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TRF1 binds a bipartite telomeric site with extreme spatial flexibility.

TRF1 is a key player in telomere length regulation. Because length control was proposed to depend on the architecture of telomeres, we studied how TRF1 binds telomeric TTAGGG repeat DNA and alters its conformation. Although the single Myb-type helix-turn-helix motif of a TRF1 monomer can interact wi...

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Hlavní autoři: Bianchi, A, Stansel, R M, Fairall, L, Griffith, J D, Rhodes, D, de Lange, T
Médium: Artigo
Jazyk:Inglês
Vydáno: 1999
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1171640/
https://ncbi.nlm.nih.gov/pubmed/10523316
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.20.5735
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