Electron Optic Documents

JEOL CRYOARM - BIBLIOGRAPHY

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14. Monté, Didier et al. “Structural basis of human Mediator recruitment by the phosphorylated transcription factor Elk-1.” Nature communications vol. 16,1 3772. 22 Apr. 2025, doi:10.1038/s41467-025-59014-8
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18. Toyonaga, Takuma et al. “Dimeric assembly of F1-like ATPase for the gliding motility of Mycoplasma.” Science advances vol. 11,9 (2025): eadr9319. doi:10.1126/sciadv.adr9319
19. Xu, Mengxin et al. “IgA class switching enhances neutralizing potency against SARS-CoV-2 by increased antibody hinge flexibility.” Antiviral research vol. 235 (2025): 106082. doi:10.1016/j.antiviral.2025.106082
20. Vizarraga, David et al. “Dynamics of the adhesion complex of the human pathogens Mycoplasma pneumoniae and Mycoplasma genitalium.” PLoS pathogens vol. 21,3 e1012973. 28 Mar. 2025, doi:10.1371/journal.ppat.1012973
21. Ma, Cheng-Bao et al. “Multiple independent acquisitions of ACE2 usage in MERS-related coronaviruses.” Cell vol. 188,6 (2025): 1693-1710.e18. doi:10.1016/j.cell.2024.12.031
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24. Jia, Xiaoying et al. “An adenosine analog shows high antiviral potency against coronavirus and arenavirus mainly through an unusual base pairing mode.” Nature communications vol. 15,1 10750. 30 Dec. 2024, doi:10.1038/s41467-024-54918-3
25. Lewis, Charlotte B. et al. “Conformational Flexibility in Capsids Encoded by the Caliciviridae.” Viruses, 26 Nov. 2024, 16, 1835. doi:10.3390/v16121835
    
26. Abe, Kazuhiro et al. “Molecular Structure of the Na+,K+-ATPase α4β1 Isoform in Its Ouabain-Bound Conformation.” International journal of molecular sciences vol. 25,22 12397. 19 Nov. 2024, doi:10.3390/ijms252212397
27. Zmyslia, Mariia et al. “A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor.” RSC chemical biology, vol. 6,1 21–35. 4 Nov. 2024, doi:10.1039/d4cb00127c
28. Yang, Mengsi et al. “Transformation of a Viral Capsid from Nanocages to Nanotubes and Then to Hydrogels: Redirected Self-Assembly and Effects on Immunogenicity.” ACS nano vol. 18,21 (2024): 13755-13767. doi:10.1021/acsnano.4c01969
29. Kato, Koji et al. “Structural basis for molecular assembly of fucoxanthin chlorophyll a/c-binding proteins in a diatom photosystem I supercomplex.” eLife vol. 13 RP99858. 31 Oct. 2024, doi:10.7554/eLife.99858
30. Rangarajan, Erumbi S et al. “High-resolution snapshots of the talin auto-inhibitory states suggest roles in cell adhesion and signaling.” Nature communications vol. 15,1 9270. 28 Oct. 2024, doi:10.1038/s41467-024-52581-2
31. Yamaguchi, Hiroki et al. “Open and closed structures of L-arginine oxidase by cryo-electron microscopy and X-ray crystallography.” Journal of biochemistry, mvae070. 18 Oct. 2024, doi:10.1093/jb/mvae070
32. Tani, Kazutoshi et al. “Structure of endothelin ETB receptor-Gi complex in a conformation stabilized by unique NPxxL motif.” Communications biology vol. 7,1 1303. 16 Oct. 2024, doi:10.1038/s42003-024-06905-z
33. Štěrbová, Petra et al. “Molecular Mechanism of pH-Induced Protrusion Configuration Switching in Piscine Betanodavirus Implies a Novel Antiviral Strategy.” ACS infectious diseases vol. 10,9 (2024): 3304-3319. doi:10.1021/acsinfecdis.4c00407
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36. Li, Chenyao et al. “Rapid small-scale nanobody-assisted purification of ryanodine receptors for cryo-EM.” The Journal of biological chemistry, vol. 300,10 107734. 2 Sep. 2024, doi:10.1016/j.jbc.2024.107734
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38. Yang, Jie et al. “Structural basis for the activity of the type VII CRISPR-Cas system.” Nature vol. 633,8029 (2024): 465-472. doi:10.1038/s41586-024-07815-0
39. Wakabayashi, Taiki et al. “CryoEM-sampling of metastable conformations appearing in cofactor-ligand association and catalysis of glutamate dehydrogenase.” Scientific reports vol. 14,1 11165. 15 May. 2024, doi:10.1038/s41598-024-61793-x
40. Tarău, Daniela et al. “Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment.” Nucleic acids research vol. 52,10 (2024): 6017-6035. doi:10.1093/nar/gkae282
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42. Holvec, Samuel et al. “The structure of the human 80S ribosome at 1.9 Å resolution reveals the molecular role of chemical modifications and ions in RNA.” Nature structural & molecular biology, 10.1038/s41594-024-01274-x. 6 Jun. 2024, doi:10.1038/s41594-024-01274-x
43. Fukawa, Eole et al. “Structural and electrochemical elucidation of biocatalytic mechanisms in direct electron transfer-type D-fructose dehydrogenase.” Electrochimica Acta vol. 490, 144271, 20 Jun. 2024, doi:10.1016/j.electacta.2024.144271.
44. Galicia, Christian et al. “Structural insights into the GTP-driven monomerization and activation of a bacterial LRRK2 homolog using allosteric nanobodies.” eLife vol. 13 RP94503. 26 Apr. 2024, doi:10.7554/eLife.94503
45. Odorčić, Ivica et al. “Apo and Aβ46-bound γ-secretase structures provide insights into amyloid-β processing by the APH-1B isoform.” Nature communications vol. 15,1 4479. 27 May. 2024, doi:10.1038/s41467-024-48776-2
46. Ishimaru, Hanako et al. “Epitopes of an antibody that neutralizes a wide range of SARS-CoV-2 variants in a conserved subdomain 1 of the spike protein.” Journal of virology vol. 98,5 (2024): e0041624. doi:10.1128/jvi.00416-24
47. Watanabe, Satoshi et al. “Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport.” Nature communications vol. 15,1 2404. 16 Mar. 2024, doi:10.1038/s41467-024-46747-1
48. Li, Zhiqiang et al. “Cryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes.” Nature communications vol. 15,1 2284. 13 Mar. 2024, doi:10.1038/s41467-024-46624-x
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50. Tanaka, Mayuki et al. “Boric acid intercepts 80S ribosome migration from AUG-stop by stabilizing eRF1.” Nature chemical biology, 10.1038/s41589-023-01513-0. 24 Jan. 2024, doi:10.1038/s41589-023-01513-0
51. Tani, Kazutoshi et al. “High-resolution structure and biochemical properties of the LH1-RC photocomplex from the model purple sulfur bacterium, Allochromatium vinosum.” Communications biology vol. 7,1 176. 12 Feb. 2024, doi:10.1038/s42003-024-05863-w
52. Tomono, Junta et al. “Direct visualization of ribosomes in the cell-free system revealed the functional evolution of aminoglycoside.” Journal of biochemistry, mvae002. 16 Jan. 2024, doi:10.1093/jb/mvae002
53. Bloch, Yehudi et al. “Structures of complete extracellular receptor assemblies mediated by IL-12 and IL-23.” Nature structural & molecular biology, 10.1038/s41594-023-01190-6. 29 Jan. 2024, doi:10.1038/s41594-023-01190-6
54. Acar, Delphine Diana et al. “Integrating artificial intelligence-based epitope prediction in a SARS-CoV-2 antibody discovery pipeline: caution is warranted.” EBioMedicine vol. 100 (2024): 104960. doi:10.1016/j.ebiom.2023.104960
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56. Artigas, Pablo et al. “A Na pump with reduced stoichiometry is up-regulated by brine shrimp in extreme salinities.” Proceedings of the National Academy of Sciences of the United States of America vol. 120,52 (2023): e2313999120. doi:10.1073/pnas.2313999120
57. Suzuki Yohei et al. “Essential Insight of Direct Electron Transfer-Type Bioelectrocatalysis by Membrane-Bound d-Fructose Dehydrogenase with Structural Bioelectrochemistry.” ACS Catalysis 2023 13 (20), 13828-13837, doi: 10.1021/acscatal.3c03769
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60. Bui, Han Ba et al. “Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus.” Nature communications vol. 14,1 4770. 8 Aug. 2023, doi:10.1038/s41467-023-40521-5
61. Yang, Shangyu et al. “Structural and functional insights into the modulation of T cell costimulation by monkeypox virus protein M2.” Nature communications vol. 14,1 5186. 25 Aug. 2023, doi:10.1038/s41467-023-40748-2
62. Abe, Kazuhiro et al. “Deep learning driven de novo drug design based on gastric proton pump structures.” Communications biology vol. 6,1 956. 19 Sep. 2023, doi:10.1038/s42003-023-05334-8
63. Zhao, Yan et al. “Cryo-EM structures of African swine fever virus topoisomerase.” mBio vol. 14,5 (2023): e0122823. doi:10.1128/mbio.01228-23
64. Torino, Stefania et al. “Time-resolved cryo-EM using a combination of droplet microfluidics with on-demand jetting.” Nature methods vol. 20,9 (2023): 1400-1408. doi:10.1038/s41592-023-01967-z
65. Anzai, Itsuki et al. “Characterization of a neutralizing antibody that recognizes a loop region adjacent to the receptor-binding interface of the SARS-CoV-2 spike receptor-binding domain.” Microbiology spectrum, e0365523. 28 Feb. 2024, doi:10.1128/spectrum.03655-23
66. Adachi Taiki et al. “Experimental and Theoretical Insights into Bienzymatic Cascade for Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases.” ACS Catalysis 2023 13 (12), 7955-7965. doi: 10.1021/acscatal.3c01962
67. Li, Long et al. “Spatiotemporal Landscape for the Sophisticated Transformation of Protein Assemblies Defined by Multiple Supramolecular Interactions.” ACS nano vol. 17,15 (2023): 15001-15011. doi:10.1021/acsnano.3c04029
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76. Gupta, Jyoti et al. “Plakophilin-3 Binds the Membrane and Filamentous Actin without Bundling F-Actin.” International journal of molecular sciences vol. 24,11 9458. 29 May. 2023, doi:10.3390/ijms24119458
77. Pei, Xudong et al. “Cryogenic electron ptychographic single particle analysis with wide bandwidth information transfer.” Nature communications vol. 14,1 3027. 25 May. 2023, doi:10.1038/s41467-023-38268-0
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84. Himiyama, Tomoki et al. “Unnaturally Distorted Hexagonal Protein Ring Alternatingly Reorganized from Two Distinct Chemically Modified Proteins.” Bioconjugate chemistry, 10.1021/acs.bioconjchem.3c00057. 8 Mar. 2023, doi:10.1021/acs.bioconjchem.3c00057
85. Pöll, Gisela et al. “Impact of the yeast S0/uS2-cluster ribosomal protein rpS21/eS21 on rRNA folding and the architecture of small ribosomal subunit precursors.” PloS one vol. 18,3 e0283698. 30 Mar. 2023, doi:10.1371/journal.pone.0283698
86. Rangarajan, Erumbi S et al. “Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments.” Communications biology vol. 6,1 276. 16 Mar. 2023, doi:10.1038/s42003-023-04610-x
87. Nagao, Ryo et al. “Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120.” Nature communications vol. 14,1 920. 17 Feb. 2023, doi:10.1038/s41467-023-36504-1
88. Fujita, Junso et al. “Epoxidized graphene grid for highly efficient high-resolution cryoEM structural analysis.” Scientific reports vol. 13,1 2279. 8 Feb. 2023, doi:10.1038/s41598-023-29396-0
89. Yuya Sasajima et al. “Cryo-electron microscopy of cytoskeletal ‘fibril’ involved in Spiroplasma swimming” bioRxiv 2023.06.28.546849; doi:10.1101/2023.06.28.546849
90. Yamamoto, Eiichi et al. “Folded, undulating, and fibrous doxorubicin sulfate crystals in liposomes.” Nanomedicine : nanotechnology, biology, and medicine vol. 47 (2023): 102631. doi:10.1016/j.nano.2022.102631
91. Nakanishi, Atsuko et al. “Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding.” The Journal of biological chemistry, 102884. 7 Jan. 2023, doi:10.1016/j.jbc.2023.102884
92. Yin, Jiayi et al. “Structural transitions during the cooperative assembly of baculovirus single-stranded DNA-binding protein on ssDNA.” Nucleic acids research vol. 50,22 (2022): 13100-13113. doi:10.1093/nar/gkac1142
93. Wang, Xiaoshen et al. “Target RNA-guided protease activity in type III-E CRISPR-Cas system.” Nucleic acids research vol. 50,22 (2022): 12913-12923. doi:10.1093/nar/gkac1151
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95. Nakano, Atsuki et al. “Structural basis of unisite catalysis of bacterial F0F1-ATPase.” PNAS nexus vol. 1,3 pgac116. 11 Jul. 2022, doi:10.1093/pnasnexus/pgac116
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98. Yu, Guimei et al. “Structure and function of a bacterial type III-E CRISPR-Cas7-11 complex.” Nature microbiology vol. 7,12 (2022): 2078-2088. doi:10.1038/s41564-022-01256-z
99. Shkumatov, Alexander V et al. “Structural insight into Tn3 family transposition mechanism.” Nature communications vol. 13,1 6155. 18 Oct. 2022, doi:10.1038/s41467-022-33871-z
100. Haney, Joanne et al. “Coinfection by influenza A virus and respiratory syncytial virus produces hybrid virus particles.” Nature microbiology vol. 7,11 (2022): 1879-1890. doi:10.1038/s41564-022-01242-5
101. Fréchin, Léo et al. “High-resolution cryo-EM performance comparison of two latest-generation cryo electron microscopes on the human ribosome.” Journal of structural biology, vol. 215,1 107905. 12 Oct. 2022, doi:10.1016/j.jsb.2022.107905
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109. Hogrel, Gaëlle et al. “Cyclic nucleotide-induced helical structure activates a TIR immune effector.” Nature vol. 608,7924 (2022): 808-812. doi:10.1038/s41586-022-05070-9
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111. Shi, Yun et al. “Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules.” Molecular cell vol. 82,9 (2022): 1643-1659.e10. doi:10.1016/j.molcel.2022.03.007
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