PubRank

G H Lorimer

Author PubWeight™ 120.38‹?›

Top papers

Rank Title Journal Year PubWeight™‹?›
1 The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications. Biochemistry 1976 9.91
2 Ribulose-1,5-bisphosphate carboxylase-oxygenase. Annu Rev Biochem 1983 8.54
3 D-Ribulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities. Anal Biochem 1977 7.51
4 Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction-1 protein of leaves. Biochemistry 1973 5.19
5 GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 1989 5.15
6 Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 1999 4.57
7 Ribulose diphosphate oxygenase. II. Further proof of reaction products and mechanism of action. Biochemistry 1973 4.19
8 Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase. Biochemistry 1981 3.99
9 Chaperonin-mediated protein folding. Annu Rev Biophys Biomol Struct 2001 3.24
10 Fixation of O(2) during Photorespiration: Kinetic and Steady-State Studies of the Photorespiratory Carbon Oxidation Cycle with Intact Leaves and Isolated Chloroplasts of C(3) Plants. Plant Physiol 1978 3.20
11 Carbamate formation on the epsilon-amino group of a lysyl residue as the basis for the activation of ribulosebisphosphate carboxylase by CO2 and Mg2+. Biochemistry 1980 3.00
12 Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 1994 2.88
13 Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. Biochemistry 1990 2.62
14 Isolation, identification, and synthesis of 2-carboxyarabinitol 1-phosphate, a diurnal regulator of ribulose-bisphosphate carboxylase activity. Proc Natl Acad Sci U S A 1987 2.49
15 Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris. Purification, prosthetic groups, and molecular properties. J Biol Chem 1975 2.12
16 Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J Biol Chem 1991 1.92
17 Chaperonin function: folding by forced unfolding. Science 1999 1.83
18 Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci U S A 1996 1.79
19 Ribulosebisphosphate carboxylase: amino acid sequence of a peptide bearing the activator carbon dioxide. Biochemistry 1981 1.78
20 Incorporation of molecular oxygen into glycine and serine during photorespiration in spinach leaves. Biochemistry 1971 1.76
21 Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry 1991 1.71
22 Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Sci 1992 1.64
23 Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring. J Biol Chem 1992 1.59
24 The activation of ribulose 1,5-bisphosphate carboxylase/oxygenase. Basic Life Sci 1978 1.52
25 Glycolate synthesis by intact chloroplasts. Studies with inhibitors of photophosphorylation. Arch Biochem Biophys 1977 1.51
26 The presence of bound cyanide in the naturally inactivated form of nitrate reductase of Chlorella vulgaris. J Biol Chem 1974 1.48
27 Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry 1993 1.47
28 On the role of groES in the chaperonin-assisted folding reaction. Three case studies. J Biol Chem 1994 1.43
29 Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60. Biochemistry 1992 1.38
30 Catalytic properties of a hybrid between cyanobacterial large subunits and higher plant small subunits of ribulose bisphosphate carboxylase-oxygenase. J Biol Chem 1985 1.32
31 Factors affecting interconversion between kinetic forms of ribulose diphosphate carboxylase-oxygenase from spinach. Arch Biochem Biophys 1975 1.32
32 The stereochemical course of ribulosebisphosphate carboxylase. Reductive trapping of the 6-carbon reaction-intermediate. J Biol Chem 1982 1.31
33 A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc Natl Acad Sci U S A 1996 1.31
34 Diffusion and osmotic transfer in corn mitochondria. Plant Physiol 1970 1.27
35 On the mechanism of glycolate synthesis by Chromatium and Chlorella. Arch Biochem Biophys 1978 1.24
36 Reaction intermediate partitioning by ribulose-bisphosphate carboxylases with differing substrate specificities. J Biol Chem 1986 1.22
37 Evidence for the existence of discrete activator and substrate sites for CO2 on ribulose-1,5-bisphosphate carboxylase. J Biol Chem 1979 1.21
38 Activation of ribulose-1, 5-bisphosphate oxygenase, The role of Mg2+, CO2, and pH. Arch Biochem Biophys 1976 1.21
39 Identification of a groES-like chaperonin in mitochondria that facilitates protein folding. Proc Natl Acad Sci U S A 1990 1.18
40 Interactions of hydrogen peroxide with ribulose bisphosphate carboxylase oxygenase. J Biol Chem 1980 1.11
41 The incorporation of (18O)oxygen into glycolate by intact isolated chloroplasts. FEBS Lett 1977 1.10
42 Functional characterization of the higher plant chloroplast chaperonins. J Biol Chem 1995 1.01
43 Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Proc Natl Acad Sci U S A 1993 0.99
44 Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures. J Biol Chem 1992 0.98
45 Dethiobiotin synthetase: the carbonylation of 7,8-diaminonanoic acid proceeds regiospecifically via the N7-carbamate. Biochemistry 1995 0.94
46 Presence of HCN in chlorella vulgaris and its possible role in controlling the reduction of nitrate. Nature 1974 0.93
47 Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry. J Biol Chem 1991 0.92
48 Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation. J Biol Chem 1995 0.91
49 Unassisted refolding of urea unfolded rhodanese. J Biol Chem 1991 0.90
50 Three partial reactions of ribulose-bisphosphate carboxylase require both large and small subunits. J Biol Chem 1986 0.88
51 Determination of glycolic acid by the Eegriwe (Calkins) methods. Anal Biochem 1977 0.88
52 Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase. Biochemistry 1993 0.87
53 Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria. Trends Biotechnol 1990 0.81
54 Criteria for assessing the purity and quality of GroEL. Methods Enzymol 1998 0.81
55 GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides. FEBS Lett 1995 0.81
56 GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism. Proc Natl Acad Sci U S A 1999 0.79
57 Structural biology. Unraveling a membrane protein. Science 2000 0.79
58 GroE structures galore. Nat Struct Biol 1996 0.79
59 Retention of the oxygen atoms at carbon-2 and carbon-3 during the carboxylation of ribulose 1,5-bisphosphate. Eur J Biochem 1978 0.75
60 Plurality of protein conformations of ribulose-1,5-bisphosphate carboxylase/oxygenase monomers probed by high pressure electrophoresis. J Biol Chem 1993 0.75
61 On the distribution of ligands within the asymmetric chaperonin complex, GroEL14.ADP7.GroES7. FEBS Lett 1995 0.75