PubRank

C R Matthews

Author PubWeight™ 78.83‹?›

Top papers

Rank Title Journal Year PubWeight™‹?›
1 Aminoacyl-transfer RNA populations in mammalian cells chromatographic profiles and patterns of codon recognition. Biochim Biophys Acta 1979 1.87
2 Effect of point mutations on the folding of globular proteins. Methods Enzymol 1987 1.87
3 Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry 1995 1.78
4 Folding and stability of trp aporepressor from Escherichia coli. Biochemistry 1990 1.59
5 Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Sci 1993 1.56
6 Folding of dihydrofolate reductase from Escherichia coli. Biochemistry 1986 1.51
7 Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 1991 1.47
8 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
9 A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry 1993 1.40
10 Barriers in protein folding reactions. Adv Protein Chem 2000 1.24
11 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
12 Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system. J Mol Biol 2000 1.23
13 Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry 1987 1.22
14 Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry 2000 1.19
15 The pentaammineruthenium(III)-histidine complex in ribonuclease A as an optical probe of conformational change. Biochim Biophys Acta 1980 1.18
16 Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci 1995 1.16
17 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
18 Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc Natl Acad Sci U S A 1997 1.10
19 Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli. Biochemistry 1990 1.10
20 Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry 1994 1.10
21 Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Sci 1997 1.09
22 Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry 1989 1.06
23 Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry 1995 1.05
24 Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase. Biochemistry 1989 1.04
25 Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli. Biochemistry 1986 1.03
26 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
27 A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. J Biochem 1995 1.00
28 Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. Biochemistry 1997 1.00
29 Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase. Biochemistry 1992 0.98
30 Ligand binding is the principal determinant of stability for the p21(H)-ras protein. Biochemistry 1998 0.98
31 Rehospitalization among home healthcare patients: results of a prospective study. Home Healthc Nurse 2001 0.98
32 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
33 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
34 Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. Biochemistry 1996 0.95
35 Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase. Proteins 1987 0.95
36 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
37 Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1. Biochemistry 2001 0.94
38 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
39 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
40 Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase. Biochemistry 1980 0.93
41 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
42 Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models. Protein Sci 1993 0.93
43 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
44 Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthase. Biochemistry 1983 0.92
45 The pentaammineruthenium(III)histidine complex in ribonuclease A: application to the assignment of histidine proton resonances. Anal Biochem 1981 0.91
46 Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein. Biochemistry 1997 0.90
47 Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. Biochemistry 1992 0.90
48 Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels. J Mol Biol 2001 0.89
49 A hydrophobic cluster forms early in the folding of dihydrofolate reductase. Proteins 1989 0.89
50 Mutant sequences as probes of protein folding mechanisms. Bioessays 1987 0.89
51 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
52 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
53 Unraveling the mechanism of protein folding: new tricks for an old problem. Protein Eng 1993 0.87
54 Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. Biochemistry 1986 0.87
55 Mutagenic and toxic effects of ruthenium. Chem Biol Interact 1980 0.87
56 Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process. Biochemistry 1981 0.87
57 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
58 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
59 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
60 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
61 Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coli. Biochemistry 1995 0.85
62 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
63 Mutational analysis of protein folding mechanisms. Methods Enzymol 1991 0.84
64 Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis. Biochemistry 1993 0.83
65 Characterization of an early intermediate in the folding of the alpha subunit of tryptophan synthase by hydrogen exchange measurement. Biochemistry 1985 0.82
66 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
67 Proline isomerization and the slow folding reactions of the alpha subunit of tryptophan synthase from Escherichia coli. Biochim Biophys Acta 1987 0.81
68 Folding under the influence. Nat Struct Biol 1999 0.81
69 The role of ligand binding in the kinetic folding mechanism of human p21(H-ras) protein. Biochemistry 1998 0.81
70 Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry 1998 0.80
71 Nuclear magnetic resonance studies of residual structure in thermally unfolded ribonuclease A. Biochemistry 1975 0.80
72 Nuclear magnetic resonance titration curves of histidine ring protons. The effect of temperature on ribonuclease A. J Biol Chem 1975 0.79
73 Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains. Protein Eng 1992 0.79
74 A Fourier transform NMR study of the thermal denaturation of ribonuclease A at low pH. Ann N Y Acad Sci 1973 0.78
75 Prediction of the tertiary structure of the alpha-subunit of tryptophan synthase. Proteins 1987 0.78
76 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
77 Luminescence studies with trp repressor and its single-tryptophan mutants. Biochemistry 1993 0.76
78 Characterization of the slow steps in the folding of the alpha subunit of tryptophan synthase. Biochemistry 1981 0.75
79 Site-directed mutagenesis and its application to protein folding. Biotechnology 1990 0.75
80 The role of protein folding in the evolution of protein sequences. Cold Spring Harb Symp Quant Biol 1987 0.75