132 related articles for article (PubMed ID: 4927804)
1. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with aspartate analogs.
Hammes GG; Wu CW
Biochemistry; 1971 Mar; 10(6):1051-7. PubMed ID: 4927804
[No Abstract] [Full Text] [Related]
2. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate.
Hammes GG; Wu CW
Biochemistry; 1971 May; 10(11):2150-6. PubMed ID: 4935107
[No Abstract] [Full Text] [Related]
3. Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate.
Hammes GG; Porter RW; Stark GR
Biochemistry; 1971 Mar; 10(6):1046-50. PubMed ID: 4927803
[No Abstract] [Full Text] [Related]
4. Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit.
Eckfeldt J; Hammes GG; Mohr SC; Wu CW
Biochemistry; 1970 Aug; 9(17):3353-62. PubMed ID: 4941833
[No Abstract] [Full Text] [Related]
5. Aspartate transcarbamylase. Studies of the catalytic subunit by ultraviolet difference spectroscopy.
Collins KD; Stark GR
J Biol Chem; 1969 Apr; 244(7):1869-77. PubMed ID: 4889009
[No Abstract] [Full Text] [Related]
6. Studies with aspartate transcarbamylase.
Gregory DS; Wilson IB
Biochemistry; 1971 Jan; 10(1):154-61. PubMed ID: 4922542
[No Abstract] [Full Text] [Related]
7. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5'-triphosphate analog.
Wu CW; Hammes GG
Biochemistry; 1973 Mar; 12(7):1400-8. PubMed ID: 4572360
[No Abstract] [Full Text] [Related]
8. Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands.
Gerhart JC; Schachman HK
Biochemistry; 1968 Feb; 7(2):538-52. PubMed ID: 4868540
[No Abstract] [Full Text] [Related]
9. Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits.
Changeux JP; Gerhart JC; Schachman HK
Biochemistry; 1968 Feb; 7(2):531-8. PubMed ID: 4868539
[No Abstract] [Full Text] [Related]
10. A model for nucleotide regulation of aspartate transcarbamylase.
London RE; Schmidt PG
Biochemistry; 1972 Aug; 11(16):3136-42. PubMed ID: 4557519
[No Abstract] [Full Text] [Related]
11. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with cytidine 5'-triphosphate.
Harrison LW; Hammes GG
Biochemistry; 1973 Mar; 12(7):1395-400. PubMed ID: 4572359
[No Abstract] [Full Text] [Related]
12. Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux.
Changeux JP; Rubin MM
Biochemistry; 1968 Feb; 7(2):553-61. PubMed ID: 4868541
[No Abstract] [Full Text] [Related]
13. An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate.
Matsumoto S; Hammes GG
Biochemistry; 1973 Mar; 12(7):1388-94. PubMed ID: 4572358
[No Abstract] [Full Text] [Related]
14. Aspartate transcarbamylase. Stereospecific restrictions on the binding site for L-aspartate.
Davies GE; Vanaman TC; Stark GR
J Biol Chem; 1970 Mar; 245(5):1175-9. PubMed ID: 4906845
[No Abstract] [Full Text] [Related]
15. Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.
Porter RW; Modebe MO; Stark GR
J Biol Chem; 1969 Apr; 244(7):1846-59. PubMed ID: 4889008
[No Abstract] [Full Text] [Related]
16. Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate.
Collins KD; Stark GR
J Biol Chem; 1971 Nov; 246(21):6599-605. PubMed ID: 4943676
[No Abstract] [Full Text] [Related]
17. Spin-labeling studies of aspartate transcarbamylase. I. Effects of nucleotide binding and subunit separation.
Buckman T
Biochemistry; 1970 Aug; 9(16):3255-65. PubMed ID: 4321370
[No Abstract] [Full Text] [Related]
18. Aspartate transcarbamylase. A study by transient nuclear magnetic resonance of the binding of succinate to the native enzyme and its catalytic subunit.
Sykes BD; Schmidt PG; Stark GR
J Biol Chem; 1970 Mar; 245(5):1180-9. PubMed ID: 4906846
[No Abstract] [Full Text] [Related]
19. A nuclear magnetic resonance study of the binding of substrate analogues to a modified aspartate transcarbamylase.
McMurray CH; Evans DR; Sykes BD
Biochem Biophys Res Commun; 1972 Aug; 48(3):572-7. PubMed ID: 4558610
[No Abstract] [Full Text] [Related]
20. A study of the sulfhydryl groups of the catalytic subunit of Escherichia coli aspartate transcarbamylase. The use of enzyme--5-thio-2-nitrobenzoate mixed disulfides as intermediates in modifying enzyme sulfhydryl groups.
Vanaman TC; Stark GR
J Biol Chem; 1970 Jul; 245(14):3565-73. PubMed ID: 4919212
[No Abstract] [Full Text] [Related]
[Next] [New Search]
