Published in Proc Natl Acad Sci U S A on September 03, 1996
GroEL-mediated protein folding. Protein Sci (1997) 1.99
Chaperonin function: folding by forced unfolding. Science (1999) 1.83
Diffusion control in an elementary protein folding reaction. Proc Natl Acad Sci U S A (1997) 1.69
Chaperone rings in protein folding and degradation. Proc Natl Acad Sci U S A (1999) 1.66
Topologies of a substrate protein bound to the chaperonin GroEL. Mol Cell (2007) 1.52
GroEL-mediated protein folding: making the impossible, possible. Crit Rev Biochem Mol Biol (2006) 1.51
Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proc Natl Acad Sci U S A (2005) 1.47
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc Natl Acad Sci U S A (2008) 1.37
Expansion and compression of a protein folding intermediate by GroEL. Mol Cell (2004) 1.36
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL. Proc Natl Acad Sci U S A (2004) 1.30
Chaperonins. Biochem J (1998) 1.22
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc Natl Acad Sci U S A (1997) 1.10
The unfolding action of GroEL on a protein substrate. Biophys J (2004) 1.04
Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein. Proc Natl Acad Sci U S A (2007) 0.96
Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented. FEBS Lett (2011) 0.95
Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104. Proc Natl Acad Sci U S A (2003) 0.92
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR. Proc Natl Acad Sci U S A (2013) 0.91
Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones. Proc Natl Acad Sci U S A (2007) 0.90
Protein folding: how the mechanism of GroEL action is defined by kinetics. Proc Natl Acad Sci U S A (1997) 0.90
Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL. Protein Sci (2011) 0.80
Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates. J Biol Chem (2013) 0.79
Strategies for folding of affinity tagged proteins using GroEL and osmolytes. J Struct Funct Genomics (2008) 0.78
Identifying protein stabilizing ligands using GroEL. Biopolymers (2010) 0.77
Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle. Front Mol Biosci (2016) 0.76
Role of nonspecific interactions in molecular chaperones through model-based bioinformatics. Biophys J (2012) 0.75
Probing the kinetic stabilities of Friedreich's ataxia clinical variants using a solid phase GroEL chaperonin capture platform. Biomolecules (2014) 0.75
Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem (1989) 29.15
Protein denaturation. Adv Protein Chem (1968) 11.58
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry (1988) 9.18
Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem (1993) 7.53
The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature (1994) 6.72
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins (1989) 5.72
Labeling of proteins by reductive methylation using sodium cyanoborohydride. J Biol Chem (1979) 5.42
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature (1989) 5.19
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature (1999) 4.57
Residues in chaperonin GroEL required for polypeptide binding and release. Nature (1994) 4.30
Reexamination of the folding of BPTI: predominance of native intermediates. Science (1991) 3.63
Folding and association of proteins. Prog Biophys Mol Biol (1987) 3.53
The bonds that tie: catalyzed disulfide bond formation. Cell (1993) 3.20
Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci (1994) 3.03
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science (1994) 2.88
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell (1994) 2.84
Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell (1995) 2.67
Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature (1996) 2.46
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J Biol Chem (1988) 2.42
The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase. FEBS Lett (1993) 2.17
Three-state analysis of sperm whale apomyoglobin folding. Biochemistry (1993) 1.96
Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu Rev Biophys Biomol Struct (1993) 1.94
Specific protein-nucleic acid recognition in ribonuclease T1-2'-guanylic acid complex: an X-ray study. Nature (1982) 1.60
Folding of dihydrofolate reductase from Escherichia coli. Biochemistry (1986) 1.51
Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry (1979) 1.49
Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry (1993) 1.47
Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science (1996) 1.42
Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J Mol Biol (1995) 1.36
Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast. Biochemistry (1991) 1.34
Refolding of barnase in the presence of GroE. J Mol Biol (1993) 1.24
Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry (1990) 1.23
Kinetics of unfolding and refolding of proteins. I. Mathematical analysis. J Mol Biol (1973) 1.19
Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1. J Mol Biol (1992) 1.12
Ribonuclease T1, Structure and function. Adv Biophys (1970) 1.09
Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry (1989) 1.06
Quaternary structure, subunit activity, and in vitro association of porcine mitochondrial malic dehydrogenase. Biochemistry (1979) 1.05
Nature and consequences of GroEL-protein interactions. Biochemistry (1995) 1.02
Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry (1994) 1.02
Preferential binding of an unfolded protein to DsbA. EMBO J (1996) 0.99
Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate. Proteins (1992) 0.99
Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites. Proc Natl Acad Sci U S A (1990) 0.95
Intact disulfide bonds decelerate the folding of ribonuclease T1. J Mol Biol (1994) 0.93
Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation. J Biol Chem (1995) 0.91
Conformational stability of ribonuclease T1. I. Thermal denaturation and effects of salts. J Biochem (1979) 0.87
Reassociation of dimeric cytoplasmic malate dehydrogenase is determined by slow and very slow folding reactions. Biochemistry (1986) 0.86
Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1. J Mol Biol (1995) 0.83
A purification method for labile variants of ribonuclease T1. Protein Expr Purif (1993) 0.83
Role of the Cys 2-Cys 10 disulfide bond for the structure, stability, and folding kinetics of ribonuclease T1. Protein Sci (1994) 0.81
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
Ribulose-1,5-bisphosphate carboxylase-oxygenase. Annu Rev Biochem (1983) 8.54
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature (1989) 8.48
D-Ribulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities. Anal Biochem (1977) 7.51
Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction-1 protein of leaves. Biochemistry (1973) 5.19
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature (1989) 5.15
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature (1999) 4.57
Ribulose diphosphate oxygenase. II. Further proof of reaction products and mechanism of action. Biochemistry (1973) 4.19
Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase. Biochemistry (1981) 3.99
Two exposed amino acid residues confer thermostability on a cold shock protein. Nat Struct Biol (2000) 3.27
Chaperonin-mediated protein folding. Annu Rev Biophys Biomol Struct (2001) 3.24
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
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
GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry (1991) 2.92
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science (1994) 2.88
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. Biochemistry (1990) 2.68
Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. Biochemistry (1990) 2.62
The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J (1997) 2.50
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
Extremely rapid protein folding in the absence of intermediates. Nat Struct Biol (1995) 2.43
Catalysis of protein folding by prolyl isomerase. Nature (1987) 2.21
The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J (2001) 2.12
Reduced nicotinamide adenine dinucleotide-nitrate reductase of Chlorella vulgaris. Purification, prosthetic groups, and molecular properties. J Biol Chem (1975) 2.12
Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J Biol Chem (1991) 1.92
Surgical treatment of pulmonary artery sarcoma. J Thorac Cardiovasc Surg (2001) 1.91
Chaperonin function: folding by forced unfolding. Science (1999) 1.83
Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci U S A (1996) 1.79
A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J (1995) 1.79
Ribulosebisphosphate carboxylase: amino acid sequence of a peptide bearing the activator carbon dioxide. Biochemistry (1981) 1.78
Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proc Natl Acad Sci U S A (1978) 1.78
Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol (1998) 1.78
Incorporation of molecular oxygen into glycine and serine during photorespiration in spinach leaves. Biochemistry (1971) 1.76
Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding. Nature (1990) 1.74
Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry (1991) 1.71
Diffusion control in an elementary protein folding reaction. Proc Natl Acad Sci U S A (1997) 1.69
Role of proline isomerization in folding of ribonuclease A at low temperatures. Proc Natl Acad Sci U S A (1979) 1.65
Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Sci (1992) 1.64
Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring. J Biol Chem (1992) 1.59
Catalysis of protein folding by cyclophilins from different species. J Biol Chem (1991) 1.56
Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange. J Mol Biol (1979) 1.55
The activation of ribulose 1,5-bisphosphate carboxylase/oxygenase. Basic Life Sci (1978) 1.52
Glycolate synthesis by intact chloroplasts. Studies with inhibitors of photophosphorylation. Arch Biochem Biophys (1977) 1.51
Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J (1997) 1.49
The presence of bound cyanide in the naturally inactivated form of nitrate reductase of Chlorella vulgaris. J Biol Chem (1974) 1.48
Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry (1993) 1.47
Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry (1996) 1.45
Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. Biochemistry (1983) 1.45
On the role of groES in the chaperonin-assisted folding reaction. Three case studies. J Biol Chem (1994) 1.43
Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60. Biochemistry (1992) 1.38
Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models. J Mol Biol (1992) 1.37
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
Factors affecting interconversion between kinetic forms of ribulose diphosphate carboxylase-oxygenase from spinach. Arch Biochem Biophys (1975) 1.32
The stereochemical course of ribulosebisphosphate carboxylase. Reductive trapping of the 6-carbon reaction-intermediate. J Biol Chem (1982) 1.31
Diffusion and osmotic transfer in corn mitochondria. Plant Physiol (1970) 1.27
Diffusional barrier crossing in a two-state protein folding reaction. Nat Struct Biol (1999) 1.25
On the mechanism of glycolate synthesis by Chromatium and Chlorella. Arch Biochem Biophys (1978) 1.24
Stabilization of a protein by guanidinium chloride. Biochemistry (1993) 1.23
Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry (1990) 1.23
Reaction intermediate partitioning by ribulose-bisphosphate carboxylases with differing substrate specificities. J Biol Chem (1986) 1.22
Evidence for the existence of discrete activator and substrate sites for CO2 on ribulose-1,5-bisphosphate carboxylase. J Biol Chem (1979) 1.21
Activation of ribulose-1, 5-bisphosphate oxygenase, The role of Mg2+, CO2, and pH. Arch Biochem Biophys (1976) 1.21
Modular structure of the trigger factor required for high activity in protein folding. J Mol Biol (1997) 1.21
Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry (1990) 1.18
Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeast. Protein Sci (1992) 1.18
Identification of a groES-like chaperonin in mitochondria that facilitates protein folding. Proc Natl Acad Sci U S A (1990) 1.18
Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. Biochemistry (1990) 1.15
Electrostatic stabilization of a thermophilic cold shock protein. J Mol Biol (2001) 1.13
Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1. J Mol Biol (1992) 1.12
Microsecond folding of the cold shock protein measured by a pressure-jump technique. Biochemistry (1999) 1.12
Interactions of hydrogen peroxide with ribulose bisphosphate carboxylase oxygenase. J Biol Chem (1980) 1.11
Dynamic association of trigger factor with protein substrates. J Mol Biol (2001) 1.11
Selecting proteins with improved stability by a phage-based method. Nat Biotechnol (1998) 1.10
Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein. J Mol Biol (2000) 1.10
The incorporation of (18O)oxygen into glycolate by intact isolated chloroplasts. FEBS Lett (1977) 1.10
Protein folding as a diffusional process. Biochemistry (1999) 1.10
A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A. Eur J Biochem (1981) 1.09
Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding. Nature (1988) 1.07
In-vitro selection of highly stabilized protein variants with optimized surface. J Mol Biol (2001) 1.07
Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease. Proc Natl Acad Sci U S A (1986) 1.06
Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry (1994) 1.02
Functional characterization of the higher plant chloroplast chaperonins. J Biol Chem (1995) 1.01
Combinations of the alpha-helix-turn-alpha-helix motif of TetR with respective residues from LacI or 434Cro: DNA recognition, inducer binding, and urea-dependent denaturation. Biochemistry (1997) 1.00
Fast-folding and slow-folding forms of unfolded proteins. Methods Enzymol (1986) 1.00
A native-like intermediate on the ribonuclease A folding pathway. 1. Detection by tyrosine fluorescence changes. Eur J Biochem (1981) 0.99
The mechanism of action of FK 506. Transplant Proc (1990) 0.99
Preferential binding of an unfolded protein to DsbA. EMBO J (1996) 0.99
Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate. Proteins (1992) 0.99
Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Proc Natl Acad Sci U S A (1993) 0.99
Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. Proteins (1998) 0.99
The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo. J Biol Chem (1999) 0.98
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
Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci (1992) 0.98
A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin. J Biol Chem (1995) 0.97
Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions. Biochemistry (1998) 0.97
Reassessment of the putative chaperone function of prolyl-cis/trans-isomerases. FEBS Lett (1994) 0.97
Structure of a rapidly formed intermediate in ribonuclease T1 folding. Protein Sci (1992) 0.95
Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding. J Mol Biol (1995) 0.94
Dethiobiotin synthetase: the carbonylation of 7,8-diaminonanoic acid proceeds regiospecifically via the N7-carbamate. Biochemistry (1995) 0.94
The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentration. J Mol Biol (1979) 0.94
Intact disulfide bonds decelerate the folding of ribonuclease T1. J Mol Biol (1994) 0.93