6 results on '"Dufour, Fabrice"'
Search Results
2. Phosphorylation of Microtubule-associated Protein STOP by Calmodulin Kinase II
- Author
-
Baratier, Julie, Peris, Leticia, Brocard, Jacques, Gory-Fauré, Sylvie, Dufour, Fabrice, Bosc, Christophe, Fourest-Lieuvin, Anne, Blanchoin, Laurent, Salin, Paul, Job, Didier, and Andrieux, Annie
- Published
- 2006
- Full Text
- View/download PDF
3. MAP6 interacts with Tctex1 and Cav 2.2/N-type calcium channels to regulate calcium signalling in neurons
- Author
-
Brocard, Jacques, Dufour, Fabrice, Gory‐Fauré, Sylvie, Arnoult, Christophe, Bosc, Christophe, Denarier, Eric, Peris, Leticia, Saoudi, Yasmina, De Waard, Michel, Andrieux, Annie, Physiopathologie du Cytosquelette, [GIN] Grenoble Institut des Neurosciences (GIN), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), INSERM U836, équipe 1, Physiopathologie du cytosquelette, Grenoble Institut des Neurosciences (GIN), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), 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]), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Inserm, U1216, Grenoble, France., Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Groupe Physiopathologie du Cytosquelette (GPC), 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), unité de recherche de l'institut du thorax UMR1087 UMR6291 (ITX), Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), 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]), 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)-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), Unité de recherche de l'institut du thorax (ITX-lab), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), and Université de Nantes (UN)-Université de Nantes (UN)
- Subjects
Mice, Knockout ,Neurons ,vesicles ,Binding Sites ,yeast two-hybrid ,hippocampal neurons ,[SDV]Life Sciences [q-bio] ,Dyneins ,in vitro interactions ,Molecular and Synaptic Mechanisms ,plasma membrane ,Hippocampus ,microtubules ,Mice ,Calcium Channels, N-Type ,Animals ,Female ,Calcium Signaling ,yeast two‐hybrid ,Microtubule-Associated Proteins ,Cells, Cultured ,Protein Binding - Abstract
International audience; MAP6 proteins were first described as microtubule-stabilizing agents, whose properties were thought to be essential for neuronal development and maintenance of complex neuronal networks. However, deletion of all MAP6 isoforms in MAP6 KO mice does not lead to dramatic morphological aberrations of the brain but rather to alterations in multiple neurotransmissions and severe behavioural impairments. A search for protein partners of MAP6 proteins identified Tctex1 - a dynein light chain with multiple non-microtubule-related functions. The involvement of Tctex1 in calcium signalling led to investigate it in MAP6 KO neurons. In this study, we show that functional Cav 2.2/N-type calcium channels are deficient in MAP6 KO neurons, due to improper location. We also show that MAP6 proteins interact directly with both Tctex1 and the C-terminus of Cav 2.2/N-type calcium channels. A balance of these two interactions seems to be crucial for MAP6 to modulate calcium signalling in neurons.
- Published
- 2017
- Full Text
- View/download PDF
4. Continuous Downstream Processing of Amino Acids in a Modular Miniplant.
- Author
-
Hohmann, Lukas, Löbnitz, Lisa, Menke, Christina, Santhirakumaran, Bavatharani, Stier, Patrick, Stenger, Frank, Dufour, Fabrice, Wiese, Georg, zur Horst-Meyer, Santer zur, Kusserow, Burkhard, Zang, Werner, Nirschl, Hermann, and Kockmann, Norbert
- Subjects
AMINO acids ,CHEMICAL industry ,CRYSTALLIZATION ,BATCH processing ,MODULAR design ,EVAPORATORS - Abstract
Abstract: Global competition leads to a need for a fast time to market and increased resource efficiency. Continuous processing, module‐based plant design, and multipurpose equipment are recently discussed approaches for the fine‐chemical industry. As a representative, the downstream process of amino acid production is discussed herein. A conventional batch procedure was transferred to a continuous process and realized in a modular miniplant, which comprised of evaporation in a wiped‐film evaporator, seeded cooling crystallization in a coiled tubular crystallizer, and solid/liquid separation on a vacuum belt filter. The operations were realized on‐skid with individual automation systems and integrated sensors. L‐Alanine was successfully processed in steady‐state operation. [ABSTRACT FROM AUTHOR]
- Published
- 2018
- Full Text
- View/download PDF
5. MAP6 interacts with Tctex1 and Cav2.2/N-type calcium channels to regulate calcium signalling in neurons.
- Author
-
Brocard, Jacques, Dufour, Fabrice, Gory‐Fauré, Sylvie, Arnoult, Christophe, Bosc, Christophe, Denarier, Eric, Peris, Leticia, Saoudi, Yasmina, De Waard, Michel, and Andrieux, Annie
- Subjects
- *
HIPPOCAMPUS (Brain) , *NEURONS , *MICROTUBULES , *CELL membranes , *SYNAPTIC vesicles - Abstract
MAP6 proteins were first described as microtubule-stabilizing agents, whose properties were thought to be essential for neuronal development and maintenance of complex neuronal networks. However, deletion of all MAP6 isoforms in MAP6 KO mice does not lead to dramatic morphological aberrations of the brain but rather to alterations in multiple neurotransmissions and severe behavioural impairments. A search for protein partners of MAP6 proteins identified Tctex1 - a dynein light chain with multiple non-microtubule-related functions. The involvement of Tctex1 in calcium signalling led to investigate it in MAP6 KO neurons. In this study, we show that functional Cav2.2/N-type calcium channels are deficient in MAP6 KO neurons, due to improper location. We also show that MAP6 proteins interact directly with both Tctex1 and the C-terminus of Cav2.2/N-type calcium channels. A balance of these two interactions seems to be crucial for MAP6 to modulate calcium signalling in neurons. [ABSTRACT FROM AUTHOR]
- Published
- 2017
- Full Text
- View/download PDF
6. MAP6 interacts with Tctex1 and Ca v 2.2/N-type calcium channels to regulate calcium signalling in neurons.
- Author
-
Brocard J, Dufour F, Gory-Fauré S, Arnoult C, Bosc C, Denarier E, Peris L, Saoudi Y, De Waard M, and Andrieux A
- Subjects
- Animals, Binding Sites, Cells, Cultured, Female, Hippocampus cytology, Mice, Mice, Knockout, Microtubule-Associated Proteins genetics, Protein Binding, Calcium Channels, N-Type metabolism, Calcium Signaling physiology, Dyneins metabolism, Microtubule-Associated Proteins metabolism, Neurons metabolism
- Abstract
MAP6 proteins were first described as microtubule-stabilizing agents, whose properties were thought to be essential for neuronal development and maintenance of complex neuronal networks. However, deletion of all MAP6 isoforms in MAP6 KO mice does not lead to dramatic morphological aberrations of the brain but rather to alterations in multiple neurotransmissions and severe behavioural impairments. A search for protein partners of MAP6 proteins identified Tctex1 - a dynein light chain with multiple non-microtubule-related functions. The involvement of Tctex1 in calcium signalling led to investigate it in MAP6 KO neurons. In this study, we show that functional Ca
v 2.2/N-type calcium channels are deficient in MAP6 KO neurons, due to improper location. We also show that MAP6 proteins interact directly with both Tctex1 and the C-terminus of Cav 2.2/N-type calcium channels. A balance of these two interactions seems to be crucial for MAP6 to modulate calcium signalling in neurons., (© 2017 The Authors. European Journal of Neuroscience published by Federation of European Neuroscience Societies and John Wiley & Sons Ltd.)- Published
- 2017
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.