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Genetic regulatory mechanisms in the synthesis of proteins.
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The cistron concept proved useful to Jacob and Monod in experiments leading to the discovery of the lactose operon, the first effective model of how gene expression is controlled.
“This genetic concept of the gene proved immensely useful to a number of molecular biologists, in particular François Jacob and Jacques Monod, who used it abundantly in the experiments that led them to the discovery of the lactose operon, which offered the first effective model of how the expression of genes is controlled.”
From From Mendel to epigenetics: History of genetics (2016) · cites this paper as [15]
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- Adelberg, 1953, J. Biol. Chem., 205, 475, 10.1016/S0021-9258(19)77271-8 · DOI
- Ames, 1959, Proc. Nat. Acad. Sci., Wash., 45, 1453, 10.1073/pnas.45.10.1453 · DOI
- Ames, 1960, J. Gen. Microbiol., 22, 369, 10.1099/00221287-22-2-369 · DOI
- Benzer, 1953, Biochim. biophys. Acta, 11, 383, 10.1016/0006-3002(53)90057-2 · DOI
- Bertani, 1953, 18, 65
- Bertani, 1958, Advanc. Virus Bes., 5, 151, 10.1016/S0065-3527(08)60673-9 · DOI
- Brenner, 1961, Nature, 190, 576, 10.1038/190576a0 · DOI
- Bussard, 1960, C. R. Acad. Sci., Paris, 250, 4049
- Buttin, 1956, Diplôme Et. Sup., Paris
- Buttin, 1961, C. R. Acad. Sci., Paris
- Cohen, 1959, C. R. Acad. Sci., Paris, 248, 3490
- Cohen, 1957, Bact. Rev., 21, 169, 10.1128/br.21.3.169-194.1957 · DOI · Paper page
- Cohen, 1949, Bact. Rev., 13, 1, 10.1128/br.13.1.1-24.1949 · DOI
- Cohen-Bazire, 1953, Ann. Inst. Pasteur, 84, 1
- Cohn, 1957, Bact. Rev., 21, 140, 10.1128/br.21.3.140-168.1957 · DOI
- Cohn, 1953, G. R. Acad. Sci., Paris, 236, 746
- Cohn, 1959, Bact., 78, 624, 10.1128/JB.78.5.624-635.1959 · DOI
- Cohn, 1952, J. Immunol., 69, 471, 10.4049/jimmunol.69.5.471 · DOI
- Davern, 1960, J. Mol. Biol., 2, 153, 10.1016/S0022-2836(60)80017-4 · DOI
- Demerec, 1956, 21, 113
- Dienert, 1900, Ann. Inst. Pasteur, 14, 139
- Echols, 1961, J. Mol. Biol.
- Flaks, 1959, J. Biol. Chem., 234, 1501, 10.1016/S0021-9258(18)70038-0 · DOI
- Gale, 1943, Bact. Rev., 7, 139, 10.1128/br.7.3.139-173.1943 · DOI
- Giles, 1958, 1, 261
- Gorini, 1957, Biochim. biophys. Acta, 25, 208, 10.1016/0006-3002(57)90450-X · DOI
- Gros, 1961, Nature, 190, 581, 10.1038/190581a0 · DOI
- Halvorson, 1960, Advanc. Enzymol
- Hartman, 1960, J. Gen. Microbiol., 22, 323, 10.1099/00221287-22-2-323 · DOI
- Herzenberg, 1959, Biochim. biophys. Acta, 31, 525, 10.1016/0006-3002(59)90029-0 · DOI
- Hogness, 1955, Biochim. biophys. Acta, 16, 99, 10.1016/0006-3002(55)90188-8 · DOI
- Jacob, 1960, Harvey Lectures, 1958–1959, series, 54, 1
- Jacob, 1959, C.R. Acad. Sci., Paris, 249, 189
- Jacob, 1959, C.R. Acad. Sci., Paris, 248, 3219
- Jacob, 1957, Ann. Inst. Pasteur, 93, 724
- Jacob, 1959, C.R. Acad. Sci., Paris, 249, 1282
- Jacob, 1960, C.R. Acad. Sci., Paris, 250, 1727
- Jacob, 1953, 18, 101
- Jacob, 1956, Ann. Inst. Pasteur, 91, 486
- Kaiser, 1957, Virology, 3, 42, 10.1016/0042-6822(57)90022-3 · DOI
- Kaiser, 1957, Virology, 4, 509, 10.1016/0042-6822(57)90083-1 · DOI
- Kalckar, 1959, Proc. Nat. Acad. Sci., Wash., 45, 1776, 10.1073/pnas.45.12.1776 · DOI
- Karstrom, 1938, Ergebn. Enzymforsch., 7, 350
- Képès, 1960, Biochim. biophys. Acta, 40, 70, 10.1016/0006-3002(60)91316-0 · DOI
- Kogut, 1956, Biochem. J., 62, 391, 10.1042/bj0620391 · DOI
- Kornberg, 1959, Proc. Nat. Acad. Sci., Wash., 45, 772, 10.1073/pnas.45.6.772 · DOI
- Kruh, 1961, Biochim. biophys. Acta
- Lamfroin, 1961, J. Mol. Biol., 3, 241, 10.1016/S0022-2836(61)80064-8 · DOI
- Luria, 1950, J. Bact., 59, 551, 10.1128/JB.59.4.551-560.1950 · DOI
- Lwoff, 1953, Bact. Rev., 17, 269, 10.1128/br.17.4.269-337.1953 · DOI
- Lwoff, 1950, Ann. Inst. Pasteur, 79, 815
- Monod, 1958, Rec. Trav. Chim. des Pays-Bas, 77, 569, 10.1002/recl.19580770607 · DOI
- Monod, 1959, Angew. Chem., 71, 685, 10.1002/ange.19590712202 · DOI
- Monod, 1946, Ann. Inst. Pasteur, 72, 868
- Monod, 1953, C.R. Acad. Sci., Paris, 236, 530
- Monod, 1952, Advanc. Enzymol., 13, 67
- Monod, 1952, Biochim. biophys. Acta, 9, 648, 10.1016/0006-3002(52)90227-8 · DOI
- Monod, 1947, Ann. Inst. Pasteur, 73, 937
- Naono, 1960, C.R. Acad. Sci., Paris, 250, 3527
- Naono, 1960, C.R. Acad. Sci., Paris, 250, 3889
- Neidhardt, 1956, Nature, 178, 801, 10.1038/178801b0 · DOI
- Neidhardt, 1956, Biochim. biophys. Acta, 21, 324, 10.1016/0006-3002(56)90016-6 · DOI
- Novick, 1955, Ann. Rev. Microbiol., 9, 97, 10.1146/annurev.mi.09.100155.000525 · DOI
- Pardee, 1957, J. Bact., 73, 376, 10.1128/JB.73.3.376-385.1957 · DOI
- Pardee, 1959, J. Mol. Biol., 1, 165, 10.1016/S0022-2836(59)80045-0 · DOI
- Pardee, 1959, Biochim. biophys. Acta, 36, 545, 10.1016/0006-3002(59)90202-1 · DOI
- Perrin, 1959, C.R. Acad. Sci., Paris, 249, 778
- Perrin, 1960, C.R. Acad. Sci., Paris, 250, 155
- Pollock, 1950, Brit. J. Exp. Pathol., 4, 739
- Pollock, 1951, Brit. J. Exp. Pathol., 5, 387
- Rickenberg, 1956, Ann. Inst. Pasteur, 91, 829
- Riley, 1960, J. Mol. Biol., 2, 216, 10.1016/S0022-2836(60)80039-3 · DOI
- Rotman, 1954, J. Bact., 68, 419, 10.1002/path.1700680215 · DOI
- Siminovitch, 1952, Ann. Inst. Pasteur, 83, 745
- Stanier, 1951, Ann. Rev. Microbiol., 5, 35, 10.1146/annurev.mi.05.100151.000343 · DOI
- Szilard, 1960, Proc. Nat. Acad. Sci., Wash., 46, 277, 10.1073/pnas.46.3.277 · DOI
- Torriani, 1960, Biochim. biophys. Acta, 38, 460, 10.1016/0006-3002(60)91281-6 · DOI
- Umbarger, 1956, Science, 123, 848, 10.1126/science.123.3202.848 · DOI
- Vogel, 1957, Proc. Nat. Acad. Sci., Wash., 43, 491, 10.1073/pnas.43.6.491 · DOI
- Went, 1901, J. Wiss. Bot., 36, 611
- Wijesundera, 1953, Biochem. J., 55, viii
- Yanofsky, 1960, Bact. Rev., 24, 221, 10.1128/br.24.2.221-245.1960 · DOI
- Yanofsky, 1959, Virology, 8, 425, 10.1016/0042-6822(59)90046-7 · DOI
- Yarmolinsky, 1960, Proc. Nat. Acad. Sci., Wash
- Yates, 1956, J. Biol. Chem., 221, 757, 10.1016/S0021-9258(18)65188-9 · DOI
- Yates, 1957, J. Biol. Chem., 227, 677, 10.1016/S0021-9258(18)70748-5 · DOI
- Yčas, 1960, Proc. Nat. Acad. Sci., Wash., 46, 804, 10.1073/pnas.46.6.804 · DOI
- Zabin, 1959, Biochem. Biophys. Res. Comm., 1, 289, 10.1016/0006-291X(59)90040-3 · DOI
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Metadata
- Authors
- Jacob, F., & Monod, J.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1961-06
- Volume
- 3
- Issue
- 3
- Pages
- 318-356
- ISSN
- 0022-2836
- Cited by
- 5,300
- References
- 0
- Language
- en
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