Literatura académica sobre el tema "Cryo EM 2"
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Artículos de revistas sobre el tema "Cryo EM 2"
Fujiyoshi, Yoshinori. "Drug Rescuing by Cryo-EM". Proceedings for Annual Meeting of The Japanese Pharmacological Society WCP2018 (2018): SY16–2. http://dx.doi.org/10.1254/jpssuppl.wcp2018.0_sy16-2.
Texto completoChen, Xizi, Mengjie Liu, Yuan Tian, Jiabei Li, Yilun Qi, Dan Zhao, Zihan Wu et al. "Cryo-EM structure of human mTOR complex 2". Cell Research 28, n.º 5 (22 de marzo de 2018): 518–28. http://dx.doi.org/10.1038/s41422-018-0029-3.
Texto completoHenderson, Richard y Samar Hasnain. "`Cryo-EM': electron cryomicroscopy, cryo electron microscopy or something else?" IUCrJ 10, n.º 5 (1 de septiembre de 2023): 519–20. http://dx.doi.org/10.1107/s2052252523006759.
Texto completoSherman, M. B., F. Nasar y S. C. Weaver. "Cryo-EM Reconstruction Of Eilat Alphavirus". Microscopy and Microanalysis 18, S2 (julio de 2012): 74–75. http://dx.doi.org/10.1017/s143192761200222x.
Texto completoKamyshinsky, Roman, Yury Chesnokov, Liubov Dadinova, Andrey Mozhaev, Alexander Vasiliev y Eleonora Shtykova. "Abstract OR-2: The Formation of Dps-DNA Complexes under Different Conditions According to Cryo-EM and SAXS". International Journal of Biomedicine 11, Suppl_1 (1 de junio de 2021): S7. http://dx.doi.org/10.21103/ijbm.11.suppl_1.or2.
Texto completoMei, Kunrong, Yan Li, Shaoxiao Wang, Guangcan Shao, Jia Wang, Yuehe Ding, Guangzuo Luo et al. "Cryo-EM structure of the exocyst complex". Nature Structural & Molecular Biology 25, n.º 2 (15 de enero de 2018): 139–46. http://dx.doi.org/10.1038/s41594-017-0016-2.
Texto completoZhu, Xing, Dhiraj Mannar, Shanti S. Srivastava, Alison M. Berezuk, Jean-Philippe Demers, James W. Saville, Karoline Leopold et al. "Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies". PLOS Biology 19, n.º 4 (29 de abril de 2021): e3001237. http://dx.doi.org/10.1371/journal.pbio.3001237.
Texto completoZeng, Lingxiao, Wei Ding y Quan Hao. "Using cryo-electron microscopy maps for X-ray structure determination". IUCrJ 5, n.º 4 (11 de mayo de 2018): 382–89. http://dx.doi.org/10.1107/s2052252518005857.
Texto completoSi, Dong y Jing He. "Modeling Beta-Traces for Beta-Barrels from Cryo-EM Density Maps". BioMed Research International 2017 (2017): 1–9. http://dx.doi.org/10.1155/2017/1793213.
Texto completoCerutti, Gabriele, Yicheng Guo, Lihong Liu, Liyuan Liu, Zhening Zhang, Yang Luo, Yiming Huang et al. "Cryo-EM structure of the SARS-CoV-2 Omicron spike". Cell Reports 38, n.º 9 (marzo de 2022): 110428. http://dx.doi.org/10.1016/j.celrep.2022.110428.
Texto completoTesis sobre el tema "Cryo EM 2"
Zuniga, Dania. "Structural and functional studies of a human potassium channel, Kir2.1. Mechanism and consequences of mutations". Electronic Thesis or Diss., Sorbonne université, 2022. http://www.theses.fr/2022SORUS336.
Texto completoThe ability of a cell to facilitate the selective and rapid movement of ions and small molecules across the plasma membrane is one of the most fundamental biological processes. Inward rectifier potassium (Kir) channels are integral membrane proteins that provide K+-selective pathways across the otherwise impermeable cell membrane along the electrochemical gradients. Kir channels support the flow of K+ ions into and out of the cell and regulate various functions in the human body, including heart rate, vascular tone, insulin secretion, and salt and fluid balance. The physiological significance of Kir channels is highlighted by the fact that genetically-inherited defects in these genes result in human diseases (channelopathies). We are particularly interested in Andersen’s syndrome, where mutations in the KCNJ2 gene coding for Kir2.1 protein are directly involved. Andersen’s syndrome (AS) is a rare disease characterized by cardiac arrhythmias, dysmorphic features, and periodic paralysis. The available treatment for AS patients is empirical rather than rational due to the lack of knowledge of this Kir2.1 channel. This thesis aimed to identify the differences between the wild-type Kir2.1 channel and two mutant AS-causing channels to find links between the structure and the function of human Kir2.1 using a combination of biochemical, structural, and functional approaches. In this study, we recombinantly expressed the human Kir2.1 channel in yeast and purified it in detergent. We characterized the interaction between Kir2.1 and the essential activator PIP2, solved the first human Kir channel structure by cryo-EM, and explored reconstitution in detergent-free systems like amphipols and nanodiscs. The findings of this study will provide a structural and functional base to understand better the mechanisms involved in Kir channels and the effects of their mutations. This manuscript is divided into three parts. The first part introduces Kir channels and state-of-the-art. The second part focuses on the characterization of the human potassium channel Kir2.1, the determination of its structure by cryo-EM, and the impact of mutations on its structure and function. The third part presents two mutations in the bacterial homolog KirBac3.1, which shares structural features with Kir2.1, to provide insight into the gating mechanism of Kir channels
Tabaroni, Rachel. "Etude structurale du complexe de remodelage de la chromatine NuRD et sa sous-unité MBD3 liée à l'ADN". Thesis, Strasbourg, 2018. http://www.theses.fr/2018STRAJ094.
Texto completoTranscription regulation of chromatin is a very dynamic process regulated through the recruitment of chromatin-remodeling complexes. My work focuses on NuRD for Nucleosome remodeling and histones deacetylation complex a 1 MDa multi-subunit protein complex and its subunit MBD3 a CpG-binding protein and more precisely on an integrated biology approach of this molecular assembly and its interaction with DNA. It combines biochemical preparation, biophysical characterization, single particle cryo-eletron microscopy and x-ray crystallography. Biophysical analysis show that MBD domain of MBD3 interacts with unmodified CpG DNA, a crystal diffracting up to 3.9 Å were obtained. Moreover a C-terminal intrinsically disordered region of MBD3 were identified and despite is inherent disorder seems to increase the binding affinity of MBD3 for DNA. Crystals were obtained for both constructs in complex with DNA and are currently optimized.Cryo-EM study of NuRD complex allows us to develop and optimized purification and grids preparation for the visualization of the complex. The present results reveal a domain organization of the complex never identify before
Torchy, Morgan. "Etude structure-fonction du complexe de remodelage de la chromatine NuRD". Thesis, Strasbourg, 2014. http://www.theses.fr/2014STRAJ113/document.
Texto completoAn integrative structural biology approach has been used to study the structural organization of the NuRD complex.My work focused especially on three subunits of this complex: MBD3, RbAp46 and RbAp48. I set up the preparation of the individual subunits and characterized them by various biophysical methods. We next carried out binding assays with homemade human nucleosomes. For MBD3, optimization of the complex led to crystals diffracting up to 7 Å. In parallel, a preliminary 3-D reconstruction at 25 Å resolution has been solved in cryo-EM. For RbAp46/48, crystal we were able to show that these proteins form stable complexes with the nucleosome, paving the way for future structural analysis by cryo-EM or X-ray crystallography
Bertram, Karl. "High-resolution structure determination of human spliceosome complexes by cryo-EM". Thesis, 2018. http://hdl.handle.net/11858/00-1735-0000-002E-E592-2.
Texto completoCapítulos de libros sobre el tema "Cryo EM 2"
Frank, Joachim. "Generalized Single-Particle Cryo-EM: A Historical Perspective". En Novel Developments in Cryo‐EM of Biological Molecules, 9–23. New York: Jenny Stanford Publishing, 2023. http://dx.doi.org/10.1201/9781003456100-2.
Texto completoSztain, Terra, Surl-Hee Ahn, Anthony T. Bogetti, Lorenzo Casalino, Jory A. Goldsmith, Evan Seitz, Ryan S. McCool et al. "A Glycan Gate Controls Opening of the SARS-CoV-2 Spike Protein". En Novel Developments in Cryo‐EM of Biological Molecules, 241–56. New York: Jenny Stanford Publishing, 2023. http://dx.doi.org/10.1201/9781003456100-13.
Texto completoVolkmann, Niels. "Methods for Segmentation and Interpretation of Electron Tomographic Reconstructions". En Cryo-EM, Part C: Analyses, Interpretation, and Case studies, 31–46. Elsevier, 2010. http://dx.doi.org/10.1016/s0076-6879(10)83002-2.
Texto completoHanson, Robin. "Signals". En The Age of Em. Oxford University Press, 2016. http://dx.doi.org/10.1093/oso/9780198754626.003.0033.
Texto completoActas de conferencias sobre el tema "Cryo EM 2"
Jesus, Ariane Silva de, Meire Cristina Novelli e. Castro, éssica Aparecida Luciano Venancio, Mariana Corrêa Andrade Marcia y Milena Temer Jamas. "Estratégia pedagógica para ensino da classificação de risco em obstetrícia para residência de enfermagem". En Simpósio Internacional Programa de Pós-Graduação em Enfermagem. Universidade Estadual de Campinas, 2024. http://dx.doi.org/10.20396/sippgenf.3.e023029.
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