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161 related items for PubMed ID: 21289039
1. Engineered dimer interface mutants of triosephosphate isomerase: the role of inter-subunit interactions in enzyme function and stability. Banerjee M, Balaram H, Joshi NV, Balaram P. Protein Eng Des Sel; 2011 May; 24(5):463-72. PubMed ID: 21289039 [Abstract] [Full Text] [Related]
5. Probing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzyme. Bandyopadhyay D, Murthy MR, Balaram H, Balaram P. FEBS J; 2015 Oct; 282(20):3863-82. PubMed ID: 26206206 [Abstract] [Full Text] [Related]
7. Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant. Gokhale RS, Ray SS, Balaram H, Balaram P. Biochemistry; 1999 Jan 05; 38(1):423-31. PubMed ID: 9890925 [Abstract] [Full Text] [Related]
9. Revisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue. Samanta M, Murthy MR, Balaram H, Balaram P. Chembiochem; 2011 Aug 16; 12(12):1886-96. PubMed ID: 21671330 [Abstract] [Full Text] [Related]
10. Three hTIM mutants that provide new insights on why TIM is a dimer. Mainfroid V, Terpstra P, Beauregard M, Frère JM, Mande SC, Hol WG, Martial JA, Goraj K. J Mol Biol; 1996 Mar 29; 257(2):441-56. PubMed ID: 8609635 [Abstract] [Full Text] [Related]
11. A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. Schliebs W, Thanki N, Jaenicke R, Wierenga RK. Biochemistry; 1997 Aug 12; 36(32):9655-62. PubMed ID: 9245397 [Abstract] [Full Text] [Related]
12. Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer. Espinoza-Fonseca LM, Wong-Ramírez C, Trujillo-Ferrara JG. Arch Biochem Biophys; 2010 Feb 01; 494(1):46-57. PubMed ID: 19914198 [Abstract] [Full Text] [Related]
14. Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability. González-Mondragón E, Zubillaga RA, Saavedra E, Chánez-Cárdenas ME, Pérez-Montfort R, Hernández-Arana A. Biochemistry; 2004 Mar 23; 43(11):3255-63. PubMed ID: 15023076 [Abstract] [Full Text] [Related]
18. Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM. Alahuhta M, Casteleijn MG, Neubauer P, Wierenga RK. Acta Crystallogr D Biol Crystallogr; 2008 Feb 14; 64(Pt 2):178-88. PubMed ID: 18219118 [Abstract] [Full Text] [Related]
20. Structure-based protein engineering efforts with a monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties. Alahuhta M, Salin M, Casteleijn MG, Kemmer C, El-Sayed I, Augustyns K, Neubauer P, Wierenga RK. Protein Eng Des Sel; 2008 Apr 14; 21(4):257-66. PubMed ID: 18239072 [Abstract] [Full Text] [Related] Page: [Next] [New Search]