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Article

The Human Telomeric Protein TRF1 Specifically Recognizes Nucleosomal Binding Sites and Alters Nucleosome Structure

20 May 2006

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Share to DNA Repair Mechanisms
Share to Genomics and Chromatin Dynamics
Share to Telomeres, Telomerase, and Senescence

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 16756990
DOI: 10.1016/j.jmb.2006.04.071

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Human Telomeric Protein TRF1 Specifically Recognizes Nucleosomal Binding Sites and Alters Nucleosome StructurePMID 16756990Read ↗

How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high‐resolution crystal structuresSemantic proximity Read ↗

The human telomeric protein hTRF1 induces telomere-specific nucleosome mobilitySemantic proximity Read ↗

Structure of the TRFH Dimerization Domain of the Human Telomeric Proteins TRF1 and TRF2Semantic proximity Read ↗

Human telomeric protein TRF2 associates with genomic double-strand breaks as an early response to DNA damageSemantic proximity Read ↗

Human telomeres contain two distinct Myb–related proteins, TRF1 and TRF2Semantic proximity Read ↗

Identification and characterization of a TRF2-like telomere-binding protein in ArabidopsisSemantic proximity Read ↗

Cyclin B-dependent kinase 1 regulates human TRF1 to modulate the resolution of sister telomeresSemantic proximity Read ↗

Structural basis of telomeric nucleosome recognition by shelterin factor TRF1Semantic proximity Read ↗

Telomeric localization of TRF2, a novel human telobox proteinSemantic proximity Read ↗

Human telomeric proteins occupy selective interstitial sitesSemantic proximity Read ↗

Solution Structure of a Telomeric DNA Complex of Human TRF1Semantic proximity Read ↗

TRF1 promotes parallel pairing of telomeric tracts in vitroSemantic proximity Read ↗

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