Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES

[1]  T. Langer,et al.  The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding , 1993, Nature.

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

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

[4]  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.

[5]  C Sander,et al.  Progress in protein structure prediction? , 1993, Trends in biochemical sciences.

[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]  B. Haley,et al.  Identification of a guanine binding domain peptide of the GTP binding site of glutamate dehydrogenase: isolation with metal-chelate affinity chromatography. , 1993, Biochemistry.

[8]  J. Crabb.  Techniques in Protein Chemistry IV , 1993 .

[9]  H. Erdjument-Bromage,et al.  Successful Peptide Sequencing With Femtomole Level PTH-Analysis: A Commentary , 1993 .

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

[11]  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.

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

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

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

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

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

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

[18]  S. Hemmingsen,et al.  Unique composition of plastid chaperonin-60: α and β polypeptide-encoding genes are highly divergent , 1990 .

[19]  P. Tempst,et al.  Internal sequence analysis of proteins separated on polyacrylamide gels at the submicrogram level: Improved methods, applications and gene cloning strategies , 1990, Electrophoresis.

[20]  P. Tempst,et al.  Examination of automated polypeptide sequencing using standard phenyl isothiocyanate reagent and subpicomole high-performance liquid chromatographic analysis. , 1989, Analytical biochemistry.

[21]  B. Chait,et al.  Factors affecting the ultraviolet laser desorption of proteins. , 1989, Rapid communications in mass spectrometry : RCM.

[22]  H. Schägger,et al.  Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. , 1987, Analytical biochemistry.

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

[24]  A. Mildvan,et al.  ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[25]  K. McEntee,et al.  Tyrosine 264 in the recA protein from Escherichia coli is the site of modification by the photoaffinity label 8-azidoadenosine 5'-triphosphate. , 1985, The Journal of biological chemistry.

[26]  J. Walker,et al.  The sites of labeling of the beta-subunit of bovine mitochondrial F1-ATPase with 8-azido-ATP. , 1983, The Journal of biological chemistry.