The Hsp70 and Hsp60 chaperone machines

[1] TO FOLD OR NOT TO FOLD [J]. SCIENCE, 1993, 260 (5116) : 1903 - 1904

[2] [Anonymous], CHAPERONINS

[3] BOCHKAREVA ES, 1994, J BIOL CHEM, V269, P23869

[4] BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P6796

[5] HOLDEM AND FOLDEM - CHAPERONES AND SIGNAL-TRANSDUCTION [J]. SCIENCE, 1995, 268 (5215) : 1303 - 1304

[6] The 2.4 angstrom crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S [J]. NATURE STRUCTURAL BIOLOGY, 1996, 3 (02): : 170 - 177

[7] THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J]. NATURE, 1994, 371 (6498) : 578 - 586

[8] A POLYPEPTIDE BOUND BY THE CHAPERONIN GROEL IS LOCALIZED WITHIN A CENTRAL CAVITY [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (09) : 3978 - 3982

[9] NUCLEOTIDE-INDUCED CONFORMATIONAL-CHANGES IN THE ATPASE AND SUBSTRATE-BINDING DOMAINS OF THE DNAK CHAPERONE PROVIDE EVIDENCE FOR INTERDOMAIN COMMUNICATION [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (28) : 16903 - 16910

[10] Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding [J]. JOURNAL OF MOLECULAR BIOLOGY, 1996, 261 (03) : 328 - 333

[1] TO FOLD OR NOT TO FOLD [J]. SCIENCE, 1993, 260 (5116) : 1903 - 1904

[2] [Anonymous], CHAPERONINS

[3] BOCHKAREVA ES, 1994, J BIOL CHEM, V269, P23869

[4] BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P6796

[5] HOLDEM AND FOLDEM - CHAPERONES AND SIGNAL-TRANSDUCTION [J]. SCIENCE, 1995, 268 (5215) : 1303 - 1304

[6] The 2.4 angstrom crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S [J]. NATURE STRUCTURAL BIOLOGY, 1996, 3 (02): : 170 - 177

[7] THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J]. NATURE, 1994, 371 (6498) : 578 - 586

[8] A POLYPEPTIDE BOUND BY THE CHAPERONIN GROEL IS LOCALIZED WITHIN A CENTRAL CAVITY [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (09) : 3978 - 3982

[9] NUCLEOTIDE-INDUCED CONFORMATIONAL-CHANGES IN THE ATPASE AND SUBSTRATE-BINDING DOMAINS OF THE DNAK CHAPERONE PROVIDE EVIDENCE FOR INTERDOMAIN COMMUNICATION [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (28) : 16903 - 16910

[10] Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding [J]. JOURNAL OF MOLECULAR BIOLOGY, 1996, 261 (03) : 328 - 333