| Year |
Citation |
Score |
| 1982 |
Shen TC, Ramadoss CS, Vennesland B. Effect of reduced pyridine nucleotides and tungstate on the in vitro insertion of molybdenum into demolybdo-nitrate reductase of Chlorella vulgaris. Biochimica Et Biophysica Acta. 704: 227-34. PMID 7201857 DOI: 10.1016/0167-4838(82)90150-9 |
0.336 |
|
| 1982 |
Vennesland B, Castric PA, Conn EE, Solomonson LP, Volini M, Westley J. Cyanide metabolism. Federation Proceedings. 41: 2639-48. PMID 7106306 |
0.447 |
|
| 1980 |
Gewitz HS, Piefke J, Langowska K, Vennesland B. The formation of hydrogen cyanide from histidine in the presence of amino acid oxidase and peroxidase. Biochimica Et Biophysica Acta. 611: 11-26. PMID 7350910 DOI: 10.1016/0005-2744(80)90037-6 |
0.346 |
|
| 1978 |
Gewitz HS, Piefke J, Vennesland B. Nitrate reductase of Chlorella fusca: Partial purification, cytochrome content and presence of HCN after in vivo inactivation. Planta. 141: 323-8. PMID 24414880 DOI: 10.1007/Bf00388351 |
0.382 |
|
| 1976 |
Pistorius EK, Gewitz HS, Voss H, Vennesland B. Reversible inactivation of nitrate reductase in Chlorella vulgaris in vivo. Planta. 128: 73-80. PMID 24430609 DOI: 10.1007/Bf00397181 |
0.395 |
|
| 1976 |
Gewitz HS, Pistorius EK, Voss H, Vennesland B. Cyanide formation in preparations from Chlorella vulgaris Beijerinck: Effect of sonication and amygdalin addition. Planta. 131: 145-8. PMID 24424763 DOI: 10.1007/Bf00389986 |
0.303 |
|
| 1975 |
Guerrero MG, Vennesland B. Stereospecificity of hydrogen removal from pyridine nucleotide: the reactions catalyzed by nitrate reductase and by xanthine oxidase. Febs Letters. 51: 284-6. PMID 235456 DOI: 10.1016/0014-5793(75)80908-2 |
0.324 |
|
| 1975 |
Gerster R, Lorimer GH, Vennesland B. The extra O2 evolved during nitrate utilization by chlorella Plant Science Letters. 5: 255-260. DOI: 10.1016/0304-4211(75)90020-6 |
0.53 |
|
| 1974 |
Gewitz HS, Lorimer GH, Solomonson LP, Vennesland B. Presence of HCN in chlorella vulgaris and its possible role in controlling the reduction of nitrate. Nature. 249: 79-81. PMID 4364357 DOI: 10.1038/249079A0 |
0.574 |
|
| 1973 |
Solomonson LP, Jetschmann K, Vennesland B. Reversible inactivation of the nitrate reductase of Chlorella vulgaris Beijerinck. Biochimica Et Biophysica Acta. 309: 32-43. PMID 4145352 DOI: 10.1016/0005-2744(73)90314-8 |
0.36 |
|
| 1972 |
Solomonson LP, Vennesland B. Nitrate Reductase and Chlorate Toxicity in Chlorella vulgaris Beijerinck. Plant Physiology. 50: 421-4. PMID 16658189 DOI: 10.1104/Pp.50.4.421 |
0.351 |
|
| 1972 |
Jetschmann K, Solomonson LP, Vennesland B. Activation of nitrate reductase by oxidation. Biochimica Et Biophysica Acta. 275: 276-8. PMID 5077863 DOI: 10.1016/0005-2728(72)90048-5 |
0.361 |
|
| 1972 |
Solomonson LP, Vennesland B. Properties of a nitrate reductase of Chlorella. Biochimica Et Biophysica Acta. 267: 544-57. PMID 4340061 DOI: 10.1016/0005-2728(72)90183-1 |
0.42 |
|
| 1966 |
Gupta NK, Vennesland B. Glyoxylate carboligase of Escherichia coli: some properties of the enzyme. Archives of Biochemistry and Biophysics. 113: 255-64. PMID 5328735 DOI: 10.1016/0003-9861(66)90185-8 |
0.41 |
|
| 1966 |
Gupta NK, Vennesland B. [124] Glyoxylate carboligase from Escherichia coli Methods in Enzymology. 9: 693-698. DOI: 10.1016/0076-6879(66)09140-7 |
0.354 |
|
| 1959 |
NAKAMOTO T, KROGMANN DW, VENNESLAND B. The effect of oxygen on riboflavin phosphate-dependent photosynthetic phosphorylation by spinach chloroplasts. The Journal of Biological Chemistry. 234: 2783-8. PMID 14425893 |
0.615 |
|
| 1959 |
UDAKA S, KOUKOL J, VENNESLAND B. Lactic oxidase of Pneumococcus. Journal of Bacteriology. 78: 714-25. PMID 13840149 DOI: 10.1128/Jb.78.5.714-725.1959 |
0.335 |
|
| 1959 |
KROGMANN DW, VENNESLAND B. Oxidative photosynthetic phosphorylation by spinach chloroplasts. The Journal of Biological Chemistry. 234: 2205-10. PMID 13673038 |
0.523 |
|
| 1958 |
Marcus A, Vennesland B. Formation of keto-pyruvate in the dehydrogenation catalyzed by yeast lactic oxidase Journal of the American Chemical Society. 80: 1123-1125. DOI: 10.1021/Ja01538A027 |
0.338 |
|
| 1957 |
Mazelis M, Vennesland B. Carbon Dioxide Fixation into Oxalacetate in Higher Plants. Plant Physiology. 32: 591-600. PMID 16655053 DOI: 10.1104/Pp.32.6.591 |
0.325 |
|
| 1954 |
STAFFORD HA, MAGALDI A, VENNESLAND B. Enzymatic oxidation of DPNH by diketosuccinate and dihydroxyfumarate. Science (New York, N.Y.). 120: 265-6. PMID 13186829 DOI: 10.1126/Science.120.3111.265 |
0.34 |
|
| 1953 |
Barnett RC, Stafford HA, Conn EE, Vennesland B. Phosphogluconic Dehydrogenase in Higher Plants. Plant Physiology. 28: 115-22. PMID 16654515 DOI: 10.1104/Pp.28.1.115 |
0.567 |
|
| 1953 |
FISHER HF, CONN EE, VENNESLAND B, WESTHEIMER FH. The enzymatic transfer of hydrogen. I. The reaction catalyzed by alcohol dehydrogenase. The Journal of Biological Chemistry. 202: 687-97. PMID 13061492 |
0.491 |
|
| 1953 |
STAFFORD HA, VENNESLAND B. Alcohol dehydrogenase of wheat germ. Archives of Biochemistry and Biophysics. 44: 404-14. PMID 13058397 DOI: 10.1016/0003-9861(53)90058-7 |
0.358 |
|
| 1952 |
Anderson DG, Stafford HA, Conn EE, Vennesland B. THE DISTRIBUTION IN HIGHER PLANTS OF TRIPHOSPHOPYRIDINE NUCLEOTIDE-LINKED ENZYME SYSTEMS CAPABLE OF REDUCING GLUTATHIONE. Plant Physiology. 27: 675-84. PMID 16654493 DOI: 10.1104/Pp.27.4.675 |
0.566 |
|
| 1952 |
CONN EE, KRAEMER LM, LIU PN, VENNESLAND B. The aerobic oxidation of reduced triphosphopyridine nucleotide by a wheat germ enzyme system. The Journal of Biological Chemistry. 194: 143-51. PMID 14927602 |
0.591 |
|
| 1951 |
CONN EE, VENNESLAND B. Glutathione reductase of wheat germ. The Journal of Biological Chemistry. 192: 17-28. PMID 14917646 |
0.544 |
|
| 1951 |
CONN EE, VENNESLAND B. Enzymatic reduction of glutathione by triphosphopyridine nucleotide (co-enzyme II). Nature. 167: 976-7. PMID 14843137 DOI: 10.1038/167976B0 |
0.581 |
|
| 1951 |
KRAEMER LM, CONN EE, VENNESLAND B. The beta-carboxylases of plants. III. Oxalacetic-carboxylase of wheat germ. The Journal of Biological Chemistry. 188: 583-91. PMID 14824145 |
0.468 |
|
| 1940 |
Vennesland B, Hanke ME. The Oxidation-Reduction Potential Requirements of a Non-Spore-Forming, Obligate Anaerobe. Journal of Bacteriology. 39: 139-69. PMID 16560282 DOI: 10.1128/Jb.39.2.139-169.1940 |
0.66 |
|
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