Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Samantha L. Sanford"'
Autor:
Angela M. Hinchie, Samantha L. Sanford, Kelly E. Loughridge, Rachel M. Sutton, Anishka H. Parikh, Agustin A. Gil Silva, Daniel I. Sullivan, Pattra Chun-On, Matthew R. Morrell, John F. McDyer, Patricia L. Opresko, Jonathan K. Alder
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract The telomere sequence, TTAGGG, is conserved across all vertebrates and plays an essential role in suppressing the DNA damage response by binding a set of proteins termed shelterin. Changes in the telomere sequence impair shelterin binding, i
Externí odkaz:
https://doaj.org/article/1d8229a837ff47dab3abeb379196b575
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Telomerase enzymes add telomeric repeats to the end of linear chromosomes. Here the authors reveal mechanisms by which oxidized dNTPs and therapeutic dNTPs inhibit telomerase-mediated telomere elongation.
Externí odkaz:
https://doaj.org/article/22fa7349443040f6a588333c1ddf1b4e
Autor:
Matthew A Schaich, Samantha L Sanford, Griffin A Welfer, Samuel A Johnson, Thu H Khoang, Patricia L Opresko, Bret D Freudenthal
Publikováno v:
eLife, Vol 9 (2020)
Telomerase extends telomere sequences at chromosomal ends to protect genomic DNA. During this process it must select the correct nucleotide from a pool of nucleotides with various sugars and base pairing properties, which is critically important for
Externí odkaz:
https://doaj.org/article/4e22fc7309344751ac64f8a5732134ad
Autor:
Samantha L. Sanford, Tapas Paul, Arindam Bose, Hui Ting Lee, Sua Myong, Joshua Choe, Patricia L. Opresko
Publikováno v:
Biochemistry
Telomeres are hot spots for mutagenic oxidative and methylation base damage due to their high guanine content. We used single-molecule fluorescence resonance energy transfer detection and biochemical assays to determine how different positions and ty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::671582f5f4ad0e0c17b62d5561e8fae8
https://doi.org/10.1021/acs.biochem.0c00434
https://doi.org/10.1021/acs.biochem.0c00434
Publikováno v:
DNA Repair. 122:103446
Understanding how benign nevi can progress to invasive and metastatic Department of Environmental and Occupational Health, University of Pittsburgh School of Public Health, USAelanoma is critical for developing interventions and therapeutics for this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88ad55b0df3f2bd9b6f4cbcdcfb3bbb4
https://doi.org/10.1016/j.dnarep.2022.103446
https://doi.org/10.1016/j.dnarep.2022.103446
Publikováno v:
DNA Repair (Amst)
Telomeres at the ends of linear chromosomes are essential for genome maintenance and sustained cellular proliferation, but shorten with each cell division. Telomerase, a specialized reverse transcriptase with its own integral RNA template, compensate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73830b887984257dc718608f59e0109d
https://europepmc.org/articles/PMC8526386/
https://europepmc.org/articles/PMC8526386/
Autor:
Dhruv Bhattaram, Ming Liu, Samantha L. Sanford, Ariana C. Detwiler, Robert Riehn, Guozhou Xu, Pengyu Hao, Pengning Xu, Jacob Piehler, Patricia L. Opresko, Changjiang You, Warren Lu, Hai Pan, Chelsea Mahn, Hong Wang, Xinyun Gu, Ryan P. Barnes, Qingyu Tang, Parminder Kaur, Keith Weninger
Publikováno v:
The Journal of Biological Chemistry
TIN2 is a core component of the shelterin complex linking double-stranded telomeric DNA-binding proteins (TRF1 and TRF2) and single-strand overhang-binding proteins (TPP1-POT1). In vivo, the large majority of TRF1 and TRF2 exist in complexes containi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fad43c1ddf3cd2ca8b078cc7c09526cc
https://doi.org/10.1016/j.jbc.2021.101080
https://doi.org/10.1016/j.jbc.2021.101080
Publikováno v:
Biophysical Journal. 116:39a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f6aa47b3b82769895c4c91ef4a6fd13
https://doi.org/10.1016/j.bpj.2018.11.256
https://doi.org/10.1016/j.bpj.2018.11.256