Primary Literature
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- Barth R, et al. (2025) SMC motor proteins extrude DNA asymmetrically and can switch directions. Cell 188(3):749-763.e21 PMID: 39824185
- Phipps J, et al. (2025) Cohesin complex oligomerization maintains end-tethering at DNA double-strand breaks. Nat Cell Biol 27(1):118-129 PMID: 39482358
- Jeppsson K, et al. (2024) Loop-extruding Smc5/6 organizes transcription-induced positive DNA supercoils. Mol Cell 84(5):867-882.e5 PMID: 38295804
- Li Q, et al. (2024) Cryo-EM structures of Smc5/6 in multiple states reveal its assembly and functional mechanisms. Nat Struct Mol Biol 31(10):1532-1542 PMID: 38890552
- Li S, et al. (2023) Molecular basis for Nse5-6 mediated regulation of Smc5/6 functions. Proc Natl Acad Sci U S A 120(45):e2310924120 PMID: 37903273
- Taschner M and Gruber S (2023) DNA segment capture by Smc5/6 holocomplexes. Nat Struct Mol Biol 30(5):619-628 PMID: 37012407
- Hallett ST, et al. (2022) Cryo-EM structure of the Smc5/6 holo-complex. Nucleic Acids Res 50(16):9505-9520 PMID: 35993814
- Li S, et al. (2022) Multifaceted regulation of the sumoylation of the Sgs1 DNA helicase. J Biol Chem 298(7):102092 PMID: 35654140
- Yu Y, et al. (2022) Cryo-EM structure of DNA-bound Smc5/6 reveals DNA clamping enabled by multi-subunit conformational changes. Proc Natl Acad Sci U S A 119(23):e2202799119 PMID: 35648833
- Agashe S, et al. (2021) Smc5/6 functions with Sgs1-Top3-Rmi1 to complete chromosome replication at natural pause sites. Nat Commun 12(1):2111 PMID: 33833229
- Dyson S, et al. (2021) Condensin minimizes topoisomerase II-mediated entanglements of DNA in vivo. EMBO J 40(1):e105393 PMID: 33155682
- Hallett ST, et al. (2021) Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex. Nucleic Acids Res 49(8):4534-4549 PMID: 33849072
- Taschner M, et al. (2021) Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding. EMBO J 40(15):e107807 PMID: 34191293
- Varejão N, et al. (2021) Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs. Nat Commun 12(1):7013 PMID: 34853311
- Gutierrez-Escribano P, et al. (2020) Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction. Mol Cell 80(6):1039-1054.e6 PMID: 33301732
- Wani S, et al. (2018) Interaction of the Saccharomyces cerevisiae RING-domain protein Nse1 with Nse3 and the Smc5/6 complex is required for chromosome replication and stability. Curr Genet 64(3):599-617 PMID: 29119272
- Bustard DE, et al. (2016) Non-Smc element 5 (Nse5) of the Smc5/6 complex interacts with SUMO pathway components. Biol Open 5(6):777-85 PMID: 27215325
- Moradi-Fard S, et al. (2016) Smc5/6 Is a Telomere-Associated Complex that Regulates Sir4 Binding and TPE. PLoS Genet 12(8):e1006268 PMID: 27564449
- Bermúdez-López M, et al. (2015) ATPase-dependent control of the Mms21 SUMO ligase during DNA repair. PLoS Biol 13(3):e1002089 PMID: 25764370
- Kanno T, et al. (2015) The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker. Cell Rep 12(9):1471-82 PMID: 26299966
- Leung GP, et al. (2011) Rtt107 is required for recruitment of the SMC5/6 complex to DNA double strand breaks. J Biol Chem 286(29):26250-7 PMID: 21642432
- Betts Lindroos H, et al. (2006) Chromosomal association of the Smc5/6 complex reveals that it functions in differently regulated pathways. Mol Cell 22(6):755-767 PMID: 16793545
- Zhao X and Blobel G (2005) A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc Natl Acad Sci U S A 102(13):4777-82 PMID: 15738391
- Fujioka Y, et al. (2002) Identification of a novel non-structural maintenance of chromosomes (SMC) component of the SMC5-SMC6 complex involved in DNA repair. J Biol Chem 277(24):21585-91 PMID: 11927594