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Journal Abstract Search
177 related items for PubMed ID: 7990142
1. Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. Zhang Y, Liang JY, Huang S, Lipscomb WN. J Mol Biol; 1994 Dec 16; 244(5):609-24. PubMed ID: 7990142 [Abstract] [Full Text] [Related]
7. Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution. Weeks CM, Roszak AW, Erman M, Kaiser R, Jörnvall H, Ghosh D. Acta Crystallogr D Biol Crystallogr; 1999 Jan 15; 55(Pt 1):93-102. PubMed ID: 10089399 [Abstract] [Full Text] [Related]
16. Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography. Villeret V, Huang S, Zhang Y, Lipscomb WN. Biochemistry; 1995 Apr 04; 34(13):4307-15. PubMed ID: 7703244 [Abstract] [Full Text] [Related]
17. Unraveling multistate unfolding of pig kidney fructose-1,6-bisphosphatase using single tryptophan mutants. Ludwig HC, Pardo FN, Asenjo JL, Maureira MA, Yañez AJ, Slebe JC. FEBS J; 2007 Oct 04; 274(20):5337-49. PubMed ID: 17894826 [Abstract] [Full Text] [Related]
19. The C1-C2 interface residue lysine 50 of pig kidney fructose-1, 6-bisphosphatase has a crucial role in the cooperative signal transmission of the AMP inhibition. Cárcamo JG, Yañez AJ, Ludwig HC, León O, Pinto RO, Reyes AM, Slebe JC. Eur J Biochem; 2000 Apr 04; 267(8):2242-51. PubMed ID: 10759847 [Abstract] [Full Text] [Related]
20. Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition. Hines JK, Chen X, Nix JC, Fromm HJ, Honzatko RB. J Biol Chem; 2007 Dec 07; 282(49):36121-31. PubMed ID: 17933867 [Abstract] [Full Text] [Related] Page: [Next] [New Search]