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Leonhard Schnittger Jürgen May Christina Kretschmer Peter G. Kremsner C. G. Meyer 《Immunogenetics》1996,44(5):405-406
The nucleotide sequence data reported in this paper have been submitted to the EMBL nucleotide sequence database and have
been assigned the accession number X96986. The nameDPB1
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6601 was officially assigned by the WHO Nomenclature Committee in May 1996. This follows the agreed policy that, subject to the
conditions stated in the most recent Nomenclature Report (Bodmer et al. 1995), names will be assigned to new sequences as
they are identified. Lists of such sequences will be published in the following WHO Nomenclature Report 相似文献
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Ishida H 《Journal of biomolecular structure & dynamics》2002,19(5):839-851
To elucidate the effect of guanine lesion produced by the oxidative damage on DNA, 1 nanosecond molecular dynamics simulations of native and oxidized DNA were performed. The target DNA molecules are dodecamer duplex d(CGCGAATTCGCG)(2) and its derivative duplex d(C(1)G(2)C(3)(8-oxoG)(4)A(5)A(6)T(7)T(8)C(9)G(10)C(11)G(12).d(C(13)G(14)C(15)G(16)A(17)A(18)T(19)T(20)C(21)G(22)C(23)G(24), which has one oxidized guanine, 7, 8-dihydro-8-oxoguanine (8-oxoG), at the fourth position. The local structural change due to the lesion of 8-oxoG and the global dynamic structure of the 8-oxoG DNA were studied. It was found that the 8-oxoG DNA remained structurally stable during the simulation due to newly produced hydrogen bonds around the (8-oxoG)(4) residue. However, there were distinguishable differences in structural parameters and dynamic property in the 8-oxoG DNA. The conformation around the (8-oxoG)(4) residue departed from the usual conformation of native DNA and took an unique conformation of epsilon-zeta in B(II) conformation and chi in high anti orientation at the (8-oxoG)(4) residue, and adopted a very low helical twist angle at the C(3):G(22)-(8-oxoG)(4):C21) step. Further analysis by principal component analysis indicated that the formation of the hydrogen bonds around the (8-oxoG)(4) residue plays a role as a trigger for the conformational transition of the 8-oxoG DNA in the conformational space. 相似文献
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Hisashi Ishida 《Journal of biomolecular structure & dynamics》2013,31(5):839-851
Abstract To elucidate the effect of guanine lesion produced by the oxidative damage on DNA, 1 nanosecond molecular dynamics simulations of native and oxidized DNA were performed. The target DNA molecules are dodecamer duplex d(CGCGAATTCGCG)2 and its derivative duplex d(C1G2C3(8-oxoG)4A5A6T7T8C9G10C11G12)·d(C13G14C15G16A17A18T19T20C21G22C23G24), which has one oxidized guanine, 7, 8-dihydro-8-oxoguanine (8-oxoG), at the fourth position. The local structural change due to the lesion of 8-oxoG and the global dynamic structure of the 8-oxoG DNA were studied. It was found that the 8-oxoG DNA remained structurally stable during the simulation due to newly produced hydrogen bonds around the (8-oxoG)4 residue. However, there were distinguishable differences in structural parameters and dynamic property in the 8-oxoG DNA. The conformation around the (8- oxoG)4 residue departed from the usual conformation of native DNA and took an unique conformation of ?-ζ in BII conformation and χ in high anti orientation at the (8-oxoG)4 residue, and adopted a very low helical twist angle at the C3:G22—(8-oxoG)4:C21 step. Further analysis by principal component analysis indicated that the formation of the hydrogen bonds around the (8-oxoG)4 residue plays a role as a trigger for the conformational transition of the 8-oxoG DNA in the conformational space. 相似文献
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Genetic and physical interactions between DPB11 and DDC1 in the yeast DNA damage response pathway 总被引:1,自引:0,他引:1
DPB11 is essential for DNA replication and S/M checkpoint control in Saccharomyces cerevisiae. The Dpb11 protein contains four BRCT domains, which have been proposed to be involved in protein-protein interactions. To further investigate the regulation and function of Dpb11, a yeast two-hybrid screen was carried out to identify proteins that physically interact with Dpb11. One positive clone isolated from the screen encoded a carboxyl-terminal fragment of Ddc1 (339-612 aa). Ddc1 is a DNA damage checkpoint protein, which, together with Mec3 and Rad17, has been proposed to form a PCNA-like complex and acts upstream in the DNA damage checkpoint pathways. We further determined that the carboxyl region of Dpb11 is required for its interaction with Ddc1. DDC1 and DPB11 also interact genetically. The Deltaddc1 dpb11-1 double mutant is more UV and MMS sensitive than the Deltaddc1 or the dpb11-1 single mutants. Furthermore, the double mutant is more hydroxyurea sensitive and displayed a lower restrictive temperature than dpb11-1. These results suggest that DPB11 and DDC1 may function in the same or parallel pathways after DNA damage and that DDC1 may play a role in responding to replication defects. 相似文献
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