J
Jean Paul Armache
Researcher at University of California, San Francisco
Publications - 46
Citations - 9434
Jean Paul Armache is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Eukaryotic Ribosome & Ribosomal protein. The author has an hindex of 24, co-authored 38 publications receiving 6835 citations. Previous affiliations of Jean Paul Armache include Ludwig Maximilian University of Munich & Pennsylvania State University.
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Journal ArticleDOI
MotionCor2: Anisotropic Correction of Beam-Induced Motion for Improved Cryo-Electron Microscopy
Shawn Q. Zheng,Eugene Palovcak,Jean Paul Armache,Kliment A. Verba,Yifan Cheng,David A. Agard +5 more
TL;DR: MotionCor2 software corrects for beam-induced sample motion, improving the resolution of cryo-EM reconstructions.
Journal ArticleDOI
Structure of the TRPA1 ion channel suggests regulatory mechanisms
TL;DR: Single-particle electron cryo- microscopy is used to determine the structure of full-length human TRPA1 to ∼4 Å resolution and establish a blueprint for structure-based design of analgesic and anti-inflammatory agents.
Journal ArticleDOI
Structures of the human and Drosophila 80S ribosome
Andreas M. Anger,Jean Paul Armache,Otto Berninghausen,Michael Habeck,Marion Subklewe,Daniel N. Wilson,Roland Beckmann +6 more
TL;DR: In this paper, the structure of metazoan 80S ribosomes with the translation factor eEF2, E-site transfer RNA and Stm1-like proteins has been determined.
Journal ArticleDOI
Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome
Thomas Becker,Shashi Bhushan,Alexander Jarasch,Jean Paul Armache,Soledad Funes,Soledad Funes,Fabrice Jossinet,James C. Gumbart,Thorsten Mielke,Thorsten Mielke,Otto Berninghausen,Klaus Schulten,Eric Westhof,Reid Gilmore,Elisabet C. Mandon,Roland Beckmann +15 more
TL;DR: Subnanometer-resolution cryo–electron microscopy structures of eukaryotic ribosome-Sec61 complexes are determined and it is found that in both idle and active states, the Sec complex is not oligomeric and interacts mainly via two cytoplasmic loops with the universal ribosomal adaptor site.
Journal ArticleDOI
Structural insight into nascent polypeptide chain-mediated translational stalling.
Birgit Seidelt,C. Axel Innis,Daniel N. Wilson,Marco Gartmann,Jean Paul Armache,Elizabeth Villa,Leonardo G. Trabuco,Thomas Becker,Thorsten Mielke,Thorsten Mielke,Klaus Schulten,Thomas A. Steitz,Thomas A. Steitz,Roland Beckmann +13 more
TL;DR: A model whereby interactions within the tunnel are relayed to the peptidyltransferase center to inhibit translation is proposed, and it is shown that nascent chains adopt distinct conformations within the ribosomal exit tunnel.