Subunit interface mutation disrupting an aromatic cluster in Plasmodium falciparum triosephosphate isomerase: effect on dimer stability.
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Hemalatha Balaram | H. Balaram | P. Balaram | P Balaram | G. Ravindra | G Nagaraj | K. Maithal | G. Nagaraj | S. Singh | Kapil Maithal | Gudihal Ravindra | S Kumar Singh
[1] I M Klotz,et al. Quaternary structure of proteins. , 1970, Annual review of biochemistry.
[2] G. Petsko,et al. On the origin of enzymatic species. , 1993, Trends in biochemical sciences.
[3] L. Banaszak,et al. Engineering the quaternary structure of an enzyme: Construction and analysis of a monomeric form of malate dehydrogenase from Escherichia coli , 1994, Protein science : a publication of the Protein Society.
[4] N. Thanki,et al. A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. , 1997, Biochemistry.
[5] N. Thanki,et al. Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies , 1996, Protein science : a publication of the Protein Society.
[6] M. Noble,et al. The crystal structure of the “open” and the “closed” conformation of the flexible loop of trypanosomal triosephosphate isomerase , 1991, Proteins.
[7] J. Nielsen,et al. The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase. , 2000, European journal of biochemistry.
[8] M. M. Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.
[9] H. Balaram,et al. Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli. , 1993, Molecular and biochemical parasitology.
[10] B. Matthews,et al. High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer. , 1996, Biochemistry.
[11] A J Olson,et al. Soluble proteins: size, shape and function. , 1993, Trends in biochemical sciences.
[12] M. Esnouf,et al. The denaturation-renaturation of chicken-muscle triosephosphate isomerase in guanidinium chloride. , 1977, European journal of biochemistry.
[13] H. Savithri,et al. 3'NON-TEMPLATED 'A' ADDITION BY TAQ DNA POLYMERASE : AN ADVANTAGE IN THE CONSTRUCTION OF SINGLE AND DOUBLE MUTANTS , 1996 .
[14] R Abagyan,et al. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[15] E. Greisheimer,et al. The proteins. , 1955, Journal of the American Medical Women's Association.
[16] M. Kokkinidis,et al. Subunit interactions provide a significant contribution to the stability of the dimeric four-alpha-helical-bundle protein ROP. , 1993, Biochemistry.
[17] W G Hol,et al. Three hTIM mutants that provide new insights on why TIM is a dimer. , 1996, Journal of molecular biology.
[18] S. Jones,et al. Protein domain interfaces: characterization and comparison with oligomeric protein interfaces. , 2000, Protein engineering.
[19] R. Jaenicke,et al. Folding and Association of Triose Phosphate Isomerase from Rabbit Muscle , 1980, Zeitschrift fur Naturforschung. Section C, Biosciences.
[20] C. Dobson,et al. A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase. , 2000, Journal of molecular biology.
[21] K. Yüksel,et al. Deamidation of triosephosphate isomerase in reverse micelles: effects of water on catalysis and molecular wear and tear. , 1994, Biochemistry.
[22] A. Sun,et al. Terminal marking of triosephosphate isomerase: consequences of deamidation. , 1995, Archives of biochemistry and biophysics.
[23] Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant. , 1999, Biochemistry.
[24] B. Zerner,et al. [8] Reassessment of Ellman's reagent , 1983 .
[25] E. Amann,et al. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. , 1988, Gene.
[26] K. Kirschner,et al. Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate. , 1990, Biochemistry.
[27] A. Sun,et al. Interactions between the catalytic centers and subunit interface of triosephosphate isomerase probed by refolding, active site modification, and subunit exchange. , 1992, The Journal of biological chemistry.
[28] R. Schirmer,et al. Folding of the four domains and dimerization are impaired by the Gly446-->Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs. , 1993, Biochemistry.
[29] A. Sun,et al. The hinged lid of yeast triose-phosphate isomerase. Determination of the energy barrier between the two conformations. , 1994, The Journal of biological chemistry.
[30] D W Banner,et al. On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase. , 1981, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.
[31] A. Akamine,et al. Biochemical properties of the monomeric mutant of human cathepsin E expressed in Chinese hamster ovary cells: comparison with dimeric forms of the natural and recombinant cathepsin E. , 1996, Journal of biochemistry.
[32] W G Hol,et al. Stabilization of human triosephosphate isomerase by improvement of the stability of individual alpha-helices in dimeric as well as monomeric forms of the protein. , 1996, Biochemistry.
[33] C. Chothia. The nature of the accessible and buried surfaces in proteins. , 1976, Journal of molecular biology.
[34] J. Knowles,et al. Enzyme catalysis: not different, just better , 1991, Nature.
[35] J. Knowles,et al. pH-dependence of the triose phosphate isomerase reaction. , 1972, The Biochemical journal.
[36] G A Petsko,et al. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. , 1985, Science.
[37] L. Wyns,et al. The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures , 1999, Proteins.
[38] Cavity-creating mutation at the dimer interface of Plasmodium falciparum triosephosphate isomerase: restoration of stability by disulfide cross-linking of subunits. , 1999, Biochemistry.
[39] P. Terpstra,et al. Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences. , 1993, Journal of molecular biology.
[40] S. Ferreira,et al. Kinetics and energetics of subunit dissociation/unfolding of TIM: the importance of oligomerization for conformational persistence and chemical stability of proteins. , 1998, Biochemistry.
[41] G. Petsko,et al. Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution. , 1994, Biochemistry.
[42] K. H. Kalk,et al. Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution. , 1987, Journal of molecular biology.
[43] H. Balaram,et al. Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. , 1997, Structure.
[44] J. Richard,et al. Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance. , 1991, Biochemistry.
[45] R. Jaenicke,et al. [12]Refolding and association of oligomeric proteins , 1986 .
[46] E. W. Kauffman,et al. Reversible self-association of bovine growth hormone during equilibrium unfolding. , 1986, Biochemistry.
[47] M. Noble,et al. Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant. , 1993, European journal of biochemistry.
[48] F. Young. Biochemistry , 1955, The Indian Medical Gazette.
[49] B. Sykes,et al. Neutrophil activation by monomeric interleukin-8 , 1994 .
[50] G. H. Hoa,et al. Second derivative spectroscopy of enolase at high hydrostatic pressure: an approach to the study of macromolecular interactions. , 1995, Biochemistry.
[51] R. Sauer,et al. Critical side-chain interactions at a subunit interface in the Arc repressor dimer. , 1995, Biochemistry.
[52] G. Petsko,et al. Weakly polar interactions in proteins. , 1988, Advances in protein chemistry.
[53] A. Coulson,et al. Specificity and kinetics of triose phosphate isomerase from chicken muscle. , 1972, The Biochemical journal.
[54] F. Opperdoes,et al. Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein. , 1994, European journal of biochemistry.
[55] F. C. Hartman,et al. Structure of yeast triosephosphate isomerase at 1.9-A resolution. , 1990, Biochemistry.
[56] P. Horowitz,et al. Interactive intermediates are formed during the urea unfolding of rhodanese. , 1993, The Journal of biological chemistry.
[57] F. Opperdoes,et al. Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes. , 1987, European journal of biochemistry.
[58] F. Opperdoes,et al. Inhibition of triosephosphate isomerase from Trypanosoma brucei with cyclic hexapeptides. , 1992, European journal of biochemistry.
[59] I. M. Klotz,et al. Subunit constitution of proteins: a table. , 1975, Archives of biochemistry and biophysics.
[60] N. C. Price,et al. The unfolding and refolding of glutamate dehydrogenases from bovine liver, baker's yeast and Clostridium symbosium. , 1988, The Biochemical journal.
[61] J M Thornton,et al. Protein-protein interactions: a review of protein dimer structures. , 1995, Progress in biophysics and molecular biology.
[62] H. Mohrenweiser,et al. Characterization of two new electrophoretic variants of human triosephosphate isomerase: Stability, kinetic, and immunological properties , 1982, Biochemical Genetics.
[63] N. Scrutton,et al. Altering kinetic mechanism and enzyme stability by mutagenesis of the dimer interface of glutathione reductase. , 1995, The Biochemical journal.
[64] A. Rojo-Domínguez,et al. Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase. , 1996, European journal of biochemistry.
[65] G A Petsko,et al. Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme. , 1987, Biochemistry.
[66] I. Becker,et al. Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi. , 1997, European journal of biochemistry.
[67] M. Hennig,et al. Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. , 2000, Structure.