The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

[1]  F. Hartl,et al.  Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES , 1993, Nature.

[2]  G. Lorimer,et al.  Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. , 1993, Biochemistry.

[3]  Lila M. Gierasch,et al.  Characterization of a functionally important mobile domain of GroES , 1993, Nature.

[4]  S. Chen,et al.  ATP induces large quaternary rearrangements in a cage-like chaperonin structure , 1993, Current Biology.

[5]  K. Braig,et al.  A polypeptide bound by the chaperonin groEL is localized within a central cavity. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[6]  T. Atkinson,et al.  Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. , 1993, Biochemistry.

[7]  N. Lissin,et al.  The strongly conserved carboxyl‐terminus glycine‐methionine motif of the Escherichia coli GroEL chaperonin is dispensable , 1993, Molecular microbiology.

[8]  F. Hartl,et al.  Molecular chaperone functions of heat-shock proteins. , 1993, Annual review of biochemistry.

[9]  E. Bochkareva,et al.  A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL. , 1992, The Journal of biological chemistry.

[10]  W. Baumeister,et al.  Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. , 1992, The EMBO journal.

[11]  R. Jaenicke,et al.  Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60. , 1992, Biochemistry.

[12]  J. Rothman,et al.  Positive cooperativity in the functioning of molecular chaperone GroEL. , 1992, The Journal of biological chemistry.

[13]  L. Gierasch,et al.  Renaturation of citrate synthase: Influence of denaturant and folding assistants , 1992, Protein science : a publication of the Protein Society.

[14]  G. Lorimer,et al.  Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring. , 1992, The Journal of biological chemistry.

[15]  J. Sambrook,et al.  Protein folding in the cell , 1992, Nature.

[16]  A. Fersht,et al.  Cooperativity in ATP hydrolysis by GroEL is increased by GroES , 1991, FEBS letters.

[17]  G. Lorimer,et al.  Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. , 1991, Biochemistry.

[18]  H. Saibil,et al.  Binding of chaperonins , 1991, Nature.

[19]  G. Lorimer,et al.  Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. , 1991, The Journal of biological chemistry.

[20]  T. Creighton.  Unfolding protein folding , 1991, Nature.

[21]  F. Hartl,et al.  Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate , 1991, Nature.

[22]  R. Jaenicke,et al.  GroE facilitates refolding of citrate synthase by suppressing aggregation. , 1991, Biochemistry.

[23]  G. Lorimer,et al.  Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. , 1990, Biochemistry.

[24]  G. Lorimer,et al.  Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP , 1989, Nature.

[25]  Roger W. Hendrix,et al.  Homologous plant and bacterial proteins chaperone oligomeric protein assembly , 1988, Nature.

[26]  C. Georgopoulos,et al.  Purification and properties of the groES morphogenetic protein of Escherichia coli. , 1986, The Journal of biological chemistry.

[27]  R. Hendrix.  Purification and properties of groE, a host protein involved in bacteriophage assembly. , 1979, Journal of molecular biology.

[28]  A. Engel,et al.  Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. , 1979, Journal of molecular biology.