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101 related items for PubMed ID: 2920838
21. AMP deaminase as a cell-age marker in transient erythroblastopenia of childhood and its role in the adenylate economy of erythrocytes. Paglia DE, Valentine WN, Nakatani M, Brockway RA. Blood; 1989 Nov 01; 74(6):2161-5. PubMed ID: 2804355 [Abstract] [Full Text] [Related]
28. Modification by liposomes of the adenosine triphosphate-activating effect on adenylate deaminase from pig heart. Purzycka-Preis J, Prus E, Woźniak M, Zydowo M. Biochem J; 1978 Nov 01; 175(2):607-12. PubMed ID: 743213 [Abstract] [Full Text] [Related]
29. The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency. Sabina RL, Waldenström A, Ronquist G. Haematologica; 2006 May 01; 91(5):652-5. PubMed ID: 16670071 [Abstract] [Full Text] [Related]
30. AMP deaminase from human erythrocytes. Nathans GR, Chang D, Deuel TF. Methods Enzymol; 1978 May 01; 51():497-502. PubMed ID: 692397 [No Abstract] [Full Text] [Related]
31. Complete deficiency of AMP deaminase in human erythrocytes. Ogasawara N, Goto H, Yamada Y, Nishigaki I, Itoh T, Hasegawa I. Biochem Biophys Res Commun; 1984 Aug 16; 122(3):1344-9. PubMed ID: 6477565 [Abstract] [Full Text] [Related]
32. Deficiency of AMP deaminase in human erythrocytes. Zydowo MM, Purzycka-Preis J, Ogasawara N. Adv Exp Med Biol; 1989 Aug 16; 253A():31-4. PubMed ID: 2624209 [No Abstract] [Full Text] [Related]
38. Calcium-induced conversion of adenine nucleotides to inosine monophosphate in human red cells. Almaraz L, García-Sancho J, Lew VL. J Physiol; 1988 Dec 16; 407():557-67. PubMed ID: 3151496 [Abstract] [Full Text] [Related]
39. Adenylate metabolism in the heart. Regulatory properties of rabbit cardiac adenylate deaminase. Barsacchi R, Ranieri-Raggi M, Bergamini C, Raggi A. Biochem J; 1979 Aug 15; 182(2):361-6. PubMed ID: 41518 [Abstract] [Full Text] [Related]
40. Erythrocyte pyruvate kinase deficiency. The influence of physiologically important metabolites on the function of normal and defective enzymes. Lakomek M, Winkler H, Pekrun A, Krüger N, Sander M, Huppke P, Schröter W. Enzyme Protein; 1979 Aug 15; 48(3):149-63. PubMed ID: 8589802 [Abstract] [Full Text] [Related] Page: [Previous] [Next] [New Search]