences, Uiversité de Lyon, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de biochimie théorique [Paris] (LBT (UPR_9080)), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Santé de la vigne et qualité du vin (SVQV), Université Louis Pasteur - Strasbourg I-Institut National de la Recherche Agronomique (INRA), Centre Léon Bérard [Lyon], Department of Medical Biology and Genetics, School of Medicine-Dokuz Eylul University, Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), Institut cellule souche et cerveau (U846 Inserm - UCBL1), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris sciences et lettres (PSL), Synchronous programming for the trusted component-based engineering of embedded systems and mission-critical systems (ESPRESSO), Institut de Recherche en Informatique et Systèmes Aléatoires (IRISA), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Inria Rennes – Bretagne Atlantique, Institut National de Recherche en Informatique et en Automatique (Inria), Waseda University, Molecular Biology and Genetics Unit [Bangalore, India] (Transcription and Disease Laboratory), Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR)-Indian Institute of Science, Biologie moléculaire et cellulaire de la différenciation, Université Joseph Fourier - Grenoble 1 (UJF)-Institut Albert Bonniot-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de biologie moléculaire eucaryote (LBME), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Architecture et réactivité de l'ARN (ARN), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Spectrométrie Physique (LSP), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), INSERM U823, équipe 4 (Chromatine et Epigénétique), Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université Louis Pasteur - Strasbourg I-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)-Réseau nanophotonique et optique, Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut National de la Recherche Agronomique (INRA)-Université de Strasbourg (UNISTRA), School of Medicine-Dokuz Eylül Üniversitesi = Dokuz Eylül University [Izmir] (DEÜ), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-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), Centre National de la Recherche Scientifique (CNRS)-Université Louis Pasteur - Strasbourg I, Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Institut de Chimie du CNRS (INC), Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Bioimagerie et Pathologie (LBP), Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7), Institut National de la Recherche Agronomique (INRA)-Université Louis Pasteur - Strasbourg I, Centre National de la Recherche Scientifique (CNRS), Institut cellule souche et cerveau / Stem Cell and Brain Research Institute (SBRI), PSL Research University (PSL), Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC), and Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Histone-modifying enzymes, Molecular Sequence Data, Biophysics, Biochemistry, Histones, 03 medical and health sciences, Structural Biology, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Genetics, Animals, Humans, Nucleosome, Histone code, Amino Acid Sequence, Molecular Biology, ComputingMilieux_MISCELLANEOUS, Chromatin Fiber, 030102 biochemistry & molecular biology, biology, Chromatin Assembly and Disassembly, Linker DNA, Nucleosomes, Chromatin, 030104 developmental biology, Histone, Gene Expression Regulation, Chromatosome, biology.protein
Abstract

Linker histones are three domain proteins and consist of a structured (globular) domain, flanked by two likely non-structured NH2- and COOH-termini. The binding of the linker histones to the nucleosome was characterized by different methods in solution. Apparently, the globular domain interacts with the linker DNA and the nucleosome dyad, while the binding of the large and rich in lysines COOH-terminus results in "closing" the linker DNA of the nucleosome and the formation of the "stem" structure. What is the mode of binding of the linker histones within the chromatin fiber remains still elusive. Nonetheless, it is clear that linker histones are essential for both the assembly and maintenance of the condensed chromatin fiber. Interestingly, linker histones are post-translationally modified and how this affects both their binding to chromatin and functions is now beginning to emerge. In addition, linker histones are highly mobile in vivo, but not in vitro. No explanation of this finding is reported for the moment. The higher mobility of the linker histones should, however, have strong impact on their function. Linker histones plays an important role in gene expression regulation and other chromatin related process and their function is predominantly regulated by their posttranslational modifications. However, the detailed mechanism how the linker histones do function remains still not well understood despite numerous efforts. Here we will summarize and analyze the data on the linker histone binding to the nucleosome and the chromatin fiber and will discuss its functional consequences.

Published
2016

28. The Flexible Ends of CENP-A Nucleosome Are Required for Mitotic Fidelity

Author

Roulland, Yohan, primary, Ouararhni, Khalid, additional, Naidenov, Mladen, additional, Ramos, Lorrie, additional, Shuaib, Muhammad, additional, Syed, Sajad Hussain, additional, Lone, Imtiaz Nizar, additional, Boopathi, Ramachandran, additional, Fontaine, Emeline, additional, Papai, Gabor, additional, Tachiwana, Hiroaki, additional, Gautier, Thierry, additional, Skoufias, Dimitrios, additional, Padmanabhan, Kiran, additional, Bednar, Jan, additional, Kurumizaka, Hitoshi, additional, Schultz, Patrick, additional, Angelov, Dimitar, additional, Hamiche, Ali, additional, and Dimitrov, Stefan, additional

Published
2016
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29. FACT Assists Base Excision Repair by Boosting the Remodeling Activity of RSC

Author

Charles Richard, John Lalith, primary, Shukla, Manu Shubhdarshan, additional, Menoni, Hervé, additional, Ouararhni, Khalid, additional, Lone, Imtiaz Nisar, additional, Roulland, Yohan, additional, Papin, Christophe, additional, Ben Simon, Elsa, additional, Kundu, Tapas, additional, Hamiche, Ali, additional, Angelov, Dimitar, additional, and Dimitrov, Stefan, additional

Published
2016
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36. Trim24 (Tif1α).

Author

Khetchoumian, Konstantin, Teletin, Marius, Tisserand, Johan, Herquel, Benjamin, Ouararhni, Khalid, and Losson, Régine

Published
2008
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37. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.

Author

Dranèc), Pascal, Ouararhni, Khalid, Depaux, Arnaud, Shuaib, Muhammad, and Hamiche, Ali

Subjects
*HISTONES, *CHROMATIN, *DNA replication, *LEUKEMIA, *THALASSEMIA
Abstract

The histone variant H3.3 marks active chromatin by replacing the conventional histone H3.1. In this study, we investigate the detailed mechanism of H3.3 replication-independent deposition. We found that the death domain-associated protein DAXX and the chromatin remodeling factor ATRX (α-thalassemia/mental retardation syndrome protein) are specifically associated with the H3.3 deposition machinery. Bacterially expressed DAXX has a marked binding preference for H3.3 and assists the deposition of (H3.3-H4)2 tetramers on naked DNA, thus showing that DAXX is a H3.3 histone chaperone. In DAXX-depleted cells, a fraction of H3.3 was found associated with the replication-dependent machinery of deposition, suggesting that cells adapt to the depletion. The reintroduced DAXX in these cells colocalizes with H3.3 into the promyelocytic leukemia protein (PML) bodies. Moreover, DAXX associates with pericentric DNA repeats, and modulates the transcription from these repeats through assembly of H3.3 nucleosomes. These findings establish a new link between the PML bodies and the regulation of pericentric DNA repeat chromatin structure. Taken together, our data demonstrate that DAXX functions as a bona fide histone chaperone involved in the replication-independent deposition of H3.3. [ABSTRACT FROM AUTHOR]

Published
2010
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38. Pembrolizumab Interferes with the Differentiation of Human FOXP3+-Induced T Regulatory Cells, but Not with FOXP3 Stability, through Activation of mTOR.

Author

Nair, Varun Sasidharan, Toor, Salman M., Taouk, Ghina, Pfister, Gerald, Ouararhni, Khalid, Alajez, Nehad M., and Elkord, Eyad

Subjects
*SUPPRESSOR cells, *PEMBROLIZUMAB, *DNA repair, *TUMOR microenvironment, *PROGRAMMED cell death 1 receptors
Abstract

Programmed cell death 1 (PD-1) is critical for T regulatory cells (Tregs) to maintain peripheral tolerance to self-antigens. In the tumor microenvironment, interaction between PD-1 and its ligands supports tumor immune evasion. Pembrolizumab blocks interactions of PD-1 with its ligands, enhancing antitumor and clinical responses. We and others have reported that pembrolizumab does not affect function or phenotype of thymic-derived Tregs; however, little is known about its effect on extrathymic differentiation of peripheral Tregs. In this study, we investigated the effect of pembrolizumab on in vitro-induced Tregs (iTregs). Our work showed that PD-1 blockade interferes with iTreg differentiation and has no potential effect on the stability of FOXP3 after differentiation. Additionally, we found that both nontreated and pembrolizumab-treated iTregs were suppressive. However, pembrolizumab-treated iTregs were relatively less suppressive in higher Treg ratios and failed to produce IL-10 compared with their nontreated counterparts. Different methods including transcriptomic analyses confirmed that the downregulation of FOXP3 was mediated by activating mTOR and STAT1 and inhibiting MAPK pathways, shifting the iTreg polarization in favor of Th1 and Th17 subsets. To confirm the role of mTOR activation, we found that rapamycin diminished the effect of pembrolizumab-mediated downregulation of FOXP3. Ingenuity pathway analysis revealed that pembrolizumab-treated iTregs showed upregulation of genes promoting DNA repair and immune cell trafficking, in addition to downregulation of genes supporting cellular assembly and organization. To our knowledge, this is the first study to show that pembrolizumab interferes with differentiation of human FOXP3+ iTregs and to disclose some of the molecular pathways involved. [ABSTRACT FROM AUTHOR]

Published
2020
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39. Transcriptomic Profiling of Tumor-Infiltrating CD4 + TIM-3 + T Cells Reveals Their Suppressive, Exhausted, and Metastatic Characteristics in Colorectal Cancer Patients.

Author

Sasidharan Nair V, Toor SM, Taha RZ, Ahmed AA, Kurer MA, Murshed K, Soofi ME, Ouararhni K, Alajez NM, Abu Nada M, and Elkord E

Abstract

T cell immunoglobulin mucin-3 (TIM-3) is an immune checkpoint identified as one of the key players in regulating T-cell responses. Studies have shown that TIM-3 is upregulated in the tumor microenvironment (TME). However, the precise role of TIM-3 in colorectal cancer (CRC) TME is yet to be elucidated. We performed phenotypic and molecular characterization of TIM-3 + T cells in the TME and circulation of CRC patients by analyzing tumor tissues (TT, TILs), normal tissues (NT, NILs), and peripheral blood mononuclear cells (PBMC). TIM-3 was upregulated on both CD4 + and CD3 + CD4 - (CD8 + ) TILs. CD4 + TIM-3 + TILs expressed higher levels of T regulatory cell (Tregs)-signature genes, including FoxP3 and Helios, compared with their TIM-3 - counterparts. Transcriptomic and ingenuity pathway analyses showed that TIM-3 potentially activates inflammatory and tumor metastatic pathways. Moreover, NF-κB-mediated transcription factors were upregulated in CD4 + TIM-3 + TILs, which could favor proliferation/invasion and induce inflammatory and T-cell exhaustion pathways. In addition, we found that CD4 + TIM-3 + TILs potentially support tumor invasion and metastasis, compared with conventional CD4 + CD25 + Tregs in the CRC TME. However, functional studies are warranted to support these findings. In conclusion, this study discloses some of the functional pathways of TIM-3 + TILs, which could improve their targeting in more specific therapeutic approaches in CRC patients., Competing Interests: The authors declare no conflicts of interest.

Published
2020
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40. Pembrolizumab Interferes with the Differentiation of Human FOXP3 + -Induced T Regulatory Cells, but Not with FOXP3 Stability, through Activation of mTOR.

Author

Sasidharan Nair V, Toor SM, Taouk G, Pfister G, Ouararhni K, Alajez NM, and Elkord E

Subjects
Cell Differentiation drug effects, Cell Differentiation immunology, Demethylation drug effects, Forkhead Transcription Factors immunology, Healthy Volunteers, Humans, Protein Stability drug effects, T-Lymphocytes, Regulatory immunology, Up-Regulation drug effects, Antibodies, Monoclonal, Humanized pharmacology, Antineoplastic Agents, Immunological pharmacology, Forkhead Transcription Factors antagonists & inhibitors, T-Lymphocytes, Regulatory drug effects, TOR Serine-Threonine Kinases immunology
Abstract

Programmed cell death 1 (PD-1) is critical for T regulatory cells (Tregs) to maintain peripheral tolerance to self-antigens. In the tumor microenvironment, interaction between PD-1 and its ligands supports tumor immune evasion. Pembrolizumab blocks interactions of PD-1 with its ligands, enhancing antitumor and clinical responses. We and others have reported that pembrolizumab does not affect function or phenotype of thymic-derived Tregs; however, little is known about its effect on extrathymic differentiation of peripheral Tregs. In this study, we investigated the effect of pembrolizumab on in vitro-induced Tregs (iTregs). Our work showed that PD-1 blockade interferes with iTreg differentiation and has no potential effect on the stability of FOXP3 after differentiation. Additionally, we found that both nontreated and pembrolizumab-treated iTregs were suppressive. However, pembrolizumab-treated iTregs were relatively less suppressive in higher Treg ratios and failed to produce IL-10 compared with their nontreated counterparts. Different methods including transcriptomic analyses confirmed that the downregulation of FOXP3 was mediated by activating mTOR and STAT1 and inhibiting MAPK pathways, shifting the iTreg polarization in favor of Th1 and Th17 subsets. To confirm the role of mTOR activation, we found that rapamycin diminished the effect of pembrolizumab-mediated downregulation of FOXP3. Ingenuity pathway analysis revealed that pembrolizumab-treated iTregs showed upregulation of genes promoting DNA repair and immune cell trafficking, in addition to downregulation of genes supporting cellular assembly and organization. To our knowledge, this is the first study to show that pembrolizumab interferes with differentiation of human FOXP3 + iTregs and to disclose some of the molecular pathways involved., (Copyright © 2019 by The American Association of Immunologists, Inc.)

Published
2020
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41. Trim24 (Tif1 alpha): an essential 'brake' for retinoic acid-induced transcription to prevent liver cancer.

Author

Khetchoumian K, Teletin M, Tisserand J, Herquel B, Ouararhni K, and Losson R

Subjects
Aging drug effects, Aging metabolism, Aging pathology, Animals, Cell Proliferation drug effects, Hepatocytes cytology, Hepatocytes drug effects, Hepatocytes metabolism, Homeostasis drug effects, Mice, Nuclear Proteins deficiency, Phenotype, Polyploidy, Receptors, Retinoic Acid metabolism, Retinoic Acid Receptor alpha, Transcription Factors deficiency, Liver Neoplasms genetics, Liver Neoplasms prevention & control, Nuclear Proteins metabolism, Transcription Factors metabolism, Transcription, Genetic drug effects, Tretinoin pharmacology
Abstract

Retinoic acid (RA), the active derivative of vitamin A, is an important signaling molecule that controls various developmental processes and influence the proliferation and differentiation of a variety of cell types. RA exerts its biological functions primarily through binding to and activating nuclear RA receptors (RARs, which include the RAR alpha, beta and gamma isotypes RARA, RARB and RARC). Aberrant expression or impaired function of these nuclear receptors has been linked to diverse types of cancer. RARs are RA-dependent transcription factors that regulate gene expression through the recruitment of different co-regulators (co-activators and co-repressors). TRIM24 (formerly known as TIF1 alpha) was among the first co-regulators identified as interacting with RARs in a ligand-dependent fashion, and it was recently shown to function in mice as a potent liver-specific tumor suppressor by attenuating Rara-mediated transcription. The fact that Trim24(-/-), but not Trim24(-/-)Rara(+/-), mutant mice are highly predisposed to the development of hepatocellular carcinoma (HCC) has significant implications in cancer research. This result, along with the observation that in response to pharmacological inhibition of the RA signaling, hepatocytes lacking Trim24 loose their ability to proliferate, strongly implicates Rara as a proto-oncogene in hepatocytes and demonstrates that overactivated RA signaling is deleterious to liver homeostasis.

Published
2008
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