120 related articles for article (PubMed ID: 4334489)
1. Structure-function studies on glyceraldehyde 3-phosphate dehydrogenase. IV. Subunit interactions of the rabbit muscle and yeast enzymes.
Fensleau A
J Biol Chem; 1972 Feb; 247(4):1074-9. PubMed ID: 4334489
[No Abstract] [Full Text] [Related]
2. Analysis of the allosteric basis for positive and negative co-operativity and half-of-the-sites reactivity in yeast and rabbit muscle glyceraldehyde 3-phosphate dehydrogenase.
Herzfeld J; Schlesinger PA
J Mol Biol; 1975 Oct; 97(4):483-517. PubMed ID: 171419
[No Abstract] [Full Text] [Related]
3. Relationship between structure and chemical reactivity in D-glyceraldehyde 3-phosphate dehydrogenase. Trinitrophenylation of the lysine residues in yeast, sturgeon and rabbit muscle enzyme.
Nakano M; Foucault G; Pudles J
J Mol Biol; 1976 Aug; 105(2):275-91. PubMed ID: 184288
[No Abstract] [Full Text] [Related]
4. Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase.
Cook RA; Koshland DE
Biochemistry; 1970 Aug; 9(17):3337-42. PubMed ID: 4330855
[No Abstract] [Full Text] [Related]
5. Regulation of glyceraldehyde 3-phosphate dehydrogenase by phosphocreatine and adenosine triphosphate. IV. Factors affecting in vivo control of enzymatic activity.
Oguchi M; Gerth E; Fitzgerald B; Park JH
J Biol Chem; 1973 Aug; 248(16):5571-6. PubMed ID: 4353270
[No Abstract] [Full Text] [Related]
6. D-glyceraldehyde-3-phosphate dehydrogenase subunit cooperativity studied using immobilized enzyme forms.
Douzhenkova IV; Asryants RA; Nagradova NK
Biochim Biophys Acta; 1988 Nov; 957(1):60-70. PubMed ID: 3179321
[TBL] [Abstract][Full Text] [Related]
7. Structure-function studies on glyceraldehyde-3-phosphate dehydrogenase. 3. Dependency of proteolysis on NAD+ concentration.
Fenselau A
Biochem Biophys Res Commun; 1970 Jul; 40(2):481-8. PubMed ID: 4319826
[No Abstract] [Full Text] [Related]
8. Inactivation of ADH from yeast and GAPDH from rabbit muscle by structural analogues of NAD.
Woenckhaus C; Jeck R; Schättle E; Dietz G; Jentsch G
FEBS Lett; 1973 Aug; 34(2):175-8. PubMed ID: 4355902
[No Abstract] [Full Text] [Related]
9. Binding of NAD + and NADH to rabbit-muscle glyceraldehydephosphate dehydrogenase.
Boers W; Oosthuizen C; Slater EC
Biochim Biophys Acta; 1971 Oct; 250(1):35-46. PubMed ID: 4334857
[No Abstract] [Full Text] [Related]
10. Role of lysine-183 in D-glyceraldehyde-3-phosphate dehydrogenases. Properties of the N-acetylated yeast, sturgeon muscle and rabbit muscle enzymes.
Foucault G; Nakano M; Pudles J
Eur J Biochem; 1978 Feb; 83(1):113-23. PubMed ID: 342241
[No Abstract] [Full Text] [Related]
11. Subunit interactions in glyceraldehyde-3-phosphate dehydrogenases. Their involvement in nucleotide binding and cooperativity.
Scheek RM; Kalkman ML; Berden JA; Slater EC
Biochim Biophys Acta; 1980 Jun; 613(2):275-91. PubMed ID: 7004489
[TBL] [Abstract][Full Text] [Related]
12. Structure-function relationship in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Trinitrophenylation of the lysine residues.
Foucault G; Traore F; Levilliers J; Pudles J
Eur J Biochem; 1974 Jul; 46(1):43-57. PubMed ID: 4369222
[No Abstract] [Full Text] [Related]
13. Mechanism of alkylation of rabbit muscle glyceraldehyde 3-phosphate dehydrogenase.
MacQuarrie RA; Bernhard SA
Biochemistry; 1971 Jun; 10(13):2456-66. PubMed ID: 4326767
[No Abstract] [Full Text] [Related]
14. The effect of NAD+ on the catalytic efficiency of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle.
Teipel J; Koshland DE
Biochim Biophys Acta; 1970 Feb; 198(2):183-91. PubMed ID: 4313530
[No Abstract] [Full Text] [Related]
15. [Comparative study of glyceraldehyde-3-phosphate dehydrogenases isolated from rabbit skeletal muscles and baker's yeast using cationic fluorescent probes].
Klichko VI; Ivanov MV; Nagradova NK
Biokhimiia; 1986 Sep; 51(9):1465-75. PubMed ID: 3533163
[TBL] [Abstract][Full Text] [Related]
16. [Effect of adenine nucleotides on the activity of glyceraldehyde-3-phosphate dehydrogenases from different sources].
Nagradova NK; Vorona MK; Asriiants RA
Biokhimiia; 1969; 34(3):627-32. PubMed ID: 4309682
[No Abstract] [Full Text] [Related]
17. Sequence variability and structure of D-glyceraldehyde-3-phosphate dehydrogenase.
Olsen KW; Moras D; Rossmann MG
J Biol Chem; 1975 Dec; 250(24):9313-21. PubMed ID: 1104621
[TBL] [Abstract][Full Text] [Related]
18. Structure and reactivity relationship in glyceraldehyde-3-phosphate dehydrogenase. Dinitrophenylation of cysteine residues of yeast and rabbit muscle enzymes.
Foucault G; Bodo JM; Nakano M
Eur J Biochem; 1981 Oct; 119(3):625-32. PubMed ID: 7030743
[TBL] [Abstract][Full Text] [Related]
19. Pseudoconservative transition: a two-state model for the co-operative behavior of oligomeric proteins.
Viratelle OM; Seydoux FJ
J Mol Biol; 1975 Feb; 92(2):193-205. PubMed ID: 167173
[No Abstract] [Full Text] [Related]
20. Selective inhibition of an enzyme in crude cell extracts. The use of subunits modified with a half-of-the-sites reagent.
Muronetz VI; Ashmarina LI; Nagradova NK
Biochem Int; 1983 Apr; 6(4):443-50. PubMed ID: 6385975
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
