Molecular basis and quantitative assessment of TRF1 and TRF2 protein interactions with TIN2 and Apollo peptides
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/s00249-016-1157-7.pdf
Reference42 articles.
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3. Bianchi A, Smith S, Chong L, Elias P, deLange T (1997) TRF1 is a dimer and bends telomeric DNA. EMBO J 16:1785–1794
4. Bianchi A, Stansel R, Fairall L, Griffith J, Rhodes D, deLange T (1999) TRF1 binds a bipartite telomeric site with extreme spatial flexibility. EMBO J 18:5735–5744
5. Bidzinska J, Baginski M, Skladanowski A (2014) Novel anticancer strategy aimed at targeting shelterin complexes by the induction of structural changes in telomeric DNA: hitting two birds with one stone. Curr Cancer Drug Targets 14:201–216
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1. TRF1 and TRF2: pioneering targets in telomere-based cancer therapy;Journal of Cancer Research and Clinical Oncology;2024-07-16
2. Modified Peptide Molecules As Potential Modulators of Shelterin Protein Functions; TRF1;Chemistry – A European Journal;2023-09-04
3. Therapeutic strategies for targeting telomerase in cancer;Medicinal Research Reviews;2020-03
4. Expression of telomere repeat binding factor 1 and TRF2 in Alzheimer’s disease and correlation with clinical parameters;Neurological Research;2019-02-14
5. The structurally similar TRFH domain of TRF1 and TRF2 dimers shows distinct behaviour towards TIN2;Archives of Biochemistry and Biophysics;2018-03
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