E
Erik Lindahl
Researcher at Science for Life Laboratory
Publications - 192
Citations - 69645
Erik Lindahl is an academic researcher from Science for Life Laboratory. The author has contributed to research in topics: Ligand-gated ion channel & Ion channel. The author has an hindex of 55, co-authored 174 publications receiving 54950 citations. Previous affiliations of Erik Lindahl include Stanford University & Swiss Institute of Bioinformatics.
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Journal ArticleDOI
Using Scipion for stream image processing at Cryo-EM facilities.
Josué Gómez-Blanco,J.M. de la Rosa-Trevín,Roberto Marabini,L. del Cano,A. Jimenez,María Jesús Martínez,Remedios Melero,Tomáš Majtner,David Maluenda,Jordi Mota,Y. Rancel,Erney Ramírez-Aportela,José Luis Vilas,Marta Carroni,Stefan Fleischmann,Erik Lindahl,Erik Lindahl,Alun W. Ashton,Mark Basham,Daniel K. Clare,K. Savage,C. A. Siebert,Grigory Sharov,Carlos Oscar S. Sorzano,Pablo Conesa,José María Carazo +25 more
TL;DR: A major extension of Scipion is presented that allows processing of EM images while the data is being acquired, which helps to detect problems at early stages, saves computing time and provides users with a detailed evaluation of the data quality before the acquisition is finished.
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Modeling anesthetic binding sites within the glycine alpha one receptor based on prokaryotic ion channel templates: the problem with TM4.
TL;DR: This model of the glycine alpha one receptor (GlyRa1) is built based on the open-state structures of two new high-resolution ion channel templates from the prokaryote, Gloebacter violaceus (GLIC).
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Human skin barrier formation takes place via a cubic to lamellar lipid phase transition as analyzed by cryo-electron microscopy and EM-simulation
Ali Narangifard,Ali Narangifard,L. den Hollander,Christian L. Wennberg,Christian L. Wennberg,Magnus Lundborg,Erik Lindahl,Erik Lindahl,Ichiro Iwai,H. Han,Sergej Masich,Bertil Daneholt,Lars Norlén,Lars Norlén +13 more
TL;DR: The data support that human skin barrier formation takes place via a cubic to lamellar lipid phase transition and that the barrier formation process was analysed in situ in its near‐native state using cryo‐EM combined with molecular dynamics modeling and EM simulation.
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Inhibition versus potentiation of ligand-gated ion channels can be altered by a single mutation that moves ligands between intra- and intersubunit sites.
Torben Brömstrup,Rebecca J. Howard,James R. Trudell,R. Adron Harris,Erik Lindahl,Erik Lindahl +5 more
TL;DR: It is shown that a single-site mutation at the F14' site in the GLIC transmembrane domain turns desflurane and chloroform from inhibitors to potentiators, and that this is explained by competing allosteric sites.
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Internal duplications in α-helical membrane protein topologies are common but the nonduplicated forms are rare.
TL;DR: It is found that the majority of large transmembrane (TM) proteins contain an internal duplication, and homologs to all human membrane proteins were used to detect the presence of duplicated and nonduplicated proteins, confirming that only in rare cases can homologicals with different duplication status be found.