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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 HorovitzCurrent Opinion in Structural Biology|April 29, 2019
Double-mutant cycles: new directions and applicationsAmnon Horovitz, Rachel C Fleisher, Tridib MondalCurrent Microbiology|December 1, 2016
The Archaeal Signal Recognition Particle: Present Understanding and Future PerspectiveSayandeep Gupta, Mousam Roy, Abhrajyoti GhoshFrontiers 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 GhoshJournal 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.Biochemistry|May 1, 2002
Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GroEL ring distal to GroESYael Fridmann, Galit Kafri, Oded Danziger, 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.Pageof 8