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Alessandro Bianchi
Researcher at University of Sussex
Publications - 33
Citations - 5780
Alessandro Bianchi is an academic researcher from University of Sussex. The author has contributed to research in topics: Telomere & Telomerase. The author has an hindex of 19, co-authored 32 publications receiving 5450 citations. Previous affiliations of Alessandro Bianchi include Rockefeller University & University of Geneva.
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Journal ArticleDOI
Mammalian Telomeres End in a Large Duplex Loop
Jack D. Griffith,Laurey Comeau,Soraya Rosenfield,Rachel M. Stansel,Alessandro Bianchi,Heidi Moss,Titia de Lange +6 more
TL;DR: Electron microscopy reported here demonstrated that TRF2 can remodel linear telomeric DNA into large duplex loops (t loops) in vitro, which may provide a general mechanism for the protection and replication of telomeres.
Journal ArticleDOI
Control of human telomere length by TRF1 and TRF2.
Agata Smogorzewska,Bas van Steensel,Alessandro Bianchi,Stefan Oelmann,Matthias Schaefer,Gisela Schnapp,Titia de Lange +6 more
TL;DR: In this paper, the authors reported that TRF2, a TRF1-related protein previously implicated in protection of chromosome ends, is a second negative regulator of telomere length.
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TRF1 is a dimer and bends telomeric DNA
TL;DR: It is shown that TRF1 binds DNA as a dimer using a large conserved domain near the N‐terminus of the protein for TRF2–TRF1 interactions, suggesting that DNA bending is important for the function of telomeres in yeast and mammals.
Journal ArticleDOI
53BP1-RIF1-shieldin counteracts DSB resection through CST- and Polα-dependent fill-in.
Zachary Mirman,Francisca Lottersberger,Francisca Lottersberger,Hiroyuki Takai,Tatsuya Kibe,Yi Gong,Kaori K. Takai,Alessandro Bianchi,Alessandro Bianchi,Michal Zimmermann,Michal Zimmermann,Daniel Durocher,Titia de Lange +12 more
TL;DR: Data suggest that CST–Polα-mediated fill-in helps to control the repair of double-strand breaks by 53BP1, RIF1 and shieldin.
Journal ArticleDOI
TRF1 binds a bipartite telomeric site with extreme spatial flexibility
Alessandro Bianchi,Alessandro Bianchi,Rachel M. Stansel,Louise Fairall,Jack D. Griffith,Daniela Rhodes,Titia de Lange +6 more
TL;DR: It is proposed that a flexible segment in TRF1 allows the two Myb domains of the homodimer to interact independently with variably positioned half‐sites, directly relevant to the proposed architectural role ofTRF1.