GroEL-substrate interactions: Molding the fold, or folding the mold?

[1] Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60) [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (08) : 5105 - 5111

[2] A structural model for GroEL-polypeptide recognition [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (08) : 3571 - 3575

[3] Kinetic studies of β-sheet protein folding [J]. CURRENT OPINION IN STRUCTURAL BIOLOGY, 1998, 8 (01) : 86 - 92

[4] The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity [J]. CELL, 1999, 99 (07) : 757 - 768

[5] LOCATION OF A FOLDING PROTEIN AND SHAPE CHANGES IN GROEL-GROES COMPLEXES IMAGED BY CRYOELECTRON MICROSCOPY [J]. NATURE, 1994, 371 (6494) : 261 - 264

[6] Coyle JE, 1999, NAT STRUCT BIOL, V6, P683

[7] In vivo observation of polypeptide flux through the bacterial chaperonin system [J]. CELL, 1997, 90 (03) : 491 - 500

[8] RESIDUES IN CHAPERONIN GROEL REQUIRED FOR POLYPEPTIDE BINDING AND RELEASE [J]. NATURE, 1994, 371 (6498) : 614 - 619

[9] Identification of in vivo substrates of the chaperonin GroEL [J]. NATURE, 1999, 402 (6758) : 147 - 154

[10] NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution [J]. JOURNAL OF MOLECULAR BIOLOGY, 1999, 292 (01) : 181 - 190

[1] Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60) [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (08) : 5105 - 5111

[2] A structural model for GroEL-polypeptide recognition [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (08) : 3571 - 3575

[3] Kinetic studies of β-sheet protein folding [J]. CURRENT OPINION IN STRUCTURAL BIOLOGY, 1998, 8 (01) : 86 - 92

[4] The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity [J]. CELL, 1999, 99 (07) : 757 - 768

[5] LOCATION OF A FOLDING PROTEIN AND SHAPE CHANGES IN GROEL-GROES COMPLEXES IMAGED BY CRYOELECTRON MICROSCOPY [J]. NATURE, 1994, 371 (6494) : 261 - 264

[6] Coyle JE, 1999, NAT STRUCT BIOL, V6, P683

[7] In vivo observation of polypeptide flux through the bacterial chaperonin system [J]. CELL, 1997, 90 (03) : 491 - 500

[8] RESIDUES IN CHAPERONIN GROEL REQUIRED FOR POLYPEPTIDE BINDING AND RELEASE [J]. NATURE, 1994, 371 (6498) : 614 - 619

[9] Identification of in vivo substrates of the chaperonin GroEL [J]. NATURE, 1999, 402 (6758) : 147 - 154

[10] NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution [J]. JOURNAL OF MOLECULAR BIOLOGY, 1999, 292 (01) : 181 - 190