Published in Biochemistry on April 25, 1995
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Measuring how much work the chaperone GroEL can do. Proc Natl Acad Sci U S A (2013) 0.96
Biomolecular robotics for chemomechanically driven guest delivery fuelled by intracellular ATP. Nat Chem (2013) 0.94
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Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state. Proc Natl Acad Sci U S A (2008) 0.88
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Design of an optical switch for studying conformational dynamics in individual molecules of GroEL. Bioconjug Chem (2008) 0.82
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A mobile loop order-disorder transition modulates the speed of chaperonin cycling. Protein Sci (2004) 0.82
Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding. J Biol Chem (2013) 0.81
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Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis. Biophys J (2012) 0.77
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Putting handcuffs on the chaperonin GroEL. Proc Natl Acad Sci U S A (2013) 0.76
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GroEL2 of Mycobacterium tuberculosis Reveals the Importance of Structural Pliability in Chaperonin Function. J Bacteriol (2015) 0.75
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