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181 related items for PubMed ID: 1311162
1. 25Mg NMR studies of yeast enolase and rabbit muscle pyruvate kinase. Lee ME, Nowak T. Arch Biochem Biophys; 1992 Mar; 293(2):264-73. PubMed ID: 1311162 [Abstract] [Full Text] [Related]
2. Dual divalent cation requirement for activation of pyruvate kinase; essential roles of both enzyme- and nucleotide-bound metal ions. Gupta RK, Oesterling RM. Biochemistry; 1976 Jun 29; 15(13):2881-7. PubMed ID: 7293 [Abstract] [Full Text] [Related]
3. Conformational changes in yeast pyruvate kinase studied by 205Tl+ NMR. Loria JP, Nowak T. Biochemistry; 1998 May 12; 37(19):6967-74. PubMed ID: 9578583 [Abstract] [Full Text] [Related]
4. 7Li, 31P, and 1H NMR studies of interactions between ATP, monovalent cations, and divalent cation sites on rabbit muscle pyruvate kinase. Van Divender JM, Grisham CM. J Biol Chem; 1985 Nov 15; 260(26):14060-9. PubMed ID: 2997192 [Abstract] [Full Text] [Related]
5. Structure of the bis divalent cation complex with phosphonoacetohydroxamate at the active site of enolase. Poyner RR, Reed GH. Biochemistry; 1992 Aug 11; 31(31):7166-73. PubMed ID: 1322695 [Abstract] [Full Text] [Related]
9. Structure of the oxalate-ATP complex with pyruvate kinase: ATP as a bridging ligand for the two divalent cations. Lodato DT, Reed GH. Biochemistry; 1987 Apr 21; 26(8):2243-50. PubMed ID: 3040085 [Abstract] [Full Text] [Related]
14. 31P NMR studies of enzyme-bound substrate complexes of yeast 3-phosphoglycerate kinase. 2. Structure measurements using paramagnetic relaxation effects of Mn(II) and Co(II). Ray BD, Rao BD. Biochemistry; 1988 Jul 26; 27(15):5579-85. PubMed ID: 3052581 [Abstract] [Full Text] [Related]
15. Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel. Larsen TM, Benning MM, Rayment I, Reed GH. Biochemistry; 1998 May 05; 37(18):6247-55. PubMed ID: 9572839 [Abstract] [Full Text] [Related]
16. A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Larsen TM, Wedekind JE, Rayment I, Reed GH. Biochemistry; 1996 Apr 09; 35(14):4349-58. PubMed ID: 8605183 [Abstract] [Full Text] [Related]