J
John H. Bushweller
Researcher at University of Virginia
Publications - 133
Citations - 7921
John H. Bushweller is an academic researcher from University of Virginia. The author has contributed to research in topics: RUNX1 & Fusion protein. The author has an hindex of 46, co-authored 128 publications receiving 7179 citations. Previous affiliations of John H. Bushweller include Karolinska Institutet & University of New Hampshire.
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Journal ArticleDOI
Haploinsufficiency of CBFA2 causes familial thrombocytopenia with propensity to develop acute myelogenous leukaemia
W.-J. Song,M. G. Sullivan,R. D. Legare,S Hutchings,Xiaolian Tan,Dubravka Kufrin,Janina Ratajczak,I. C. Resende,C. Haworth,R. Hock,Mignon L. Loh,C. Felix,Denis-Claude Roy,Lambert Busque,David M. Kurnit,Cheryl L. Willman,Alan M. Gewirtz,Nancy A. Speck,John H. Bushweller,Fugen Li,K. Gardiner,Mortimer Poncz,John M. Maris,D. G. Gilliland,D. G. Gilliland +24 more
TL;DR: The findings support a model for FPD/AML in which haploinsufficiency of CBFA2 causes an autosomal dominant congenital platelet defect and predisposes to the acquisition of additional mutations that cause leukaemia.
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The CBFβ Subunit Is Essential for CBFα2 (AML1) Function In Vivo
Qing Wang,Terryl Stacy,Janelle Miller,Amy F. Lewis,Ting Lei Gu,Xuemei Huang,John H. Bushweller,Jean Christophe Bories,Frederick W. Alt,Gabriella Ryan,Pengfei Liu,Anthony Wynshaw-Boris,Michael Binder,Miguel Marin-Padilla,Arlene H. Sharpe,Nancy A. Speck +15 more
TL;DR: It is demonstrated that homozygous mutation of the Cbfb gene results in the same phenotype as the Cbfa2 gene and that the CBFβ subunit is required for CBFα2 function in vivo.
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Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin.
TL;DR: The N-terminal domain of the influenza hemagglutinin is deduced to be a kinked, predominantly helical amphipathic structure that could perturb lipid packing and facilitate lipid mixing between juxtaposed membranes.
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Targeting transcription factors in cancer - from undruggable to reality.
TL;DR: This Review discusses the various approaches that are being explored to target transcription factors in cancer, with many of the inhibitors developed from such approaches now advancing to early clinical trials.
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Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
TL;DR: The three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solution is determined using heteronuclear NMR.