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Israel S. Fernández
Researcher at Columbia University
Publications - 45
Citations - 3237
Israel S. Fernández is an academic researcher from Columbia University. The author has contributed to research in topics: Ribosome & Eukaryotic Ribosome. The author has an hindex of 21, co-authored 41 publications receiving 2661 citations. Previous affiliations of Israel S. Fernández include Medical Research Council & Spanish National Research Council.
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Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
TL;DR: It is shown that ribosome reconstructions with unprecedented resolutions may be calculated from almost two orders of magnitude fewer particles than used previously, which may expand the scope of high-resolution cryo-EM to a broad range of biological specimens.
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Structure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution
TL;DR: Comparison of the maps from idle and translating complexes suggests how conformational changes to the Sec61 channel could facilitate translocation of a secreted polypeptide and provides a valuable reference for future functional and structural studies.
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Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine
Wilson Wong,Xiao Chen Bai,Alan Brown,Israel S. Fernández,Eric Hanssen,Melanie Condron,Melanie Condron,Yan Hong Tan,Yan Hong Tan,Jake Baum,Jake Baum,Sjors H.W. Scheres +11 more
TL;DR: The cryo-EM structure of the cytoplasmic ribosome from the human malaria parasite, Plasmodium falciparum, in complex with emetine at 3.2 Å resolution is solved, establishing cryo -EM as a powerful tool for screening and guiding the design of drugs that target parasite translation machinery.
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Initiation of Translation by Cricket Paralysis Virus IRES Requires Its Translocation in the Ribosome
TL;DR: The structure and accompanying factor-binding data show that CrPV-IRES binding mimics a pretranslocation rather than initiation state of the ribosome, which allows initiation of translation in the absence of any host initiation factors.
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Elongation factor G bound to the ribosome in an intermediate state of translocation.
TL;DR: Comparison with the posttranslocational state suggests that interactions between the tRNA and L1 stalk are preserved throughout translocation and that these are probably an essential feature of translocation required for stabilization of the hybrid P/E state.