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Bioinformatics (Oxford, England)|November 17, 2007
Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteinsOrly Noivirt-Brik, Ron Unger, Amnon Horovitz
Current Opinion in Structural Biology|April 29, 2019
Double-mutant cycles: new directions and applicationsAmnon Horovitz, Rachel C Fleisher, Tridib Mondal
Current Microbiology|December 1, 2016
The Archaeal Signal Recognition Particle: Present Understanding and Future PerspectiveSayandeep Gupta, Mousam Roy, Abhrajyoti Ghosh
Frontiers in Molecular Biosciences|June 1, 2022
Minimal Yet Powerful: The Role of Archaeal Small Heat Shock Proteins in Maintaining Protein HomeostasisMousam Roy, Koustav Bhakta, Abhrajyoti Ghosh
Journal of Molecular Biology|June 17, 2008
Concerted release of substrate domains from GroEL by ATP is demonstrated with FRETNiv Papo, Yakov Kipnis, Gilad Haran, et al.
Elife|July 28, 2020
Measuring protein stability in the GroEL chaperonin cage reveals massive destabilizationIlia Korobko, Hisham Mazal, Gilad Haran, et al.
Biophysical Journal|December 23, 2018
Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroELBoudhayan Bandyopadhyay, Tridib Mondal, Ron Unger, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 16, 2007
Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none mannerYakov Kipnis, Niv Papo, Gilad Haran, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 22, 2002
Phi value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ringAmnon Horovitz, Amnon Amir, Oded Danziger, et al.
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