Literatura científica selecionada sobre o tema "Membrane nanodomains"
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Artigos de revistas sobre o assunto "Membrane nanodomains"
Okamoto, Yukihiro, Kaito Hamaguchi, Mayo Watanabe, Nozomi Watanabe e Hiroshi Umakoshi. "Characterization of Phase Separated Planar Lipid Bilayer Membrane by Fluorescence Ratio Imaging and Scanning Probe Microscope". Membranes 12, n.º 8 (9 de agosto de 2022): 770. http://dx.doi.org/10.3390/membranes12080770.
Texto completo da fonteSamhan-Arias, Alejandro K., Joana Poejo, Dorinda Marques-da-Silva, Oscar H. Martínez-Costa e Carlos Gutierrez-Merino. "Are There Lipid Membrane-Domain Subtypes in Neurons with Different Roles in Calcium Signaling?" Molecules 28, n.º 23 (2 de dezembro de 2023): 7909. http://dx.doi.org/10.3390/molecules28237909.
Texto completo da fonteSilvius, John R. "Membrane Nanodomains". Colloquium Series on Building Blocks of the Cell: Cell Structure and Function 1, n.º 1 (28 de fevereiro de 2013): 1–103. http://dx.doi.org/10.4199/c00076ed1v01y201303bbc001.
Texto completo da fonteLiang, Pengbo, Thomas F. Stratil, Claudia Popp, Macarena Marín, Jessica Folgmann, Kirankumar S. Mysore, Jiangqi Wen e Thomas Ott. "Symbiotic root infections in Medicago truncatula require remorin-mediated receptor stabilization in membrane nanodomains". Proceedings of the National Academy of Sciences 115, n.º 20 (30 de abril de 2018): 5289–94. http://dx.doi.org/10.1073/pnas.1721868115.
Texto completo da fonteFukata, Yuko, Ariane Dimitrov, Gaelle Boncompain, Ole Vielemeyer, Franck Perez e Masaki Fukata. "Local palmitoylation cycles define activity-regulated postsynaptic subdomains". Journal of Cell Biology 202, n.º 1 (8 de julho de 2013): 145–61. http://dx.doi.org/10.1083/jcb.201302071.
Texto completo da fonteDrab, Mitja, David Stopar, Veronika Kralj-Iglič e Aleš Iglič. "Inception Mechanisms of Tunneling Nanotubes". Cells 8, n.º 6 (21 de junho de 2019): 626. http://dx.doi.org/10.3390/cells8060626.
Texto completo da fonteMesarec, Luka, Mitja Drab, Samo Penič, Veronika Kralj-Iglič e Aleš Iglič. "On the Role of Curved Membrane Nanodomains and Passive and Active Skeleton Forces in the Determination of Cell Shape and Membrane Budding". International Journal of Molecular Sciences 22, n.º 5 (26 de fevereiro de 2021): 2348. http://dx.doi.org/10.3390/ijms22052348.
Texto completo da fonteCebecauer, Marek, Mariana Amaro, Piotr Jurkiewicz, Maria João Sarmento, Radek Šachl, Lukasz Cwiklik e Martin Hof. "Membrane Lipid Nanodomains". Chemical Reviews 118, n.º 23 (26 de outubro de 2018): 11259–97. http://dx.doi.org/10.1021/acs.chemrev.8b00322.
Texto completo da fonteMa, Yuanqing, Elizabeth Hinde e Katharina Gaus. "Nanodomains in biological membranes". Essays in Biochemistry 57 (6 de fevereiro de 2015): 93–107. http://dx.doi.org/10.1042/bse0570093.
Texto completo da fonteTraeger, Jeremiah, Dehong Hu, Mengran Yang, Gary Stacey e Galya Orr. "Super-Resolution Imaging of Plant Receptor-Like Kinases Uncovers Their Colocalization and Coordination with Nanometer Resolution". Membranes 13, n.º 2 (21 de janeiro de 2023): 142. http://dx.doi.org/10.3390/membranes13020142.
Texto completo da fonteTeses / dissertações sobre o assunto "Membrane nanodomains"
Legrand, Anthony. "Anchoring mechanism of the plant protein remorin to membrane nanodomains". Thesis, Bordeaux, 2020. http://www.theses.fr/2020BORD0285.
Texto completo da fonteGroup 1 isoform 3 remorin from Solanum tuberosum (StREM1.3) is a membrane protein belonging to the multigenic family of plant proteins called remorins (REMs), involved in plant immunity, symbiosis, abiotic stress resistance and hormone signalling. REMs’ most well known feature is their ability to segregate into nanodomains at the plasma membrane’s (PM) inner leaflet. For StREM1.3, this is achieved by an interaction between two lysines of the remorin C-terminal anchor (RemCA) and negatively charged phosphatidylinositol 4-phosphate (PI4P). Thus, RemCA undergoes conformational changes and partially buries itself in the PM, resulting in an intrinsic membrane anchoring. Capitalising on pre-existing structural data about this isoform, we investigate StREM1.3’s membrane-interacting properties further, using a wide array of techniques, ranging from fluorescence microscopy and solid-state nuclear magnetic resonance (ssNMR) to atomic force microscopy (AFM), cryo-electron microscopy (cryoEM) and computational modelling. We aim to discover the impact of StREM1.3’s oligomerisation and phosphorylation on its membrane interactions and biological activity, and to assess its influence on lipid dynamics as well as its lipid requirements for membrane binding and nanoclustering. Finally, based on all available structural data, we will undertake the in vitro reconstruction and characterisation of minimal nanodomains of StREM1.3
Hebisch, Elke [Verfasser], e Stefan W. [Akademischer Betreuer] Hell. "STED microscopy of cardiac membrane nanodomains / Elke Hebisch ; Betreuer: Stefan W. Hell". Heidelberg : Universitätsbibliothek Heidelberg, 2017. http://d-nb.info/1180740068/34.
Texto completo da fonteHebisch, Elke [Verfasser], e Stefan [Akademischer Betreuer] Hell. "STED microscopy of cardiac membrane nanodomains / Elke Hebisch ; Betreuer: Stefan W. Hell". Heidelberg : Universitätsbibliothek Heidelberg, 2017. http://nbn-resolving.de/urn:nbn:de:bsz:16-heidok-227475.
Texto completo da fonteDeroubaix, Anne-Flore. "Rôle de la rémorine et des nanodomaines membranaires dans la signalisation de la réponse aux phytovirus". Thesis, Bordeaux, 2019. http://www.theses.fr/2019BORD0292.
Texto completo da fonteIn the battle against viruses, plants have evolved various defence mechanisms to protect themselves against pathogens. Membrane-bound plant proteins such as Remorin (REM) may restrict viral infection. REMs belong to a plant-specific multigene family, classified in six phylogenetic groups that are localized in plasma membrane nanodomains and for some of them in plasmodesmata. Our team previously showed that in tomato and Nicotiana benthamiana, overexpression of Solanum tuberosum group 1 isoform 3 (StREM1.3) limits the cell-to-cell spread of the potexvirus Potato virus X (PVX) without affecting viral replication. During my thesis, our data allowed to built a working model in which the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3 (AtCPK3) is able to interact with group 1 REM in vivo, phosphorylates the N-terminal domain of StREM1.3 and, finally, with the help of uncharacterized proteins lead to the restriction of PVX cell-to-cell movement in N.benthamiana. N.benthamiana is perfect for viral experimentation, but is allo-tetraploid, making it difficult for genetic studies. Because of CPKs have 34 isoforms with likely functional redundancy between them, we switched to another pathosystem using the genetic toolbox of Arabidopsis thaliana and a potexvirus species able to infect A. thaliana, the Plantago Asiatica Mosaic Virus (PlAMV). The objectives are 1/ to study the contribution of different REM clades in potexvirus intercellular movement; 2/ to understand which CPKs are involved in this process using REM and CPKs single and multiple mutants, as well as AtCPKs over-expressors; 3/ To study the contribution of Group 1 REM and CPK3 on systemic potexvirus movement. We previously showed that, like PVX, PlAMV local movement is restricted by StREM1.3 and AtCPK3 in N.benthamiana. We optimized the experimental conditions to track and compare GFP-tagged PlAMV in different Arabidopsis genetic backgrounds. By using this method, we were able to track both local virus cell-to-cell movement and systemic infection through the whole plant. Group 1 REM and CPK single and multiple knock out mutants, as well as CPK over-expressors wereused. Interestingly, we did not detect any difference in propagation compared with control on various CPKs KO, except in cpk3 mutant. Indeed, both in local and systemic, PlAMV propagation is enhanced on cpk3 mutant while CPK3 overexpressing lines display an opposite effect, demonstrating the great involvement of CPK3 in potexvirus propagation. Similarly, we demonstrate the redundancy of each isoform from group 1 REM on the restriction of the intercellular movement of PlAMV. Interestingly, REM promotes intercellular propagation of another viral genus, the potyvirus genus, suggesting that REM functions are not general for all genera. Globally, our results classify group 1 REM and CPK3 as antiviral defence protein both in local and systemic potexvirus infection, and suggest that REM function is viral genus dependent. This research will pave the way toward new host targets to fight phytovirus infection
Gronnier, Julien. "Function of Plant Plasma Membrane Nanodomains : Study of Group 1 REMORINs during Plant-Virus Interactions". Electronic Thesis or Diss., Bordeaux, 2016. http://www.theses.fr/2016BORD0327.
Texto completo da fonteOrganization by compartmentalization is a general property of natural systems coordinating biological events in space and time. Over the past three decades, it has been demonstrated that multiple micrometric to nano-metric sub-compartments co-exist at a single membrane level. Such membrane organization seems critical for most all cell bioactivities and therefore critical for development and survival of potentially all living organisms. Plants respond to pathogens by activating highly regulated plasma membrane-bound signalling pathways. Plant plasma membrane (PM) displays a great diversity of compartments, but underlying functions and molecular mechanisms governing such organization are not well understood. To get insight in how and why plant PM is compartmentalized, we choose to study the plant PM nanodomain goup 1 REMORIN during the interaction between N. benthamiana and the Potato Virus X (PVX). Using a multidisciplinary approach we decipher a molecular mechanism involved in defining REMORIN PM domains localization. Making mutants we provide a functional link between REMORIN PM organization at single molecule level, its phosphostatus, regulation of plasmodesmata permeability and PVX cell-to-cell movement restriction. We then provide evidences that during N.benthamiana PVX sensing, PM organization appears critical for the modulation plant defence mechanisms and cell signaling. This study provides a unique mechanistic insight into how tight control of protein spatio-temporal organization at PM level is crucial to confer membrane domains identity and functionality
Liang, Pengbo [Verfasser], e Thomas [Akademischer Betreuer] Ott. "The role of membrane nanodomains and the cell wall-plasma membrane-cytoskeleton continuum during symbiotic infection in Medicago truncatula". Freiburg : Universität, 2020. http://d-nb.info/1220631760/34.
Texto completo da fonteKirsch, Sonja [Verfasser], Rainer [Akademischer Betreuer] Böckmann e Rainer [Gutachter] Böckmann. "The Role of Membrane Nanodomains in Permeation / Sonja Kirsch ; Gutachter: Rainer Böckmann ; Betreuer: Rainer Böckmann". Erlangen : Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), 2019. http://d-nb.info/1196875901/34.
Texto completo da fonteYandrapalli, Naresh. "Role of HIV-1 Gag protein multimerization in the generation of nanodomains in lipid membranes". Thesis, Montpellier, 2016. http://www.theses.fr/2016MONTT097/document.
Texto completo da fonteGag polyprotein of HIV-1 is made of four main domains Matrix (MA), Capsid (CA), Nucleocapsid (NC), and P6 and is the prime orchestrator of virus assembly that occurs during the late phase of replication. It is well known that Gag interacts with host cell lipids and self-assemble along the inner-leaflet of the plasma membrane in order to generate virus like particles (VLPs). Budding of these VLPs out of the living cell is described to be ESCRT dependent. Structural, functional and simulation based studies has shown that Gag membrane binding is mediated by a bipartite interaction. One specific electrostatic interaction, between the highly basic region (HBR) of its MA domain and the host cell acidic lipid phosphatidyl inositol bisphophate (PI(4,5)P2), plus a hydrophobic interaction through Gag’s myristate insertion in the plasma membrane. It is still an opened question whether Gag would specifically recognize pre-existing lipid domains such as rafts to optimize its multimerization or, on the contrary, would reorganize lipids during its multimerization. During my Ph.D. I explored the second hypothesis using purified myr(-) Gag protein and model membranes containing fluorescently labelled PI(4,5)P2.Bonding experiments have shown strong affinities of these purified proteins towards PI(4,5)P2 containing lipid bilayers. Using PI(4,5)P2 fluorescence self-quenching properties, I found that multimerization Gag generates PI(4,5)P2/Cholesterol enriched nanoclusters. On the opposite, sphingomyelin was excluded from these nanoclusters. In addition to this, using a fluorescently labelled myr(-) Gag, I have observed its preferable partitioning into lipid disordered (Ld) phases of giant unilamellar vesicles (GUVs). Further, possibility of whether HIV-1 Gag alone, as a minimal system, can induce the formation of vesicles on PI(4,5)P2/PS containing supported lipid bilayers (SLBs) & GUVs was tested. Using quartz crystal microbalance (QCM-D) and fluorescence microscopy techniques, I monitored the self-assembly of HIV-1 Gag with time and found that Gag was sufficient to generate membrane curvature and vesicle release. Moreover, using mutants of this protein, I found that having MA and CA domain is enough for Gag to produce vesicle like structures. Taken together, these results suggest that binding and multimerization of Gag protein does not occur in pre-existing lipid domains (such as “rafts”) but this multimerization is more likely to induce PI(4,5)P2/Cholesterol nanoclusters. This nanophase separation could locally play a role in the membrane curvature needed for the budding of the virus
Yu, Chao. "Quantitative Study of Membrane Nano-organization by Single Nanoparticle Imaging". Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLX054.
Texto completo da fonteIn this thesis, EGF, CPεT and transferrin receptors were labeled with luminescent nanoparticles, , and were tracked both in their local environment in the cell membrane and under a hydrodynamic flow. Bayesian inference, Bayesian decision tree, and data clustering techniques can then be applied to obtain quantitative information on the receptor motion parameters. Furthermore, we introduced hydrodynamic force application in vitro to study biomolecule dissociation between membrane receptors and their pharmaceutical ligands in high affinity receptor- ligand pairs, such as HB-EGF and DTR. Finally, three different modes of membrane organization and receptor confinement were revealed: the confinement of CPεTR is determined by the interaction between the receptors and the lipid/protein constituents of the raft; the confining potential of EGFR results from the interaction with lipids and proteins of the raft environment and from the interaction with F-actin; transferrin receptors diffuse freely in the membrane, only sterically limited by actin barriers, according to the “picket-and-fence” model. We moreover showed that all raft nanodomains are attached to the actin cytoskeleton
Noack, Lise. "Rôle du complexe AtPI4Kalpha1 dans l’établissement de l’identité de la membrane plasmique et le développement chez Arabidopsis thaliana". Thesis, Lyon, 2020. http://www.theses.fr/2020LYSEN066.
Texto completo da fonteEukaryotic cells are composed of several membrane-surrounded compartments. Each compartment has a unique physicochemical environment delimited by a membrane with a specific biochemical and biophysical identity. The membrane identity includes the nature of the lipids, the curvature, the electrostaticity and the density of lipids at the membrane. The identity of each membrane allows the proper localization of membrane-associated proteins. Phosphoinositides are rare anionic lipids present in membranes. Five types of phosphoinositides exist in plants - PI3P, PI4P, PI5P, PI(4,5)P2 and PI(3,5)P2 - depending of the number and the position of phosphates around the inositol ring. They accumulate differently at the plasma membrane and in intracellular compartments and interact with proteins through stereo-specific or electrostatic interactions. Recent work uncovered that PI4P concentrates according to an inverted gradient by comparison to their yeast and animal counterpart. In plants, PI4P massively accumulates at the plasma membrane and is present in fewer amounts at the trans-Golgi Network (TGN). This PI4P accumulation at the cell surface drives the plasma membrane electrostatic field, which in turn recruits a host of signalling proteins to this compartment. Moreover the plant TGN is the place of vesicular secretion but is also involved in endocytic sorting and recycling, which might imply regulatory mechanisms of lipid exchanges or membrane identity maintenance between the plasma membrane and the TGN. Here, we characterized PI4Kα1 mutants and showed that pi4kα1 loss-of-function leads to pollen grain lethality and distortion in the allele transmission via the female gametophyte, while its knockdown displayed strong developmental phenotypes. Using yeast two hybrid screening and mass spectrometry, we identified that PI4Kα1 is part of an heterotetrameric complex composed of NO POLLEN GERMINATION (NPG), EFR3 OF PLANTS (EFOP) and HYCCIN (HYC). The interaction between PI4Kα1 and the structural subunits of the complex is essential to target PI4Kα1 at the plasma membrane. In addition, we showed that PI4Kα1 complex is anchored in immobile and predefined subdomains of the plasma membrane. This work opens new perspectives on the role of the PI4Kα1 complex in plasma membrane suborganization
Livros sobre o assunto "Membrane nanodomains"
Silvius, John R. Membrane Nanodomains. Morgan & Claypool Life Science Publishers, 2013.
Encontre o texto completo da fonteSilvius, John R. Membrane Nanodomains. Morgan & Claypool Life Science Publishers, 2013.
Encontre o texto completo da fonteCambi, Alessandra, e Diane Lidke. Cell Membrane Nanodomains. Taylor & Francis Group, 2021.
Encontre o texto completo da fonteCambi, Alessandra, e Diane Lidke. Cell Membrane Nanodomains. Taylor & Francis Group, 2014.
Encontre o texto completo da fonteCell Membrane Nanodomains: From Biochemistry to Nanoscopy. Taylor & Francis Group, 2014.
Encontre o texto completo da fonteCambi, Alessandra, e Diane S. Lidke. Cell Membrane Nanodomains: From Biochemistry to Nanoscopy. Taylor & Francis Group, 2014.
Encontre o texto completo da fonteCambi, Alessandra, e Diane S. Lidke. Cell Membrane Nanodomains: From Biochemistry to Nanoscopy. Taylor & Francis Group, 2014.
Encontre o texto completo da fonteCapítulos de livros sobre o assunto "Membrane nanodomains"
Senapati, Subhadip, e Paul S. H. Park. "Investigating the Nanodomain Organization of Rhodopsin in Native Membranes by Atomic Force Microscopy". In Methods in Molecular Biology, 61–74. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8894-5_4.
Texto completo da fonte"Membrane Nanodomains". In Nanostructures in Biological Systems, 171–96. Jenny Stanford Publishing, 2015. http://dx.doi.org/10.1201/b18607-10.
Texto completo da fonte"Protein and Lipid Nanodomains". In Cell Membrane Nanodomains, 1–2. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-2.
Texto completo da fontevan den Bogaart, Geert, e Martin ter Beest. "Domains of Phosphoinositides in the Plasma Membrane". In Cell Membrane Nanodomains, 173–98. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-10.
Texto completo da fonteEisenberg, Sharon, e Sergio Grinstein. "Signaling Phagocytosis: Role of Specialized Lipid Domains". In Cell Membrane Nanodomains, 199–212. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-11.
Texto completo da fonte"Advanced Ensemble Imaging Techniques". In Cell Membrane Nanodomains, 213–14. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-12.
Texto completo da fonteDigman, Michelle. "Fluctuation Spectroscopy Methods for the Analysis of Membrane Processes". In Cell Membrane Nanodomains, 215–38. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-13.
Texto completo da fonteGodin, Antoine, Benjamin Rappaz, Laurent Potvin-Trottier, Yves De Koninck e Paul Wiseman. "Spatial Intensity Distribution Analysis (SpIDA): A Method to Probe Membrane Receptor Organization in Intact Cells". In Cell Membrane Nanodomains, 239–60. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-14.
Texto completo da fonteHoppe, Adam, e Shalini Low-Nam. "Live-Cell TIRF Imaging of Molecular Assembly and Plasma Membrane Topography". In Cell Membrane Nanodomains, 261–80. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-15.
Texto completo da fonte"Expanding the Fluorescence Toolbox". In Cell Membrane Nanodomains, 281–82. CRC Press, 2014. http://dx.doi.org/10.1201/b17634-16.
Texto completo da fonteTrabalhos de conferências sobre o assunto "Membrane nanodomains"
Rong, Xi, Kenneth M. Pryse, Jordan A. Whisler, Yanfei Jiang, William B. McConnaughey, Artem Melnykov, Guy M. Genin e Elliot L. Elson. "Confidence Intervals for Estimation of the Concentration and Brightness of Multiple Diffusing Species". In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80921.
Texto completo da fonteJiang, Yanfei, Guy M. Genin, Srikanth Singamaneni e Elliot L. Elson. "Interfacial Phases on Giant Unilamellar Vesicles". In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80942.
Texto completo da fonteParmryd, Ingela. "The Importance of Plasma Membrane Nanodomains in Signal Transduction and Drug Repurposing". In RExPO23. REPO4EU, 2023. http://dx.doi.org/10.58647/rexpo.23011.
Texto completo da fonteLee, Yerim, Kai Tao, Carey Phelps, Tao Huang, Barmak Mostofian, Daniel Zuckerman e Xiaolin Nan. "Probing the spatiotemporal dynamics of Ras-associated membrane nanodomains with high-throughput single particle tracking via photoactivated localization microscopy (spt-PALM)". In High-Speed Biomedical Imaging and Spectroscopy V, editado por Keisuke Goda e Kevin K. Tsia. SPIE, 2020. http://dx.doi.org/10.1117/12.2547699.
Texto completo da fonteXu, Xia, Yixiong Wang, Wonshik Choi e Roseline Godbout. "Abstract 2886: The mechanistic effect of DHA on FABP7 associated membrane lipid order & nanodomain distribution in glioblastoma migration". In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2886.
Texto completo da fonte