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• W4317685533 abstract "In this issue of Molecular Cell, Rotheneder et al. 1 Rotheneder M. Stakyte K. van de Logt E. Bartho J.D. Lammens K. Fan Y. Alt A. Kessler B. Jung C. Roos W.P. et al. Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions. Mol. Cell. 2022; 83: 167-185https://doi.org/10.1016/j.molcel.2022.12.003 Abstract Full Text Full Text PDF PubMed Scopus (4) Google Scholar elucidate the eukaroytic Mre11-Rad50-Nbs1 (MRN) complex quaternary architecture, which together with cryo-EM structures of bacterial Mre11-Rad50-DNA complexes, 2 Gut F. Kashammer L. Lammens K. Bartho J.D. Boggusch A.M. van de Logt E. Kessler B. Hopfner K.P. Structural mechanism of endonucleolytic processing of blocked DNA ends and hairpins by Mre11-Rad50. Mol. Cell. 2022; 82: 3513-3522.e6https://doi.org/10.1016/j.molcel.2022.07.019 Abstract Full Text Full Text PDF PubMed Scopus (4) Google Scholar resolves the basis for MRN assembly and its broad nuclease specificity regulating DNA double-strand break repair. In this issue of Molecular Cell, Rotheneder et al. 1 Rotheneder M. Stakyte K. van de Logt E. Bartho J.D. Lammens K. Fan Y. Alt A. Kessler B. Jung C. Roos W.P. et al. Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions. Mol. Cell. 2022; 83: 167-185https://doi.org/10.1016/j.molcel.2022.12.003 Abstract Full Text Full Text PDF PubMed Scopus (4) Google Scholar elucidate the eukaroytic Mre11-Rad50-Nbs1 (MRN) complex quaternary architecture, which together with cryo-EM structures of bacterial Mre11-Rad50-DNA complexes, 2 Gut F. Kashammer L. Lammens K. Bartho J.D. Boggusch A.M. van de Logt E. Kessler B. Hopfner K.P. Structural mechanism of endonucleolytic processing of blocked DNA ends and hairpins by Mre11-Rad50. Mol. Cell. 2022; 82: 3513-3522.e6https://doi.org/10.1016/j.molcel.2022.07.019 Abstract Full Text Full Text PDF PubMed Scopus (4) Google Scholar resolves the basis for MRN assembly and its broad nuclease specificity regulating DNA double-strand break repair. Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functionsRotheneder et al.Molecular CellDecember 27, 2022In BriefRotheneder et al. determine the structure of eukaryotic Mre11-Rad50-Nbs1, reveal the basis for Nbs1 interaction with the Mre11 dimer, uncover ATP-dependent and -independent DNA-binding modes for DNA ends and internal DNA, and reveal that Rad50 coiled-coil apex tetramers form DNA-tethering structures in DNA double-strand break repair. Full-Text PDF" @default.
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• W4317685533 title "The ends in sight: Mre11-Rad50-Nbs1 complex structures come into focus" @default.
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