Year |
Citation |
Score |
1977 |
Steinhardt J, Scott JR, Birdi KS. Differences in the solubilizing effectiveness of the sodium dodecyl sulfate complexes of various proteins. Biochemistry. 16: 718-25. PMID 836811 DOI: 10.1021/Bi00623A025 |
0.396 |
|
1977 |
Kowalczykowski S, Steinhardt J. Kinetics of hemoglobin S gelation followed by continuously sensitive low-shear viscosity. Journal of Molecular Biology. 115: 201-13. PMID 592363 DOI: 10.1016/0022-2836(77)90097-3 |
0.425 |
|
1974 |
Steinhardt J, Stocker N, Carroll D, Birdi KS. The nonspecific large binding of amphiphiles by proteins. Biochemistry. 13: 4461-8. PMID 4213461 DOI: 10.1021/Bi00718A032 |
0.411 |
|
1973 |
Steinhardt J, Stocker N. Effects of high pH and sodium dodecyl sulfate on the hidden tyrosines of human serum albumin. Biochemistry. 12: 1789-97. PMID 4735492 DOI: 10.1021/Bi00733A020 |
0.389 |
|
1973 |
Steinhardt J, Stocker N. Remasking of hidden tyrosines of human serum albumins after exposure to high and low pH. Biochemistry. 12: 2798-802. PMID 4719118 DOI: 10.1021/Bi00739A004 |
0.342 |
|
1972 |
Steinhardt J, Leidy JG, Mooney JP. Effects of n-alkyl ligands on the difference spectra of bovine and human serum albumin. Biochemistry. 11: 1809-17. PMID 5063535 DOI: 10.1021/Bi00760A012 |
0.346 |
|
1971 |
Halfman CJ, Steinhardt J. Electrostatic methods for measuring the binding of ionic ligands to proteins. Biochemistry. 10: 3564-9. PMID 5169542 DOI: 10.1021/Bi00795A012 |
0.386 |
|
1971 |
Steinhardt J, Krijn J, Leidy JG. Differences between bovine and human serum albumins: binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence effects. Biochemistry. 10: 4005-15. PMID 5168610 DOI: 10.1021/Bi00798A001 |
0.405 |
|
1970 |
Reynolds JA, Gallagher JP, Steinhardt J. Effect of pH on the binding of N-alkyl sulfates to bovine serum albumin. Biochemistry. 9: 1232-8. PMID 5461511 DOI: 10.1021/Bi00807A026 |
0.629 |
|
1970 |
Allis JW, Steinhardt J. Acid denaturation of carbonylhemoglobin. Protein unfolding without heme detachment. Biochemistry. 9: 2286-93. PMID 5424203 DOI: 10.1021/Bi00813A010 |
0.311 |
|
1969 |
Cassel JM, Steinhardt J. Limitations inherent in the delta pH method of determining binding isotherms of bovine serum albumin. Biochemistry. 8: 2603-9. PMID 5816385 DOI: 10.1021/Bi00834A052 |
0.477 |
|
1969 |
Cassel J, Gallagher J, Reynolds JA, Steinhardt J. The role of transport phenomena in ion binding studies of serum albumin. Biochemistry. 8: 1706-13. PMID 5805305 DOI: 10.1021/Bi00832A054 |
0.601 |
|
1969 |
Cassel J, Steinhardt J. Correction - Limitiations Inherent in the ΔpH Method of Determining Binding Isotherms of Bovine Serum Albumin Biochemistry. 8: 3488-3488. DOI: 10.1021/Bi00836A606 |
0.466 |
|
1968 |
Reynolds J, Herbert S, Steinhardt J. The binding of some long-chain fatty acid anions and alcohols by bovine serum albumin. Biochemistry. 7: 1357-61. PMID 5677825 DOI: 10.1021/Bi00844A016 |
0.603 |
|
1968 |
Polet H, Steinhardt J. Binding-induced alterations in ultraviolet absorption of native serum albumin. Biochemistry. 7: 1348-56. PMID 5677824 DOI: 10.1021/Bi00844A015 |
0.454 |
|
1967 |
Reynolds JA, Herbert S, Polet H, Steinhardt J. The binding of divers detergent anions to bovine serum albumin. Biochemistry. 6: 937-47. PMID 6025573 DOI: 10.1021/Bi00855A038 |
0.65 |
|
1966 |
Ray A, Reynolds JA, Polet H, Steinhardt J. Binding of large organic anions and neutral molecules by native bovine serum albumin. Biochemistry. 5: 2606-16. PMID 5968571 DOI: 10.1021/Bi00872A019 |
0.623 |
|
1959 |
Beychok S, Steinhardt J. Increase in Acid-binding Sites on Denaturation of Horse Ferrihemoglobin at 0°1 Journal of the American Chemical Society. 81: 5679-5687. DOI: 10.1021/Ja01530A039 |
0.403 |
|
1958 |
Steinhardt J, Zaiser EM, Beychok S. Kinetic and Equilibrium Measurements of the Regeneration of Acid-denatured Horse Ferrihemoglobin1 Journal of the American Chemical Society. 80: 4634-4644. DOI: 10.1021/Ja01550A057 |
0.301 |
|
1955 |
STEINHARDT J, ZAISER EM. Hydrogen ion equilibria in native and denatured proteins. Advances in Protein Chemistry. 10: 151-226. PMID 13282762 DOI: 10.1016/S0065-3233(08)60105-9 |
0.314 |
|
1954 |
Zaiser EM, Steinhardt J. A Specific Effect of Formate Ion on the Reversible Acid Denaturation of Horse Ferrihemoglobin1 Journal of the American Chemical Society. 76: 1788-1791. DOI: 10.1021/Ja01636A017 |
0.315 |
|
1953 |
Steinhardt J, Zaiser EM. Kinetic Study of the Reversible Acid Denaturation of Ferrihemoglobin1 Journal of the American Chemical Society. 75: 1599-1605. DOI: 10.1021/Ja01103A025 |
0.324 |
|
1951 |
STEINHARDT J, ZAISER EM. Masking of acid-binding groups in native horse carbonylhemoglobin. The Journal of Biological Chemistry. 190: 197-210. PMID 14841166 |
0.329 |
|
1951 |
Zaiser EM, Steinhardt J. Kinetic Evidence on the Mechanism of the Acid Denaturation of Horse CO Hemoglobin1 Journal of the American Chemical Society. 73: 5568-5572. DOI: 10.1021/Ja01156A017 |
0.313 |
|
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