Two conformational states of β-lactamase bound to GroEL: a biophysical characterization 1 1Edited by A. R. Fersht

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

K. Braig, Zbyszek Otwinowski, Rashmi S. Hegde et al. · Nature · 1994 · 1.3K citations

Life Sciences, Biochemistry, Molecular Biology +14

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

Zhaohui Xu, Arthur L. Horwich, Paul B. Sigler · Nature · 1997 · 1.3K citations

Life Sciences, Biochemistry, Molecular Biology +16

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

Jörg Martin, Thomas Langer, Raina Boteva et al. · Nature · 1991 · 860 citations

Life Sciences, Biochemistry, Molecular Biology +14

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

Olivier Fayet, Thomas Ziegelhoffer, Costa Georgopoulos · Journal of Bacteriology · 1989 · 700 citations · Full text

Life Sciences, Genetics, Microbiology +14

Evidence for a molten globule state as a general intermediate in protein folding

Oleg B. Ptitsyn, Roger H. Pain, Gennady V. Semisotnov et al. · FEBS Letters · 1990 · 678 citations

Life Sciences, Biochemistry, Biophysics +15