Year |
Citation |
Score |
2010 |
Cohn M. Magnetic Resonance Studies of Metal-Enzyme-Substrate Interactions. Science (New York, N.Y.). 136: 325. PMID 17745916 DOI: 10.1126/science.136.3513.325-a |
0.303 |
|
1996 |
COHN M. MAGNETIC RESONANCE STUDIES OF METAL ACTIVATION OF ENZYMIC REACTIONS OF NUCLEOTIDES AND OTHER PHOSPHATE SUBSTRATES. Biochemistry. 2: 623-9. PMID 14075088 DOI: 10.1021/BI00904A001 |
0.324 |
|
1988 |
Park JH, Brown RL, Park CR, Cohn M, Chance B. Energy metabolism of the untrained muscle of elite runners as observed by 31P magnetic resonance spectroscopy: evidence suggesting a genetic endowment for endurance exercise. Proceedings of the National Academy of Sciences of the United States of America. 85: 8780-4. PMID 3194388 DOI: 10.1073/Pnas.85.23.8780 |
0.4 |
|
1987 |
Park JH, Brown RL, Park CR, McCully K, Cohn M, Haselgrove J, Chance B. Functional pools of oxidative and glycolytic fibers in human muscle observed by 31P magnetic resonance spectroscopy during exercise. Proceedings of the National Academy of Sciences of the United States of America. 84: 8976-80. PMID 3480522 DOI: 10.1073/Pnas.84.24.8976 |
0.401 |
|
1986 |
Scheffler JE, Cohn M. Photochemically induced dynamic nuclear polarization NMR study of yeast and horse muscle phosphoglycerate kinase. Biochemistry. 25: 3788-96. PMID 3527256 DOI: 10.1021/Bi00361A009 |
0.387 |
|
1982 |
Smith LT, Cohn M. Reactions of thio analogues of adenosine 5′-triphosphate catalyzed by methionyl-tRNA synthetase from Escherichia coli and metal dependence of stereospecificity Biochemistry. 21: 1530-1534. PMID 7044416 DOI: 10.1021/Bi00536A010 |
0.331 |
|
1982 |
Cohn M, Reed GH. Magnetic resonance studies of active sites in enzymic complexes Annual Review of Biochemistry. 51: 365-394. PMID 6287918 DOI: 10.1146/Annurev.Bi.51.070182.002053 |
0.344 |
|
1982 |
Cohn M. Some properties of the phosphorothioate analogs of adenosine triphosphate as substrates of enzymic reactions Accounts of Chemical Research. 15: 326-332. DOI: 10.1021/Ar00082A005 |
0.323 |
|
1979 |
Rao BD, Cohn M. Measurement of interconversion rates of bound substrates of phosphoryl transfer enzymes by (31)P nuclear magnetic resonance. Biophysical Journal. 24: 258-9. PMID 213134 DOI: 10.1016/S0006-3495(78)85370-3 |
0.304 |
|
1978 |
Nageswara Rao BD, Cohn M. Asymmetric binding of the inhibitor di(adenosine-5') pentaphosphate (Ap5A) to adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America. 74: 5355-7. PMID 202953 DOI: 10.1073/Pnas.74.12.5355 |
0.345 |
|
1978 |
Jaffe EK, Cohn M. 31P nuclear magnetic resonance spectra of the thiophosphate analogues of adenine nucleotides; effects of pH and Mg2+ binding. Biochemistry. 17: 652-7. PMID 23826 DOI: 10.1021/Bi00597A014 |
0.363 |
|
1976 |
McLaughlin AC, Leigh JS, Cohn M. Magnetic resonance study of the three-dimensional structure of creatine kinase-substrate complexes. Implications for substrate specificity and catalytic mechanism. The Journal of Biological Chemistry. 251: 2777-87. PMID 177421 |
0.543 |
|
1975 |
Daniel WE, Cohn M. Proton nuclear magnetic resonance of spin-labeled Escherichia coli tRNAf1MET. Proceedings of the National Academy of Sciences of the United States of America. 72: 2582-6. PMID 1101259 DOI: 10.1073/Pnas.72.7.2582 |
0.359 |
|
1974 |
Du Vigneaud V, Cohn M, Chandler JP, Schenck JR, Simmonds S. Nutrition classics from The Journal of Biological Chemistry 140:625-641, 1941. The utilization of the methyl group of methionine in the biological synthesis of choline and creatine. Nutrition Reviews. 32: 144-6. PMID 4597510 DOI: 10.1111/J.1753-4887.1974.Tb06306.X |
0.613 |
|
1973 |
James TL, Ludwig ML, Cohn M. Dependence of the proton magnetic resonance spectra on the oxidation state of flavodoxin from Clostridium MP and from Peptostreptococcus elsdenii. Proceedings of the National Academy of Sciences of the United States of America. 70: 3292-5. PMID 4519623 DOI: 10.1073/Pnas.70.12.3292 |
0.319 |
|
1973 |
Price NC, Reed GH, Cohn M. Magnetic resonance studies of substrate and inhibitor binding to porcine muscle adenylate kinase Biochemistry. 12: 3322-3327. PMID 4354608 DOI: 10.1021/Bi00741A026 |
0.403 |
|
1972 |
Cohn M, Leigh JS, Reed GH. Mapping active sites of phosphoryl-transferring enzymes by magnetic resonance methods. Cold Spring Harbor Symposia On Quantitative Biology. 36: 533-40. PMID 4343722 |
0.512 |
|
1971 |
Cohn M, Reuben J. Paramagnetic probes in magnetic resonance studies of phosphoryl transfer enzymes Accounts of Chemical Research. 4: 214-222. DOI: 10.1021/Ar50042A004 |
0.422 |
|
1970 |
Mildvan AS, Cohn M. Aspects of enzyme mechanisms studies by nuclear spin relazation induced by paramagnetic probes. Advances in Enzymology and Related Areas of Molecular Biology. 33: 1-70. PMID 4916855 |
0.468 |
|
1970 |
Cohn M. Magnetic resonance studies of enzyme-substrate complexes with paramagnetic probes as illustrated by creatine kinase. Quarterly Reviews of Biophysics. 3: 61-89. PMID 4314327 DOI: 10.1017/S0033583500004418 |
0.339 |
|
1969 |
Taylor JS, Leigh JS, Cohn M. Magnetic resonance studies of spin-labeled creatine kinase system and interaction of two paramagnetic probes. Proceedings of the National Academy of Sciences of the United States of America. 64: 219-26. PMID 4312750 DOI: 10.1073/Pnas.64.1.219 |
0.522 |
|
1967 |
Mildvan AS, Leigh JS, Cohn M. Kinetic and magnetic resonance studies of pyruvate kinase. 3. The enzyme-metal-phosphoryl bridge complex in the fluorokinase reaction. Biochemistry. 6: 1805-18. PMID 6035920 DOI: 10.1021/Bi00858A032 |
0.652 |
|
1966 |
Mildvan AS, Cohn M. Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates. The Journal of Biological Chemistry. 241: 1178-93. PMID 5933875 |
0.568 |
|
1965 |
MILDVAN AS, COHN M. KINETIC AND MAGNETIC RESONANCE STUDIES OF THE PYRUVATE KINASE REACTION. I. DIVALENT METAL COMPLEXES OF PYRUVATE KINASE. The Journal of Biological Chemistry. 240: 238-46. PMID 14253420 |
0.542 |
|
1964 |
Mildvan A, Cohn M. Corrections - Magnetic Resonance Studies of the Interaction of the Manganous Ion with Bovine Serum Albumin Biochemistry. 3: 469-469. DOI: 10.1021/Bi00891A604 |
0.493 |
|
1963 |
MILDVAN AS, COHN M. MAGNETIC RESONANCE STUDIES OF THE INTERACTION OF THE MANGANOUS ION WITH BOVINE SERUM ALBUMIN. Biochemistry. 2: 910-9. PMID 14087380 DOI: 10.1021/Bi00905A003 |
0.493 |
|
1962 |
COHN M, LEIGH JS. Magnetic resonance investigations of ternary complexes of enzyme-metal-substrate. Nature. 193: 1037-40. PMID 13880360 DOI: 10.1038/1931037A0 |
0.542 |
|
1948 |
COHN M, CORI GT. On the mechanism of action of muscle and potato phosphorylase. The Journal of Biological Chemistry. 175: 89-93. PMID 18873282 |
0.522 |
|
1946 |
Du VIGNEAUD V, SIMMONDS S, COHN M. A further investigation of the ability of sarcosine to serve as a labile methyl donor. The Journal of Biological Chemistry. 166: 47-52. PMID 20273672 |
0.444 |
|
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