T
Tyler T. Hickman
Researcher at Massachusetts Eye and Ear Infirmary
Publications - 15
Citations - 5704
Tyler T. Hickman is an academic researcher from Massachusetts Eye and Ear Infirmary. The author has contributed to research in topics: Stress granule & Cochlea. The author has an hindex of 11, co-authored 14 publications receiving 4813 citations. Previous affiliations of Tyler T. Hickman include Tufts Medical Center & Tufts University.
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Journal ArticleDOI
Selective inhibition of BET bromodomains.
Panagis Filippakopoulos,Jun Qi,Sarah Picaud,Yao Shen,William B. Smith,Oleg Fedorov,Elizabeth M. Morse,T. Keates,Tyler T. Hickman,I. Felletar,Martin Philpott,Shonagh Munro,Michael R. McKeown,Yuchuan Wang,Amanda L. Christie,Nathan West,Michael J. Cameron,Brian E. Schwartz,Tom D. Heightman,Nicholas B. La Thangue,Christopher A. French,Olaf Wiest,Andrew L. Kung,Stefan Knapp,Stefan Knapp,James E. Bradner +25 more
TL;DR: A cell-permeable small molecule (JQ1) that binds competitively to acetyl-lysine recognition motifs, or bromodomains is reported, establishing proof-of-concept for targeting protein–protein interactions of epigenetic ‘readers’, and providing a versatile chemical scaffold for the development of chemical probes more broadly throughout the b romodomain family.
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G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits
Nancy Kedersha,Marc D. Panas,Christopher A. Achorn,Shawn M. Lyons,Sarah Tisdale,Tyler T. Hickman,Marshall P. Thomas,Judy Lieberman,Gerald M. McInerney,Pavel Ivanov,Pavel Ivanov,Paul A. Anderson +11 more
TL;DR: Stress granule condensation of translationally arrested mRNAs requires G3BP and requires its RGG region for SGC and for interactions with 40S ribosomal subunits.
Journal ArticleDOI
Angiogenin-induced tRNA-derived Stress-induced RNAs Promote Stress-induced Stress Granule Assembly
Mohamed Emara,Pavel Ivanov,Tyler T. Hickman,Nemisha Dawra,Sarah Tisdale,Nancy Kedersha,Guo-fu Hu,Paul A. Anderson +7 more
TL;DR: It is shown that ANG inhibits protein synthesis and promotes arsenite- and pateamine A-induced assembly of stress granules (SGs) that are abrogated in cells transfected with the ANG inhibitor RNH1.
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BRD-NUT oncoproteins: a family of closely related nuclear proteins that block epithelial differentiation and maintain the growth of carcinoma cells.
Christopher A. French,Cherie L. Ramirez,J. Kolmakova,Tyler T. Hickman,Michael J. Cameron,M.E. Thyne,Jeffrey L. Kutok,Jeffrey A. Toretsky,A.K. Tadavarthy,Ursula R. Kees,Jonathan A. Fletcher,Jon C. Aster +11 more
TL;DR: Together, these data suggest that BRD–NUT fusion proteins contribute to carcinogenesis by associating with chromatin and interfering with epithelial differentiation.
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A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly.
TL;DR: The results suggest that O-GlcNAc modification of the translational machinery is required for aggregation of untranslated messenger ribonucleoproteins into SGs and the lack of enzymes of the hexosamine biosynthetic pathway in budding yeast may contribute to differences between mammalian SGs