Year |
Citation |
Score |
2023 |
Singh V, Itoh Y, Del'Olio S, Hassan A, Naschberger A, Flygaard RK, Nobe Y, Izumikawa K, Aibara S, Andréll J, Whitford PC, Barrientos A, Taoka M, Amunts A. Structure of mitoribosome reveals mechanism of mRNA binding, tRNA interactions with L1 stalk, roles of cofactors and rRNA modifications. Biorxiv : the Preprint Server For Biology. PMID 37503168 DOI: 10.1101/2023.05.24.542018 |
0.785 |
|
2021 |
Aibara S, Dienemann C, Cramer P. Structure of an inactive RNA polymerase II dimer. Nucleic Acids Research. 49: 10747-10755. PMID 34530439 DOI: 10.1093/nar/gkab783 |
0.302 |
|
2021 |
Fianu I, Dienemann C, Aibara S, Schilbach S, Cramer P. Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2. Communications Biology. 4: 606. PMID 34021257 DOI: 10.1038/s42003-021-02088-z |
0.349 |
|
2021 |
Sighel D, Notarangelo M, Aibara S, Re A, Ricci G, Guida M, Soldano A, Adami V, Ambrosini C, Broso F, Rosatti EF, Longhi S, Buccarelli M, D'Alessandris QG, Giannetti S, et al. Inhibition of mitochondrial translation suppresses glioblastoma stem cell growth. Cell Reports. 35: 109024. PMID 33910005 DOI: 10.1016/j.celrep.2021.109024 |
0.644 |
|
2021 |
Rengachari S, Schilbach S, Aibara S, Dienemann C, Cramer P. Structure of human Mediator-RNA polymerase II pre-initiation complex. Nature. PMID 33902108 DOI: 10.1038/s41586-021-03555-7 |
0.308 |
|
2021 |
Tobiasson V, Gahura O, Aibara S, Baradaran R, Zíková A, Amunts A. Interconnected assembly factors regulate the biogenesis of mitoribosomal large subunit. The Embo Journal. e106292. PMID 33576519 DOI: 10.15252/embj.2020106292 |
0.75 |
|
2020 |
Forsberg BO, Aibara S, Howard RJ, Mortezaei N, Lindahl E. Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex. Nature Communications. 11: 4667. PMID 32938938 DOI: 10.1038/S41467-020-18401-Z |
0.451 |
|
2020 |
Aibara S, Singh V, Modelska A, Amunts A. Structural basis of mitochondrial translation. Elife. 9. PMID 32812867 DOI: 10.7554/Elife.58362 |
0.747 |
|
2020 |
Aibara S, Singh V, Modelska A, Amunts A. Author response: Structural basis of mitochondrial translation Elife. DOI: 10.7554/Elife.58362.Sa2 |
0.687 |
|
2019 |
Bigalke JM, Aibara S, Roth R, Dahl G, Gordon E, Dorbéus S, Amunts A, Sandmark J. Cryo-EM structure of the activated RET signaling complex reveals the importance of its cysteine-rich domain. Science Advances. 5: eaau4202. PMID 31392261 DOI: 10.1126/Sciadv.Aau4202 |
0.671 |
|
2018 |
Aibara S, Andréll J, Singh V, Amunts A. Rapid Isolation of the Mitoribosome from HEK Cells. Journal of Visualized Experiments : Jove. PMID 30346389 DOI: 10.3791/57877 |
0.704 |
|
2018 |
Perez Boerema A, Aibara S, Paul B, Tobiasson V, Kimanius D, Forsberg BO, Wallden K, Lindahl E, Amunts A. Publisher Correction: Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor. Nature Plants. PMID 30038411 DOI: 10.1038/S41477-018-0203-0 |
0.712 |
|
2018 |
Boerema AP, Aibara S, Paul B, Tobiasson V, Kimanius D, Forsberg BO, Wallden K, Lindahl E, Amunts A. Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor. Nature Plants. 4: 212-217. PMID 29610536 DOI: 10.2210/Pdb6Eri/Pdb |
0.741 |
|
2017 |
Forsberg BO, Aibara S, Kimanius D, Paul B, Lindahl E, Amunts A. Cryo-EM reconstruction of the chlororibosome to 3.2 Å resolution within 24 h. Iucrj. 4: 723-727. PMID 29123673 DOI: 10.1107/S205225251701226X |
0.61 |
|
2017 |
Rorbach J, Aibara S, Amunts A. Ribosome origami. Nature Structural & Molecular Biology. 24: 879-881. PMID 29112687 DOI: 10.1038/nsmb.3497 |
0.663 |
|
2017 |
Matzov D, Aibara S, Basu A, Zimmerman E, Bashan A, Yap MF, Amunts A, Yonath AE. The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus. Nature Communications. 8: 723. PMID 28959035 DOI: 10.1038/S41467-017-00753-8 |
0.741 |
|
2017 |
Brown A, Rathore S, Kimanius D, Aibara S, Bai XC, Rorbach J, Amunts A, Ramakrishnan V. Structures of the human mitochondrial ribosome in native states of assembly. Nature Structural & Molecular Biology. PMID 28892042 DOI: 10.1038/Nsmb.3464 |
0.774 |
|
2017 |
Gordon JM, Aibara S, Stewart M. Structure of the Sac3 RNA-binding M-region in the Saccharomyces cerevisiae TREX-2 complex. Nucleic Acids Research. PMID 28334829 DOI: 10.1093/Nar/Gkx158 |
0.612 |
|
2017 |
Aibara S, Gordon JM, Riesterer AS, McLaughlin SH, Stewart M. Structural basis for the dimerization of Nab2 generated by RNA binding provides insight into its contribution to both poly(A) tail length determination and transcript compaction in Saccharomyces cerevisiae. Nucleic Acids Research. 45: 1529-1538. PMID 28180315 DOI: 10.1093/Nar/Gkw1224 |
0.637 |
|
2016 |
Aibara S, Gordon JM, Riesterer AS, McLaughlin SH, Stewart M. Structural basis for the dimerization of Nab2 generated by RNA binding provides insight into its contribution to both poly(A) tail length determination and transcript compaction in Saccharomyces cerevisiae. Nucleic Acids Research. PMID 27932457 DOI: 10.1093/nar/gkw1224 |
0.601 |
|
2016 |
Wiedmann MM, Tan YS, Wu Y, Aibara S, Xu W, Sore HF, Verma CS, Itzhaki L, Stewart M, Brenton JD, Spring DR. Development of Cell-Permeable, Non-Helical Constrained Peptides to Target a Key Protein-Protein Interaction in Ovarian Cancer. Angewandte Chemie (International Ed. in English). PMID 27918136 DOI: 10.1002/Anie.201609427 |
0.567 |
|
2016 |
Li Q, Chang L, Aibara S, Yang J, Zhang Z, Barford D. WD40 domain of Apc1 is critical for the coactivator-induced allosteric transition that stimulates APC/C catalytic activity. Proceedings of the National Academy of Sciences of the United States of America. PMID 27601667 DOI: 10.1073/Pnas.1607147113 |
0.336 |
|
2016 |
Aibara S, Bai XC, Stewart M. The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. Journal of Structural Biology. PMID 27422657 DOI: 10.1016/J.Jsb.2016.07.007 |
0.594 |
|
2016 |
Wiedmann MM, Aibara S, Spring DR, Stewart M, Brenton JD. Structural and calorimetric studies demonstrate that the Hepatocyte Nuclear Factor1β (HNF1β) transcription factor is imported into the nucleus via a monopartite NLS sequence. Journal of Structural Biology. PMID 27346421 DOI: 10.1016/J.Jsb.2016.06.018 |
0.599 |
|
2015 |
Aibara S, Valkov E, Lamers MH, Dimitrova L, Hurt E, Stewart M. Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum. Acta Crystallographica. Section F, Structural Biology Communications. 71: 876-88. PMID 26144233 DOI: 10.1107/S2053230X15008766 |
0.637 |
|
2015 |
Dimitrova L, Valkov E, Aibara S, Flemming D, McLaughlin SH, Hurt E, Stewart M. Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2. Structure (London, England : 1993). PMID 26051714 DOI: 10.1016/J.Str.2015.05.002 |
0.642 |
|
2015 |
Aibara S, Katahira J, Valkov E, Stewart M. The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA. Nucleic Acids Research. 43: 1883-93. PMID 25628361 DOI: 10.1093/Nar/Gkv032 |
0.631 |
|
2015 |
Aibara S, Valkov E, Lamers M, Stewart M. Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface. Nucleic Acids Research. 43: 1927-36. PMID 25618852 DOI: 10.1093/Nar/Gkv030 |
0.608 |
|
2015 |
Aibara S, Valkov E, Lamers MH, Dimitrova L, Hurt E, Stewart M. Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum Acta Crystallographica Section:F Structural Biology Communications. 71: 876-888. DOI: 10.1107/S2053230X15008766 |
0.567 |
|
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