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Nature Structural & Molecular Biology|July 10, 2024
Resolving chaperone-assisted protein folding on the ribosome at the peptide levelThomas E Wales, Aleksandra Pajak, Alžběta Roeselová, et al.Cell|April 9, 2008
Monitoring protein conformation along the pathway of chaperonin-assisted foldingShruti Sharma, Kausik Chakraborty, Barbara K Müller, et al.Molecular Microbiology|October 22, 2009
Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazeiAngela M Hirtreiter, Giulia Calloni, Francesca Forner, et al.Proceedings of the National Academy of Sciences of the United States of America|January 11, 2003
Chaperones increase association of tau protein with microtubulesFei Dou, William J Netzer, Kentaro Tanemura, et al.Molecular Cell|July 1, 2004
Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivationGregor Schaffar, Peter Breuer, Raina Boteva, et al.The Journal of Biological Chemistry|December 16, 2006
Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish modelNiclas W Schiffer, Sarah A Broadley, Thomas Hirschberger, et al.The EMBO Journal|December 17, 2017
High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteinsLisa Vincenz-Donnelly, Hauke Holthusen, Roman Körner, et al.The Journal of Biological Chemistry|September 14, 2006
Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial importAnna C Y Fan, Melanie K Bhangoo, Jason C YoungNature|August 21, 2024
Visualizing chaperonin function in situ by cryo-electron tomographyJonathan Wagner, Alonso I Carvajal, Andreas Bracher, et al.Journal of Virology|May 28, 2005
Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targetsUwe Bertsch, Konstanze F Winklhofer, Thomas Hirschberger, et al.Pageof 21