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212 related items for PubMed ID: 4401168
1. Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 . Subunit molecular weight and nicotinamide-adenine dinucleotide phosphate binding. Clark RB, Ogilvie JW. Biochemistry; 1972 Mar 28; 11(7):1278-82. PubMed ID: 4401168 [No Abstract] [Full Text] [Related]
3. 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. Véron M, Falcoz-Kelly F, Cohen GN. Eur J Biochem; 1972 Aug 04; 28(4):520-7. PubMed ID: 4562990 [No Abstract] [Full Text] [Related]
5. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Binding of threonine and of pyridine nucleotides: stoichiometry and optical effects. Janin J, van Rapenbusch R, Truffa-Bachi P, Cohen GN. Eur J Biochem; 1969 Mar 04; 8(1):128-38. PubMed ID: 4388664 [No Abstract] [Full Text] [Related]
6. Revised structure of aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12. Evidence for four identical subunits. Falcoz-Kelly F, Janin J, Saari JC, Véron M, Truffa-Bachi P, Cohen GN. Eur J Biochem; 1972 Aug 04; 28(4):507-19. PubMed ID: 4562989 [No Abstract] [Full Text] [Related]
7. Dissociation properties of aspartokinase I-homoserine dehydrogenase I extracted from a missense mutant of E. coli K12. Theze J, Veron M. Biochem Biophys Res Commun; 1974 Sep 09; 60(1):219-25. PubMed ID: 4371346 [No Abstract] [Full Text] [Related]
8. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex. Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W. Biochemistry; 1972 Feb 29; 11(5):677-87. PubMed ID: 4551091 [No Abstract] [Full Text] [Related]
9. Circular dichroic and optical rotatory dispersion spectra of the threonine-inhibited aspartokinase-homoserine dehydrogenase of Escherichia coli K 12. Effects of ligand binding and protein denaturation. Heck H d'A, Truffa-Bachi P. Biochemistry; 1970 Jul 07; 9(14):2776-83. PubMed ID: 4394092 [No Abstract] [Full Text] [Related]
10. Studies on the quaternary structure of the threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli. A proposed subunit-interaction model. Mackall JC, Neet KE. Eur J Biochem; 1974 Feb 15; 42(1):275-82. PubMed ID: 4364397 [No Abstract] [Full Text] [Related]
11. 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. Truffa-Bachi P, Van Rapenbusch R, Janin J, Gros C, Cohen GN. Eur J Biochem; 1968 Jun 15; 5(1):73-80. PubMed ID: 4873312 [No Abstract] [Full Text] [Related]
12. Relaxation studies on an allosteric enzyme: aspartokinase I-homoserine dehydrogenase I. Janin J. Cold Spring Harb Symp Quant Biol; 1972 Jun 15; 36():193-8. PubMed ID: 4404442 [No Abstract] [Full Text] [Related]
13. Modulation of threonine control of aspartokinase activity. Starnes WL, Wells MC, Shive W. Biochem Biophys Res Commun; 1971 Aug 06; 44(3):634-8. PubMed ID: 4399361 [No Abstract] [Full Text] [Related]
14. Structure, function, and possible origin of a bifunctional allosteric enzyme, Escherichia coli aspartokinase I-homoserine dehydrogenase I. Truffa-Bachi P, Veron M, Cohen GN. CRC Crit Rev Biochem; 1974 Aug 06; 2(3):379-415. PubMed ID: 4155358 [No Abstract] [Full Text] [Related]
15. Multiple interactions of threonine with an aspartokinase-homoserine dehydrogenase complex. Cunningham GN, Maul SB, Shive W. Biochem Biophys Res Commun; 1968 Jan 25; 30(2):159-65. PubMed ID: 4868092 [No Abstract] [Full Text] [Related]
16. Variation of the size of the reacting form of Escherichia coli K12 threonine-sensitive aspartokinase--homoserine dehydrogenase with pH and effectors. Mackall JC, Neet KE. Biochemistry; 1973 Aug 28; 12(18):3483-9. PubMed ID: 4581333 [No Abstract] [Full Text] [Related]
17. 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. Falcoz-Kelly F, van Rapenbusch R, Cohen GN. Eur J Biochem; 1969 Mar 28; 8(1):146-52. PubMed ID: 4889171 [No Abstract] [Full Text] [Related]
18. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K-12. Incubation of the enzyme in alkaline conditions: dissociation and disulfide-bridge formation. Jacques Y, Truffa-Bachi P. Eur J Biochem; 1976 Mar 01; 62(3):485-90. PubMed ID: 4302 [Abstract] [Full Text] [Related]
19. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Specific inactivation of the homoserine dehydrogenase activity by the affinity label, 2-amino-4-oxo-5-chloropentanoic acid. Hirth CG, Véron M, Villar-Palasi C, Hurion N, Cohen GN. Eur J Biochem; 1975 Jan 02; 50(2):425-30. PubMed ID: 236185 [Abstract] [Full Text] [Related]
20. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Relaxations of the allosteric equilibrium. Janin J, Iwatsubo M. Eur J Biochem; 1969 Dec 02; 11(3):530-40. PubMed ID: 4904703 [No Abstract] [Full Text] [Related] Page: [Next] [New Search]