| Year |
Citation |
Score |
| 2011 |
Bellinzoni M, Bastard K, Perret A, Zaparucha A, Perchat N, Vergne C, Wagner T, de Melo-Minardi RC, Artiguenave F, Cohen GN, Weissenbach J, Salanoubat M, Alzari PM. 3-Keto-5-aminohexanoate cleavage enzyme: a common fold for an uncommon Claisen-type condensation. The Journal of Biological Chemistry. 286: 27399-405. PMID 21632536 DOI: 10.1074/Jbc.M111.253260 |
0.384 |
|
| 2010 |
Fonknechten N, Chaussonnerie S, Tricot S, Lajus A, Andreesen JR, Perchat N, Pelletier E, Gouyvenoux M, Barbe V, Salanoubat M, Le Paslier D, Weissenbach J, Cohen GN, Kreimeyer A. Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence. Bmc Genomics. 11: 555. PMID 20937090 DOI: 10.1186/1471-2164-11-555 |
0.332 |
|
| 2005 |
Cohen GN. Looking back. Annual Review of Microbiology. 59: 1-17. PMID 16153161 DOI: 10.1146/annurev.micro.59.030804.121329 |
0.324 |
|
| 2004 |
Barbe V, Vallenet D, Fonknechten N, Kreimeyer A, Oztas S, Labarre L, Cruveiller S, Robert C, Duprat S, Wincker P, Ornston LN, Weissenbach J, Marlière P, Cohen GN, Médigue C. Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium. Nucleic Acids Research. 32: 5766-79. PMID 15514110 DOI: 10.1093/Nar/Gkh910 |
0.325 |
|
| 2004 |
COHEN GN, COHEN-BAZIRE G. Reduction by molecular hydrogen of acetoacetate to butyrate by butyric acid bacteria. Nature. 166: 1077-8. PMID 14796701 DOI: 10.1038/1661077B0 |
0.31 |
|
| 2003 |
TRUDINGER PA, COHEN GN. The effect of 4-methyltryptophan on growth and enzyme systems of Escherichia coli. The Biochemical Journal. 62: 488-91. PMID 13304003 DOI: 10.1042/Bj0620488 |
0.335 |
|
| 2003 |
Cohen GN, Barbe V, Flament D, Galperin M, Heilig R, Lecompte O, Poch O, Prieur D, Quérellou J, Ripp R, Thierry JC, Van der Oost J, Weissenbach J, Zivanovic Y, Forterre P. An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi. Molecular Microbiology. 47: 1495-512. PMID 12622808 DOI: 10.1046/J.1365-2958.2003.03381.X |
0.309 |
|
| 2000 |
MUNIER R, COHEN GN. [Incorporation of structural analogues of amino acids into bacterial proteins during their synthesis in vivo]. Biochimica Et Biophysica Acta. 31: 378-91. PMID 13628664 DOI: 10.1016/0006-3002(59)90011-3 |
0.366 |
|
| 2000 |
COHEN GN, MUNIER R. [Effects of structural analogues of amino acids on growth, protein synthesis, and enzyme synthesis in Escherichia coli]. Biochimica Et Biophysica Acta. 31: 347-56. PMID 13628660 DOI: 10.1016/0006-3002(59)90007-1 |
0.372 |
|
| 1998 |
PATTE JC, LOVINY T, COHEN GN. [Repression of meso-alpha, epsilon-diaminopimelic acid decarboxylase by L-lysine in Escherichia coli]. Biochimica Et Biophysica Acta. 58: 359-60. PMID 14484389 DOI: 10.1016/0006-3002(62)91024-7 |
0.309 |
|
| 1994 |
Cohen GN. Studies on beta-galactosidase and their impact on molecular biology: a personal view. Structure (London, England : 1993). 2: 569-70. PMID 7922034 DOI: 10.1016/S0969-2126(00)00057-5 |
0.399 |
|
| 1989 |
Iapalucci S, Lopez R, Rey O, Lopez N, Franze-Fernandez MT, Cohen GN, Lucero M, Ochoa A, Zakin MM. Tacaribe virus L gene encodes a protein of 2210 amino acid residues. Virology. 170: 40-7. PMID 2718387 DOI: 10.1016/0042-6822(89)90349-8 |
0.322 |
|
| 1989 |
Phillips SE, Manfield I, Parsons I, Davidson BE, Rafferty JB, Somers WS, Margarita D, Cohen GN, Saint-Girons I, Stockley PG. Cooperative tandem binding of met repressor of Escherichia coli. Nature. 341: 711-5. PMID 2677754 DOI: 10.1038/341711A0 |
0.331 |
|
| 1988 |
Parsot C, Cohen GN. Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II. The Journal of Biological Chemistry. 263: 14654-60. PMID 3139660 |
0.33 |
|
| 1988 |
Parsot C, Boyen A, Cohen GN, Glansdorff N. Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes. Gene. 68: 275-83. PMID 2851495 DOI: 10.1016/0378-1119(88)90030-3 |
0.389 |
|
| 1987 |
Yang PW, Mantsch HH, Arrondo JL, Saint-Girons I, Guillou Y, Cohen GN, Bârzu O. Fourier transform infrared investigation of the Escherichia coli methionine aporepressor. Biochemistry. 26: 2706-11. PMID 3300769 DOI: 10.1021/Bi00384A009 |
0.304 |
|
| 1986 |
Belfaiza J, Parsot C, Martel A, de la Tour CB, Margarita D, Cohen GN, Saint-Girons I. Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Proceedings of the National Academy of Sciences of the United States of America. 83: 867-71. PMID 3513164 DOI: 10.1073/Pnas.83.4.867 |
0.384 |
|
| 1986 |
Cassan M, Parsot C, Cohen GN, Patte JC. Nucleotide sequence of lysC gene encoding the lysine-sensitive aspartokinase III of Escherichia coli K12. Evolutionary pathway leading to three isofunctional enzymes. The Journal of Biological Chemistry. 261: 1052-7. PMID 3003049 |
0.336 |
|
| 1985 |
Shoeman R, Redfield B, Coleman T, Brot N, Weissbach H, Greene RC, Smith AA, Saint-Girons I, Zakin MM, Cohen GN. Regulation of the methionine regulon in Escherichia coli. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 3: 210-3. PMID 3916153 DOI: 10.1002/Bies.950030506 |
0.315 |
|
| 1985 |
Cohen GN, Véron M, Zakin MM. Recent biochemical and genetic studies on the amino acid biosynthetic pathway of the aspartate family in Escherichia coli. Current Topics in Cellular Regulation. 26: 445-54. PMID 3907996 DOI: 10.1016/B978-0-12-152826-3.50042-5 |
0.309 |
|
| 1985 |
Veron M, Guillou Y, Fazel A, Cohen GN. Reversible dissociation of aspartokinase I/homoserine dehydrogenase I from Escherichia coli K 12. The active species is the tetramer. European Journal of Biochemistry / Febs. 151: 521-4. PMID 3896789 DOI: 10.1111/J.1432-1033.1985.Tb09133.X |
0.408 |
|
| 1985 |
Cohen GN. Aspartate kinases I, II, and III from Escherichia coli. Methods in Enzymology. 113: 596-9. PMID 3003511 DOI: 10.1016/S0076-6879(85)13079-X |
0.387 |
|
| 1985 |
Veron M, Guillou Y, Cohen GN. Isolation of the aspartokinase domain of bifunctional aspartokinase I-homoserine dehydrogenase I from E.coli K12. Febs Letters. 181: 381-4. PMID 2982665 DOI: 10.1016/0014-5793(85)80297-0 |
0.43 |
|
| 1985 |
Cohen GN. Aspartate-semialdehyde dehydrogenase from Escherichia coli. Methods in Enzymology. 113: 600-2. PMID 2868399 DOI: 10.1016/S0076-6879(85)13080-6 |
0.395 |
|
| 1984 |
Belfaiza J, Fazel A, Müller K, Cohen GN. E. coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure. Biochemical and Biophysical Research Communications. 123: 16-20. PMID 6383377 DOI: 10.1016/0006-291X(84)90373-5 |
0.313 |
|
| 1984 |
Ferrara P, Duchange N, Zakin MM, Cohen GN. Internal homologies in the two aspartokinase-homoserine dehydrogenases of Escherichia coli K-12. Proceedings of the National Academy of Sciences of the United States of America. 81: 3019-23. PMID 6374650 DOI: 10.1073/Pnas.81.10.3019 |
0.374 |
|
| 1983 |
Saint-girons I, Duchange N, Zakin MM, Park I, Margarita D, Ferrara P, Cohen GN. Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylene tetrahydrofolate reductase and of its control region Nucleic Acids Research. 11: 6723-6732. PMID 6356036 DOI: 10.1093/Nar/11.19.6723 |
0.358 |
|
| 1983 |
Fazel A, Müller K, Le Bras G, Garel JR, Véron M, Cohen GN. A triglobular model for the polypeptide chain of aspartokinase I-homoserine dehydrogenase I of Escherichia coli. Biochemistry. 22: 158-65. PMID 6338915 DOI: 10.1021/Bi00270A023 |
0.397 |
|
| 1983 |
Parsot C, Cossart P, Saint-girons I, Cohen GN. Nucleotide sequence of thrC and of the transcription tennination region of the threonine operon in Escherichia coli K12 Nucleic Acids Research. 11: 7331-7345. PMID 6316258 DOI: 10.1093/Nar/11.21.7331 |
0.395 |
|
| 1982 |
Zakin MM, Greene RC, Dautry-Varsat A, Duchange N, Ferrara P, Py MC, Margarita D, Cohen GN. Construction and physical mapping of plasmids containing the metJBLF gene cluster of E. coli K12 Mgg Molecular & General Genetics. 187: 101-106. PMID 6219268 DOI: 10.1007/Bf00384390 |
0.316 |
|
| 1981 |
Cohen GN. Multifunctional enzymes involved in the synthesis of threonine and methionine in E. coli structural and evolutionary aspects Biochemical Society Transactions. 9: 45P. DOI: 10.1042/Bst009045P |
0.381 |
|
| 1980 |
Zakin MM, Hirth C, Garel JR, Cohen GN. Detection of the homology among proteins by immunochemical cross-reactivity between denatured antigens. Application to the glyceraldehyde 3-phosphate dehydrogenase from different species Molecular Immunology. 17: 1373-1379. PMID 6162095 DOI: 10.1016/0161-5890(80)90006-1 |
0.396 |
|
| 1979 |
Cossart P, Katinka M, Yaniv M, Girons IS, Cohen GN. Construction and expression of a hybrid plasmid containing the Escherichia coli thrA and thrB genes Mgg Molecular & General Genetics. 175: 39-44. PMID 390305 DOI: 10.1007/Bf00267853 |
0.359 |
|
| 1979 |
Sibilli L, Le Bras G, Cossart P, Chalvignac MA, Le Bras G, Briley PA, Cohen GN. The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I : sequence of cyanogen bromide peptide CB 3. Biochimie. 61: 733-9. PMID 387092 DOI: 10.1016/S0300-9084(79)80174-1 |
0.334 |
|
| 1979 |
Zakin MM, Garel JR, Dautry-Varsat A, Cohen GN, Boulot G. Detection of the homology among proteins by immunochemical cross-reactivity between denatured antigens. Application to the threonine and methionine regulated aspartokinases-homoserine dehydrogenases from Escherichia coli K 12. Biochemistry. 17: 4318-23. PMID 361077 DOI: 10.1021/Bi00613A032 |
0.402 |
|
| 1979 |
Dautry-Varsat A, Cohen GN, Stadtman ER. Some properties of Escherichia coli glutamine synthetase after limited proteolysis by subtilisin. The Journal of Biological Chemistry. 254: 3124-8. PMID 34613 |
0.523 |
|
| 1978 |
Cossart-Gheerbrant P, Sibilli-Weill L, Briley PA, Chalvignac MA, Le Bras G, Cohen GN. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I-Isolation and characterisation of the peptides produced by cyanogen bromide. Biochimica Et Biophysica Acta. 535: 206-15. PMID 354697 DOI: 10.1016/0005-2795(78)90086-7 |
0.349 |
|
| 1977 |
Sibilli L, Cossart P, Chalvignac MA, Briley PA, Costrejean JM, Le Bras G, Cohen GN. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Distribution of the methioninyl residues and of the cysteinyl and tryptophanyl tryptic peptides. Biochimie. 59: 943-6. PMID 343821 DOI: 10.1016/S0300-9084(78)80712-3 |
0.325 |
|
| 1977 |
Dautry Varsat A, Sibilli Weill L, Cohen GN. Subunit structure of the methionine repressible aspartokinase II - homoserine dehydrogenase II from Escherichia coli K12 European Journal of Biochemistry. 76: 1-6. PMID 328280 DOI: 10.1111/J.1432-1033.1977.Tb11563.X |
0.379 |
|
| 1977 |
Cohen GN, Saint-Girons I, Truffa-Bachi P. The evolution of biosynthetic pathways Trends in Biochemical Sciences. 2: 97-99. DOI: 10.1016/0968-0004(77)90170-0 |
0.394 |
|
| 1976 |
Burr B, Walker J, Truffa Bachi P, Cohen GN. Homoserine kinase from Escherichia coli K12 European Journal of Biochemistry. 62: 519-526. PMID 177283 DOI: 10.1111/J.1432-1033.1976.Tb10186.X |
0.42 |
|
| 1975 |
Hirth CG, Veron M, Villar Palasi C, Hurion N, Cohen GN. The threonine sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Specific inactivation of the homoserine dehydrogenase activity by the affinity label, 2 amino 4 oxo 5 chloropentanoic acid European Journal of Biochemistry. 50: 425-430. PMID 236185 DOI: 10.1111/J.1432-1033.1975.Tb09819.X |
0.43 |
|
| 1975 |
Truffa-Bachi P, Guiso N, Cohen GN, Theze J, Burr B. Evolution of biosynthetic pathways: immunological approach Proceedings of the National Academy of Sciences of the United States of America. 72: 1268-1271. PMID 48255 DOI: 10.1073/Pnas.72.4.1268 |
0.331 |
|
| 1975 |
Costrejean JM, Guiso N, Cowie DB, Cohen GN, Truffa-Bachi P. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Distribution and accessibility to antibodies of some epitopes of the bifunctional enzyme. European Journal of Biochemistry / Febs. 50: 431-5. PMID 47808 DOI: 10.1111/J.1432-1033.1975.Tb09820.X |
0.386 |
|
| 1974 |
Truffa-Bachi P, Costrejean JM, Py MC, Cohen GN. Preliminary analysis of the effects of ATP-Mg on Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I, at low potassium concentration Biochimie. 56: 215-219. PMID 4367416 DOI: 10.1016/S0300-9084(74)80380-9 |
0.356 |
|
| 1974 |
Theze J, Margarita D, Cohen GN, Borne F, Patte JC. Mapping of the structural genes of the three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K 12 Journal of Bacteriology. 117: 133-143. PMID 4148765 DOI: 10.1128/Jb.117.1.133-143.1974 |
0.314 |
|
| 1973 |
Cowie DB, Truffa-Bachi P, Costrejean JM, Py MC, Cohen GN. A preliminary immunochemical study of E. coli aspartokinase I-homoserine dehydrogenase I. Biochemical and Biophysical Research Communications. 53: 188-93. PMID 4354927 DOI: 10.1016/0006-291X(73)91418-6 |
0.398 |
|
| 1973 |
Veron M, Saari JC, Villar Palasi C, Cohen GN. The threonine sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Intra and intersubunit interactions between the catalytic regions of the bifunctional enzyme European Journal of Biochemistry. 38: 325-335. PMID 4149354 DOI: 10.1111/J.1432-1033.1973.Tb03065.X |
0.424 |
|
| 1973 |
BURR B, COSSART P, FRANÇOISE F, GUISO N, JOËL J, SAARI JC, SIBILLI L, THEZE J, TRUFFA-BACHI P, VERON M, COHEN GN. Regulation of Threonine Biosynthesis in Escherichia coli: Biochemical Aspects Biochemical Society Transactions. 1: 623-623. DOI: 10.1042/Bst0010623 |
0.366 |
|
| 1972 |
Robert-Gero M, Le Borgne L, Cohen GN. Concerted feedback inhibition of the aspartokinase of Rhodospirillum tenue by threonine and methionine: a novel pattern Journal of Bacteriology. 112: 251-258. PMID 5079065 DOI: 10.1128/Jb.112.1.251-258.1972 |
0.308 |
|
| 1972 |
Véron M, Falcoz-Kelly F, Cohen GN. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain European Journal of Biochemistry. 28: 520-527. PMID 4562990 DOI: 10.1111/J.1432-1033.1972.Tb01939.X |
0.459 |
|
| 1972 |
Falcoz-Kelly F, Janin J, Saari JC, Véron M, Truffa-Bachi P, Cohen GN. Revised structure of aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12. Evidence for four identical subunits. European Journal of Biochemistry / Febs. 28: 507-19. PMID 4562989 DOI: 10.1111/J.1432-1033.1972.Tb01938.X |
0.595 |
|
| 1970 |
Robert-Gero M, Poiret M, Cohen GN. Homoserine dehydrogenase of Pseudomonas putida properties and regulation Bba - Enzymology. 206: 31-37. PMID 5441405 DOI: 10.1016/0005-2744(70)90078-1 |
0.328 |
|
| 1970 |
Robert-Gero M, Poiret M, Cohen GN. The aspartate kinase of Pseudomonas putida regulation of synthesis and activity Bba - Enzymology. 206: 17-30. PMID 5441401 DOI: 10.1016/0005-2744(70)90077-X |
0.38 |
|
| 1970 |
Hegeman GD, Cohen GN, Morgan R. [93] Aspartic semialdehyde dehydrogenase (Escherichia coli K12) Methods in Enzymology. 17: 708-713. DOI: 10.1016/0076-6879(71)17268-0 |
0.383 |
|
| 1970 |
Falcoz-Kelly F, Cohen GN. [91b] Aspartokinase II and homoserine dehydrogenase II (Escherichia coli K12) Methods in Enzymology. 17: 699-702. DOI: 10.1016/0076-6879(71)17266-7 |
0.381 |
|
| 1970 |
Truffa-Bachi P, Cohen GN. [91a] Aspartokinase I and homoserine dehydrogenase I (Escherichia coli K12) Methods in Enzymology. 17: 694-699. DOI: 10.1016/0076-6879(71)17265-5 |
0.41 |
|
| 1969 |
Kaminski M, Falcoz-Kelly F, Truffa-Bachi P, Patte JC, Cohen GN. The antigenic independence of the three aspartokinases of Escherichia coli K 12 European Journal of Biochemistry. 11: 278-282. PMID 4982820 DOI: 10.1111/J.1432-1033.1969.Tb00770.X |
0.386 |
|
| 1969 |
Janin J, Cohen GN. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. A study of the allosteric equilibrium. European Journal of Biochemistry / Febs. 11: 520-9. PMID 4904702 DOI: 10.1111/J.1432-1033.1969.Tb00804.X |
0.586 |
|
| 1969 |
Truffa-Bachi P, Van Rapenbusch R, Gros C, Cohen GN, Janin J. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Subunit structure of the protein catalyzing the two activities. European Journal of Biochemistry / Febs. 7: 401-7. PMID 4893089 |
0.571 |
|
| 1969 |
Falcoz-Kelly F, van Rapenbusch R, Cohen GN. The methionine-repressible homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Preparation of the homogeneous protein catalyzing the two activities. Molecular weight of the native enzyme and of its subunits European Journal of Biochemistry. 8: 146-152. PMID 4889171 DOI: 10.1111/J.1432-1033.1969.Tb00507.X |
0.428 |
|
| 1969 |
Janin J, van Rapenbusch R, Truffa-Bachi P, Cohen GN. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Binding of threonine and of pyridine nucleotides: stoichiometry and optical effects. European Journal of Biochemistry / Febs. 8: 128-38. PMID 4388664 |
0.521 |
|
| 1968 |
Truffa-Bachi P, Van Rapenbusch R, Janin J, Gros C, Cohen GN. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. 4. Isolation, molecular weight, amino acid analysis and behaviour of the sulfhydryl groups of the protein catalyzing the two activities. European Journal of Biochemistry / Febs. 5: 73-80. PMID 4873312 DOI: 10.1111/J.1432-1033.1968.Tb00339.X |
0.612 |
|
| 1968 |
Richaud F, Cohen GN. Selection of Escherichia coli mutants devoid of one or of both the activities carried by a multifunctional protein Biochemical and Biophysical Research Communications. 30: 45-49. PMID 4866294 DOI: 10.1016/0006-291X(68)90710-9 |
0.381 |
|
| 1967 |
Janin J, Truffa-Bachi P, Cohen GN. Subunits of the complex protein carrying the threonine-sensitive aspartokinase activity in a mutant of Escherichia coli K 12. Biochemical and Biophysical Research Communications. 26: 429-34. PMID 5340504 DOI: 10.1016/0006-291X(67)90564-5 |
0.591 |
|
| 1966 |
Truffa-Bachi P, Bras GL, Cohen GN. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli Biochimica Et Biophysica Acta. 128: 440-449. DOI: 10.1016/0926-6593(66)90004-X |
0.404 |
|
| 1966 |
Patte JC, Truffa-Bachi P, Cohen GN. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli. I. Evidence that the two activities are carried by a single protein Bba - Enzymology Andbiological Oxidation. 128: 426-439. DOI: 10.1016/0926-6593(66)90003-8 |
0.428 |
|
| 1965 |
Cohen GN, Patte JC, Truffa-Bachi P. Parallel modifications caused by mutations in two enzymes concerned with the biosynthesis of threonine in Escherichia coli Biochemical and Biophysical Research Communications. 19: 546-550. PMID 14339005 DOI: 10.1016/0006-291X(65)90160-9 |
0.352 |
|
| 1965 |
Patte J, Loviny T, Cohen GN. Effets inhibiteurs cooperatifs de la L-lysine avec d’autres amino acides sur une aspartokinase de Escherichia coli Biochimica Et Biophysica Acta (Bba) - Enzymology and Biological Oxidation. 99: 523-530. DOI: 10.1016/S0926-6593(65)80205-3 |
0.319 |
|
| 1961 |
STADTMAN ER, COHEN GN, LEBRAS G. Feedback inhibition and repression of aspartokinase activity in Escherichia coli. Annals of the New York Academy of Sciences. 94: 952-9. PMID 13916055 |
0.486 |
|
| 1961 |
STADTMAN ER, COHEN GN, LE BRAS G, de ROBICHON-SZULMAJSTER. Selective feedback inhibition and repression of two aspartokinases in the metabolism of Escherichia coli. Cold Spring Harbor Symposia On Quantitative Biology. 26: 319-21. PMID 13916054 |
0.437 |
|
| 1960 |
COHEN GN, GROS F. Protein biosynthesis Annual Review of Biochemistry. 29: 525-546. PMID 13810951 DOI: 10.1146/annurev.bi.29.070160.002521 |
0.438 |
|
| 1957 |
COWIE DB, COHEN GN. Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur. Biochimica Et Biophysica Acta. 26: 252-61. PMID 13499359 DOI: 10.1016/0006-3002(57)90003-3 |
0.385 |
|
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