| Year |
Citation |
Score |
| 2000 |
STEINER RF, BEERS RF. Polynucleotides. V. Titration and spectrophotometric studies upon the interaction of synthetic polynucleotides with various dyes. Archives of Biochemistry and Biophysics. 81: 75-92. PMID 13637968 DOI: 10.1016/0003-9861(59)90177-8 |
0.318 |
|
| 1996 |
Steiner RF, Juminaga D, Albaugh S, Washington H. A comparison of the properties of the binary and ternary complexes formed by calmodulin and troponin C with two regulatory peptides of phosphorylase kinase. Biophysical Chemistry. 59: 277-88. PMID 8672716 DOI: 10.1016/0301-4622(95)00125-5 |
0.304 |
|
| 1994 |
Juminaga D, Albaugh SA, Steiner RF. Functional Zone Identification by Biophysical Techniques: The Interaction of Calmodulin with Regulatory Peptides Techniques in Protein Chemistry. 5: 339-349. DOI: 10.1016/B978-0-12-194710-1.50043-6 |
0.305 |
|
| 1992 |
Zeng BF, Bounds PL, Steiner RF, Pollack RM. Nature of the intermediate in the 3-oxo-delta 5-steroid isomerase reaction. Biochemistry. 31: 1521-8. PMID 1346570 DOI: 10.1021/Bi00120A032 |
0.316 |
|
| 1991 |
Steiner RF, Albaugh S, Kilhoffer MC. Distribution of separations between groups in an engineered calmodulin. Journal of Fluorescence. 1: 15-22. PMID 24242906 DOI: 10.1007/Bf00865254 |
0.31 |
|
| 1991 |
Gryczynski I, Steiner RF, Lakowicz JR. Intensity and anisotropy decays of the tyrosine calmodulin proteolytic fragments, as studied by GHz frequency-domain fluorescence Biophysical Chemistry. 39: 69-78. PMID 2012835 DOI: 10.1016/0301-4622(91)85007-D |
0.329 |
|
| 1990 |
Steiner RF, Albaugh S. The interaction of cyclosporin and calmodulin. Biopolymers. 29: 1005-14. PMID 2369611 DOI: 10.1002/Bip.360290612 |
0.381 |
|
| 1990 |
Garone L, Steiner RF. The interaction of calmodulin with the C-terminal M5 peptide of myosin light chain kinase. Archives of Biochemistry and Biophysics. 276: 12-8. PMID 2297218 DOI: 10.1016/0003-9861(90)90003-H |
0.342 |
|
| 1990 |
Garone L, Albaugh S, Steiner RF. The secondary structure of turkey gizzard myosin light chain kinase and the nature of its interaction with calmodulin. Biopolymers. 30: 1139-49. PMID 2081270 DOI: 10.1002/Bip.360301113 |
0.355 |
|
| 1989 |
Lan J, Albaugh S, Steiner RF. Interactions of troponin I and its inhibitory fragment (residues 104-115) with troponin C and calmodulin. Biochemistry. 28: 7380-5. PMID 2819077 DOI: 10.1021/Bi00444A035 |
0.346 |
|
| 1989 |
Eames TC, Pollack RM, Steiner RF. Orientation, accessibility, and mobility of equilenin bound to the active site of steroid isomerase. Biochemistry. 28: 6269-75. PMID 2675967 DOI: 10.1021/Bi00441A019 |
0.345 |
|
| 1988 |
Bucci E, Steiner RF. Anisotropy decay of fluorescence as an experimental approach to protein dynamics. Biophysical Chemistry. 30: 199-224. PMID 3061490 DOI: 10.1016/0301-4622(88)85017-8 |
0.333 |
|
| 1987 |
Lakowicz JR, Johnson ML, Wiczk W, Bhat A, Steiner RF. RESOLUTION OF A DISTRIBUTION OF DISTANCES BY FLUORESCENCE ENERGY TRANSFER AND FREQUENCY-DOMAIN FLUOROMETRY. Chemical Physics Letters. 138: 587-593. PMID 31839681 DOI: 10.1016/0009-2614(87)80130-6 |
0.326 |
|
| 1987 |
Steiner RF, Norris L. Fluorescence dynamics studies of troponin C. Biopolymers. 26: 1189-204. PMID 3620580 DOI: 10.1002/Bip.360260713 |
0.304 |
|
| 1987 |
Steiner RF, Norris L. Rotational modes of Ca2+-liganded calmodulin, as determined by time-domain fluorescence. Biophysical Chemistry. 27: 27-38. PMID 3607237 DOI: 10.1016/0301-4622(87)80044-3 |
0.332 |
|
| 1986 |
Steiner RF, Marshall L, Needleman D. The interaction of melittin with calmodulin and its tryptic fragments. Archives of Biochemistry and Biophysics. 246: 286-300. PMID 3963824 DOI: 10.1016/0003-9861(86)90474-1 |
0.331 |
|
| 1986 |
Steiner RF, Marshall L, Needleman D. The properties of calmodulin at physiological temperature. Biopolymers. 25: 351-71. PMID 3955195 DOI: 10.1002/Bip.360250214 |
0.303 |
|
| 1985 |
Steiner RF, Marshall L. Sites of interaction of calmodulin with trifluoperazine and glucagon. Archives of Biochemistry and Biophysics. 240: 297-311. PMID 4015106 DOI: 10.1016/0003-9861(85)90035-9 |
0.304 |
|
| 1984 |
Steiner RF. Quantitative aspects of the development of a hydrophobic binding site on calmodulin by calcium binding. Biopolymers. 23: 1121-35. PMID 6733251 DOI: 10.1002/Bip.360230612 |
0.306 |
|
| 1984 |
Steiner RF. Location of a binding site for 1-anilinonaphthalene-8-sulfonate on calmodulin. Archives of Biochemistry and Biophysics. 228: 105-12. PMID 6696426 DOI: 10.1016/0003-9861(84)90051-1 |
0.323 |
|
| 1984 |
Steiner RF. Principles of fluorescence spectroscopy Analytical Biochemistry. 137: 539. DOI: 10.1016/0003-2697(84)90125-8 |
0.31 |
|
| 1983 |
Steiner RF, Lambooy PK, Sternberg H. The dependence of the molecular dynamics of calmodulin upon pH and ionic strength. Archives of Biochemistry and Biophysics. 222: 158-69. PMID 6838218 DOI: 10.1016/0003-9861(83)90513-1 |
0.327 |
|
| 1983 |
Kubota Y, Motoda Y, Fujisaki Y, Steiner RF. Fluorescence decay studies of modified dinucleoside monophosphates containing 1-N6-ethenoadenosine. Biophysical Chemistry. 18: 225-32. PMID 6580048 DOI: 10.1016/0301-4622(83)80035-0 |
0.346 |
|
| 1982 |
Steiner RF, Sternberg H. Properties of the complexes formed by 1-anilinonaphthalene-8-sulfonate with phosphorylase kinase and calmodulin. Biopolymers. 21: 1411-25. PMID 7115897 DOI: 10.1002/Bip.360210710 |
0.369 |
|
| 1982 |
Lambooy PK, Steiner RF, Sternberg H. Molecular dynamics of calmodulin as monitored by fluorescence anisotropy. Archives of Biochemistry and Biophysics. 217: 517-28. PMID 6814364 DOI: 10.1016/0003-9861(82)90533-1 |
0.336 |
|
| 1979 |
Steiner RF, Sternberg H. The interaction of Hoechst 33258 with natural and biosynthetic nucleic acids. Archives of Biochemistry and Biophysics. 197: 580-8. PMID 92214 DOI: 10.1016/0003-9861(79)90282-0 |
0.329 |
|
| 1979 |
Bucci E, Fronticelli C, Flanigan K, Perlman J, Steiner RF. Fluorescence anisotropy decay studies upon hemoglobin A and its subunits Biopolymers. 18: 1261-1276. DOI: 10.1002/Bip.1979.360180516 |
0.331 |
|
| 1978 |
Bhat RK, Smith T, Greer L, Steiner RF. Properties of monomeric phosphorylase B formed by the action of propylurea. Archives of Biochemistry and Biophysics. 190: 677-86. PMID 214038 DOI: 10.1016/0003-9861(78)90326-0 |
0.329 |
|
| 1977 |
Kubota Y, Steiner RF. Nanosecond Fluorescence Anisotropy of the DNA–Acridine Complexes Bulletin of the Chemical Society of Japan. 50: 1502-1505. DOI: 10.1246/Bcsj.50.1502 |
0.335 |
|
| 1976 |
Tang LH, Kubota Y, Steiner RF. A comparative study on bovine alpha-lactalbumin and lysozyme by nanosecond fluorometry. Biophysical Chemistry. 4: 203-13. PMID 1260101 DOI: 10.1016/0301-4622(76)85011-9 |
0.32 |
|
| 1975 |
Tung MS, Steiner RF. The use of nanosecond fluorometry in detecting conformational transitions of an allosteric enzyme Biopolymers. 14: 1933-1949. DOI: 10.1002/Bip.1975.360140912 |
0.331 |
|
| 1974 |
Steiner RF, Lunasin A, Horan C. Specifically located fluorescent probes: Properties of a fluorescent conjugate of soy bean trypsin inhibitor containing dansylamino-tyrosine groups Biochimica Et Biophysica Acta (Bba) - Protein Structure. 336: 407-420. DOI: 10.1016/0005-2795(74)90422-X |
0.353 |
|
| 1973 |
Steiner R, Kinnier W, Lunasin A, Delac J. Fluorescent derivatives of polyribonucleotides containing ε-adenosine Biochimica Et Biophysica Acta (Bba) - Nucleic Acids and Protein Synthesis. 294: 24-37. DOI: 10.1016/0005-2787(73)90311-0 |
0.356 |
|
| 1972 |
McKenzie RL, Millar DB, Steiner RF. Fluorescent conjugates of natural and biosynthetic polynucleotides Bba Section Nucleic Acids and Protein Synthesis. 277: 306-322. PMID 5075289 DOI: 10.1016/0005-2787(72)90413-3 |
0.338 |
|
| 1958 |
Steiner RF, Beers RF. Some properties of enzymatically produced polynucleotides Journal of Polymer Science. 30: 17-28. DOI: 10.1002/Pol.1958.1203012103 |
0.32 |
|
| 1952 |
Trementozzi QA, Steiner RF, Doty P. Association of Polystyrene in Non-polar Solvents1 Journal of the American Chemical Society. 74: 2070-2073. DOI: 10.1021/Ja01128A064 |
0.421 |
|
| 1950 |
Doty PM, Steiner RF. Note on the distribution of polymer molecules in dilute solution Journal of Polymer Science. 5: 383-386. DOI: 10.1002/Pol.1950.120050312 |
0.43 |
|
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