The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

How to measure and predict the molar absorption coefficient of a protein

C. Nick Pace, F.F. Vajdos, Lanette Fee et al. · Protein Science · 1995 · 3.9K citations · Full text

Analysis of gene control signals by DNA fusion and cloning in Escherichia coli

M J Casadaban, Stanley N. Cohen · Journal of Molecular Biology · 1980 · 2.5K citations

Dna Fusion, Molecular Biotechnology, Molecular Biological Method +12

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

Crystal Structure, Biochemistry, Natural Sciences +7

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

Crystal Structure, Molecular Biology, Molecular Complex +2

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 · 858 citations

Protein Chemistry, Chaperonin-mediated Protein Folding, Protein Assembly +9