Published in J Mol Biol on March 03, 2000
Understanding protein non-folding. Biochim Biophys Acta (2010) 4.33
Full distance-resolved folding energy landscape of one single protein molecule. Proc Natl Acad Sci U S A (2010) 1.85
Malleable machines take shape in eukaryotic transcriptional regulation. Nat Chem Biol (2008) 1.76
Intrinsic disorder in scaffold proteins: getting more from less. Prog Biophys Mol Biol (2008) 1.49
Molecular basis of coiled-coil formation. Proc Natl Acad Sci U S A (2007) 1.44
Dimerization specificity of all 67 B-ZIP motifs in Arabidopsis thaliana: a comparison to Homo sapiens B-ZIP motifs. Nucleic Acids Res (2004) 1.25
Modular enzyme design: regulation by mutually exclusive protein folding. J Mol Biol (2006) 1.14
Manipulation of hydrogel assembly and growth factor delivery via the use of peptide-polysaccharide interactions. J Control Release (2006) 1.14
Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome. Protein Sci (2004) 1.13
Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension. J Am Chem Soc (2011) 1.03
The importance of being flexible: the case of basic region leucine zipper transcriptional regulators. Curr Protein Pept Sci (2009) 1.01
Fast folding of a helical protein initiated by the collision of unstructured chains. Proc Natl Acad Sci U S A (2004) 1.00
A novel nonnull ZIP1 allele triggers meiotic arrest with synapsed chromosomes in Saccharomyces cerevisiae. Genetics (2007) 0.97
Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus. Protein Sci (2007) 0.96
Single molecule mechanics of the kinesin neck. Proc Natl Acad Sci U S A (2009) 0.94
Disruption of Bcr-Abl coiled coil oligomerization by design. J Biol Chem (2011) 0.92
Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species. PLoS One (2010) 0.92
Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1. Proteins (2009) 0.91
Temperature dependence of the folding and unfolding kinetics of the GCN4 leucine zipper via 13C(alpha)-NMR. Biophys J (2001) 0.90
T-jump infrared study of the folding mechanism of coiled-coil GCN4-p1. Biophys J (2005) 0.90
Increasing the affinity of selective bZIP-binding peptides through surface residue redesign. Protein Sci (2014) 0.86
Unique features of the anti-parallel, heterodimeric coiled-coil interaction between methyl-cytosine binding domain 2 (MBD2) homologues and GATA zinc finger domain containing 2A (GATAD2A/p66α). J Biol Chem (2012) 0.82
The effects of pK(a) tuning on the thermodynamics and kinetics of folding: design of a solvent-shielded carboxylate pair at the a-position of a coiled-coil. Biophys J (2010) 0.81
Helix formation and the unfolded state of a 52-residue helical protein. Protein Sci (2004) 0.81
Refolding of the hyperthermophilic protein Ssh10b involves a kinetic dimeric intermediate. Extremophiles (2008) 0.81
The Elucidation of the Interactome of 16 Arabidopsis bZIP Factors Reveals Three Independent Functional Networks. PLoS One (2015) 0.80
An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway. Protein Sci (2001) 0.78
Sequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments. Proc Natl Acad Sci U S A (2014) 0.77
Unfoldomics of prostate cancer: on the abundance and roles of intrinsically disordered proteins in prostate cancer. Asian J Androl (2016) 0.76
Hierarchical cascades of instability govern the mechanics of coiled coils: helix unfolding precedes coil unzipping. Biophys J (2014) 0.75
Aminoacyl-transfer RNA populations in mammalian cells chromatographic profiles and patterns of codon recognition. Biochim Biophys Acta (1979) 1.87
Effect of point mutations on the folding of globular proteins. Methods Enzymol (1987) 1.87
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry (1995) 1.78
Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry (1999) 1.67
Folding and stability of trp aporepressor from Escherichia coli. Biochemistry (1990) 1.59
Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Sci (1993) 1.56
Validating genetic risk associations for ovarian cancer through the international Ovarian Cancer Association Consortium. Br J Cancer (2009) 1.54
Folding of dihydrofolate reductase from Escherichia coli. Biochemistry (1986) 1.51
Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry (1991) 1.47
A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry (1993) 1.40
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry (1999) 1.40
Progesterone receptor variation and risk of ovarian cancer is limited to the invasive endometrioid subtype: results from the Ovarian Cancer Association Consortium pooled analysis. Br J Cancer (2008) 1.38
Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins (2000) 1.37
Barriers in protein folding reactions. Adv Protein Chem (2000) 1.24
Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry (1993) 1.24
Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry (1987) 1.22
Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry (2000) 1.19
The pentaammineruthenium(III)-histidine complex in ribonuclease A as an optical probe of conformational change. Biochim Biophys Acta (1980) 1.18
Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci (1995) 1.16
The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. Protein Sci (1999) 1.15
Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli. Biochemistry (1990) 1.10
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc Natl Acad Sci U S A (1997) 1.10
Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry (1994) 1.10
Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Sci (1997) 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
Reproductive characteristics in relation to ovarian cancer risk by histologic pathways. Hum Reprod (2013) 1.06
Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry (1995) 1.05
Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase. Biochemistry (1989) 1.04
Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. Protein Sci (1999) 1.02
A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. J Biochem (1995) 1.00
Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. Biochemistry (1997) 1.00
Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase. Biochemistry (1992) 0.98
Ligand binding is the principal determinant of stability for the p21(H)-ras protein. Biochemistry (1998) 0.98
Rehospitalization among home healthcare patients: results of a prospective study. Home Healthc Nurse (2001) 0.98
Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase. Biochemistry (1994) 0.97
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry (1999) 0.97
Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. Biochemistry (1996) 0.95
Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase. Proteins (1987) 0.95
The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions. Biochemistry (1998) 0.94
Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1. Biochemistry (2001) 0.94
Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pH. Proc Natl Acad Sci U S A (1973) 0.93
Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded forms. Protein Sci (2001) 0.93
Interresidue distance measurements in proteins. Fluorescent energy transfer between tryptophans and a Ru(III)(NH3)5-histidine complex in alpha-lytic protease and lysozyme. Biochim Biophys Acta (1982) 0.93
Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase. Biochemistry (1980) 0.93
Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models. Protein Sci (1993) 0.93
Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry (1998) 0.92
Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthase. Biochemistry (1983) 0.92
The pentaammineruthenium(III)histidine complex in ribonuclease A: application to the assignment of histidine proton resonances. Anal Biochem (1981) 0.91
Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein. Biochemistry (1997) 0.90
Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. Biochemistry (1992) 0.90
Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels. J Mol Biol (2001) 0.89
A hydrophobic cluster forms early in the folding of dihydrofolate reductase. Proteins (1989) 0.89
Mutant sequences as probes of protein folding mechanisms. Bioessays (1987) 0.89
Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. Biochemistry (1988) 0.88
Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. Biochemistry (1995) 0.87
Unraveling the mechanism of protein folding: new tricks for an old problem. Protein Eng (1993) 0.87
Mutagenic and toxic effects of ruthenium. Chem Biol Interact (1980) 0.87
Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. Biochemistry (1986) 0.87
Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process. Biochemistry (1981) 0.87
Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry (1999) 0.87
1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase. J Biomol NMR (1994) 0.87
Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. Biochemistry (1993) 0.86
Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coli. Biochemistry (1995) 0.85
Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. Biochemistry (1993) 0.85
Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry (1999) 0.85
Mutational analysis of protein folding mechanisms. Methods Enzymol (1991) 0.84
Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis. Biochemistry (1993) 0.83
Characterization of an early intermediate in the folding of the alpha subunit of tryptophan synthase by hydrogen exchange measurement. Biochemistry (1985) 0.82
Conversion of Tyr361 beta to Leu in mammalian protein farnesyltransferase impairs product release but not substrate recognition. Biochemistry (2000) 0.81
The role of ligand binding in the kinetic folding mechanism of human p21(H-ras) protein. Biochemistry (1998) 0.81
Folding under the influence. Nat Struct Biol (1999) 0.81
Proline isomerization and the slow folding reactions of the alpha subunit of tryptophan synthase from Escherichia coli. Biochim Biophys Acta (1987) 0.81
Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. Biochemistry (1990) 0.81
Nuclear magnetic resonance studies of residual structure in thermally unfolded ribonuclease A. Biochemistry (1975) 0.80
Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry (1998) 0.80
Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains. Protein Eng (1992) 0.79
Nuclear magnetic resonance titration curves of histidine ring protons. The effect of temperature on ribonuclease A. J Biol Chem (1975) 0.79
A Fourier transform NMR study of the thermal denaturation of ribonuclease A at low pH. Ann N Y Acad Sci (1973) 0.78
Prediction of the tertiary structure of the alpha-subunit of tryptophan synthase. Proteins (1987) 0.78
Characterization of the tryptophan binding site of Escherichia coli tryptophan holorepressor by phosphorescence and optical detection of magnetic resonance of a tryptophan-free mutant. Biochemistry (1995) 0.77
Luminescence studies with trp repressor and its single-tryptophan mutants. Biochemistry (1993) 0.76
Characterization of the slow steps in the folding of the alpha subunit of tryptophan synthase. Biochemistry (1981) 0.75
The role of protein folding in the evolution of protein sequences. Cold Spring Harb Symp Quant Biol (1987) 0.75
A simple algal production system designed to utilize the flashing light effect. Biotechnol Bioeng (1983) 0.75
Site-directed mutagenesis and its application to protein folding. Biotechnology (1990) 0.75