Literatura académica sobre el tema "Cryo-EM structures"
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Artículos de revistas sobre el tema "Cryo-EM structures"
Lawson, Catherine L. y Wah Chiu. "Comparing cryo-EM structures". Journal of Structural Biology 204, n.º 3 (diciembre de 2018): 523–26. http://dx.doi.org/10.1016/j.jsb.2018.10.004.
Texto completoJiang, Wen y Liang Tang. "Atomic cryo-EM structures of viruses". Current Opinion in Structural Biology 46 (octubre de 2017): 122–29. http://dx.doi.org/10.1016/j.sbi.2017.07.002.
Texto completoMalhotra, Sony, Sylvain Träger, Matteo Dal Peraro y Maya Topf. "Modelling structures in cryo-EM maps". Current Opinion in Structural Biology 58 (octubre de 2019): 105–14. http://dx.doi.org/10.1016/j.sbi.2019.05.024.
Texto completoScheres, Sjors HW, Wenjuan Zhang, Benjamin Falcon y Michel Goedert. "Cryo-EM structures of tau filaments". Current Opinion in Structural Biology 64 (octubre de 2020): 17–25. http://dx.doi.org/10.1016/j.sbi.2020.05.011.
Texto completoSubroto, Toto, Rina Fajri Nuwarda, Umi Baroroh, Zuhrotun Nafisah, Bevi Lidya y Muhammad Yusuf. "IN SILICO STUDY OF CRYO-EM STRUCTURES OF ANTIGEN-ANTIBODY COMPLEX OF CHIKUNGUNYA FOR THE DEVELOPMENT OF DIAGNOSTIC AGENT". Asian Journal of Pharmaceutical and Clinical Research 10, n.º 14 (1 de mayo de 2017): 62. http://dx.doi.org/10.22159/ajpcr.2017.v10s2.19489.
Texto completoCeska, Tom, Chun-Wa Chung, Rob Cooke, Chris Phillips y Pamela A. Williams. "Cryo-EM in drug discovery". Biochemical Society Transactions 47, n.º 1 (15 de enero de 2019): 281–93. http://dx.doi.org/10.1042/bst20180267.
Texto completoGlaeser, Robert M. "Replication and validation of cryo-EM structures". Journal of Structural Biology 184, n.º 2 (noviembre de 2013): 379–80. http://dx.doi.org/10.1016/j.jsb.2013.09.007.
Texto completoChiu, Wah y Greg Pintilie. "Quantifying the resolvability in cryo-EM structures". Acta Crystallographica Section A Foundations and Advances 75, a1 (20 de julio de 2019): a351. http://dx.doi.org/10.1107/s0108767319096582.
Texto completoYang, Guanghui, Rui Zhou y Yigong Shi. "Cryo-EM structures of human γ-secretase". Current Opinion in Structural Biology 46 (octubre de 2017): 55–64. http://dx.doi.org/10.1016/j.sbi.2017.05.013.
Texto completoLawson, Catherine L., Helen M. Berman y Wah Chiu. "Evolving data standards for cryo-EM structures". Structural Dynamics 7, n.º 1 (enero de 2020): 014701. http://dx.doi.org/10.1063/1.5138589.
Texto completoTesis sobre el tema "Cryo-EM structures"
Wilkes, Martin [Verfasser], Christine [Akademischer Betreuer] [Gutachter] Ziegler y Clemens [Gutachter] Glaubitz. "Single-particle cryo-EM structures of oligomeric membrane protein complexes / Martin Wilkes ; Gutachter: Clemens Glaubitz, Christine Ziegler ; Betreuer: Christine Ziegler". Frankfurt am Main : Universitätsbibliothek Johann Christian Senckenberg, 2016. http://d-nb.info/1120493412/34.
Texto completoPreis, Anne [Verfasser] y Roland [Akademischer Betreuer] Beckmann. "Cryo-EM structures of eukaryotic translation termination and ribosome recycling complexes containing eRF1, eRF3 and ABCE1 / Anne Preis ; Betreuer: Roland Beckmann". München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2020. http://d-nb.info/1213658837/34.
Texto completoZhou, Yu. "Structural study of eIF2B by electron microscopy". Thesis, University of Manchester, 2016. https://www.research.manchester.ac.uk/portal/en/theses/structural-study-of-eif2b-by-electron-microscopy(feacd470-3139-4648-9812-c152168c930d).html.
Texto completoAbdelkareem, Moamen. "Structural basis of transcription : RNA polymerase backtracking and its reactivation". Thesis, Strasbourg, 2019. http://www.theses.fr/2019STRAJ062.
Texto completo[...]My Ph.D. was focused on the understanding of a transcriptional phenomenon, termed backtracking, which inactivates RNAP and halts transcription. Reactivation of halted RNAP complexes and transcription resumption, requires a protein factor called GreB. The objective of the project was to gain structural information on: i) how backtracking inactivates RNAP inE. coli; and ii) how GreB rescues backtracked RNAP to continue transcription. Using SP cryo- EM, I captured four snapshots of RNAP at different states covering the backtracking and reactivation cycle. My results show that the RNA is no longer aligned with the active center, explaining the transcription halt. Furthermore, as a result of backtracking, RNAP adopts new conformational changes allowing GreB binding. As a consequence, the NTD of GreB contacts RNAP active center and donates acidic residues that increase the affinity towards a magnesium ion, which is required for cleavage catalysis of the misaligned RNA. These four reconstructions give insights on the catalytic mechanism and dynamics of RNA cleavage and extension. [...]
Brito, Querido Jailson Fernando. "Structural study of mRNA translation in kinetoplastids by Cryo-electron microscopy". Thesis, Strasbourg, 2017. http://www.theses.fr/2017STRAJ108.
Texto completoKinetoplastid is a group of flagellated protozoans, which threatens more than 400 million people world-wide. They possess unusual large rRNA expansion segments (ES) in the 40S, such as ES6S, ES7S and ES9S and their location suggests an involvement in the initiation process. Furthermore, all mature mRNAs possess a conserved 5’ spliced-leader. Here, we purified from T. cruzi cell lysates native initiation complexes and native 40S subunits that we then analysed by cryo-EM. The structure of native initiation complexes reveals several kinetoplastid-specific aspects of translation, such as an intricate interaction network between eIF3 and ES6S and ES7S. Furthermore, it reveals the role of DDX60 in translation initiation in kinetoplastids. The structure of native 40S subunits reveals the existence of an uncharacterized factor (termed ηF) bound at platform of the 40S. The binding site of ηF suggests a role in translational control. Moreover, we reported a novel kinetoplastid-specific ribosomal (r-) protein (KSRP) bound to the 40S subunit. Our work represents the first structural characterization of kinetoplastids-specific aspects of translation initiation
Spikes, Tobias Edward. "Structural studies of the mitochondrial F-ATPase". Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/274349.
Texto completoHe, Shaoda. "Helical reconstruction in RELION". Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/284086.
Texto completoNojima, Shingo. "Cryo-EM Structure of the Prostaglandin E Receptor EP4 Coupled to G Protein". Doctoral thesis, Kyoto University, 2021. http://hdl.handle.net/2433/263574.
Texto completoTorchy, 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
Guo, Xieyang. "Regulation of transcription : structural studies of an RNA polymerase elongation complex bound to transcription factor NusA". Thesis, Strasbourg, 2018. http://www.theses.fr/2018STRAJ071/document.
Texto completoTranscriptional pausing by RNA polymerases (RNAPs) is a key mechanism to regulate gene expression in all kingdoms of life and is a prerequisite for transcription termination. The essential bacterial transcription factor NusA stimulates both pausing and termination of transcription, thus playing a central role. Here, I present single-particle electron cryo-microscopy (cryo-EM) reconstructions of NusA bound to paused elongation complexes with and without a pause-enhancing hairpin in the RNA exit channel. The structures reveal four interactions between NusA and RNAP that suggest how NusA stimulates RNA folding, pausing, and termination. An asymmetric translocation intermediate of RNA and DNA converts the active site of the enzyme into an inactive state, providing a structural explanation for the inhibition of catalysis. Comparing RNAP at different stages of pausing provides insights on the dynamic nature of the process and the role of NusA as a regulatory factor
Libros sobre el tema "Cryo-EM structures"
service), ScienceDirect (Online, ed. Cryo-EM: Sample preparation and data collection. San Diego, Calif: Academic Press/Elsevier, 2010.
Buscar texto completoservice), ScienceDirect (Online. Cryo-EM: Analyses, interpretation, and case studies. San Diego, Calif: Academic Press/Elsevier, 2010.
Buscar texto completoCapítulos de libros sobre el tema "Cryo-EM structures"
Pilsl, Michael y Christoph Engel. "Structural Studies of Eukaryotic RNA Polymerase I Using Cryo-Electron Microscopy". En Ribosome Biogenesis, 71–80. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_5.
Texto completoPilsl, Michael, Florian B. Heiss, Gisela Pöll, Mona Höcherl, Philipp Milkereit y Christoph Engel. "Preparation of RNA Polymerase Complexes for Their Analysis by Single-Particle Cryo-Electron Microscopy". En Ribosome Biogenesis, 81–96. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_6.
Texto completoNatesh, Ramanathan. "Single-Particle cryo-EM as a Pipeline for Obtaining Atomic Resolution Structures of Druggable Targets in Preclinical Structure-Based Drug Design". En Challenges and Advances in Computational Chemistry and Physics, 375–400. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-05282-9_12.
Texto completoAgirrezabala, Xabier, Hstau Y. Liao, Eduard Schreiner, Jie Fu, Rodrigo F. Ortiz-Meoz, Klaus Schulten, Rachel Green y Joachim Frank. "Structural Characterization of mRNA-tRNA Translocation Intermediates". En Novel Developments in Cryo‐EM of Biological Molecules, 87–107. New York: Jenny Stanford Publishing, 2023. http://dx.doi.org/10.1201/9781003456100-6.
Texto completoFrank, Joachim y Abbas Ourmazd. "Continuous Changes in Structure Mapped by Manifold Embedding of Single-Particle Data in Cryo-EM". En Novel Developments in Cryo‐EM of Biological Molecules, 127–46. New York: Jenny Stanford Publishing, 2023. http://dx.doi.org/10.1201/9781003456100-8.
Texto completoChen, Bo, Sandip Kaledhonkar, Ming Sun, Bingxin Shen, Zonghuan Lu, David Barnard, Toh-Ming Lu, Ruben L. Gonzalez y Joachim Frank. "Structural Dynamics of Ribosome Subunit Association Studied by Mixing-Spraying Time-Resolved Cryogenic Electron Microscopy". En Novel Developments in Cryo‐EM of Biological Molecules, 315–41. New York: Jenny Stanford Publishing, 2023. http://dx.doi.org/10.1201/9781003456100-16.
Texto completoMei, Kunrong y Wei Guo. "Modeling the Cryo-EM Structure of the Exocyst Complex". En Methods in Molecular Biology, 247–62. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2639-9_16.
Texto completoHillen, Hauke S. "Cryo-EM for Structure Determination of Mitochondrial Ribosome Samples". En Methods in Molecular Biology, 89–100. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3171-3_6.
Texto completoFu, Ziao, Gabriele Indrisiunaite, Sandip Kaledhonkar, Binita Shah, Ming Sun, Bo Chen, Robert A. Grassucci, Mans Ehrenberg y Joachim Frank. "The Structural Basis for Release-Factor Activation During Translation Termination Revealed by Time-Resolved Cryogenic Electron Microscopy". En Novel Developments in Cryo‐EM of Biological Molecules, 481–500. New York: Jenny Stanford Publishing, 2023. http://dx.doi.org/10.1201/9781003456100-23.
Texto completoAgrawal, Rajendra K., Manjuli R. Sharma, Aymen Yassin, Indrajit Lahiri y inda L. Spremulli. "Structure and function of organellar ribosomes as revealed by cryo-EM". En Ribosomes, 83–96. Vienna: Springer Vienna, 2011. http://dx.doi.org/10.1007/978-3-7091-0215-2_8.
Texto completoActas de conferencias sobre el tema "Cryo-EM structures"
Haslam, Devin, Mohammad Zubair, Desh Ranjan, Abhishek Biswas y Jing He. "Challenges in matching secondary structures in cryo-EM: An exploration". En 2016 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2016. http://dx.doi.org/10.1109/bibm.2016.7822776.
Texto completoChen, Lin y Jing He. "Using Combined Features to Analyze Atomic Structures derived from Cryo-EM Density Maps". En BCB '18: 9th ACM International Conference on Bioinformatics, Computational Biology and Health Informatics. New York, NY, USA: ACM, 2018. http://dx.doi.org/10.1145/3233547.3233709.
Texto completoZhong, Ellen D., Adam Lerer, Joseph H. Davis y Bonnie Berger. "CryoDRGN2: Ab initio neural reconstruction of 3D protein structures from real cryo-EM images". En 2021 IEEE/CVF International Conference on Computer Vision (ICCV). IEEE, 2021. http://dx.doi.org/10.1109/iccv48922.2021.00403.
Texto completoHaslam, Devin, Tao Zeng, Rongjian Li y Jing He. "Exploratory Studies Detecting Secondary Structures in Medium Resolution 3D Cryo-EM Images Using Deep Convolutional Neural Networks". En BCB '18: 9th ACM International Conference on Bioinformatics, Computational Biology and Health Informatics. New York, NY, USA: ACM, 2018. http://dx.doi.org/10.1145/3233547.3233704.
Texto completoMu, Yongcheng, Jiangwen Sun y Jing He. "The Combined Focal Cross Entropy and Dice Loss Function for Segmentation of Protein Secondary Structures from Cryo-EM 3D Density maps". En 2022 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2022. http://dx.doi.org/10.1109/bibm55620.2022.9995469.
Texto completoNOGALES, EVA. "CRYO-EM VISUALIZATION OF MACROMOLECULAR STRUCTURE AND DYNAMICS". En 25th Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2021. http://dx.doi.org/10.1142/9789811228216_0037.
Texto completoScheres, Sjors H. W. "A Bayesian view on cryo-EM structure determination". En 2012 IEEE 9th International Symposium on Biomedical Imaging (ISBI 2012). IEEE, 2012. http://dx.doi.org/10.1109/isbi.2012.6235807.
Texto completoPenczek, Pawel A. y Francisco J. Asturias. "Ab initio cryo-EM structure determination as a validation problem". En 2014 IEEE International Conference on Image Processing (ICIP). IEEE, 2014. http://dx.doi.org/10.1109/icip.2014.7025419.
Texto completoGolubev, A., B. Fatkhullin, I. Khusainov, L. Jenner, A. Gabdulkhakov, Sh Validov, G. Yusupova, M. Yusupov y K. Usachev. "Cryo-EM structure of the 70 initiation complex from S. aurues". En XXVIII Российская конференция по электронной микроскопии и VI школа молодых учёных "Современные методы электронной, зондовой микроскопии и комплементарные методы в исследованиях наноструктур и наноматериалов". Crossref, 2020. http://dx.doi.org/10.37795/rcem.2020.51.47.049.
Texto completoHennig, Michael. "CRYO-EM ENABLED STRUCTURE BASED DRUG DISCOVERY ON CHALLENGING MEMBRANE PROTEIN TARGETS". En European Microscopy Congress 2020. Royal Microscopical Society, 2021. http://dx.doi.org/10.22443/rms.emc2020.26.
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