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Alexis Rohou
Researcher at Genentech
Publications - 36
Citations - 6074
Alexis Rohou is an academic researcher from Genentech. The author has contributed to research in topics: Biology & Image processing. The author has an hindex of 18, co-authored 32 publications receiving 4081 citations. Previous affiliations of Alexis Rohou include Howard Hughes Medical Institute & Brandeis University.
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Journal ArticleDOI
CTFFIND4: Fast and accurate defocus estimation from electron micrographs.
Alexis Rohou,Nikolaus Grigorieff +1 more
TL;DR: Modifications to the CTFFIND algorithm are described which make it significantly faster and more suitable for use with images collected using modern technologies such as dose fractionation and phase plates.
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cisTEM, user-friendly software for single-particle image processing
TL;DR: New open-source software called cisTEM (computational imaging system for transmission electron microscopy) for the processing of data for high-resolution electron cryo-microscopy and single-particle averaging is developed, optimized to enable processing of typical datasets on a high-end, CPU-based workstation in half a day or less, comparable to GPU-accelerated processing.
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Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
Anna Zhou,Alexis Rohou,Daniel G Schep,John V. Bason,Martin G. Montgomery,John E. Walker,Nikolaus Grigorieff,John L. Rubinstein +7 more
TL;DR: Cryo-EM analysis of the bovine mitochondrial ATP synthase revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthases, suggesting a proton translocation path through the FO region that involves both the a and b subunits.
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Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM
Matthias Schmidt,Alexis Rohou,Keren Lasker,Jay Kant Yadav,Cordelia Schiene-Fischer,Marcus Fändrich,Nikolaus Grigorieff,Nikolaus Grigorieff +7 more
TL;DR: The model reveals that the individual layers of the Aβ fibril are formed by peptide dimers with face-to-face packing, explaining why aggregation inhibitors are most potent when targeting the C terminus, and explains how addition of C-terminal amino acids may stabilize peptide interaction.
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Molecular Architecture of the "Stressosome," a Signal Integration and Transduction Hub
Jon Marles-Wright,Tim Grant,Olivier Delumeau,Gijs van Duinen,Susan J. Firbank,Peter J. Lewis,James W. Murray,J.A. Newman,Maureen B. Quin,Paul R. Race,Alexis Rohou,Willem Tichelaar,Marin van Heel,Richard J. Lewis +13 more
TL;DR: It is suggested that the different sensory extensions respond to different signals, whereas the conserved domains in the core integrate the varied signals, and the architecture of the stressosome provides the potential for cooperativity.