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167 results on '"Pflieger, Delphine"'

2. A bivalent histone mark reader, AtDEK2 governs plant immunity

Author

Rayapuram, Naganand, primary, Alhoraibi, Hanna, additional, Alejandro-Martinez, Santiago, additional, Latrasse, David, additional, Mandal, Papita, additional, Faivre, Lea, additional, He, Xiaoning, additional, Mianza, Déborah Manza, additional, Abulfaraj, Aala, additional, Alhrabi, Siba, additional, Mariappan, Kiruthiga, additional, Artyukh, Olga, additional, Abdulhakim, Fatimah, additional, Aljedaani, Fatimah, additional, David, Stephan, additional, Almeida-Trapp, Marilia, additional, Bigeard, Jean, additional, Pflieger, Delphine, additional, Fischle, Wolfgang, additional, Arold, Stefan, additional, Colcombet, Jean, additional, Schubert, Daniel, additional, Benhamed, Moussa, additional, Blilou, Ikram, additional, and Hirt, Heribert, additional

Published
2024
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3. Microenvironment of metastatic site reveals key predictors of PD-1 blockade response in renal cell carcinoma

Author

Jeanneret, Florian, primary, Bazelle, Pauline, additional, Schoch, Sarah, additional, Pillet, Catherine, additional, Um, In Hwa, additional, Bouzit, Assilah, additional, Evrard, Bertrand, additional, Seffar, Evan, additional, Chalmel, Frederic, additional, Alfaro, Javier A, additional, Pesquita, Catia, additional, Zanzotto, Fabio Massimo, additional, Stares, Mark, additional, Symeonides, Stefan N, additional, Laird, Alexander, additional, Long, Jean-Alexandre, additional, Descotes, Jean Luc, additional, Pflieger, Delphine, additional, Harrison, David J, additional, Filhol, Odile, additional, Axelson, Hakan, additional, and Battail, Christophe, additional

Published
2023
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5. The histone methyltransferase DOT1L regulates chromatin reorganization and gene expression during the postmeiotic differentiation of male germ cells

Author

Blanco, Mélina, Khattabi, Laila El, Gobé, Clara, Crespo, Marion, Coulée, Manon, de la Iglesia, Alberto, Ialy-Radio, Côme, Lapoujade, Clementine, Givelet, Maëlle, Delessard, Marion, Seller-Corona, Ivan, Yamaguchi, Kosuke, Vernet, Nadège, van Leeuwen, Fred, Lermine, Alban, Okada, Yuki, Daveau, Romain, Oliva, Rafael, Fouchet, Pierre, Ziyyat, Ahmed, Pflieger, Delphine, Cocquet, Julie, Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), CHU Trousseau [APHP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), BioSanté (UMR BioSanté), Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-Université Grenoble Alpes (UGA), Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Universitat de Barcelona (UB), Institut de Radiobiologie Cellulaire et Moléculaire (IRCM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, The University of Tokyo (UTokyo), 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), Netherlands Cancer Institute (NKI), Antoni van Leeuwenhoek Hospital, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Hôpital Cochin [AP-HP], ANR-17-CE12-0004,CHROMATOZOA,(Dé)régulation génique et chromatinienne pendant la spermiogénèse: acteurs & conséquences sur la descendance(2017), ANR-10-INBS-0008,ProFI,Infrastructure Française de Protéomique(2010), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), PFLIEGER, Delphine, (Dé)régulation génique et chromatinienne pendant la spermiogénèse: acteurs & conséquences sur la descendance - - CHROMATOZOA2017 - ANR-17-CE12-0004 - AAPG2017 - VALID, Infrastructure Française de Protéomique - - ProFI2010 - ANR-10-INBS-0008 - INBS - VALID, and CBH-EUR-GS - - CBH-EUR-GS2017 - ANR-17-EURE-0003 - EURE - VALID

Subjects
histone-to-protamine replacement, chromatin compaction, flagellum development, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], DOT1L, H3K79 methylation, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], gene regulation, [SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], spermatogenesis, [SDV.BDD.GAM]Life Sciences [q-bio]/Development Biology/Gametogenesis
Abstract

International audience; Spermatozoa have a unique genome organization: their chromatin is almost completely devoid of histones and is formed instead of protamines which confer a higher level of compaction than nucleosomes and preserve paternal genome integrity until fertilization. Histone-to-protamine transition takes place in postmeiotic male germ cells called spermatids, and is indispensable for the production of functional spermatozoa and thus for male fertility. Here we show that the H3K79 (histone 3 lysine 79) methyltransferase DOT1L controls spermatid chromatin remodelling and subsequent reorganization and compaction of spermatozoon genome. Using a mouse model in which Dot1l is knocked-out in adult male germ cells, we found that the chromatin of Dot1l -knockout (KO) spermatozoa is less compact and characterized by a higher level of retained histones and of immature forms of protamine 2. Proteomic analyses performed on differentiating male germ cells reveal that Dot1l KO extensively modifies the spermatid chromatin prior to histone removal. By transcriptomics, we also show that Dot1l KO deregulates the expression of ~1500 genes, many of which are involved in other essential aspects of spermatid differentiation such as flagellum formation. As a consequence of all these chromatin and gene expression defects, Dot1l -KO spermatozoa have misshapen and less compact heads, and are less motile, which results in impaired fertility.

Published
2023

6. DOT1L regulates chromatin reorganization and gene expression during sperm differentiation

Author

Blanco, Mélina, primary, El Khattabi, Laila, additional, Gobé, Clara, additional, Crespo, Marion, additional, Coulée, Manon, additional, de la Iglesia, Alberto, additional, Ialy‐Radio, Côme, additional, Lapoujade, Clementine, additional, Givelet, Maëlle, additional, Delessard, Marion, additional, Seller‐Corona, Ivan, additional, Yamaguchi, Kosuke, additional, Vernet, Nadège, additional, Van Leeuwen, Fred, additional, Lermine, Alban, additional, Okada, Yuki, additional, Daveau, Romain, additional, Oliva, Rafael, additional, Fouchet, Pierre, additional, Ziyyat, Ahmed, additional, Pflieger, Delphine, additional, and Cocquet, Julie, additional

Published
2023
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7. The histone methyltransferase DOT1L regulates chromatin reorganization and gene expression during the postmeiotic differentiation of male germ cells

Author

Blanco, Mélina, primary, Khattabi, Laila El, additional, Gobé, Clara, additional, Crespo, Marion, additional, Coulée, Manon, additional, de la Iglesia, Alberto, additional, Ialy-Radio, Côme, additional, Lapoujade, Clementine, additional, Givelet, Maëlle, additional, Delessard, Marion, additional, Seller-Corona, Ivan, additional, Yamaguchi, Kosuke, additional, Vernet, Nadège, additional, Van Leeuwen, Fred, additional, Lermine, Alban, additional, Okada, Yuki, additional, Daveau, Romain, additional, Oliva, Rafael, additional, Fouchet, Pierre, additional, Ziyyat, Ahmed, additional, Pflieger, Delphine, additional, and Cocquet, Julie, additional

Published
2022
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9. Analysis of the Arabidopsiscoilinmutant reveals a positive role of AtCOILIN in plant immunity

Author

Abulfaraj, Aala A, primary, Alhoraibi, Hanna M, additional, Mariappan, Kiruthiga, additional, Bigeard, Jean, additional, Zhang, Huoming, additional, Almeida-Trapp, Marilia, additional, Artyukh, Olga, additional, Abdulhakim, Fatimah, additional, Parween, Sabiha, additional, Pflieger, Delphine, additional, Blilou, Ikram, additional, Hirt, Heribert, additional, and Rayapuram, Naganand, additional

Published
2022
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12. Chromatin phosphoproteomics unravels a function for AT-hook motif nuclear localized protein AHL13 in PAMP-triggered immunity

Author

Agence Nationale de la Recherche (France), Centre Européen de Recherche en Biologie et en Médecine (France), King Abdullah University of Science and Technology, Institute of Plant Sciences Paris-Saclay, Rayapuram, Naganand, Jarad, Mai, Alhoraibi, Hanna M., Bigeard, Jean, Abulfaraj, Aala A., Völz, Ronny, Gayathri Mariappan, Kiruthiga, Almeida-Trapp, Marilia, Schlöffel, Maria, Lastrucci, Emmanuelle, Bonhomme, Ludovic, Gust, Andrea A., Mithöfer, Axel, Arold, Stefan T., Pflieger, Delphine, Hirt, Heribert, Agence Nationale de la Recherche (France), Centre Européen de Recherche en Biologie et en Médecine (France), King Abdullah University of Science and Technology, Institute of Plant Sciences Paris-Saclay, Rayapuram, Naganand, Jarad, Mai, Alhoraibi, Hanna M., Bigeard, Jean, Abulfaraj, Aala A., Völz, Ronny, Gayathri Mariappan, Kiruthiga, Almeida-Trapp, Marilia, Schlöffel, Maria, Lastrucci, Emmanuelle, Bonhomme, Ludovic, Gust, Andrea A., Mithöfer, Axel, Arold, Stefan T., Pflieger, Delphine, and Hirt, Heribert

Abstract

In many eukaryotic systems during immune responses, mitogen-activated protein kinases (MAPKs) link cytoplasmic signaling to chromatin events by targeting transcription factors, chromatin remodeling complexes, and the RNA polymerase machinery. So far, knowledge on these events is scarce in plants and no attempts have been made to focus on phosphorylation events of chromatin-associated proteins. Here we carried out chromatin phosphoproteomics upon elicitor-induced activation of Arabidopsis. The events in WT were compared with those in mpk3, mpk4, and mpk6 mutant plants to decipher specific MAPK targets. Our study highlights distinct signaling networks involving MPK3, MPK4, and MPK6 in chromatin organization and modification, as well as in RNA transcription and processing. Among the chromatin targets, we characterized the AT-hook motif containing nuclear localized (AHL) DNA-binding protein AHL13 as a substrate of immune MAPKs. AHL13 knockout mutant plants are compromised in pathogen-associated molecular pattern (PAMP)-induced reactive oxygen species production, expression of defense genes, and PAMP-triggered immunity. Transcriptome analysis revealed that AHL13 regulates key factors of jasmonic acid biosynthesis and signaling and affects immunity toward Pseudomonas syringae and Botrytis cinerea pathogens. Mutational analysis of the phosphorylation sites of AHL13 demonstrated that phosphorylation regulates AHL13 protein stability and thereby its immune functions.

Published
2021

14. Additional file 3 of Systematic genetic and proteomic screens during gametogenesis identify H2BK34 methylation as an evolutionary conserved meiotic mark

Author

Crespo, Marion, Luense, Lacey J., Arlotto, Marie, Jialei Hu, Dorsey, Jean, Encar García-Oliver, Parisha P. Shah, Pflieger, Delphine, Berger, Shelley L., and Govin, Jérôme

Abstract

Additional file 3. MS/MS spectra of the modified histone tryptic peptides identified during yeast sporulation.

Published
2020
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15. Additional file 1 of Systematic genetic and proteomic screens during gametogenesis identify H2BK34 methylation as an evolutionary conserved meiotic mark

Author

Crespo, Marion, Luense, Lacey J., Arlotto, Marie, Jialei Hu, Dorsey, Jean, Encar García-Oliver, Parisha P. Shah, Pflieger, Delphine, Berger, Shelley L., and Govin, Jérôme

Subjects
ComputingMethodologies_DOCUMENTANDTEXTPROCESSING, ComputingMilieux_COMPUTERSANDEDUCATION, Data_FILES, ComputerApplications_COMPUTERSINOTHERSYSTEMS
Abstract

Additional file 1. Supplementary Figures and Tables.

Published
2020
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16. Systematic quantitative analysis of H2A and H2B variants by targeted proteomics

Author

El Kennani, Sara, Adrait, Annie, Permiakova, Olga, Hesse, Anne-Marie, Ialy-Radio, Côme, Ferro, Myriam, Brun, Virginie, Cocquet, Julie, Govin, Jérôme, Pflieger, Delphine, Etude de la dynamique des protéomes (EDyP ), Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-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)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), This work was supported by CEA by a PhD fellowship to SEK, by the Fondd’Intervention of the Univ. Grenoble Alpes (to JG), the French NationalResearch Agency (ANR-11-PDOC-0011 EpiGam to JG, ANR-14-CE19-0014-01 toDP, ANR-12-JSV2-0005-01 to JC, ANR-10-INBS-08 ProFI and ANR-10-LABX-49-01GRAL) and the European Union FP7 Marie Curie Action 'Career IntegrationGrant' (304003 to JG), BMC, BMC, Etude de la dynamique des protéomes (EDyP), 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)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)

Subjects
Male, Proteomics, SRM, lcsh:QH426-470, [SDV]Life Sciences [q-bio], PRM, Mass Spectrometry, Epigenesis, Genetic, Histones, Mice, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Testis, Animals, Humans, Amino Acid Sequence, Spermatogenesis, Targeted proteomics, ComputingMilieux_MISCELLANEOUS, Histone variants, Methodology, Chromatin, [SDV] Life Sciences [q-bio], lcsh:Genetics, Organ Specificity, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Peptides
Abstract

Background Histones organize DNA into chromatin through a variety of processes. Among them, a vast diversity of histone variants can be incorporated into chromatin and finely modulate its organization and functionality. Classically, the study of histone variants has largely relied on antibody-based assays. However, antibodies have a limited efficiency to discriminate between highly similar histone variants. Results In this study, we established a mass spectrometry-based analysis to address this challenge. We developed a targeted proteomics method, using selected reaction monitoring or parallel reaction monitoring, to quantify a maximum number of histone variants in a single multiplexed assay, even when histones are present in a crude extract. This strategy was developed on H2A and H2B variants, using 55 peptides corresponding to 25 different histone sequences, among which a few differ by a single amino acid. The methodology was then applied to mouse testis extracts in which almost all histone variants are expressed. It confirmed the abundance profiles of several testis-specific histones during successive stages of spermatogenesis and the existence of predicted H2A.L.1 isoforms. This methodology was also used to explore the over-expression pattern of H2A.L.1 isoforms in a mouse model of male infertility. Conclusions Our results demonstrate that targeted proteomics is a powerful method to quantify highly similar histone variants and isoforms. The developed method can be easily transposed to the study of human histone variants, whose abundance can be deregulated in various diseases. Electronic supplementary material The online version of this article (10.1186/s13072-017-0172-y) contains supplementary material, which is available to authorized users.

Published
2018

17. A thiol peroxidase is an H(sub)2O(sub)2 receptor and redox-transducer in gene activation

Author

Delaunay, Agnes, Pflieger, Delphine, Barrault, Marie-Benedicte, Vinh, Joelle, and Toledano, Michel B.

Subjects
Brewer's yeast -- Physiological aspects, Cellular signal transduction -- Physiological aspects, Oxidation-reduction reaction -- Analysis, Enzyme activation -- Physiological aspects, Biological sciences
Abstract

Research demonstrates that the thiol peroxidase Gpx3 is the hydrogenperoxide sensor that catalyzes transcription factor Yap1 oxidation in the process of its conversion to activated regulator in Saccharomyces cerevisiae. Data suggest that glutathione peroxidase Gpx functions as a redox-signaling function and a hydroperoxide receptor.

Published
2002

18. Systematic identification of mitochondrial proteins by LC--MS/MS

Author

Pflieger, Delphine, Le Caer, Jean-Pierre, Lemaire, Claire, Bernard, Bruno Alain, Dujardin, Genevieve, and Rossier, Jean

Subjects
Chemistry, Analytic -- Research, Mitochondria -- Research, Gel electrophoresis -- Research, Chemistry
Abstract

In eukaryotic cells, the mitochondrion is the key organelle for cellular respiration. Mitochondrial proteome analysis is difficult to perform by the classical proteomic approach involving two-dimensional gel electrophoresis (2DE), because this organelle contains a large number of membrane-associated and highly alkaline proteins usually requiting specific treatments to be successfully analyzed. Here, an alternative approach was evaluated and led to the rapid and sensitive identification of ~35% of the yeast mitochondrial proteins. It consists of an SDS-PAGE gel electrophoresis of the total mitochondrial protein in combination with the LC-MS/MS analysis of the digestion products of gel slices. The use of only 40 [micro]g of mitochondrial protein enabled the identification of 179 different gene products divided into similar proportions of membrane and soluble proteins. The distribution of the identified proteins in terms of pi and hydrophobicity revealed that the present analytical strategy is largely unbiased. The identification of 28 proteins of previously unknown sub-cellular localization demonstrated the ability of SDSPAGE-LC-MS/MS to rapidly supplement the knowledge of the mitochondrial proteome.

Published
2002

20. Multi-omic analysis of gametogenesis reveals a novel signature at the promoters and distal enhancers of active genes

Author

Crespo, Marion, primary, Damont, Annelaure, primary, Blanco, Melina, primary, Lastrucci, Emmanuelle, primary, Kennani, Sara El, primary, Ialy-Radio, Côme, primary, Khattabi, Laila El, primary, Terrier, Samuel, primary, Louwagie, Mathilde, primary, Kieffer-Jaquinod, Sylvie, primary, Hesse, Anne-Marie, primary, Bruley, Christophe, primary, Chantalat, Sophie, primary, Govin, Jérôme, primary, Fenaille, François, primary, Battail, Christophe, primary, Cocquet, Julie, primary, and Pflieger, Delphine, primary

Published
2020
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22. Quantitative phosphoproteomic analysis reveals shared and specific targets of Arabidopsis MAPkinases MPK3, MPK4 and MPK6 in the cytoplasm and in the nucleus

Author

Rayapuram, N., Bigeard, Jean, Alhoraibi, H., Abulfaraj, A., Volz, R., Hesse, A.M., Lastrucci, E., Vinh, J., Bonhomme, Ludovic, Hirt, Heribert, Pflieger, Delphine, Center for Desert Agriculture, King Abdullah University of Science and Technology (KAUST), Institut des Sciences des Plantes de Paris-Saclay (IPS2 (UMR_9213 / UMR_1403)), Institut National de la Recherche Agronomique (INRA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11), King Abdulaziz University, Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)-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), Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS), SMBP, Ecole Supérieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI ParisTech), Génétique Diversité et Ecophysiologie des Céréales (GDEC), Institut National de la Recherche Agronomique (INRA)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP), CEA, Institut National de la Recherche Agronomique (INRA)-Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Institut National de la Recherche Agronomique (INRA), and Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])

Subjects
nut, arabidopsis, noyau, cytoplasme, [SDV]Life Sciences [q-bio], [SDE]Environmental Sciences, cytoplasm, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, ComputingMilieux_MISCELLANEOUS
Abstract

Quantitative phosphoproteomic analysis reveals shared and specific targets of Arabidopsis MAPkinases MPK3, MPK4 and MPK6 in the cytoplasm and in the nucleus. 35. SFEAP Congress

Published
2018

23. Proteomic Analysis of Histone Variants and Their PTMs: Strategies and Pitfalls

Author

El Kennani, Sara, Crespo, Marion, Govin, Jérôme, Pflieger, Delphine, Etude de la dynamique des protéomes (EDyP ), Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), 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)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
computational tools, [SDV]Life Sciences [q-bio], post-translational modifications, lcsh:QR1-502, Review, bottom-up analysis, histone variants, lcsh:Microbiology, ComputingMilieux_MISCELLANEOUS, mass spectrometry, crosstalk
Abstract

Epigenetic modifications contribute to the determination of cell fate and differentiation. The molecular mechanisms underlying histone variants and post-translational modifications (PTMs) have been studied in the contexts of development, differentiation, and disease. Antibody-based assays have classically been used to target PTMs, but these approaches fail to reveal combinatorial patterns of modifications. In addition, some histone variants are so similar to canonical histones that antibodies have difficulty distinguishing between these isoforms. Mass spectrometry (MS) has progressively developed as a powerful technology for the study of histone variants and their PTMs. Indeed, MS analyses highlighted exquisitely complex combinations of PTMs, suggesting “crosstalk” between them, and also revealed that PTM patterns are often variant-specific. Even though the sensitivity and acquisition speed of MS instruments have considerably increased alongside the development of computational tools for the study of multiple PTMs, it remains challenging to correctly describe the landscape of histone PTMs, and in particular to confidently assign modifications to specific amino acids. Here, we provide an inventory of MS-based strategies and of the pitfalls inherent to histone PTM and variant characterization, while stressing the complex interplay between PTMs and histone sequence variations. We will particularly illustrate the roles played by MS-based analyses in identifying and quantifying histone variants and modifications.

Published
2018

24. MOESM6 of Systematic quantitative analysis of H2A and H2B variants by targeted proteomics

Author

Kennani, Sara El, Adrait, Annie, Permiakova, Olga, Hesse, Anne-Marie, Ialy-Radio, Côme, Ferro, Myriam, Brun, Virginie, Cocquet, Julie, Govin, Jérôme, and Pflieger, Delphine

Abstract

Additional file 6. Reproducibility of the LC-SRM analysis. R² values are indicated for each technical replicate with increasing matrix amounts or increasing standard peptide amounts. Plotted data are presented in Fig. 5.

Published
2018
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25. Hepatitis C virus core protein targets 4E-BP1 expression and phosphorylation and potentiates Myc-induced liver carcinogenesis in transgenic mice

Author

Abdallah, Cosette, Lejamtel, Charlène, Benzoubir, Nassima, Battaglia, Serena, Sidahmed-Adrar, Nazha, Desterke, Christophe, Lemasson, Matthieu, Rosenberg, Arielle R., Samuel, Didier, Bréchot, Christian, Pflieger, Delphine, Le Naour, François, Bourgeade, Marie-Françoise, Agroécologie [Dijon], Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement (LAMBE - UMR 8587), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Pathogénèse et traitement de l'hépatite fulminante et du cancer du foie, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut André Lwoff, Unité de service de l'Institut André Lwoff (US 33 Inserm), AP-HP Hôpital Paul Brousse [Paris]-Institut André Lwoff [Villejuif] (IAL), Virologie de l'hépatite C (EA 4474), Université Paris Descartes - Paris 5 (UPD5), Centre hépato-biliaire (CHB), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM), Agence Universitaire de la Francophonie (AUF), Physiopathologie et traitement des maladies du foie, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AP-HP Hôpital Paul Brousse, Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université d'Évry-Val-d'Essonne (UEVE)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine, Université Paris-Sud - Paris 11 (UP11)-Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement (LAMBE), Université Paris-Seine-Université Paris-Seine-Université d'Évry-Val-d'Essonne (UEVE)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Saclay (COmUE), Unité mixte de service UMS33 [Institut André Lwoff] (UMS33 Inserm/IAL), Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut André Lwoff [Villejuif] (IAL), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM), Etude de la dynamique des protéomes (EDyP ), Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-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)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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), Hôpital Paul Brousse-Institut André Lwoff [Villejuif] (IAL), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Hôpital Paul Brousse-Université Paris-Sud - Paris 11 (UP11)

Subjects
mitogen activated protein kinase p38, host cell, gene amplification, complementary DNA, animal cell, SILAC, initiation factor 4E binding protein 1, vimentin, hepatocellular carcinoma cell line, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Huh-7 cell line, membrane protein, insulin receptor, 4E-BP1 phosphorylation, Hermes antigen, quantitative analysis, Hepatitis C virus, liver cell, virus diseases, phosphoproteomics, hepatocellular carcinoma, unclassified drug, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, tumor growth, liver carcinogenesis, protein transport, transcription regulation, signal transduction, in vitro study, animal experiment, [SDV.CAN]Life Sciences [q-bio]/Cancer, Article, cancer growth, animal tissue, in vivo study, HCV core, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], core protein, controlled study, human, protein expression, mouse, nonhuman, protein MTA1, RNA translation, animal model, human cell, intracellular signaling, [SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, digestive system diseases, protein phosphorylation, transgenic mouse, validation process, initiation factor 4E, Myc protein, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], upregulation
Abstract

International audience; Hepatitis C virus (HCV) is a leading cause of liver diseases including the development of hepatocellular carcinoma (HCC). Particularly, core protein has been involved in HCV-related liver pathologies. However, the impact of HCV core on signaling pathways supporting the genesis of HCC remains largely elusive. To decipher the host cell signaling pathways involved in the oncogenic potential of HCV core, a global quantitative phosphoproteomic approach was carried out. This study shed light on novel differentially phosphorylated proteins, in particular several components involved in translation. Among the eukaryotic initiation factors that govern the translational machinery, 4E-BP1 represents a master regulator of protein synthesis that is associated with the development and progression of cancers due to its ability to increase protein expression of oncogenic pathways. Enhanced levels of 4E-BP1 in non-modified and phosphorylated forms were validated in human hepatoma cells and in mouse primary hepatocytes expressing HCV core, in the livers of HCV core transgenic mice as well as in HCV-infected human primary hepatocytes. The contribution of HCV core in carcinogenesis and the status of 4E-BP1 expression and phosphorylation were studied in HCV core/ Myc double transgenic mice. HCV core increased the levels of 4E-BP1 expression and phosphorylation and significantly accelerated the onset of Myc-induced tumorigenesis in these double transgenic mice. These results reveal a novel function of HCV core in liver carcinogenesis potentiation. They position 4E-BP1 as a tumor-specific target of HCV core and support the involvement of the 4E-BP1/eIF4E axis in hepatocarcinogenesis.

Published
2017

26. The Trihelix transcription factor GT2-like 1 (GTL1) promotes salicylic acid metabolism, and regulates bacterial-triggered immunity

Author

Völz, Ronny, primary, Kim, Soon-Kap, additional, Mi, Jianing, additional, Mariappan, Kiruthiga G., additional, Guo, Xiujie, additional, Bigeard, Jean, additional, Alejandro, Santiago, additional, Pflieger, Delphine, additional, Rayapuram, Naganand, additional, Al-Babili, Salim, additional, and Hirt, Heribert, additional

Published
2018
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30. Proteomic and phosphoproteomic analyses of chromatin-associated proteins from Arabidopsis thaliana

Author

Bigeard, Jean, Rayapuram, Naganand, Bonhomme, Ludovic, Hirt, Heribert, Pflieger, Delphine, Unité de recherche en génomique végétale (URGV), Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Recherche Agronomique (INRA), Spectroscopie, Modélisation, Interfaces pour L'Environnement et la Santé (SMiLES), Laboratoire de Chimie de la Matière Condensée de Paris (LCMCP), Université Pierre et Marie Curie - Paris 6 (UPMC)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement (LAMBE - UMR 8587), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Cergy Pontoise (UCP), and Université Paris-Seine-Université Paris-Seine-Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
Arabidopsis thaliana, Proteome, Molecular Sequence Data, Arabidopsis, plant, protein localization, chromatin assembly and disassembly, chemistry, Article, protein database, Databases, proteomics, nuclear protein, molecular biology, controlled study, Amino Acid Sequence, cell protein, protein motif, cellular distribution, chromatin associated protein, nonhuman, Arabidopsis protein, Arabidopsis Proteins, Protein, protein domain, Nuclear Proteins, protein function, phosphoprotein, Phosphoproteins, Chromatin, unclassified drug, enzyme activity, protein phosphorylation, protein stability, RNA processing, classification, protein analysis, molecular genetics, RNA, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], transcription regulation, metabolism
Abstract

International audience; The nucleus is the organelle where basically all DNA-related processes take place in eukaryotes, such as replication, transcription, and splicing as well as epigenetic regulation. The identification and description of the nuclear proteins is one of the requisites toward a comprehensive understanding of the biological functions accomplished in the nucleus. Many of the regulatory mechanisms of protein functions rely on their PTMs among which phosphorylation is probably one of the most important properties affecting enzymatic activity, interaction with other molecules, localization, or stability. So far, the nuclear and subnuclear proteome and phosphoproteome of the model plant Arabidopsis thaliana have been the subject of very few studies. In this work, we developed a purification protocol of Arabidopsis chromatin-associated proteins and performed proteomic and phosphoproteomic analyses identifying a total of 879 proteins of which 198 were phosphoproteins that were mainly involved in chromatin remodeling, transcriptional regulation, and RNA processing. From 230 precisely localized phosphorylation sites (phosphosites), 52 correspond to hitherto unidentified sites. This protocol and data thereby obtained should be a valuable resource for many domains of plant research.

Published
2014

31. Linking the proteins—Elucidation of proteome-scale networks using mass spectrometry

Author

Pflieger, Delphine, Gonnet, Florence, van Bentem, Sergio de la Fuente, Hirt, Heribert, de la Fuente, Alberto, Université d'Évry-Val-d'Essonne (UEVE), Syngenta BV, Partenaires INRAE, Unité de recherche en génomique végétale (URGV), Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Recherche Agronomique (INRA), University of Vienna [Vienna], CRS4 Bioinformat, Austrian Science Foundation, Regional Authorities of Sardinia, and Institut National de la Recherche Agronomique (INRA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)

Subjects
TYROSINE PHOSPHORYLATION SITES, phosphorylation, network biology, [SDV]Life Sciences [q-bio], TANDEM AFFINITY PURIFICATION, systems biology, CELLULAR SIGNALING NETWORKS, TRANSCRIPTIONAL REGULATORY NETWORK, SINGLE-STEP PURIFICATION, proteomics, METAL CHELATE ADSORBENT, QUANTITATIVE PHOSPHOPROTEOME ANALYSIS, CHEMICAL CROSS-LINKING, TRANSFER DISSOCIATION ETD, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, GROWTH-FACTOR RECEPTOR, mass spectrometry
Abstract

International audience; Proteomes are intricate. Typically, thousands of proteins interact through physical association and post-translational modifications (PTMs) to give rise to the emergent functions of cells. Understanding these functions requires one to study proteomes as "systems" rather than collections of individual protein molecules. The abstraction of the interacting proteome to "protein networks" has recently gained much attention, as networks are effective representations, that lose specific molecular details, but provide the ability to see the proteome as a whole. Mostly two aspects of the proteome have been represented by network models: proteome-wide physical protein-protein-binding interactions organized into Protein Interaction Networks (PINs), and proteome-wide PTM relations organized into Protein Signaling Networks (PSNs). Mass spectrometry (MS) techniques have been shown to be essential to reveal both of these aspects on a proteome-wide scale. Techniques such as affinity purification followed by MS have been used to elucidate protein-protein interactions, and MS-based quantitative phosphoproteomics is critical to understand the structure and dynamics of signaling through the proteome. We here review the current state-of-the-art MS-based analytical pipelines for the purpose to characterize proteome-scale networks. (C) 2010 Wiley Periodicals, Inc., Mass Spec Rev 30: 268-297, 2011

Published
2011

33. Methylation of aquaporins in plant plasma membrane

Author

Santoni, Véronique, Verdoucq, Lionel, Sommerer, Nicolas, Vinh, Joelle, Pflieger, Delphine, Maurel, Christophe, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), and Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0106 biological sciences, Gene isoform, Spectrometry, Mass, Electrospray Ionization, Molecular Sequence Data, Arabidopsis, Aquaporin, Aquaporins, Transfection, 01 natural sciences, Biochemistry, Methylation, Cell membrane, 03 medical and health sciences, medicine, Protein Isoforms, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, 0303 health sciences, Water transport, Chemistry, Arabidopsis Proteins, Cell Membrane, Water, Life Sciences, Biological Transport, Cell Biology, Membrane transport, medicine.anatomical_structure, Membrane protein, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Mutation, Ectopic expression, lipids (amino acids, peptides, and proteins), [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], 010606 plant biology & botany, Research Article
Abstract

International audience; A thorough analysis, using mass spectrometry, of aquaporins expressed in plant root plasma membrane was performed, with the objective of revealing novel post-translational regulations. Here we show that the N-terminal tail of Plasma membrane Intrinsic Protein (PIP) aquaporins can exhibit multiple modifications and is differentially maturated between members of the PIP1 and PIP2 subclasses. Thus, the initiating methionine was acetylated or cleaved in native PIP1 and PIP2 isoforms, respectively. In addition, several residues were detected to be methylated in PIP2 aquaporins. Lys3 and Glu6 of PIP2;1, one of the most abundant aquaporins in the plasma membrane occurred as di- and mono-methylated residues, respectively. Ectopic expression in Arabidopsis suspension cells of PIP2;1, either wild-type or with altered methylation sites revealed an interplay between methylation at the two sites. Measurements of water transport in plasma membrane vesicles purified from these cells suggested that PIP2;1 methylation does not interfere with the aquaporin intrinsic water permeability. In conclusion, this study identifies methylation as a novel post-translational modification of aquaporins, and even plant membrane proteins and may represent a critical advance towards the identification of new regulatory mechanisms of membrane transport.

Published
2006

34. Intérêt de l'analyse protéomique pour l'identification des protéines

Author

Tortajada, Jeanine, Gonnet, Florence, Svinartchouk, Fédor, Duguez, Stéphanie, Pflieger, Delphine, Analyse et environnement (LAE), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Centre de recherche et d'applications sur les thérapies géniques (CRATG), and Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)-Généthon

Subjects
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Published
2005

38. A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots

Author

Vinh, Joelle, Pflieger, Delphine, Sommerer, Nicolas, Maurel, C., Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
BIOCHIMIE, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, SPECTROSCOPIE DE MASSE
Published
2003

39. Quantitative Phosphoproteomic Analysis Reveals Shared and Specific Targets of ArabidopsisMitogen-Activated Protein Kinases (MAPKs) MPK3, MPK4, and MPK6*

Author

Rayapuram, Naganand, Bigeard, Jean, Alhoraibi, Hanna, Bonhomme, Ludovic, Hesse, Anne-Marie, Vinh, Joëlle, Hirt, Heribert, and Pflieger, Delphine

Abstract

In Arabidopsis, mitogen-activated protein kinases MPK3, MPK4, and MPK6 constitute essential relays for a variety of functions including cell division, development and innate immunity. Although some substrates of MPK3, MPK4 and MPK6 have been identified, the picture is still far from complete. To identify substrates of these MAPKs likely involved in cell division, growth and development we compared the phosphoproteomes of wild-type and mpk3, mpk4, and mpk6.To study the function of these MAPKs in innate immunity, we analyzed their phosphoproteomes following microbe-associated molecular pattern (MAMP) treatment. Partially overlapping substrates were retrieved for all three MAPKs, showing target specificity to one, two or all three MAPKs in different biological processes. More precisely, our results illustrate the fact that the entity to be defined as a specific or a shared substrate for MAPKs is not a phosphoprotein but a particular (S/T)P phosphorylation site in a given protein. One hundred fifty-two peptides were identified to be differentially phosphorylated in response to MAMP treatment and/or when compared between genotypes and 70 of them could be classified as putative MAPK targets. Biochemical analysis of a number of putative MAPK substrates by phosphorylation and interaction assays confirmed the global phosphoproteome approach. Our study also expands the set of MAPK substrates to involve other protein kinases, including calcium-dependent (CDPK) and sugar nonfermenting (SnRK) protein kinases.

Published
2018
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40. Brassinosteroid-regulated GSK3/Shaggy-like Kinases Phosphorylate Mitogen-activated Protein (MAP) Kinase Kinases, Which Control Stomata Development in Arabidopsis thaliana

Author

Khan, Mamoona, primary, Rozhon, Wilfried, additional, Bigeard, Jean, additional, Pflieger, Delphine, additional, Husar, Sigrid, additional, Pitzschke, Andrea, additional, Teige, Markus, additional, Jonak, Claudia, additional, Hirt, Heribert, additional, and Poppenberger, Brigitte, additional

Published
2013
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48. Quantitative Proteomic Analysis of Protein Complexes

Author

Pflieger, Delphine, primary, Jünger, Martin A., additional, Müller, Markus, additional, Rinner, Oliver, additional, Lee, Hookeun, additional, Gehrig, Peter M., additional, Gstaiger, Matthias, additional, and Aebersold, Ruedi, additional

Published
2008
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