Published in Biochemistry on December 21, 1999
Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR. Proc Natl Acad Sci U S A (2006) 1.89
Soft protein-protein docking in internal coordinates. Protein Sci (2002) 1.60
Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link. Proc Natl Acad Sci U S A (2004) 1.17
Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules. Biochemistry (2006) 0.82
Trapping of peptide-based surrogates in an artificially created channel of cytochrome c peroxidase. Protein Sci (2003) 0.77
Salsolinol, a catechol neurotoxin, induces oxidative modification of cytochrome c. BMB Rep (2013) 0.76
An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody. Protein Sci (2016) 0.75
Interpreting the effects of small uncharged solutes on protein-folding equilibria. Annu Rev Biophys Biomol Struct (2001) 1.66
Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function. Nature (1985) 1.41
Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c. Protein Sci (2001) 1.40
Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Eng (1989) 1.35
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature. Protein Sci (1994) 1.33
Osmolyte-induced changes in protein conformational equilibria. Biopolymers (2000) 1.26
A genetic approach for identifying critical residues in the fingers and palm subdomains of HIV-1 reverse transcriptase. Proc Natl Acad Sci U S A (1998) 1.19
Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state. Biochemistry (1992) 1.15
Baseline length and automated fitting of denaturation data. Protein Sci (1998) 1.13
A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry (1995) 1.05
Native tertiary structure in an A-state. J Mol Biol (1998) 1.05
Characterization of horse cytochrome c expressed in Escherichia coli. Protein Expr Purif (2001) 1.04
Sugar-induced molten-globule model. Biochemistry (1998) 1.04
Design of a ruthenium-cytochrome c derivative to measure electron transfer to the initial acceptor in cytochrome c oxidase. J Biol Chem (1995) 1.02
Expression of 15N-labeled eukaryotic cytochrome c in Escherichia coli. J Biol Inorg Chem (1999) 1.00
Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c. Protein Sci (1993) 0.96
Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase. Biochemistry (1996) 0.94
Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix. Biochemistry (1993) 0.93
Partially formed native tertiary interactions in the A-state of cytochrome c. J Mol Biol (1999) 0.93
Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts. Biochemistry (1991) 0.92
Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position. Biochemistry (1988) 0.91
Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c. Biochemistry (1990) 0.91
Unusual effects of an engineered disulfide on global and local protein stability. Biochemistry (1996) 0.91
A rapid droplet method for Sanger dideoxy sequencing. Biotechniques (1988) 0.90
Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific cross-linking. Biochemistry (1996) 0.90
Changing the transition state for protein (Un) folding. Biochemistry (1996) 0.88
Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis. Biochemistry (1991) 0.88
Polarity of disulfide bonds. Protein Sci (1993) 0.87
Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theory. Biochemistry (2001) 0.86
Proton nuclear magnetic resonance as a probe of differences in structure between the C102T and F82S,C102T variants of iso-1-cytochrome c from the yeast Saccharomyces cerevisiae. Biochemistry (1991) 0.85
Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering. Biochemistry (1996) 0.84
Second virial coefficients as a measure of protein--osmolyte interactions. Protein Sci (2001) 0.83
Control of formation and dissociation of the high-affinity complex between cytochrome c and cytochrome c peroxidase by ionic strength and the low-affinity binding site. Biochemistry (1996) 0.83
Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants. Proc Natl Acad Sci U S A (1987) 0.83
Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure. Proc Natl Acad Sci U S A (1999) 0.82
Changes in global stability and local structure of cytochrome c upon substituting phenylalanine-82 with tyrosine. J Inorg Biochem (1993) 0.81
Dramatic stabilization of ferricytochrome c upon reduction. J Inorg Biochem (1993) 0.81
Intracomplex electron transfer between ruthenium-65-cytochrome b5 and position-82 variants of yeast iso-1-cytochrome c. Biochemistry (1993) 0.80
Electron-proton coupling in cytochrome c studied using protein variants. Eur J Biochem (1992) 0.80
Probing weakly polar interactions in cytochrome c. Protein Sci (1993) 0.80
The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector. Protein Eng (1991) 0.79
Nonideality and protein thermal denaturation. Biopolymers (1999) 0.78
Temperature-sensitive variants of Saccharomyces cerevisiae iso-1-cytochrome c produced by random mutagenesis of codons 43 to 54. J Mol Biol (1991) 0.77
Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. FEBS Lett (1991) 0.77
The role of the internal hydrogen bond network in first-order protein electron transfer between Saccharomyces cerevisiae iso-1-cytochrome c and bovine microsomal cytochrome b5. Eur J Biochem (1991) 0.77
Requirements for perpendicular helix pairing. Proteins (1996) 0.76
Effect of a polyhistidine terminal extension on eglin c stability. Anal Biochem (1998) 0.76
The cytoplasmic region of mouse Fc gamma RIIb1, but not Fc gamma RIIb2, binds phospholipid membranes. Biochemistry (1999) 0.76
Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science (1988) 0.76
Design, synthesis, expression, and characterization of the genes for mouse Fc gamma RIIb1 and Fc gamma RIIb2 cytoplasmic regions. Protein Sci (1997) 0.75
Quantification of azo-coupled lysine in azo proteins by amino acid analysis. Anal Biochem (1986) 0.75
Structural studies of yeast iso-1 cytochrome c mutants by resonance Raman spectroscopy. Eur J Biochem (1991) 0.75