14 results on '"Texier, Yves"'
Search Results
2. Interplay between NIN-LIKE PROTEINs 6 and 7 in nitrate signaling.
- Author
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Yu-Hsuan Cheng, Durand, Mickael, Brehaut, Virginie, Fu-Chiun Hsu, Kelemen, Zsolt, Texier, Yves, Krapp, Anne, and Yi-Fang Tsay
- Published
- 2023
- Full Text
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3. Applying SILAC for the Differential Analysis of Protein Complexes
- Author
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Boldt, Karsten, primary, Gloeckner, Christian J., additional, Texier, Yves, additional, von Zweydorf, Felix, additional, and Ueffing, Marius, additional
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- 2014
- Full Text
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4. Disruption of intraflagellar protein transport in photoreceptor cilia causes Leber congenital amaurosis in humans and mice
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Boldt, Karsten, Mans, Dorus A., Won, Jungyeon, van Reeuwijk, Jeroen, Vogt, Andreas, Kinkl, Norbert, Letteboer, Stef J.F., Hicks, Wanda L., Hurd, Ron E., Naggert, Jurgen K., Texier, Yves, den Hollander, Anneke I., Koenekoop, Robert K., Bennett, Jean, Cremers, Frans P.M., Gloeckner, Christian J., Nishina, Patsy M., Roepman, Ronald, and Ueffing, Marius
- Subjects
Blindness ,Genetic disorders ,Health care industry - Abstract
The mutations that cause Leber congenital amaurosis (LCA) lead to photoreceptor cell death at an early age, causing childhood blindness. To unravel the molecular basis of LCA, we analyzed how [...]
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- 2011
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5. The nodule inception-like protein 7 modulates nitrate sensing and metabolism in Arabidopsis
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Castaings, Loren, Camargo, Antonio, Pocholle, Delphine, Gaudon, Virginie, Texier, Yves, Boutet-Mercey, Stéphanie, Taconnat, Ludivine, Renou, Jean-Pierre, Daniel-Vedele, Françoise, Fernandez, Emilio, Meyer, Christian, and Krapp, Anne
- Published
- 2009
6. CiliaCarta: An integrated and validated compendium of ciliary genes
- Author
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van Dam, Teunis J. P., primary, Kennedy, Julie, additional, van der Lee, Robin, additional, de Vrieze, Erik, additional, Wunderlich, Kirsten A., additional, Rix, Suzanne, additional, Dougherty, Gerard W., additional, Lambacher, Nils J., additional, Li, Chunmei, additional, Jensen, Victor L., additional, Leroux, Michel R., additional, Hjeij, Rim, additional, Horn, Nicola, additional, Texier, Yves, additional, Wissinger, Yasmin, additional, van Reeuwijk, Jeroen, additional, Wheway, Gabrielle, additional, Knapp, Barbara, additional, Scheel, Jan F., additional, Franco, Brunella, additional, Mans, Dorus A., additional, van Wijk, Erwin, additional, Képès, François, additional, Slaats, Gisela G., additional, Toedt, Grischa, additional, Kremer, Hannie, additional, Omran, Heymut, additional, Szymanska, Katarzyna, additional, Koutroumpas, Konstantinos, additional, Ueffing, Marius, additional, Nguyen, Thanh-Minh T., additional, Letteboer, Stef J. F., additional, Oud, Machteld M., additional, van Beersum, Sylvia E. C., additional, Schmidts, Miriam, additional, Beales, Philip L., additional, Lu, Qianhao, additional, Giles, Rachel H., additional, Szklarczyk, Radek, additional, Russell, Robert B., additional, Gibson, Toby J., additional, Johnson, Colin A., additional, Blacque, Oliver E., additional, Wolfrum, Uwe, additional, Boldt, Karsten, additional, Roepman, Ronald, additional, Hernandez-Hernandez, Victor, additional, and Huynen, Martijn A., additional
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- 2019
- Full Text
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7. An organelle-specific protein landscape identifies novel diseases and molecular mechanisms
- Author
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Boldt, Karsten, van Reeuwijk, Jeroen, Dougherty, Gerard, Lamers, Ideke J C, Coene, Karlien L M, Arts, Heleen H, Betts, Matthew J, Beyer, Tina, Bolat, Emine, Gloeckner, Christian Johannes, Haidari, Khatera, Hetterschijt, Lisette, Lu, Qianhao, Iaconis, Daniela, Jenkins, Dagan, Klose, Franziska, Knapp, Barbara, Latour, Brooke, Letteboer, Stef J F, Marcelis, Carlo L, Mitic, Dragana, Morleo, Manuela, Oud, Machteld M, Koutroumpas, Konstantinos, Riemersma, Moniek, Rix, Susan, Terhal, Paulien A, Toedt, Grischa, van Dam, Teunis J P, de Vrieze, Erik, Wissinger, Yasmin, Wu, Ka Man, Apic, Gordana, Beales, Philip L, Nguyen, Thanh-Minh T, Blacque, Oliver E, Gibson, Toby J, Huynen, Martijn A, Katsanis, Nicholas, Kremer, Hannie, Omran, Heymut, van Wijk, Erwin, Wolfrum, Uwe, Kepes, François, Davis, Erica E, Texier, Yves, Franco, Brunella, Giles, Rachel H, Ueffing, Marius, Russell, Robert B, Roepman, Ronald, Group, UK10K Rare Diseases, Al-Turki, Saeed, Anderson, Carl, Antony, Dinu, Barroso, Inês, van Beersum, Sylvia E C, Bentham, Jamie, Bhattacharya, Shoumo, Carss, Keren, Chatterjee, Krishna, Cirak, Sebahattin, Cosgrove, Catherine, Danecek, Petr, Durbin, Richard, Fitzpatrick, David, Floyd, Jamie, Horn, Nicola, Reghan Foley, A., Franklin, Chris, Futema, Marta, Humphries, Steve E, Hurles, Matt, Joyce, Chris, McCarthy, Shane, Mitchison, Hannah M, Muddyman, Dawn, Muntoni, Francesco, Willer, Jason R, O'Rahilly, Stephen, Onoufriadis, Alexandros, Payne, Felicity, Plagnol, Vincent, Raymond, Lucy, Savage, David B, Scambler, Peter, Schmidts, Miriam, Schoenmakers, Nadia, Semple, Robert, Mans, Dorus A, Serra, Eva, Stalker, Jim, van Kogelenberg, Margriet, Vijayarangakannan, Parthiban, Walter, Klaudia, Whittall, Ros, Williamson, Kathy, Boldt, K, van Reeuwijk, J, Lu, Q, Koutroumpas, K, Nguyen, Tmt, Texier, Y, van Beersum, Sec, Horn, N, Willer, Jr, Mans, Da, Dougherty, G, Lamers, Ijc, Coene, Klm, Arts, Hh, Betts, Mj, Beyer, T, Bolat, E, Gloeckner, Cj, Haidari, K, Hetterschijt, L, Iaconis, D, Jenkins, D, Klose, F, Knapp, B, Latour, B, Letteboer, Sjf, Marcelis, Cl, Mitic, D, Morleo, M, Oud, Mm, Riemersma, M, Rix, S, Terhal, Pa, Toedt, G, van Dam, Tjp, de Vrieze, E, Wissinger, Y, Wu, Km, Apic, G, Beales, Pl, Blacque, Oe, Gibson, Tj, Huynen, Ma, Katsanis, N, Kremer, H, Omran, H, van Wijk, E, Wolfrum, U, Kepes, F, Davis, Ee, Franco, B, Giles, Rh, Ueffing, M, Russell, Rb, Roepman, R, Boldt, Karsten, Van Reeuwijk, Jeroen, Lu, Qianhao, Koutroumpas, Konstantino, Nguyen, Thanh Minh T., Texier, Yve, Van Beersum, Sylvia E. C., Horn, Nicola, Willer, Jason R., Mans, Dorus A., Dougherty, Gerard, Lamers, Ideke J. C., Coene, Karlien L. M., Arts, Heleen H., Betts, Matthew J., Beyer, Tina, Bolat, Emine, Gloeckner, Christian Johanne, Haidari, Khatera, Hetterschijt, Lisette, Iaconis, Daniela, Jenkins, Dagan, Klose, Franziska, Knapp, Barbara, Latour, Brooke, Letteboer, Stef J. F., Marcelis, Carlo L., Mitic, Dragana, Morleo, Manuela, Oud, Machteld M., Riemersma, Moniek, Rix, Susan, Terhal, Paulien A., Toedt, Grischa, Van Dam, Teunis J. P., De Vrieze, Erik, Wissinger, Yasmin, Wu, Ka Man, Al Turki, Saeed, Anderson, Carl, Antony, Dinu, Barroso, Inê, Bentham, Jamie, Bhattacharya, Shoumo, Carss, Keren, Chatterjee, Krishna, Cirak, Sebahattin, Cosgrove, Catherine, Danecek, Petr, Durbin, Richard, Fitzpatrick, David, Floyd, Jamie, Foley, A. Reghan, Franklin, Chri, Futema, Marta, Humphries, Steve E., Hurles, Matt, Joyce, Chri, Mccarthy, Shane, Mitchison, Hannah M., Muddyman, Dawn, Muntoni, Francesco, O'Rahilly, Stephen, Onoufriadis, Alexandro, Payne, Felicity, Plagnol, Vincent, Raymond, Lucy, Savage, David B., Scambler, Peter, Schmidts, Miriam, Schoenmakers, Nadia, Semple, Robert, Serra, Eva, Stalker, Jim, Van Kogelenberg, Margriet, Vijayarangakannan, Parthiban, Walter, Klaudia, Whittall, Ro, Williamson, Kathy, Apic, Gordana, Beales, Philip L., Blacque, Oliver E., Gibson, Toby J., Huynen, Martijn A., Katsanis, Nichola, Kremer, Hannie, Omran, Heymut, Van Wijk, Erwin, Wolfrum, Uwe, Kepes, Françoi, Davis, Erica E., Franco, Brunella, Giles, Rachel H., Ueffing, Mariu, Russell, Robert B., and Roepman, Ronald
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Proteomics ,0301 basic medicine ,Systems Analysis ,DNA Mutational Analysis ,lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4] ,General Physics and Astronomy ,Datasets as Topic ,methods [Chromatography, Affinity] ,Sensory disorders Donders Center for Medical Neuroscience [Radboudumc 12] ,Chromatography, Affinity ,Mass Spectrometry ,Protein Interaction Mapping ,therapy [Ciliopathies] ,genetics [Ciliopathies] ,methods [Molecular Targeted Therapy] ,Molecular Targeted Therapy ,Protein Interaction Maps ,Multidisciplinary ,Cilium ,Chemistry (all) ,abnormalities [Spine] ,pathology [Ciliopathies] ,genetics [Muscle Hypotonia] ,therapy [Muscle Hypotonia] ,Metabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6] ,metabolism [Proteins] ,isolation & purification [Proteins] ,physiology [Biological Transport] ,3. Good health ,Cell biology ,Vesicular transport protein ,pathology [Dwarfism] ,metabolism [Cilia] ,Muscle Hypotonia ,ddc:500 ,pathology [Muscle Hypotonia] ,pathology [Spine] ,genetics [Dwarfism] ,Rare cancers Radboud Institute for Health Sciences [Radboudumc 9] ,Science ,Dwarfism ,Exocyst ,Biology ,Article ,General Biochemistry, Genetics and Molecular Biology ,Physics and Astronomy (all) ,03 medical and health sciences ,Intraflagellar transport ,Ciliogenesis ,Organelle ,Humans ,Cilia ,Biochemistry, Genetics and Molecular Biology (all) ,Proteins ,Biological Transport ,General Chemistry ,therapy [Dwarfism] ,Fibroblasts ,genetics [Proteins] ,Ciliopathies ,Spine ,methods [Protein Interaction Mapping] ,Renal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11] ,030104 developmental biology ,Proteostasis ,HEK293 Cells ,methods [Proteomics] - Abstract
Cellular organelles provide opportunities to relate biological mechanisms to disease. Here we use affinity proteomics, genetics and cell biology to interrogate cilia: poorly understood organelles, where defects cause genetic diseases. Two hundred and seventeen tagged human ciliary proteins create a final landscape of 1,319 proteins, 4,905 interactions and 52 complexes. Reverse tagging, repetition of purifications and statistical analyses, produce a high-resolution network that reveals organelle-specific interactions and complexes not apparent in larger studies, and links vesicle transport, the cytoskeleton, signalling and ubiquitination to ciliary signalling and proteostasis. We observe sub-complexes in exocyst and intraflagellar transport complexes, which we validate biochemically, and by probing structurally predicted, disruptive, genetic variants from ciliary disease patients. The landscape suggests other genetic diseases could be ciliary including 3M syndrome. We show that 3M genes are involved in ciliogenesis, and that patient fibroblasts lack cilia. Overall, this organelle-specific targeting strategy shows considerable promise for Systems Medicine., Mutations in proteins that localize to primary cilia cause devastating diseases, yet the primary cilium is a poorly understood organelle. Here the authors use interaction proteomics to identify a network of human ciliary proteins that provides new insights into several biological processes and diseases.
- Published
- 2016
8. CiliaCarta: an integrated and validated compendium of ciliary genes
- Author
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van Dam, Teunis J. P., primary, Kennedy, Julie, additional, Lee, Robin van der, additional, Vrieze, Erik de, additional, Wunderlich, Kirsten A., additional, Rix, Suzanne, additional, Dougherty, Gerard W., additional, Lambacher, Nils J., additional, Li, Chunmei, additional, Jensen, Victor L., additional, Leroux, Michel R., additional, Hjeij, Rim, additional, Horn, Nicola, additional, Texier, Yves, additional, Wissinger, Yasmin, additional, van Reeuwijk, Jeroen, additional, Wheway, Gabrielle, additional, Knapp, Barbara, additional, Scheel, Jan F., additional, Franco, Brunella, additional, Mans, Dorus A., additional, van Wijk, Erwin, additional, Képès, François, additional, Slaats, Gisela G., additional, Toedt, Grischa, additional, Kremer, Hannie, additional, Omran, Heymut, additional, Szymanska, Katarzyna, additional, Koutroumpas, Konstantinos, additional, Ueffing, Marius, additional, Nguyen, Thanh-Minh T., additional, Letteboer, Stef J.F., additional, Oud, Machteld M., additional, van Beersum, Sylvia E. C., additional, Schmidts, Miriam, additional, Beales, Philip L., additional, Lu, Qianhao, additional, Giles, Rachel H., additional, Szklarczyk, Radek, additional, Russell, Robert B., additional, Gibson, Toby J., additional, Johnson, Colin A., additional, Blacque, Oliver E., additional, Wolfrum, Uwe, additional, Boldt, Karsten, additional, Roepman, Ronald, additional, Hernandez-Hernandez, Victor, additional, and Huynen, Martijn A., additional
- Published
- 2017
- Full Text
- View/download PDF
9. Quantitative analysis of ciliary protein networks - Characterization of the intraflagellar transport complex B
- Author
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Texier, Yves Stephan, Hrabé de Angelis, Martin (Prof. Dr.), Adamski, Jerzy (Prof. Dr.), and Ueffing, Marius (Prof. Dr.)
- Subjects
Biowissenschaften, Biologie ,ddc:570 - Abstract
The intraflagellar transport (IFT) complex is essential for ciliary transport. To gain insight into the function of the IFT complex, a method to determine its sub-structure was developed. The components of the IFT complex B (IFT-B) and its sub-structure were determined using different biochemical and mass spectrometric methods. Furthermore, the centrosomal protein 170 was identified to be associated to the IFT-B and shown to be essential for its ciliary localization. Der Intraflagellare Transport (IFT) Komplex ist essentiell für den ziliären Transport. Um mehr über die Funktion des IFT-Komplexes zu erfahren, wurde eine Methode zur Bestimmung seiner Sub-Struktur entwickelt. Unter Verwendung verschiedener biochemischer und massenspektrometrischer Methoden, wurden die Komponenten des IFT-Komplexes B (IFT-B) bestimmt, sowie seine Sub-Struktur analysiert. Des Weiteren wurde die Assoziation des Zentrosomalen Proteins 170 an den IFT-B, sowie die essentielle Funktion für dessen ziliäre Lokalisation gezeigt.
- Published
- 2014
10. Autophosphorylation on S614 inhibits the activity and the transforming potential of BRAF
- Author
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Dernayka, Layal, primary, Rauch, Nora, additional, Jarboui, Mohamed-Ali, additional, Zebisch, Armin, additional, Texier, Yves, additional, Horn, Nicola, additional, Romano, David, additional, Gloeckner, Christian Johannes, additional, Kriegsheim, Alex von, additional, Ueffing, Marius, additional, Kolch, Walter, additional, and Boldt, Karsten, additional
- Published
- 2016
- Full Text
- View/download PDF
11. Heptad-Specific Phosphorylation of RNA Polymerase II CTD
- Author
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Schüller, Roland, primary, Forné, Ignasi, additional, Straub, Tobias, additional, Schreieck, Amelie, additional, Texier, Yves, additional, Shah, Nilay, additional, Decker, Tim-Michael, additional, Cramer, Patrick, additional, Imhof, Axel, additional, and Eick, Dirk, additional
- Published
- 2016
- Full Text
- View/download PDF
12. NINL and DZANK1 Co-function in Vesicle Transport and Are Essential for Photoreceptor Development in Zebrafish
- Author
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Dona, Margo, primary, Bachmann-Gagescu, Ruxandra, additional, Texier, Yves, additional, Toedt, Grischa, additional, Hetterschijt, Lisette, additional, Tonnaer, Edith L., additional, Peters, Theo A., additional, van Beersum, Sylvia E. C., additional, Bergboer, Judith G. M., additional, Horn, Nicola, additional, de Vrieze, Erik, additional, Slijkerman, Ralph W. N., additional, van Reeuwijk, Jeroen, additional, Flik, Gert, additional, Keunen, Jan E., additional, Ueffing, Marius, additional, Gibson, Toby J., additional, Roepman, Ronald, additional, Boldt, Karsten, additional, Kremer, Hannie, additional, and van Wijk, Erwin, additional
- Published
- 2015
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13. Elution Profile Analysis of SDS-induced Subcomplexes by Quantitative Mass Spectrometry
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Texier, Yves, primary, Toedt, Grischa, additional, Gorza, Matteo, additional, Mans, Dorus A., additional, van Reeuwijk, Jeroen, additional, Horn, Nicola, additional, Willer, Jason, additional, Katsanis, Nicholas, additional, Roepman, Ronald, additional, Gibson, Toby J., additional, Ueffing, Marius, additional, and Boldt, Karsten, additional
- Published
- 2014
- Full Text
- View/download PDF
14. Applying SILAC for the differential analysis of protein complexes.
- Author
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Boldt K, Gloeckner CJ, Texier Y, von Zweydorf F, and Ueffing M
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- Analytic Sample Preparation Methods, Cell Death, HEK293 Cells, Humans, Mass Spectrometry, Proteins isolation & purification, Amino Acids chemistry, Isotope Labeling methods, Proteins chemistry, Proteins metabolism, Proteomics methods
- Abstract
Pull-downs based on tag fusion proteins as well as immunoprecipitations (IP) are widely used methods to analyze protein interactions. Selectivity and specificity of both methods are compromised by nonspecific binding to the capture agent or carrier beads thereby generating false positives. Here, we provide a method combining stable isotope labeling of amino acids in cell culture (SILAC) with affinity purification, coupled to quantitative tandem mass spectrometry. It permits the analysis of protein interactions with high sensitivity, while being able to discriminate contaminants and nonspecific binders. Besides pruning out contaminants, high-resolution MS data combined with quantitative proteomics software allow the comparative analysis of protein interaction patterns of different protein variants, for example mutated versus normal protein variant or of regulatory changes in a given protein complex due to different states of activity.
- Published
- 2014
- Full Text
- View/download PDF
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