Published in Biochemistry on December 25, 2001
Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy. Proc Natl Acad Sci U S A (2006) 2.48
The N-terminal to C-terminal motif in protein folding and function. Proc Natl Acad Sci U S A (2005) 1.29
What lessons can be learned from studying the folding of homologous proteins? Methods (2010) 0.97
Unfolding studies on soybean agglutinin and concanavalin a tetramers: a comparative account. Biophys J (2004) 0.96
Similarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulations. Biophys J (2006) 0.91
The origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein folding. Biophys J (2010) 0.85
Tryptophan rotamers as evidenced by X-ray, fluorescence lifetimes, and molecular dynamics modeling. Biophys J (2006) 0.82
Is there an en route folding intermediate for Cold shock proteins? Protein Sci (2012) 0.82
The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state. Protein Sci (2006) 0.80
Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model. J Mol Model (2016) 0.75
Electrostatic effects control the stability and iron release kinetics of ovotransferrin. J Biol Inorg Chem (2014) 0.75
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
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
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
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
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
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
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
Photometric characteristics of haem proteins in erythropoietin-producing hepatoma cells (HepG2). Biochem J (1993) 1.03
Depth profiles of pH and PO2 in the isolated brain stem-spinal cord of the neonatal rat. Respir Physiol (1993) 1.02
Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry (1994) 1.02
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
Preferential binding of an unfolded protein to DsbA. EMBO J (1996) 0.99
The mechanism of action of FK 506. Transplant Proc (1990) 0.99
Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate. Proteins (1992) 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
Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci (1992) 0.98
Reassessment of the putative chaperone function of prolyl-cis/trans-isomerases. FEBS Lett (1994) 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
A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin. J Biol Chem (1995) 0.97
Effects of cobalt on haem proteins of erythropoietin-producing HepG2 cells in multicellular spheroid culture. FEBS Lett (1994) 0.95
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
Intact disulfide bonds decelerate the folding of ribonuclease T1. J Mol Biol (1994) 0.93
Transcatheter recanalisation and stenting of a closed ductus arteriosus in duct dependent lung perfusion. Heart (1998) 0.93
A kinetic method to evaluate the two-state character of solvent-induced protein denaturation. Biochemistry (1994) 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
Influence of glucose and buffer capacity in the culture medium on growth and pH in spheroids of human thyroid carcinoma and human glioma origin. Cancer Res (1987) 0.92
Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry (1996) 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
Enzymatic catalysis of prolyl isomerization in an unfolding protein. Biochemistry (1992) 0.92
The meaning of H2O2 generation in carotid body cells for PO2 chemoreception. J Auton Nerv Syst (1992) 0.91
Pumpless extracorporeal lung assist using an arterio-venous shunt. Applications and limitations. Minerva Anestesiol (2002) 0.91
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
Methodological aspects of microelectrode measurements in cellular spheroids. Adv Exp Med Biol (1983) 0.89
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
Mid-term results of pulmonary thromboendarterectomy for chronic thromboembolic pulmonary hypertension. Ann Thorac Surg (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
Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase. Biochemistry (1996) 0.87
Destabilization of a protein helix by electrostatic interactions. J Mol Biol (1995) 0.87
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
Effects of amiloride treatment on U-118 MG and U-251 MG human glioma and HT-29 human colon carcinoma cells. Cancer Res (1991) 0.84
Stability of recombinant Lys25-ribonuclease T1. Biochemistry (1990) 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
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 two proline-containing turns in the folding of porcine ribonuclease. J Mol Biol (1990) 0.83
Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate. FEBS Lett (1997) 0.82
Structure of human parathyroid hormone 1-37 in solution. J Biol Chem (1995) 0.82