| Year |
Citation |
Score |
| 2019 |
Lynen A, Afting E, Holzer H. Yeast phosphofructokinase IV. Reversibility of the ATP-desensitization. Febs Letters. 30: 71-73. PMID 11947064 DOI: 10.1016/0014-5793(73)80621-0 |
0.329 |
|
| 2019 |
Varricchio F, Holzer H. Independent genetic regulation of glutamine synthetase and its inactivating (adenylating) enzyme in E. coli. Febs Letters. 3: 263-264. PMID 11947024 DOI: 10.1016/0014-5793(69)80153-5 |
0.357 |
|
| 2006 |
Holzer H, Fonseca‐Wollheim Fd, Kohlhaw G, Woenckhaus CW. Active forms of acetaldehyde, pyruvate, and glycolic aldehyde. Annals of the New York Academy of Sciences. 98: 453-465. PMID 13908632 DOI: 10.1111/J.1749-6632.1962.Tb30566.X |
0.34 |
|
| 1998 |
Zähringer H, Holzer H, Nwaka S. Stability of neutral trehalase during heat stress in Saccharomyces cerevisiae is dependent on the activity of the catalytic subunits of cAMP-dependent protein kinase, Tpk1 and Tpk2. European Journal of Biochemistry. 255: 544-51. PMID 9738892 DOI: 10.1046/J.1432-1327.1998.2550544.X |
0.322 |
|
| 1996 |
Nwaka S, Mechler B, Holzer H. Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose. Febs Letters. 386: 235-8. PMID 8647289 DOI: 10.1016/0014-5793(96)00450-4 |
0.321 |
|
| 1996 |
Destruelle M, Holzer H, Klionsky DJ. Isolation and characterization of a novel yeast gene, ATH1, that is required for vacuolar acid trehalase activity. Yeast (Chichester, England). 11: 1015-25. PMID 7502577 DOI: 10.1002/Yea.320111103 |
0.318 |
|
| 1994 |
Nwaka S, Kopp M, Burgert M, Deuchler I, Kienle I, Holzer H. Is thermotolerance of yeast dependent on trehalose accumulation? Febs Letters. 344: 225-8. PMID 8187889 DOI: 10.1016/0014-5793(94)00385-8 |
0.314 |
|
| 1993 |
Kienle I, Burgert M, Holzer H. Assay of trehalose with acid trehalase purified from Saccharomyces cerevisiae. Yeast (Chichester, England). 9: 607-11. PMID 8346677 DOI: 10.1002/Yea.320090607 |
0.342 |
|
| 1991 |
Mittenbühler K, Holzer H. Characterization of different forms of yeast acid trehalase in the secretory pathway. Archives of Microbiology. 155: 217-220. PMID 2048932 DOI: 10.1007/Bf00252203 |
0.334 |
|
| 1991 |
Plankert U, Purwin C, Holzer H. Yeast fructose-2,6-bisphosphate 6-phosphatase is encoded by PHO8, the gene for nonspecific repressible alkaline phosphatase. European Journal of Biochemistry. 196: 191-6. PMID 1848184 DOI: 10.1111/J.1432-1033.1991.Tb15803.X |
0.418 |
|
| 1991 |
Winkler K, Kienle I, Burgert M, Wagner JC, Holzer H. Metabolic regulation of the trehalose content of vegetative yeast. Febs Letters. 291: 269-72. PMID 1834481 DOI: 10.1016/0014-5793(91)81299-N |
0.366 |
|
| 1991 |
Maier K, Hinze H, Holzer H. Inactivation of enzymes and an enzyme inhibitor by oxidative modification with chlorinated amines and metal-catalyzed oxidation systems. Biochimica Et Biophysica Acta. 1079: 238-41. PMID 1832966 DOI: 10.1016/0167-4838(91)90131-I |
0.338 |
|
| 1989 |
Manhart A, Holzer H. Substrate specificity of the phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae. Yeast (Chichester, England). 4: 227-32. PMID 2849261 DOI: 10.1002/Yea.320040308 |
0.408 |
|
| 1988 |
Plankert U, Purwin C, Holzer H. Characterization of yeast fructose-2,6-bisphosphate 6-phosphatase. Febs Letters. 239: 69-72. PMID 2846350 DOI: 10.1016/0014-5793(88)80547-7 |
0.407 |
|
| 1988 |
Manhart A, Kalisz H, Holzer H. Sensitivity of yeast glycolytic enzymes to chloroquine. Archives of Microbiology. 150: 309-312. PMID 2845878 DOI: 10.1007/Bf00407797 |
0.39 |
|
| 1987 |
Hinze H, Prakash D, Holzer H. Effect of ozone on ATP, cytosolic enzymes and permeability of Saccharomyces cerevisiae Archives of Microbiology. 147: 105-108. PMID 3296986 DOI: 10.1007/Bf00415269 |
0.44 |
|
| 1987 |
Schäfer W, Kalisz H, Holzer H. Evidence for non-vacuolar proteolytic catabolite inactivation of yeast fructose-1,6-bisphosphatase. Biochimica Et Biophysica Acta. 925: 150-5. PMID 3040110 DOI: 10.1016/0304-4165(87)90104-8 |
0.418 |
|
| 1987 |
Purwin C, Laux M, Holzer H. Fructofuranose 2-phosphate is the product of dephosphorylation of fructose 2,6-bisphosphate. European Journal of Biochemistry. 165: 543-5. PMID 3036508 DOI: 10.1111/J.1432-1033.1987.Tb11473.X |
0.358 |
|
| 1987 |
Kalisz H, Pohlig G, Holzer H. Inhibition of protein phosphorylation by chloroquine. Archives of Microbiology. 147: 235-239. PMID 3036036 DOI: 10.1007/Bf00463481 |
0.383 |
|
| 1987 |
Purwin C, Laux M, Holzer H. Fructose 2-phosphate, an intermediate of the dephosphorylation of fructose 2,6-bisphosphate with a purified yeast enzyme. European Journal of Biochemistry. 164: 27-30. PMID 2951255 DOI: 10.1111/J.1432-1033.1987.Tb10987.X |
0.459 |
|
| 1986 |
Hinze H, Holzer H. Analysis of the energy metabolism after incubation of Saccharomyces cerevisiae with sulfite or nitrite. Archives of Microbiology. 145: 27-31. PMID 3530169 DOI: 10.1007/Bf00413023 |
0.43 |
|
| 1986 |
Pohlig G, Schäfer W, von Herrath M, Holzer H. Modification of yeast fructose-1,6-bisphosphatase. Current Topics in Cellular Regulation. 27: 317-25. PMID 3004823 DOI: 10.1016/B978-0-12-152827-0.50034-7 |
0.468 |
|
| 1986 |
Prakash D, Hinze H, Holzer H. Synergistic effect of m-chloro-peroxybenzoic acid, sulfite and nitrite on the energy metabolism of Saccharomyces cerevisiae Fems Microbiology Letters. 34: 305-308. DOI: 10.1111/J.1574-6968.1986.Tb01426.X |
0.358 |
|
| 1985 |
Beck-Speier I, Hinze H, Holzer H. Effect of sulfite on the energy metabolism of mammalian tissues in correlation to sulfite oxidase activity. Biochimica Et Biophysica Acta. 841: 81-9. PMID 4016147 DOI: 10.1016/0304-4165(85)90276-4 |
0.304 |
|
| 1985 |
App H, Holzer H. Control of yeast neutral trehalase by distinct polyphosphates and ribonucleic acid European Food Research and Technology. 181: 276-282. PMID 3907189 DOI: 10.1007/Bf01043085 |
0.389 |
|
| 1985 |
Hinze H, Holzer H. Accumulation of nitrite and sulfite in yeast cells and synergistic depletion of the intracellular ATP content. Zeitschrift Fur Lebensmittel-Untersuchung Und -Forschung. 180: 117-20. PMID 3885619 DOI: 10.1007/Bf01042634 |
0.339 |
|
| 1985 |
Hinze H, Holzer H. Effect of sulfite or nitrite on the ATP content and the carbohydrate metabolism in yeast. Zeitschrift Fur Lebensmittel-Untersuchung Und -Forschung. 181: 87-91. PMID 2996253 DOI: 10.1007/Bf01042566 |
0.39 |
|
| 1985 |
Prakash D, Holzer H. Effects of m-Cl-peroxy benzoic acid on glycolysis in Saccharomyces cerevisiae Archives of Microbiology. 143: 220-224. PMID 2937383 DOI: 10.1007/Bf00411239 |
0.414 |
|
| 1985 |
Lenz A, Holzer H. Cleavage of thiamine pyrophosphate by sulfite in saccharomyces cerevisiae European Food Research and Technology. 181: 417-421. DOI: 10.1007/Bf01027410 |
0.383 |
|
| 1984 |
Lenz A, Holzer H. Effect of chloroquine on proteolytic processes and energy metabolism in yeast Archives of Microbiology. 137: 104-108. DOI: 10.1007/Bf00414448 |
0.357 |
|
| 1983 |
Pohlig G, Wingender-Drissen R, Noda T, Holzer H. Cyclic AMP and fructose-2,6-bisphosphate stimulated in vitro phosphorylation of yeast fructose-1,6-bisphosphatase. Biochemical and Biophysical Research Communications. 115: 317-24. PMID 6311207 DOI: 10.1016/0006-291X(83)91006-9 |
0.309 |
|
| 1982 |
Beck I, Müller M, Holzer H. Characterization of the proteolytic activity firmly attached to yeast phoshoenolpyruvate carboxykinase. Biochimica Et Biophysica Acta. 705: 163-6. PMID 7052135 DOI: 10.1016/0167-4838(82)90174-1 |
0.431 |
|
| 1982 |
Kominami E, Hoffschulte H, Leuschel L, Maier K, Holzer H. The substrate specificity of proteinase B from baker's yeast. Biochimica Et Biophysica Acta. 661: 136-41. PMID 7028121 DOI: 10.1016/0005-2744(81)90092-9 |
0.379 |
|
| 1982 |
Purwin C, Leidig F, Holzer H. Cyclic AMP-dependent phosphorylation of fructose-1,6-bisphosphatase in yeast. Biochemical and Biophysical Research Communications. 107: 1482-9. PMID 6291533 DOI: 10.1016/S0006-291X(82)80166-6 |
0.378 |
|
| 1982 |
Müller D, Holzer H. Regulation of fructose-1,6-bisphosphatase in yeast by phosphorylation/dephosphorylation. Biochemical and Biophysical Research Communications. 103: 926-33. PMID 6277324 DOI: 10.1016/0006-291X(81)90899-8 |
0.405 |
|
| 1981 |
Kominami E, Hoffschulte H, Holzer H. Purification and properties of proteinase B from yeast Biochimica Et Biophysica Acta. 661: 124-135. PMID 7028120 DOI: 10.1016/0005-2744(81)90091-7 |
0.413 |
|
| 1981 |
Tortora P, Birtel M, Lenz AG, Holzer H. Glucose-dependent metabolic interconversion of fructose-1, 6-bisphosphatase in yeast. Biochemical and Biophysical Research Communications. 100: 688-95. PMID 6268070 DOI: 10.1016/S0006-291X(81)80230-6 |
0.405 |
|
| 1980 |
Fischer EP, Holzer H. Interaction of proteinases and their inhibitors from yeast. Activation of carboxypeptidase Y. Biochimica Et Biophysica Acta. 615: 187-198. PMID 7000191 DOI: 10.1016/0005-2744(80)90022-4 |
0.415 |
|
| 1979 |
Barth R, Wolf DH, Holzer H. Studies on the carboxypeptidase Y-inhibitor complex of yeast. Biochimica Et Biophysica Acta. 527: 63-9. PMID 363166 DOI: 10.1016/0005-2744(78)90256-5 |
0.336 |
|
| 1979 |
Afting EG, Hinze H, Holzer H. A new inhibitor protein from rat uterus against yeast proteinase B. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 359: 999-1003. PMID 361536 DOI: 10.1515/Bchm2.1978.359.2.999 |
0.308 |
|
| 1979 |
Matern H, Weiser U, Holzer H. Isolation, characterization and localization of the proteinase B inhibitor IB3 from Saccharomyces carlsbergensis. European Journal of Biochemistry / Febs. 101: 325-32. PMID 118002 DOI: 10.1111/J.1432-1033.1979.Tb19724.X |
0.394 |
|
| 1979 |
Schimz K, Holzer H. Rapid decrease of ATP content in intact cells of Saccharomyces cerevisiae after incubation with low concentrations of sulfite. Archives of Microbiology. 121: 225-229. PMID 42368 DOI: 10.1007/Bf00425059 |
0.337 |
|
| 1979 |
Matern H, Barth R, Holzer H. Chemical and physical properties of the carboxypeptidase Y-inhibitor from Baker's yeast. Biochimica Et Biophysica Acta. 567: 503-10. PMID 36163 DOI: 10.1016/0005-2744(79)90136-0 |
0.346 |
|
| 1978 |
Holzer H, Bünning P, Meussdoerffer F. Characteristics and functions of proteinase A and its inhibitors in yeast. Advances in Experimental Medicine and Biology. 95: 271-89. PMID 22996 DOI: 10.1007/978-1-4757-0719-9_16 |
0.432 |
|
| 1977 |
Hansen RJ, Switzer RL, Hinze H, Holzer H. Effects of glucose and nitrogen source on the levels of proteinases, peptidases, and proteinase inhibitors in yeast Bba - General Subjects. 496: 103-114. PMID 319838 DOI: 10.1016/0304-4165(77)90119-2 |
0.331 |
|
| 1977 |
Afting EG, Lynen A, Hinze H, Holzer H. Effects of yeast proteinase A, proteinase B and carboxypeptidase Y on yeast phosphofructokinase. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 357: 1771-7. PMID 14069 DOI: 10.1515/Bchm2.1976.357.2.1771 |
0.42 |
|
| 1976 |
Jusić M, Hinze H, Holzer H. Inactivation of yeast enzymes by proteinase A and B and carboxypeptidase Y from yeast. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 357: 735-40. PMID 184028 DOI: 10.1515/Bchm2.1976.357.1.735 |
0.46 |
|
| 1976 |
Hansen RJ, Hinze H, Holzer H. Assay of phosphoenolpyruvate carboxykinase in crude yeast extracts. Analytical Biochemistry. 74: 576-84. PMID 9012 DOI: 10.1016/0003-2697(76)90240-2 |
0.352 |
|
| 1976 |
Holzer H. Chemistry and biology of macromolecular inhibitors from yeast acting on proteinases A and B, and carboxypeptidase Y. Advances in Enzyme Regulation. 13: 125-34. PMID 1974 DOI: 10.1016/0065-2571(75)90011-4 |
0.311 |
|
| 1976 |
Holzer H. Catabolite inactivation in yeast Trends in Biochemical Sciences. 1: 178-181. DOI: 10.1016/S0968-0004(76)80018-7 |
0.424 |
|
| 1975 |
Hasilik A, Müller H, Holzer H. Compartmentation of the tryptophan-synthase-proteolyzing system in Saccharomyces cerevisiae. European Journal of Biochemistry. 48: 117-7. PMID 4614972 DOI: 10.1111/J.1432-1033.1974.Tb03748.X |
0.439 |
|
| 1975 |
Matern H, Hoffmann M, Holzer H. Isolation and characterization of the carboxypeptidase Y inhibitor from yeast. Proceedings of the National Academy of Sciences of the United States of America. 71: 4874-8. PMID 4612529 DOI: 10.1073/Pnas.71.12.4874 |
0.38 |
|
| 1975 |
Matern H, Betz H, Holzer H. Compartmentation of inhibitors of proteinases A and B and carboxypeptidase Y in yeast. Biochemical and Biophysical Research Communications. 60: 1051-7. PMID 4611422 DOI: 10.1016/0006-291X(74)90419-7 |
0.521 |
|
| 1975 |
Holzer H. Possible mechanisms for a selective control of proteinase action. Advances in Enzyme Regulation. 12: 1-10. PMID 4462381 DOI: 10.1016/0065-2571(74)90004-1 |
0.423 |
|
| 1975 |
Hinze H, Betz H, Saheki T, Holzer H. Formation of a complex between yeast proteinases A and B. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 356: 1259-64. PMID 1100503 DOI: 10.1515/Bchm2.1975.356.2.1259 |
0.543 |
|
| 1975 |
Holzer H, Betz H, Ebner E. Intracellular proteinases in microorganisms. Current Topics in Cellular Regulation. 9: 103-56. PMID 1091413 DOI: 10.1016/B978-0-12-152809-6.50011-1 |
0.579 |
|
| 1975 |
Saheki T, Holzer H. Proteolytic activities in yeast. Biochimica Et Biophysica Acta. 384: 203-14. PMID 236769 DOI: 10.1016/0005-2744(75)90109-6 |
0.366 |
|
| 1974 |
Saheki T, Matsuda Y, Holzer H. Urification and characterization of macromolecular inhibitors of proteinase A from yeast. European Journal of Biochemistry. 47: 325-32. PMID 4607329 DOI: 10.1111/J.1432-1033.1974.Tb03697.X |
0.382 |
|
| 1974 |
Schött EH, Holzer H. Purification and some properties of tryptophan synthase inactivase II from yeast. European Journal of Biochemistry. 42: 61-6. PMID 4598105 DOI: 10.1111/J.1432-1033.1974.Tb03314.X |
0.399 |
|
| 1974 |
Saheki T, Holzer H. Comparisons of the tryptophan synthase inactivating enzymes with proteinases from yeast. European Journal of Biochemistry. 42: 621-6. PMID 4597849 DOI: 10.1111/J.1432-1033.1974.Tb03377.X |
0.411 |
|
| 1973 |
Holzer H, Katsunuma T, Schött EG, Ferguson AR, Hasilik A, Betz H. Studies on a tryptophan synthase inactivating system from yeast Advances in Enzyme Regulation. 11. PMID 4596223 DOI: 10.1016/0065-2571(73)90008-3 |
0.611 |
|
| 1973 |
Hasilik A, Holzer H. Participation of the tryptophan synthase inactivating system from yeast in the activation of chitin synthase. Biochemical and Biophysical Research Communications. 53: 552-9. PMID 4577587 DOI: 10.1016/0006-291X(73)90697-9 |
0.444 |
|
| 1973 |
Ferguson AR, Katsunuma T, Betz H, Holzer H. Purification and properties of an inhibitor of the tryptophan-synthase-inactivating enzymes in yeast European Journal of Biochemistry. 32: 444-450. PMID 4571064 DOI: 10.1111/J.1432-1033.1973.Tb02626.X |
0.593 |
|
| 1973 |
Holzer H, Wohlhueter R. (Glutamine synthetase) tyrosyl-O-adenylate: a new energy-rich phosphate bond. Advances in Enzyme Regulation. 10: 121-32. PMID 4143924 DOI: 10.1016/0065-2571(72)90009-X |
0.301 |
|
| 1972 |
Katsunuma T, Elsässer S, Holzer H. Purification and some properties of threonine dehydratase from yeast. European Journal of Biochemistry. 24: 83-7. PMID 5138648 DOI: 10.1111/J.1432-1033.1971.Tb19657.X |
0.341 |
|
| 1972 |
Katsunuma T, Schött E, Elsässer S, Holzer H. Purification and properties of tryptophan-synthase-inactivating enzymes from yeast. European Journal of Biochemistry. 27: 520-6. PMID 4559179 DOI: 10.1111/J.1432-1033.1972.Tb01868.X |
0.467 |
|
| 1972 |
Afting EG, Katsunuma T, Holzer H. Comparative studies on the inactivating enzymes for pyridoxal enzymes from yeast and rat. Biochemical and Biophysical Research Communications. 47: 103-10. PMID 4554810 DOI: 10.1016/S0006-291X(72)80016-0 |
0.427 |
|
| 1972 |
Schutt H, Holzer H. Biological function of the ammonia-induced inactivation of glutamine synthetase in Escherichia coli. European Journal of Biochemistry. 26: 68-72. PMID 4402918 DOI: 10.1111/J.1432-1033.1972.Tb01740.X |
0.347 |
|
| 1971 |
Ebner E, Wolf D, Gancedo C, Elsässer S, Holzer H. ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. European Journal of Biochemistry. 14: 535-44. PMID 4920894 DOI: 10.1111/J.1432-1033.1970.Tb00320.X |
0.676 |
|
| 1970 |
Ullrich J, Ostrovsky YM, Eyzaguirre J, Holzer H. Thiamine pyrophosphate-catalyzed enzymatic decarboxylation of -oxo acids. Vitamins and Hormones. 28: 365-98. PMID 4946807 DOI: 10.1016/S0083-6729(08)60903-6 |
0.353 |
|
| 1970 |
Atzpodien W, Gancedo JM, Hagmaier V, Holzer H. Desensitization of yeast phosphofructokinase to ATP-inhibition by a protein fraction from yeast. European Journal of Biochemistry. 12: 6-10. PMID 4313982 DOI: 10.1111/J.1432-1033.1970.Tb00814.X |
0.387 |
|
| 1970 |
Holzer H. Some aspects of regulation of metabolism by ATP. Advances in Enzyme Regulation. 8: 85-97. PMID 4248956 DOI: 10.1016/0065-2571(70)90010-5 |
0.439 |
|
| 1970 |
Deus B, Ullrich J, Holzer H. [45] Enzymatic preparation, isolation, and identification of 2-α-hydroxyalkylthiamine pyrophosphates Methods in Enzymology. 18: 259-266. DOI: 10.1016/0076-6879(71)18313-9 |
0.301 |
|
| 1970 |
Ebner E, Gancedo C, Holzer H. [131] ATP: Glutamine synthetase adenylyltransferase (Escherichia coli B) Methods in Enzymology. 17: 922-927. DOI: 10.1016/0076-6879(71)17306-5 |
0.678 |
|
| 1969 |
Deus B, Blum HE, Holzer H. Radiometric assay procedure for thiamine pyrophosphokinase activity. Analytical Biochemistry. 27: 492-501. PMID 5767204 DOI: 10.1016/0003-2697(69)90063-3 |
0.398 |
|
| 1969 |
Atzpodien W, Gancedo JM, Duntze W, Holzer H. Isoenzymes of malate dehydrogenase in Saccharomyces cerevisiae. European Journal of Biochemistry. 7: 58-62. PMID 5707713 DOI: 10.1111/J.1432-1033.1968.Tb19573.X |
0.354 |
|
| 1969 |
Duntze W, Neumann D, Gancedo JM, Atzpodien W, Holzer H. Studies on the regulation and localization of the glyoxylate cycle enzymes in Saccharomyces cerevisiae. European Journal of Biochemistry. 10: 83-9. PMID 5345986 DOI: 10.1111/J.1432-1033.1969.Tb00658.X |
0.439 |
|
| 1969 |
Heilmeyer L, Battig F, Holzer H. Characterization of a glutamine synthetase b activating (deadenylylating) enzyme system in Escherichia coli. European Journal of Biochemistry. 9: 259-62. PMID 4897098 DOI: 10.1111/J.1432-1033.1969.Tb00603.X |
0.441 |
|
| 1969 |
Holzer H, Mecke D, Wulff K, Liess K, Heilmeyer L. Metabolite-induced enzymatic inactivation of glutamine synthetase in E. coli. Advances in Enzyme Regulation. 5: 211-25. PMID 4880924 DOI: 10.1016/0065-2571(67)90017-9 |
0.467 |
|
| 1968 |
Liess K, Varricchio F, Mecke D, Holzer H. Vergleich verschiedener Modifikationen von Glutaminsynthetase aus Escherichia coli Febs Journal. 4: 193-200. PMID 4871904 DOI: 10.1111/J.1432-1033.1968.Tb00193.X |
0.379 |
|
| 1968 |
Gancedo C, Holzer H. Enzymatic inactivation of glutamine synthetase in Enterobacteriaceae. European Journal of Biochemistry. 4: 190-2. PMID 4871903 DOI: 10.1111/J.1432-1033.1968.Tb00192.X |
0.637 |
|
| 1967 |
Panten K, Bernhardt W, Holzer H. Studien zur oscillation der synthesegeschwindigkeit von nad-abhängiger glutamatdehydrogenase in Saccharomyces cerevisiae Biochimica Et Biophysica Acta. 139: 33-39. PMID 6033475 DOI: 10.1016/0005-2744(67)90110-6 |
0.394 |
|
| 1967 |
Duntze W, Atzpodien W, Holzer H. Glucose-dependent enzyme activities in different yeast species Archives of Microbiology. 58: 296-301. PMID 5628698 DOI: 10.1007/Bf00408811 |
0.441 |
|
| 1967 |
Mecke D, Wulff K, Liess K, Holzer H. Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli. Biochemical and Biophysical Research Communications. 24: 452-8. PMID 5338440 DOI: 10.1016/0006-291X(66)90182-3 |
0.443 |
|
| 1967 |
Heilmeyer L, Mecke D, Holzer H. Reaktivierung von Ammonium‐inaktivierter Glutaminsynthetase in Escherichia coli Febs Journal. 2: 399-402. PMID 4866004 DOI: 10.1111/J.1432-1033.1967.Tb00152.X |
0.407 |
|
| 1967 |
Wulff K, Mecke D, Holzer H. Mechanism of the enzymatic inactivation of glutamine synthetase from E. coli Biochemical and Biophysical Research Communications. 28: 740-745. PMID 4861255 DOI: 10.1016/0006-291X(67)90378-6 |
0.34 |
|
| 1967 |
Westphal H, Kröger H, Duntze W, Holzer H. Hemmung der enzymsynthese durch antirheumatika Biochemical Pharmacology. 16: 1463-1470. PMID 4860548 DOI: 10.1016/0006-2952(67)90122-0 |
0.319 |
|
| 1966 |
Bernhardt W, Zink M, Holzer H. NAD-Abhängige glutamatdehydrogenase aus reprimierter und dereprimierter Bäckerhefe Biochimica Et Biophysica Acta. 118: 549-555. DOI: 10.1016/S0926-6593(66)80096-6 |
0.417 |
|
| 1966 |
Witt I, Kronau R, Holzer H. Repression von alkoholdehydrogenase, malatdehydrogenase, isocitratlyase und malatsynthase in hefe durch glucose Biochimica Et Biophysica Acta. 118: 522-537. DOI: 10.1016/S0926-6593(66)80094-2 |
0.367 |
|
| 1966 |
Witt I, Kronau R, Holzer H. Isoenzyme der malatdehydrogenase und ihre regulation in Saccharomyces cerevisiae Biochimica Et Biophysica Acta. 128: 63-73. DOI: 10.1016/0926-6593(66)90142-1 |
0.42 |
|
| 1966 |
Mecke D, Holzer H. Repression und inaktivierung von glutaminsynthetase in Escherichia coli durch NH4 Biochimica Et Biophysica Acta. 122: 341-351. DOI: 10.1016/0926-6593(66)90074-9 |
0.388 |
|
| 1966 |
Mecke D, Wulff K, Holzer H. Metabolit-induzierte inaktivierung von glutaminsynthetase aus Escherichia coli im zellfreien system Biochimica Et Biophysica Acta. 128: 559-567. DOI: 10.1016/0926-6593(66)90016-6 |
0.44 |
|
| 1966 |
Grunicke H, Liersch M, Hinz M, Puschendorf B, Richter E, Holzer H. Die bedeutung des nikotinsäureamids für die synthese des nad in Ehrlich-Ascites-Tumorzellen Biochimica Et Biophysica Acta. 121: 228-240. DOI: 10.1016/0304-4165(66)90112-7 |
0.317 |
|
| 1965 |
Bernhardt W, Panten K, Holzer H. Gedämpftes oscillieren der synthesegeschwindigkeit von DPN-abhängiger glutamatdehydrogenase in hefezellen Biochimica Et Biophysica Acta. 99: 531-539. DOI: 10.1016/S0926-6593(65)80206-5 |
0.313 |
|
| 1964 |
Westphal H, Holzer H. Synthese von NAD-abhängiger glutamat-dehydrogenase in protoplasten von saccharomyces carlsbergensis Biochimica Et Biophysica Acta. 89: 42-46. DOI: 10.1016/0926-6569(64)90099-9 |
0.35 |
|
| 1964 |
Bernhardt W, Panten K, Holzer H. Damped Oscillation of the Enzyme Synthesis in Yeast Angewandte Chemie. 3: 803-804. DOI: 10.1002/Anie.196408032 |
0.384 |
|
| 1964 |
Holzer H, Boll M, Cennamo C. The Biochemistry of Yeast Threonine Deaminase Angewandte Chemie. 3: 101-107. DOI: 10.1002/Anie.196401011 |
0.472 |
|
| 1963 |
Schröter W, Holzer H. Zum wirkungsmechanismus der phosphoketolase: II. Umsatz von “thiaminpyrophosphat aktiviertem glycolaldehyd” Biochimica Et Biophysica Acta. 77: 474-481. PMID 14089423 DOI: 10.1016/0006-3002(63)90523-7 |
0.373 |
|
| 1963 |
Holzer H, Boll M, Cennamo C. Zur Biochemie der Threonin‐Desaminase aus Hefe Angewandte Chemie. 75: 894-900. DOI: 10.1002/Ange.19630751903 |
0.397 |
|
| 1962 |
Prochoroff NN, Kattermann R, Holzer H. Formation of sedoheptulose-7-phosphate from enzymatically obtained "active glycolic aldehyde" and ribose-5-phosphate with transketolase. Biochemical and Biophysical Research Communications. 9: 477-481. PMID 13986286 DOI: 10.1016/0006-291X(62)90038-4 |
0.337 |
|
| 1962 |
Holzer H, Schröter W. Zum wirkungsmechanismus der phosphoketolase I. Oxydation verschiedener substrate mit ferricyanid Biochimica Et Biophysica Acta. 65: 271-288. PMID 13961507 DOI: 10.1016/0006-3002(62)91046-6 |
0.361 |
|
| 1962 |
Goedde HW, Blume KG, Holzer H. Quantitative bestimmung sowie chemisches und enzymatisches verhalten von synthetischem DL-α-hydroxyäthyl-2-thiaminpyrophosphat Biochimica Et Biophysica Acta. 62: 1-10. PMID 13899451 DOI: 10.1016/0006-3002(62)90485-7 |
0.374 |
|
| 1961 |
Scriba PC, Schneider S, Holzer H. Mechanismus der enzymatischen freisetzung von acetaldehyd aud “Aktivem acetaldehyd” (α-hydroxyaethyl-2-thiaminpyrophosphat) Biochimica Et Biophysica Acta. 54: 115-120. PMID 13910053 DOI: 10.1016/0006-3002(61)90944-1 |
0.37 |
|
| 1961 |
Holzer H, Schneider S. Reinigung und charakterisierung einer TPN-abhängigen pyridoxol-dehydrogenase aus bierhefe Biochimica Et Biophysica Acta. 48: 71-76. PMID 13715611 DOI: 10.1016/0006-3002(61)90516-9 |
0.381 |
|
| 1961 |
Holzer H, Beuacamp K. Nachweis und charakterisierung von α-lactyl-thiaminpyrophosphat (“aktives pyruvat”) und α-hydroxyäthyl-thiaminpyrophosphat (“aktiver acetaldehyd”) als zwischenprodukte der decarboxylierung von pyruvat mit pyruvatdecarboxylase aus bierhefe Biochimica Et Biophysica Acta. 46: 225-243. PMID 13715607 DOI: 10.1016/0006-3002(61)90747-8 |
0.304 |
|
| 1961 |
Goedde HW, Inouye H, Holzer H. Überführung von “Aktivem acetaldehyd” (α-hydroxyyäthylthiaminpyrophosphat) in acetyl-coenzym a mit pyruvatoxydase Biochimica Et Biophysica Acta. 50: 41-44. PMID 13706227 DOI: 10.1016/0006-3002(61)91057-5 |
0.321 |
|
| 1960 |
Holzer H, Goedde HW. Bildung von erythrulose aus hydroxypyruvat durch hefeenzymen Biochimica Et Biophysica Acta. 40: 297-308. PMID 14402906 DOI: 10.1016/0006-3002(60)91354-8 |
0.405 |
|
| 1960 |
Scriba PC, Schneider S, Holzer H. Zur Wirkung von 2,5-Dimethoxy-äthoxy-3,6-bis-äthyleniminobenzochinon-1,4 (BAYER A 139) auf die Glykolyse von Ascites-Tumorzellen Zeitschrift FüR Krebsforschung. 63: 547-557. DOI: 10.1007/Bf00525121 |
0.318 |
|
| 1956 |
HOLZER H, LYNEN F, SCHULTZ G. [Determination of diphosphopyridine nucleotide/reduced diphosphopyridine nucleotide quotient in living yeast cells by analysis of constant alcohol and acetaldehyde concentrations]. Biochemische Zeitschrift. 328: 252-63. PMID 13373833 |
0.435 |
|
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