Triosephosphatisomerase (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "Triosephosphatisomerase" in German language version.

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Anderson, LE. (1971): Chloroplast and cytoplasmic enzymes. II. Pea leaf triose phosphate isomerases. In: Biochim Biophys Acta. 235(1); 237–244; PMID 5089710; doi:10.1016/0005-2744(71)90051-9.
C. Rodríguez-Almazán, R. Arreola, D. Rodríguez-Larrea, B. Aguirre-López, M. T. de Gómez-Puyou, R. Pérez-Montfort, M. Costas, A. Gómez-Puyou, A. Torres-Larios: Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. In: Journal of Biological Chemistry. Band 283, Nummer 34, August 2008, S. 23254–23263, doi:10.1074/jbc.M802145200, PMID 18562316.
K. D. Schnackerz, R. W. Gracy: Probing the catalytic sites of triosephosphate isomerase by 31P-NMR with reversibly and irreversibly binding substrate analogues. In: European Journal of Biochemistry. Band 199, Nummer 1, Juli 1991, S. 231–238, doi:10.1111/j.1432-1033.1991.tb16114.x, PMID 2065677.
A. Marchler-Bauer, Y. Bo, L. Han, J. He, C. J. Lanczycki, S. Lu, F. Chitsaz, M. K. Derbyshire, R. C. Geer, N. R. Gonzales, M. Gwadz, D. I. Hurwitz, F. Lu, G. H. Marchler, J. S. Song, N. Thanki, Z. Wang, R. A. Yamashita, D. Zhang, C. Zheng, L. Y. Geer, S. H. Bryant: CDD/SPARCLE: functional classification of proteins via subfamily domain architectures. In: Nucleic acids research. Band 45, D101 2017, S. D200–D203, doi:10.1093/nar/gkw1129, PMID 27899674, PMC 5210587 (freier Volltext).
E. Lolis, G. A. Petsko: Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. In: Biochemistry. Band 29, Nummer 28, Juli 1990, S. 6619–6625, doi:10.1021/bi00480a010, PMID 2204418.

nih.gov

ncbi.nlm.nih.gov

Anderson, LE. (1971): Chloroplast and cytoplasmic enzymes. II. Pea leaf triose phosphate isomerases. In: Biochim Biophys Acta. 235(1); 237–244; PMID 5089710; doi:10.1016/0005-2744(71)90051-9.
C. Rodríguez-Almazán, R. Arreola, D. Rodríguez-Larrea, B. Aguirre-López, M. T. de Gómez-Puyou, R. Pérez-Montfort, M. Costas, A. Gómez-Puyou, A. Torres-Larios: Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. In: Journal of Biological Chemistry. Band 283, Nummer 34, August 2008, S. 23254–23263, doi:10.1074/jbc.M802145200, PMID 18562316.
K. D. Schnackerz, R. W. Gracy: Probing the catalytic sites of triosephosphate isomerase by 31P-NMR with reversibly and irreversibly binding substrate analogues. In: European Journal of Biochemistry. Band 199, Nummer 1, Juli 1991, S. 231–238, doi:10.1111/j.1432-1033.1991.tb16114.x, PMID 2065677.
A. Marchler-Bauer, Y. Bo, L. Han, J. He, C. J. Lanczycki, S. Lu, F. Chitsaz, M. K. Derbyshire, R. C. Geer, N. R. Gonzales, M. Gwadz, D. I. Hurwitz, F. Lu, G. H. Marchler, J. S. Song, N. Thanki, Z. Wang, R. A. Yamashita, D. Zhang, C. Zheng, L. Y. Geer, S. H. Bryant: CDD/SPARCLE: functional classification of proteins via subfamily domain architectures. In: Nucleic acids research. Band 45, D101 2017, S. D200–D203, doi:10.1093/nar/gkw1129, PMID 27899674, PMC 5210587 (freier Volltext).
E. Lolis, G. A. Petsko: Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. In: Biochemistry. Band 29, Nummer 28, Juli 1990, S. 6619–6625, doi:10.1021/bi00480a010, PMID 2204418.