Diffusion control in an elementary protein folding reaction.

Single-molecule fluorescence studies of protein folding and conformational dynamics. Chem Rev (2006) 3.08

The speed limit for protein folding measured by triplet-triplet energy transfer. Proc Natl Acad Sci U S A (1999) 2.85

Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet. Chem Rev (2006) 2.48

Folding lambda-repressor at its speed limit. Biophys J (2004) 2.44

Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants. Proc Natl Acad Sci U S A (2005) 1.94

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. Proc Natl Acad Sci U S A (2000) 1.91

Folding thermodynamics of a model three-helix-bundle protein. Proc Natl Acad Sci U S A (1997) 1.89

Limited internal friction in the rate-limiting step of a two-state protein folding reaction. Proc Natl Acad Sci U S A (1998) 1.74

Non-Arrhenius kinetics for the loop closure of a DNA hairpin. Proc Natl Acad Sci U S A (2001) 1.71

Measuring internal friction of an ultrafast-folding protein. Proc Natl Acad Sci U S A (2008) 1.69

Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family. Nature (2010) 1.61

The folding of single domain proteins--have we reached a consensus? Curr Opin Struct Biol (2010) 1.42

Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with a green fluorescent protein. Protein Sci (2005) 0.94

Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains. Proc Natl Acad Sci U S A (2012) 0.92

Potential for modulation of the hydrophobic effect inside chaperonins. Biophys J (2008) 0.92

The early folding kinetics of apomyoglobin. Protein Sci (1998) 0.90

Probing the origins of two-state folding. J Chem Phys (2013) 0.90

Binary and ternary aggregation within tethered protein constructs. Biophys J (2006) 0.90

Combined NMR-observation of cold denaturation in supercooled water and heat denaturation enables accurate measurement of deltaC(p) of protein unfolding. Eur Biophys J (2005) 0.90

Solute diffusion is hindered in the mitochondrial matrix. Proc Natl Acad Sci U S A (2011) 0.89

The topomer-sampling model of protein folding. Proc Natl Acad Sci U S A (1999) 0.89

Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion. Proc Natl Acad Sci U S A (2012) 0.84

15N relaxation study of the cold shock protein CspB at various solvent viscosities. J Biomol NMR (2003) 0.83

Protein folding: adding a nucleus to guide helix docking reduces landscape roughness. J Mol Biol (2012) 0.81

Understanding the mechanism of proteasome 20S core particle gating. Proc Natl Acad Sci U S A (2014) 0.79

Folding of the Pit1 homeodomain near the speed limit. Proc Natl Acad Sci U S A (2010) 0.78

The folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours. J Mol Biol (2013) 0.77

The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding. Protein Sci (2000) 0.75

A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties. Sci Rep (2013) 0.75

How cooperative are protein folding and unfolding transitions? Protein Sci (2016) 0.75

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR (1992) 17.71

Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol (1986) 12.22

From Levinthal to pathways to funnels. Nat Struct Biol (1997) 10.58

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry (1988) 9.18

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins (1989) 5.72

Induction of proteins in response to low temperature in Escherichia coli. J Bacteriol (1987) 5.55

Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem (1982) 5.45

Theoretical studies of protein folding. Annu Rev Biophys Bioeng (1983) 5.15

Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry (1996) 4.39

The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu Rev Biophys Biomol Struct (1993) 4.36

Protein-folding dynamics. Nature (1976) 4.11

Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc Natl Acad Sci U S A (1996) 3.85

Protein folding triggered by electron transfer. Science (1996) 2.99

The barriers in protein folding. Nat Struct Biol (1994) 2.79

Pathways of protein folding. Annu Rev Biochem (1993) 2.77

Extremely rapid protein folding in the absence of intermediates. Nat Struct Biol (1995) 2.43

Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature (1993) 2.40

Submillisecond folding of monomeric lambda repressor. Proc Natl Acad Sci U S A (1995) 2.34

The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase. FEBS Lett (1993) 2.17

ON THE KINETICS OF THE HELIX-COIL TRANSITION OF POLYPEPTIDES IN SOLUTION. J Mol Biol (1965) 2.13

The nature of protein folding pathways: the classical versus the new view. J Biomol NMR (1995) 2.11

Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures. J Bacteriol (1992) 2.04

Structure in solution of the major cold-shock protein from Bacillus subtilis. Nature (1993) 2.04

Submillisecond kinetics of protein folding. Curr Opin Struct Biol (1997) 2.01

Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry (1991) 1.98

Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry (1994) 1.97

Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry (1993) 1.96

Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins (1996) 1.95

The molten globule state of alpha-lactalbumin. FASEB J (1996) 1.89

Kinetic traps in lysozyme folding. Proc Natl Acad Sci U S A (1995) 1.80

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci U S A (1996) 1.79

Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry (1989) 1.76

Intermediate states in protein folding. J Mol Biol (1996) 1.73

Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Proc Natl Acad Sci U S A (1996) 1.57

Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. Biochemistry (1995) 1.51

On-pathway versus off-pathway folding intermediates. Fold Des (1996) 1.49

Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry (1996) 1.45

Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. Biochemistry (1992) 1.32

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity. J Mol Biol (1996) 1.31

A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc Natl Acad Sci U S A (1996) 1.31

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc Natl Acad Sci U S A (1996) 1.21

Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family. J Mol Biol (1996) 1.15

Protein folding monitored at individual residues during a two-dimensional NMR experiment. Science (1996) 1.14

Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli. Biochemistry (1990) 1.10

The roles of partly folded intermediates in protein folding. FASEB J (1996) 1.00

Optical triggers of protein folding. Science (1996) 0.95

Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase. Proteins (1987) 0.95

Intact disulfide bonds decelerate the folding of ribonuclease T1. J Mol Biol (1994) 0.93

Mechanism of renaturation of a large protein, aspartokinase-homoserine dehydrogenase. Biochemistry (1987) 0.91

Calorimetric study on thermal denaturation of lysozyme in polyol-water mixtures. J Biochem (1982) 0.89

Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature (1989) 8.48

Two exposed amino acid residues confer thermostability on a cold shock protein. Nat Struct Biol (2000) 3.27

GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry (1991) 2.92

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

The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J (1997) 2.50

Extremely rapid protein folding in the absence of intermediates. Nat Struct Biol (1995) 2.43

Diagnosis, screening and management of cystic fibrosis related diabetes mellitus: a consensus conference report. Diabetes Res Clin Pract (1999) 2.32

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

Surgical treatment of pulmonary artery sarcoma. J Thorac Cardiovasc Surg (2001) 1.91

A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J (1995) 1.79

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

Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding. Nature (1990) 1.74

Role of proline isomerization in folding of ribonuclease A at low temperatures. Proc Natl Acad Sci U S A (1979) 1.65

Factors associated with burnout of physical therapists in Massachusetts rehabilitation hospitals. Phys Ther (1993) 1.57

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

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J (1997) 1.49

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

Vitamin C improves endothelial function of epicardial coronary arteries in patients with hypercholesterolaemia or essential hypertension--assessed by cold pressor testing. Eur Heart J (1999) 1.42

Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand. J Biol Chem (2000) 1.41

Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models. J Mol Biol (1992) 1.37

A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc Natl Acad Sci U S A (1996) 1.31

Diffusional barrier crossing in a two-state protein folding reaction. Nat Struct Biol (1999) 1.25

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

Modular structure of the trigger factor required for high activity in protein folding. J Mol Biol (1997) 1.21

Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin. J Mol Biol (1999) 1.20

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

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

Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase. Oncogene (2001) 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

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

Fast-folding and slow-folding forms of unfolded proteins. Methods Enzymol (1986) 1.00

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

A native-like intermediate on the ribonuclease A folding pathway. 1. Detection by tyrosine fluorescence changes. Eur J Biochem (1981) 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

The mechanism of action of FK 506. Transplant Proc (1990) 0.99

Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. Proteins (1998) 0.99

Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci (1992) 0.98

The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo. J Biol Chem (1999) 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

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

Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues. J Mol Biol (1998) 0.93

Transcatheter recanalisation and stenting of a closed ductus arteriosus in duct dependent lung perfusion. Heart (1998) 0.93

DcAGP1, a secreted arabinogalactan protein, is related to a family of basic proline-rich proteins. Plant Mol Biol (2001) 0.93

Intact disulfide bonds decelerate the folding of ribonuclease T1. J Mol Biol (1994) 0.93

A kinetic method to evaluate the two-state character of solvent-induced protein denaturation. Biochemistry (1994) 0.92

Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine. J Mol Biol (1993) 0.92

Functions of FKBP12 and mitochondrial cyclophilin active site residues in vitro and in vivo in Saccharomyces cerevisiae. Mol Biol Cell (1997) 0.92

Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry (1996) 0.92

Enzymatic catalysis of prolyl isomerization in an unfolding protein. Biochemistry (1992) 0.92

Pumpless extracorporeal lung assist using an arterio-venous shunt. Applications and limitations. Minerva Anestesiol (2002) 0.91

Role of the chain termini for the folding transition state of the cold shock protein. Biochemistry (2001) 0.90

Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability. J Mol Biol (2001) 0.90

Pacemaker therapy in premature children with high degree AV block. Pacing Clin Electrophysiol (1998) 0.90

Effect of glycosylation on the mechanism of renaturation of invertase from yeast. J Biol Chem (1988) 0.89

The extended transseptal approach in complex mitral valve surgery--evaluation of risks and benefits. Thorac Cardiovasc Surg (1996) 0.89

Reduced inotropic support after aprotinin therapy during pediatric cardiac operations. Ann Thorac Surg (1999) 0.88

Generation of a non-prolyl cis peptide bond in ribonuclease T1. J Mol Biol (1994) 0.88

Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proc Natl Acad Sci U S A (1992) 0.88

Escherichia coli peptide binding protein OppA has a preference for positively charged peptides. J Mol Biol (2011) 0.88

Mid-term results of pulmonary thromboendarterectomy for chronic thromboembolic pulmonary hypertension. Ann Thorac Surg (1996) 0.87

Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase. Biochemistry (1996) 0.87

A collapsed intermediate with nonnative packing of hydrophobic residues in the folding of TEM-1 beta-lactamase. Biochemistry (1998) 0.87

The stability of yeast invertase is not significantly influenced by glycosylation. J Biol Chem (1988) 0.87

Destabilization of a protein helix by electrostatic interactions. J Mol Biol (1995) 0.87

The pathology and biology of uremic pneumonitis. Intensive Care Med (1981) 0.86

Catalysis of protein folding by parvulin. J Mol Biol (1997) 0.86

Folding of homologous proteins. The refolding of different ribonucleases is independent of sequence variations, proline content and glycosylation. J Mol Biol (1983) 0.85

Fast- and slow-refolding forms of unfolded ribonuclease A differ in tyrosine fluorescence. Biochemistry (1982) 0.85

Use of a trypsin-pulse method to study the refolding pathway of ribonuclease. Eur J Biochem (1986) 0.85

Experimental studies of folding kinetics and structural dynamics of small proteins. Adv Biophys (1984) 0.84

Proline isomerization during refolding of ribonuclease A is accelerated by the presence of folding intermediates. FEBS Lett (1986) 0.84

The mechanism of folding of pancreatic ribonucleases is independent of the presence of covalently linked carbohydrate. J Biol Chem (1987) 0.84

Proline isomerization in unfolded ribonuclease A. The equilibrium between fast-folding and slow-folding species is independent of temperature. Eur J Biochem (1982) 0.84

Stability of recombinant Lys25-ribonuclease T1. Biochemistry (1990) 0.84

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