Results 131 to 140 of about 4,397 (170)
ROS: their roles in diminished ovarian reserve. [PDF]
Chen X, Liu D.
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Conserved and unique features of terminal telomeric sequences in ALT-positive cancer cells. [PDF]
Azeroglu B +6 more
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hTERT Increases TRF2 to Induce Telomere Compaction and Extend Cell Replicative Lifespan. [PDF]
Adam N +15 more
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Rewiring for movements in meiotic prophase: regulators, roles, and evolutionary pathways. [PDF]
Xie W +4 more
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miR-23a-mediated TRF2 repression in CD4 T cells from PLWH. [PDF]
Nguyen LNT +12 more
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Inhibition of lagging strand replication by G-rich telomeric DNA and the shelterin subunit POT1
Leonard-Booker C +6 more
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TRF1 is a dimer and bends telomeric DNA [PDF]
TRF1 is a mammalian telomeric protein that binds to the duplex array of TTAGGG repeats at chromosome ends. TRF1 has homology to the DNA-binding domain of the Myb family of transcription factors but, unlike most Myb-related proteins, TRF1 carries one rather than multiple Myb-type DNA-binding motifs.
Arnaud Bianchi +2 more
exaly +3 more sources
Solution Structure of a Telomeric DNA Complex of Human TRF1 [PDF]
Mammalian telomeres consist of long tandem arrays of double-stranded TTAGGG sequence motif packaged by TRF1 and TRF2. In contrast to the DNA binding domain of c-Myb, which consists of three imperfect tandem repeats, DNA binding domains of both TRF1 and TRF2 contain only a single Myb repeat.
Hideyasu Okamura +2 more
exaly +3 more sources
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TRF1, a mammalian telomeric protein
Trends in Genetics, 1997Telomerase adds TTAGGG repeats onto mammalian chromosome ends, replenishing the terminal sequence loss incurred during DNA replication. This maintenance of telomeric DNA preserves binding sites for telomeric proteins, which form a protective nucleoprotein complex at chromosome ends.
S, Smith, T, de Lange
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A truncated acidic domain in Xenopus TRF1
Gene, 2006Telomere function is mediated by a complex of proteins bound to double-stranded and single-stranded telomeric repeats. A key player in this complex is TRF1, which binds to duplex TTAGGG repeats and acts as a negative regulator of telomere length. This protein's domain structure, as defined by studies with mammalian orthologs, consists of an N-terminal ...
N, Crumet +3 more
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