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Beta-d-glucosyl-hydroxymethyluracil is a conserved DNA modification in kinetoplastid protozoans and is abundant in their telomeres [see comments]
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van Leeuwen F., Taylor M.C., Mondragon A., Moreau H., Gibson W., Kieft R., and Borst P. Beta-d-glucosyl-hydroxymethyluracil is a conserved DNA modification in kinetoplastid protozoans and is abundant in their telomeres [see comments]. Proc Natl Acad Sci USA 95 5 (1998) 2366-2371
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The telomeric GGGTTA repeats of Trypanosoma brucei contain the hypermodified base J in both strands
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van Leeuwen F., Wijsman E.R., Kuyl-Yeheskiely E., van der Marel G.A., van Boom J.H., and Borst P. The telomeric GGGTTA repeats of Trypanosoma brucei contain the hypermodified base J in both strands. Nucl Acids Res 24 13 (1996) 2476-2482
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Localization of the modified base J in telomeric VSG gene expression sites of Trypanosoma brucei
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Biosynthesis and function of the modified DNA base beta-d-glucosyl-hydroxymethyluracil in Trypanosoma brucei
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Expression of the human DNA glycosylase hSMUG1 in Trypanosoma brucei causes DNA damage and interferes with J biosynthesis
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Ulbert S., Cross M., Boorstein R., Teebor G.W., and Borst P. Expression of the human DNA glycosylase hSMUG1 in Trypanosoma brucei causes DNA damage and interferes with J biosynthesis. Nucl Acids Res 30 18 (2002) 3919-3926
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The modified base J is the target for a novel DNA-binding protein in kinetoplastid protozoans
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Cross M., Kieft R., Sabatini R., et al. The modified base J is the target for a novel DNA-binding protein in kinetoplastid protozoans. EMBO J 18 21 (1999) 6573-6581
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J binding protein increases the level and retention of the unusual base J in trypanosome DNA
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Cross M., Kieft R., Sabatini R., Dirks-Mulder A., Chaves I., and Borst P. J binding protein increases the level and retention of the unusual base J in trypanosome DNA. Mol Microbiol 46 (2002) 37-47
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Regulation of trypanosome DNA glycosylation by a SWI2/SNF2-like protein
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Repression of polymerase I-mediated gene expression at Trypanosoma brucei telomeres
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Activation of trypanosome surface glycoprotein genes involves a duplication-transposition leading to an altered 3′ end
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