Ruth E. Benesch - Publications

Affiliations: 
Columbia University, New York, NY 
Area:
hemoglobin
Website:
http://en.wikipedia.org/wiki/Reinhold_and_Ruth_Benesch

104 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
1999 Shorr RG, Kwong S, Gilbert C, Benesch RE. Changes in the functional properties of bovine hemoglobin induced by covalent modification with polyethylene glycol. Artificial Cells, Blood Substitutes, and Immobilization Biotechnology. 27: 185-202. PMID 10226683 DOI: 10.3109/10731199909117693  0.73
1995 Benesch RE, Kwong S. Coupled reactions in hemoglobin. Heme-globin and dimer-dimer association. The Journal of Biological Chemistry. 270: 13785-6. PMID 7775434 DOI: 10.1074/Jbc.270.23.13785  0.715
1994 Benesch RE. The stability of the heme-globin linkage: measurement of heme exchange. Methods in Enzymology. 231: 496-502. PMID 8041271 DOI: 10.1016/0076-6879(94)31033-5  0.686
1994 Benesch RE. Bis(pyridoxal) polyphosphates as specific intramolecular cross-linking agents for hemoglobin. Methods in Enzymology. 231: 267-74. PMID 8041256 DOI: 10.1016/0076-6879(94)31018-1  0.708
1994 Benesch RE, Kwong S. Quantitative transformation of hemoglobin into stable tetramers. Hemoglobin. 18: 185-92. PMID 7928375 DOI: 10.3109/03630269409043618  0.686
1991 Benesch RE, Kwong S. Hemoglobin tetramers stabilized by a single intramolecular cross-link. Journal of Protein Chemistry. 10: 503-10. PMID 1799408 DOI: 10.1007/Bf01025478  0.712
1990 Benesch RE, Kwong S. The stability of the heme-globin linkage in some normal, mutant, and chemically modified hemoglobins. The Journal of Biological Chemistry. 265: 14881-5. PMID 1697581  0.685
1989 Keipert PE, Adeniran AJ, Kwong S, Benesch RE. Functional properties of a new crosslinked hemoglobin designed for use as a red cell substitute. Transfusion. 29: 768-73. PMID 2588315  0.68
1988 Benesch RE, Kwong S. Bis-pyridoxal polyphosphates: a new class of specific intramolecular crosslinking agents for hemoglobin. Biochemical and Biophysical Research Communications. 156: 9-14. PMID 3178853 DOI: 10.1016/S0006-291X(88)80798-8  0.738
1988 Benesch RE, Kwong S, Hudson BB, Krumdieck CL. p-Aminobenzoylpolyglutamates with hydrophobic end groups. A new class of inhibitors of hemoglobin S polymerization. The Journal of Biological Chemistry. 263: 69-71. PMID 2447077  0.683
1986 Benesch RE, Benesch R, Kwong S, McCord JM. Binding of diphosphoglycerate and ATP to oxyhemoglobin dimers. Journal of Molecular Biology. 190: 481-5. PMID 3783709 DOI: 10.1016/0022-2836(86)90016-1  0.72
1986 Arnone A, Rogers PH, Benesch RE, Benesch R, Kwong S. The interaction of folylpolyglutamates with deoxyhemoglobin. Identification of the binding site. The Journal of Biological Chemistry. 261: 5853-7. PMID 3700376  0.697
1985 Benesch RE, Kwong S, Benesch R, Baugh CM. The binding of folyl- and antifolylpolyglutamates to hemoglobin. The Journal of Biological Chemistry. 260: 14653-8. PMID 4055795  0.708
1984 Benesch R, Triner L, Benesch RE, Kwong S, Verosky M. Enhanced oxygen unloading by an interdimerically crosslinked hemoglobin in an isolated perfused rabbit heart. Proceedings of the National Academy of Sciences of the United States of America. 81: 2941-3. PMID 6585838 DOI: 10.1073/Pnas.81.9.2941  0.677
1984 Schnackerz KD, Benesch RE, Benesch R, Kwong S, Ciurak M. Changes in the Bohr effect due to pyridoxylation of the alpha-chain terminal amino groups of hemoglobin. Biochimica Et Biophysica Acta. 790: 226-9. PMID 6487637 DOI: 10.1016/0167-4838(84)90026-8  0.712
1983 Benesch RE, Benesch R, Kwong S, Baugh CM. A pteroylpolyglutamate binds to tetramers in deoxyhemoglobin but to dimers in oxyhemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 80: 6202-5. PMID 6578504 DOI: 10.1073/Pnas.80.20.6202  0.729
1983 Schnackerz KD, Benesch RE, Kwong S, Benesch R, Helmreich EJ. Specific receptor sites for pyridoxal 5'-phosphate and pyridoxal 5'-deoxymethylenephosphonate at the alpha and beta NH2-terminal regions of hemoglobin. The Journal of Biological Chemistry. 258: 872-5. PMID 6296088  0.689
1982 Benesch RE, Kwong S, Benesch R. The effects of alpha chain mutations cis and trans to the beta6 mutation on the polymerization of sickle cell haemoglobin. Nature. 299: 231-4. PMID 7110343 DOI: 10.1038/299231A0  0.67
1982 Ackers GK, Benesch RE, Edalji R. Effects of inositol hexasulfate on the oxygen affinity of hemoglobin: verification of the integral function theory of thermodynamic linkage. Biochemistry. 21: 875-9. PMID 7074057 DOI: 10.1021/Bi00534A010  0.713
1982 Benesch R, Benesch RE, Kwong S, Acharya AS, Manning JM. Labeling of hemoglobin with pyridoxal phosphate. The Journal of Biological Chemistry. 257: 1320-4. PMID 7056719  0.705
1982 Benesch R, Waxman S, Benesch R, Baugh C. The binding of folyl polyglutamates by hemoglobin. Biochemical and Biophysical Research Communications. 106: 1359-63. PMID 6180751 DOI: 10.1016/0006-291X(82)91263-3  0.699
1981 Benesch R, Benesch R. Antisckiling drugs and water structure. Nature. 289: 637-8. PMID 7464930 DOI: 10.1038/289637A0  0.642
1981 Benesch R, Benesch RE. Preparation and properties of hemoglobin modified with derivatives of pyridoxal. Methods in Enzymology. 76: 147-59. PMID 7329258 DOI: 10.1016/0076-6879(81)76123-8  0.717
1981 Crepeau RH, Edelstein SJ, Szalay M, Benesch RE, Benesch R, Kwong S, Edalji R. Sickle cell hemoglobin fiber structure altered by alpha-chain mutation. Proceedings of the National Academy of Sciences of the United States of America. 78: 1406-10. PMID 6940165 DOI: 10.1073/Pnas.78.3.1406  0.68
1981 Benesch R, Benesch RE. [13] Preparation and properties of hemoglobin modified with derivatives of pyridoxal Methods in Enzymology. 76: 147-159. DOI: 10.1016/0076-6879(81)76123-8  0.658
1980 Benesch RE, Edalji R, Benesch R, Kwong S. Solubilization of hemoglobin S by other hemoglobins. Proceedings of the National Academy of Sciences of the United States of America. 77: 5130-4. PMID 6159640 DOI: 10.1073/Pnas.77.9.5130  0.687
1979 Benesch R, Edalji R, Benesch RE. Deuterated iodoacetanilide: a covalent protein label for neutron scattering studies. Journal of Biochemical and Biophysical Methods. 1: 129-32. PMID 551107 DOI: 10.1016/0165-022X(79)90019-8  0.696
1979 Benesch RE, Kwong S, Edalji R, Benesch R. alpha Chain mutations with opposite effects on the gelation of hemoglobin S. The Journal of Biological Chemistry. 254: 8169-72. PMID 468817  0.673
1978 Benesch RE, Benesch R, Edalji R, Kwong S. Intermolecular effects in the polymerization of hemoglobin S. Biochemical and Biophysical Research Communications. 81: 1307-12. PMID 666821 DOI: 10.1016/0006-291X(78)91278-0  0.681
1978 Benesch RE, Edalji R, Kwong S, Benesch R. Oxygen affinity as an index of hemoglobin S polymerization: a new micromethod. Analytical Biochemistry. 89: 162-73. PMID 30335 DOI: 10.1016/0003-2697(78)90737-6  0.713
1977 Benesch RE, Kwong S, Benesch R, Edalji R. Location and bond type of intermolecular contacts in the polymerisation of haemoglobin S. Nature. 269: 772-5. PMID 927499 DOI: 10.1038/269772A0  0.692
1977 Arnone A, Benesch RE, Benesch R. Structure of human deoxyhemoglobin specifically modified with pyridoxal compounds. Journal of Molecular Biology. 115: 627-42. PMID 592375 DOI: 10.1016/0022-2836(77)90107-3  0.691
1977 Benesch R, Benesch RE, Edalji R, Suzuki T. 5'-deoxypyridoxal as a potential anti-sickling agent. Proceedings of the National Academy of Sciences of the United States of America. 74: 1721-3. PMID 266212 DOI: 10.1073/Pnas.74.4.1721  0.719
1977 Benesch RE, Edalji R, Benesch R. Reciprocal interaction of hemoglobin with oxygen and protons. The influence of allosteric polyanions. Biochemistry. 16: 2594-7. PMID 19033 DOI: 10.1021/Bi00631A003  0.723
1976 Benesch RE, Yung S, Benesch R, Mack J, Schneider RG. alpha-Chain contacts in the polymerisation of sickle haemogloblin. Nature. 260: 219-21. PMID 1256560 DOI: 10.1038/260219A0  0.69
1976 Benesch RE, Ikeda S, Benesch R. Reaction of haptoglobin with hemoglobin covalently cross-linked between the alpha beta dimers. The Journal of Biological Chemistry. 251: 465-70. PMID 1245483  0.695
1976 Benesch R, Edalji R, Benesch RE. The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin. Biochemistry. 15: 3396-8. PMID 952863 DOI: 10.1021/Bi00660A035  0.712
1976 Edalji R, Benesch RE, Benesch R. Binding of inostiol hexaphosphate to deoxyhemoglobin. The Journal of Biological Chemistry. 251: 7720-1. PMID 12176  0.666
1976 Edalji R, Benesch RE, Benesch R. Binding of inositol hexaphosphate to deoxyhemoglobin Journal of Biological Chemistry. 251: 7720-7721.  0.666
1976 Benesch R. The recipe for success Trends in Biochemical Sciences. 1: N125.  0.611
1975 Benesch R, Edalji R, Benesch RE. Oxygenation properties of hemoglobin variants with substitutions near the polyphosphate binding site. Biochimica Et Biophysica Acta. 393: 368-72. PMID 1148220 DOI: 10.1016/0005-2795(75)90063-X  0.726
1975 Benesch R, Benesch RE, Yung S, Edalji R. Hemoglobin covalently bridged across the polyphoshate binding site. Biochemical and Biophysical Research Communications. 63: 1123-9. PMID 1131270 DOI: 10.1016/0006-291X(75)90685-3  0.726
1975 Benesch RE, Rubin H. Interaction of hemoglobin with three ligans: organic phosphates and the Bohr effect. Proceedings of the National Academy of Sciences of the United States of America. 72: 2465-7. PMID 237273 DOI: 10.1073/Pnas.72.6.2465  0.674
1974 Benesch R, Benesch RE, Yung S. Chemical modifications that inhibit gelation of sickle hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 71: 1504-5. PMID 4524653 DOI: 10.1073/Pnas.71.4.1504  0.71
1974 Benesch R, Benesch RE. Homos and heteros among the hemos. Science (New York, N.Y.). 185: 905-8. PMID 4471714 DOI: 10.1126/Science.185.4155.905  0.654
1974 Suzuki T, Benesch RE, Benesch R. The Bohr effect of pyridoxylated hemoglobins. Biochimica Et Biophysica Acta. 351: 442-5. PMID 4407316 DOI: 10.1016/0005-2795(74)90209-8  0.682
1974 Benesch RE, Benesch R. The mechanism of interaction of red cell organic phosphates with hemoglobin. Advances in Protein Chemistry. 28: 211-37. PMID 4364924 DOI: 10.1016/S0065-3233(08)60231-4  0.723
1973 Suzuki T, Benesch RE, Yung S, Benesch R. Preparative isoelectric focusing of CO hemoglobins on polyacrylamide gels and conversion to their oxy forms. Analytical Biochemistry. 55: 249-54. PMID 4796265 DOI: 10.1016/0003-2697(73)90310-2  0.683
1973 Benesch R, Benesch RE, Yung S. The solubility of hemoglobin beta 4 S, the mutant subunits of sickle cell hemoglobin. Biochemical and Biophysical Research Communications. 55: 261-5. PMID 4767302 DOI: 10.1016/0006-291X(73)91082-6  0.707
1973 Benesch RE, Benesch R, Yung S. Equations for the spectrophotometric analysis of hemoglobin mixtures. Analytical Biochemistry. 55: 245-8. PMID 4753150 DOI: 10.1016/0003-2697(73)90309-6  0.659
1973 Benesch RE, Benesch R, Yung S. A comparison of diphosphonoglyceric acid and diphosphoglyceric acid as allosteric effectors for hemoglobin. Canadian Journal of Biochemistry. 51: 1120-2. PMID 4725360 DOI: 10.1139/O73-146  0.71
1973 Benesch RE, Yung S, Suzuki T, Bauer C, Benesch R. Pyridoxal compounds as specific reagents for the alpha and beta N-termini of hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 70: 2595-9. PMID 4517674 DOI: 10.1073/Pnas.70.9.2595  0.713
1972 Benesch RE, Benesch R, Renthal RD, Maeda N. Affinity labeling of the polyphosphate binding site of hemoglobin. Biochemistry. 11: 3576-82. PMID 5053760 DOI: 10.1021/Bi00769A013  0.686
1972 Benesch RE, Maeda N, Benesch R. 2,3-Diphosphoglycerate and the relative affinity of adult and fetal hemoglobin for oxygen and carbon monoxide. Biochimica Et Biophysica Acta. 257: 178-82. PMID 5009828 DOI: 10.1016/0005-2795(72)90268-1  0.692
1971 Benesch RE, Benesch R, Renthal R, Gratzer WB. Cofactor binding and oxygen equilibria in haemoglobin. Nature: New Biology. 234: 174-6. PMID 5289836 DOI: 10.1038/Newbio234174A0  0.719
1971 Berman M, Benesch R, Benesch RE. The removal of organic phosphates from hemoglobin. Archives of Biochemistry and Biophysics. 145: 236-9. PMID 5123140 DOI: 10.1016/0003-9861(71)90031-2  0.664
1971 Maeda N, Chang H, Benesch R, Benesch RE. A simple enzymatic method for the determination of 2,3-diphosphoglycerate in small amounts of blood. The New England Journal of Medicine. 284: 1239-42. PMID 5103316 DOI: 10.1056/Nejm197106032842204  0.68
1970 Benesch RE, Benesch R. The reaction between diphosphoglycerate and hemoglobin. Federation Proceedings. 29: 1101-4. PMID 5443776  0.635
1969 Benesch RE, Benesch R, Yu CI. The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration. Biochemistry. 8: 2567-71. PMID 5799137 DOI: 10.1021/Bi00834A046  0.691
1969 Benesch R, Benesch RE. Intracellular organic phosphates as regulators of oxygen release by haemoglobin. Nature. 221: 618-22. PMID 5774935 DOI: 10.1038/221618A0  0.706
1968 Benesch R, Benesch RE. Oxygenation and ion transport in red cells. Science (New York, N.Y.). 160: 83. PMID 5642313 DOI: 10.1126/Science.160.3823.83  0.681
1968 Benesch R, Benesch RE, Enoki Y. The interaction of hemoglobin and its subunits with 2,3-diphosphoglycerate. Proceedings of the National Academy of Sciences of the United States of America. 61: 1102-6. PMID 5246545 DOI: 10.1073/Pnas.61.3.1102  0.671
1968 Benesch R, Benesch RE, Yu CI. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 59: 526-32. PMID 5238982 DOI: 10.1073/Pnas.59.2.526  0.716
1967 Benesch R, Benesch RE. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochemical and Biophysical Research Communications. 26: 162-7. PMID 6030262 DOI: 10.1016/0006-291X(67)90228-8  0.681
1967 Beychok S, Tyuma I, Benesch RE, Benesch R. Optically active absorption bands of hemoglobin and its subunits. The Journal of Biological Chemistry. 242: 2460-2. PMID 6026236  0.63
1966 Tyuma I, Benesch RE, Benesch R. The preparation and properties of the isolated alpha and beta subunits of hemoglobin A. Biochemistry. 5: 2957-62. PMID 5961883 DOI: 10.1021/Bi00873A027  0.691
1966 Benesch R, Benesch RE, Tyuma I. Subunit exchange and ligand binding. II. The mechanism of the allosteric effect in hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 56: 1268-74. PMID 5230151 DOI: 10.1073/Pnas.56.4.1268  0.695
1965 BENESCH R, MACDUFF G, BENESCH RE. DETERMINATION OF OXYGEN EQUILIBRIA WITH A VERSATILE NEW TONOMETER. Analytical Biochemistry. 11: 81-7. PMID 14328650 DOI: 10.1016/0003-2697(65)90045-X  0.697
1965 Benesch RE, Benesch R, Macduff G. Subunit exchange and ligand binding: a new hypothesis for the mechanism of oxygenation of hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 54: 535-42. PMID 5217440 DOI: 10.1073/Pnas.54.2.535  0.73
1964 BENESCH RE, BENESCH R, MACDUFF G. THE DISSOCIATION OF HEMOGLOBINS A AND H IN CONCENTRATED SODIUM CHLORIDE. Biochemistry. 3: 1132-5. PMID 14220678 DOI: 10.1021/Bi00896A021  0.675
1964 BENESCH R, BENESCH RE. PROPERTIES OF HAEMOGLOBIN H AND THEIR SIGNIFICANCE IN RELATION TO FUNCTION OF HAEMOGLOBIN. Nature. 202: 773-5. PMID 14192167 DOI: 10.1038/202773A0  0.667
1964 BENESCH R, GIBSON QH, BENESCH RE. RATES OF REACTION OF HEMOGLOBIN H WITH LIGANDS. The Journal of Biological Chemistry. 239: 1668-9. PMID 14189906  0.648
1964 BENESCH R, BENESCH RE, MACDUFF G. SPECTRA OF DEOXYGENATED HEMOGLOBIN IN THE SORET REGION. Science (New York, N.Y.). 144: 68-9. PMID 14107469 DOI: 10.1126/Science.144.3614.68  0.667
1964 Benesch R, Benesch RE. Properties of hæemoglobin H and their significance in relation to function of hæmoglobin Nature. 202: 773-775. DOI: 10.1038/202773a0  0.641
1963 RANNEY HM, BENESCH RE, BENESCH R, JACOBS AS. HYBRIDIZATION OF DEOXYGENATED HUMAN HEMOGLOBIN. Biochimica Et Biophysica Acta. 74: 544-7. PMID 14071599  0.634
1963 Benesch R, Benesch RE. Some relations between structure and function in hemoglobin Journal of Molecular Biology. 6: 498-505. DOI: 10.1016/S0022-2836(63)80061-3  0.706
1962 BENESCH RE, BENESCH R, WILLIAMSON ME. The influence of reversible oxygen binding on the interaction between hemoglobin submits. Proceedings of the National Academy of Sciences of the United States of America. 48: 2071-5. PMID 13967412 DOI: 10.1073/Pnas.48.12.2071  0.714
1962 BENESCH RE, BENESCH R. The influence of oxygenation on the reactivity of the--SH groups of hemoglobin. Biochemistry. 1: 735-8. PMID 13967411 DOI: 10.1021/Bi00911A002  0.706
1962 BENESCH R, BENESCH RE. Protein derivatives with new sulfhydryl groups. Biochimica Et Biophysica Acta. 63: 166-70. PMID 13967410 DOI: 10.1016/0006-3002(62)90349-9  0.69
1962 BENESCH R, BENESCH RE. Determination of--SH groups in proteins. Methods of Biochemical Analysis. 10: 43-70. PMID 13967409 DOI: 10.1002/9780470110270.Ch2  0.675
1962 BENESCH R, BENESCH RE, RANNEY HM, JACOBS AS. Isomeric forms of haemoglobin H. Nature. 194: 840-2. PMID 13867177 DOI: 10.1038/194840A0  0.661
1962 Benesch R, Benesch RE, Ranney HM, Jacobs AS. Isomeric forms of hæmoglobin H Nature. 194: 840-842. DOI: 10.1038/194840a0  0.635
1962 Benesch RE, Benesch R. The influence of oxygenation on the reactivity of the - SH groups of hemoglobin Biochemistry. 1: 735-738.  0.685
1961 BENESCH RE, RANNEY HM, BENESCH R, SMITH GM. The chemistry of the Bohr effect. II. Some properties of hemoglobin H. The Journal of Biological Chemistry. 236: 2926-9. PMID 13867178  0.644
1958 Benesch R, Benesch RE. THIOLATION OF PROTEINS. Proceedings of the National Academy of Sciences of the United States of America. 44: 848-53. PMID 16590281 DOI: 10.1073/Pnas.44.9.848  0.656
1958 Benesch RE, Benesch R. The mechanism of disulfide interchange in acid solution ; role of sulfenium ions Journal of the American Chemical Society. 80: 1666-1669. DOI: 10.1021/Ja01540A040  0.658
1957 BENESCH R, BENESCH RE. Determination of sulfhydryl and disulfide groups by specific proton displacement. Biochimica Et Biophysica Acta. 23: 643-4. PMID 13457372 DOI: 10.1016/0006-3002(57)90388-8  0.675
1957 BENESCH RE, BENESCH R. Electrolytic reduction of mercaptides; a new method for the isolation of thiol amino acids and peptides. Biochimica Et Biophysica Acta. 23: 658-9. PMID 13426187 DOI: 10.1016/0006-3002(57)90398-0  0.666
1957 Benesch RE, Benesch R. Electrolytic reduction of mercaptides A new method for the isolation of thiol amino acids and peptides Bba - Biochimica Et Biophysica Acta. 23: 658-659.  0.642
1956 BENESCH R, BENESCH RE, GUTCHO M, LAUFER L. New color test for thiols and thiolesters. Science (New York, N.Y.). 123: 981-2. PMID 13324124 DOI: 10.1126/Science.123.3205.981  0.651
1956 Benesch R, Benesch RE. Formation of peptide bonds by aminolysis of homocysteine thiolactones Journal of the American Chemical Society. 78: 1597-1599. DOI: 10.1021/Ja01589A025  0.65
1955 BENESCH RE, LARDY HA, BENESCH R. The sulfhydryl groups of crystalline proteins. I. Some albumins, enzymes, and hemoglobins. The Journal of Biological Chemistry. 216: 663-76. PMID 13271343  0.659
1955 Benesch RE, Benesch R. The acid strength of the -SH group in cysteine and related compounds Journal of the American Chemical Society. 77: 5877-5881. DOI: 10.1021/Ja01627A030  0.679
1955 Benesch RE, Benesch R. The stability of the silver complex of tris(hydroxymethyl)-aminomethane Journal of the American Chemical Society. 77: 2749-2750. DOI: 10.1021/Ja01615A021  0.651
1954 BENESCH RE, BENESCH R. Relation between erythrocyte integrity and sulfhydryl groups. Archives of Biochemistry and Biophysics. 48: 38-42. PMID 13125568  0.641
1953 BENESCH RE, BENESCH R. Enzymatic removal of oxygen for polarography and related methods. Science (New York, N.Y.). 118: 447-8. PMID 13101775 DOI: 10.1126/Science.118.3068.447  0.692
1953 Benesch RE, Benesch R. A model for the configuration of sulfhydryl groups in proteins [4] Journal of the American Chemical Society. 75: 4367-4369.  0.644
1952 BENESCH R, BENESCH RE. Reactions of thiols with organic mercury compounds. Archives of Biochemistry and Biophysics. 38: 425-41. PMID 12997119  0.636
1952 Benesch RE, Benesch R. The role of adsorption in the reduction of organic mercury compounds at the dropping mercury electrode Journal of Physical Chemistry. 56: 648-653. DOI: 10.1021/J150497A020  0.656
1951 Benesch R, Benesch RE. Polarographic studies of organic mercury compounds Journal of the American Chemical Society. 73: 3391-3396. DOI: 10.1021/Ja01151A115  0.655
1950 BENESCH RE, BENESCH R. Amperometric determination of soluble mercapto groups (glutathione) in blood and tissues. Archives of Biochemistry. 28: 43-7. PMID 14771924  0.651
1949 DZIEWIATKOWSKI DD, BENESCH RE, BENESCH R. On the possible utilization of sulfate sulfur by the suckling rat for the synthesis of chondroitin sulfate as indicated by the use of radioactive sulfur. The Journal of Biological Chemistry. 178: 931-8. PMID 18117015  0.631
1948 BENESCH R, BENESCH RE. Amperometric titration of sulfhydryl groups in amino acids and proteins. Archives of Biochemistry. 19: 35-45. PMID 18884357  0.656
1945 Ellinger P, Benesch R. BIOSYNTHESIS OF " NICOTINAMIDE " IN THE HUMAN GUT The Lancet. 245: 432-434.  0.628
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