Laura A. Banaszynski
University of Texas Southwestern Medical Center
47 Papers
282 Citations
Laura A. Banaszynski is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Chromatin & Biology. The author has an hindex of 20, co-authored 37 publications. Previous affiliations of Laura A. Banaszynski include Stanford University & Rockefeller University.
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Papers
Distinct Factors Control Histone Variant H3.3 Localization at Specific Genomic Regions
Aaron D Goldberg,Laura A. Banaszynski,Kyung-Min Noh,Peter W. Lewis,Simon J. Elsaesser,Sonja C. Stadler,Scott Dewell,Martin J. Law,Xingyi Guo,Xuan Li,Duancheng Wen,Duancheng Wen,Ariane Chapgier,Russell Dekelver,Jeffrey C. Miller,Ya Li Lee,Elizabeth A. Boydston,Michael C. Holmes,Philip D. Gregory,John M. Greally,Shahin Rafii,Shahin Rafii,Chingwen Yang,Peter J. Scambler,David Garrick,Richard J. Gibbons,Douglas R. Higgs,Ileana M. Cristea,Fyodor D. Urnov,Deyou Zheng,C. David Allis +30 more
TL;DR: It is demonstrated that multiple and distinct factors are responsible for H3.3 localization at specific genomic locations in mammalian cells.
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Inhibition of PRC2 Activity by a Gain-of-Function H3 Mutation Found in Pediatric Glioblastoma
Peter W. Lewis,Manuel M. Müller,Matthew S. Koletsky,Francisco Cordero,Shu Lin,Laura A. Banaszynski,Benjamin A. Garcia,Tom W. Muir,Oren J. Becher,C. David Allis +9 more
TL;DR: It is proposed that K-to-M substitutions may represent a mechanism to alter epigenetic states in a variety of pathologies and be sufficient to cause specific reduction in methylation through inhibition of SET-domain enzymes.
A Rapid, Reversible, and Tunable Method to Regulate Protein Function in Living Cells Using Synthetic Small Molecules
Laura A. Banaszynski,Ling chun Chen,Lystranne A. Maynard-Smith,A. G.Lisa Ooi,Thomas J. Wandless +4 more
TL;DR: A general technique to regulate the stability of specific proteins in mammalian cells using cell-permeable, synthetic molecules and genetic fusion of the destabilizing domain to a gene of interest ensures specificity, and the attendant small-molecule control confers speed, reversibility, and dose-dependence to this method.
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Characterization of the FKBP.rapamycin.FRB ternary complex.
TL;DR: Rapamycin's ability to bind to FRB, and by extension to mTOR, in the absence of FKBP is of little consequence under physiological conditions, and protein-protein interactions at the FK BP12-FRB interface play a role in the stability of the ternary complex.
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Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells
Simon J. Elsässer,Simon J. Elsässer,Kyung-Min Noh,Nichole Diaz,C. David Allis,Laura A. Banaszynski +5 more
TL;DR: This study identifies a unique heterochromatin state marked by the presence of both H3.3 and H3K9me3, and establishes an important role for H 3.3 in control of ERV retrotransposition in embryonic stem cells.