Cold Spring Harbor Lab Press / Tzakos AG / Dionex / Hinnebusch AG / Lawrence Livermore National Laboratory / Arnim AG / Waters Kundert Trust / Bio-Rad / Teichmann SA / /
Country
United Kingdom / / /
Event
Funding / /
Facility
Hall RJ / eIF3-IRES-40S complex / GTP complex / University of Cambridge / Cornell University / ¶Lawrence Livermore National Laboratory / Cold Spring Harbor / University of California / /
IndustryTerm
high energy conditions / interaction network / high activation energy / virus internal ribosome entry site / eIF3 solution / acceleration energy / 20S pre-rRNA processing / tandem affinity protocol / energy / established interaction networks / internal ribosome entry site / gas-phase dissociation / control solution / gas phase / iterative search algorithm / /
Organization
University of California / Structural / University of California / Berkeley / Department of Biochemistry and Molecular Biology / ¶Lawrence Livermore National Laboratory / National Academy of Sciences / Cornell University / Department of Chemistry / Biotechnology and Biological Sciences Research Council / School of Medicine / Department of Biochemistry / University of California / Davis / University of Cambridge / Subunit / European Union / Royal Society / /
Person
Jennifer A. Doudna / Gabriela Ridlova / Matthew R. Schenauer / Daniel Barsky / Julie A. Leary / John W. Hershey / Min Zhou / Elaine Stephens / Alan M. Sandercock / Carol V. Robinson / Christopher S. Fraser / Theresa Yokoi-Fong / /
Position
messenger / Prichard PM / subunits Author / Proposed model for the eIF3 /
Product
eIF3 / /
ProvinceOrState
New York / Mississippi / California / /
PublishedMedium
Molecular and Cellular Biology / Molecular Biology / /
Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3 Min Zhou*, Alan M. Sandercock*, Christopher S. Fraser†, Gabriela Ridlova*, Elaine Stephens*, Matthew