リンゴ酸シンターゼ (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "リンゴ酸シンターゼ" in Japanese language version.

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archive.org

Stryer, Lubert; Berg, Jeremy M.; Tymoczko, John L. (2003). Biochemistry (fifth ed.). New York: Freeman. ISBN 978-0-7167-4684-3. OCLC 48055706

doi.org

PDB: 5T8G; “Mycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product Exchange”. The Journal of Biological Chemistry 291 (53): 27421–32. (December 2016). doi:10.1074/jbc.m116.750877. PMC 5207166. PMID 27738104.
“Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis”. The Journal of Biological Chemistry 278 (3): 1735–43. (January 2003). doi:10.1074/jbc.M209248200. PMID 12393860.
Kumar, Ranjeet; Bhakuni, Vinod (2010-10). “A functionally active dimer of mycobacterium tuberculosis malate synthase G”. European biophysics journal: EBJ 39 (11): 1557–1562. doi:10.1007/s00249-010-0598-7. ISSN 1432-1017. PMID 20306314.
“Large-scale purification and some properties of malate synthase from baker's yeast”. European Journal of Biochemistry 114 (2): 255–62. (February 1981). doi:10.1111/j.1432-1033.1981.tb05144.x. PMID 7011808.
“Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution”. Protein Science 12 (9): 1822–32. (September 2003). doi:10.1110/ps.03174303. PMC 2323980. PMID 12930982.
“Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii”. Biochimica et Biophysica Acta 1520 (2): 154–62. (August 2001). doi:10.1016/s0167-4781(01)00263-9. PMID 11513957.
“Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications”. Biochemistry 39 (11): 3156–68. (March 2000). doi:10.1021/bi992519h. PMID 10715138.
“Malate synthase: proof of a stepwise Claisen condensation using the double-isotope fractionation test”. Biochemistry 27 (16): 5961–71. (August 1988). doi:10.1021/bi00416a020. PMID 2847778.
“The metabolism of C2-compounds in micro-organisms. VIII. A dicarboxylic acid cycle as a route for the oxidation of glycollate by Escherichia coli”. The Biochemical Journal 81: 503–13. (December 1961). doi:10.1042/bj0810503. PMC 1243371. PMID 14458448.
“C2 metabolism in Euglena”. Advances in Experimental Medicine and Biology 979: 39–45. (2017). doi:10.1007/978-3-319-54910-1_3. ISBN 978-3-319-54908-8. PMID 28429316.
“Comparative biochemistry of the glyoxylate cycle”. Comparative Biochemistry and Physiology B 70: 1–26. (1981). doi:10.1016/0305-0491(81)90118-8.
“Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants. A case study of endosymbiotic gene transfer”. European Journal of Biochemistry 269 (3): 868–83. (February 2002). doi:10.1046/j.0014-2956.2001.02722.x. PMID 11846788.
“CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activity”. Human Molecular Genetics 23 (9): 2313–23. (May 2014). doi:10.1093/hmg/ddt624. PMC 3976331. PMID 24334609.
“The Human Knockout Gene CLYBL Connects Itaconate to Vitamin B12”. Cell 171 (4): 771–782.e11. (November 2017). doi:10.1016/j.cell.2017.09.051. PMC 5827971. PMID 29056341.
“A Missing Link to Vitamin B12 Metabolism”. Cell 171 (4): 736–737. (November 2017). doi:10.1016/j.cell.2017.10.030. PMID 29100069.
“Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis”. Microbiology 155 (Pt 10): 3166–75. (October 2009). doi:10.1099/mic.0.030858-0. PMID 19684068.
“Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis”. Biochemistry 50 (32): 6879–87. (August 2011). doi:10.1021/bi2007299. PMC 3153559. PMID 21728344.
“Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation in Mycobacterium tuberculosis”. Proceedings of the National Academy of Sciences of the United States of America 114 (11): E2225–E2232. (March 2017). doi:10.1073/pnas.1617655114. PMC 5358392. PMID 28265055.
“Down-regulation of malate synthase in Mycobacterium tuberculosis H37Ra leads to reduced stress tolerance, persistence and survival in macrophages”. Tuberculosis 106: 73–81. (September 2017). doi:10.1016/j.tube.2017.07.006. PMID 28802408.
“A systems chemical biology study of malate synthase and isocitrate lyase inhibition in Mycobacterium tuberculosis during active and NRP growth”. Computational Biology and Chemistry 47: 167–80. (December 2013). doi:10.1016/j.compbiolchem.2013.07.002. PMC 4010430. PMID 24121675.
“Structural and Functional Characterization of Malate Synthase G from Opportunistic Pathogen Pseudomonas aeruginosa”. Biochemistry 56 (41): 5539–5549. (October 2017). doi:10.1021/acs.biochem.7b00852. PMID 28985053.
“Modeling, molecular docking, probing catalytic binding mode of acetyl-CoA malate synthase G in Brucella melitensis 16M”. Biochemistry and Biophysics Reports 8: 192–199. (December 2016). doi:10.1016/j.bbrep.2016.08.020. PMC 5613768. PMID 28955956.
“Utilization of acetate in Escherichia coli: structural organization and differential expression of the ace operon”. Biochimie 71 (9–10): 1043–9. (September 1989). doi:10.1016/0300-9084(89)90109-0. PMID 2512996.

nih.gov

pubmed.ncbi.nlm.nih.gov

PDB: 5T8G; “Mycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product Exchange”. The Journal of Biological Chemistry 291 (53): 27421–32. (December 2016). doi:10.1074/jbc.m116.750877. PMC 5207166. PMID 27738104.
“Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis”. The Journal of Biological Chemistry 278 (3): 1735–43. (January 2003). doi:10.1074/jbc.M209248200. PMID 12393860.
Kumar, Ranjeet; Bhakuni, Vinod (2010-10). “A functionally active dimer of mycobacterium tuberculosis malate synthase G”. European biophysics journal: EBJ 39 (11): 1557–1562. doi:10.1007/s00249-010-0598-7. ISSN 1432-1017. PMID 20306314.
“Large-scale purification and some properties of malate synthase from baker's yeast”. European Journal of Biochemistry 114 (2): 255–62. (February 1981). doi:10.1111/j.1432-1033.1981.tb05144.x. PMID 7011808.
“Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution”. Protein Science 12 (9): 1822–32. (September 2003). doi:10.1110/ps.03174303. PMC 2323980. PMID 12930982.
“Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii”. Biochimica et Biophysica Acta 1520 (2): 154–62. (August 2001). doi:10.1016/s0167-4781(01)00263-9. PMID 11513957.
“Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications”. Biochemistry 39 (11): 3156–68. (March 2000). doi:10.1021/bi992519h. PMID 10715138.
“Malate synthase: proof of a stepwise Claisen condensation using the double-isotope fractionation test”. Biochemistry 27 (16): 5961–71. (August 1988). doi:10.1021/bi00416a020. PMID 2847778.
“The metabolism of C2-compounds in micro-organisms. VIII. A dicarboxylic acid cycle as a route for the oxidation of glycollate by Escherichia coli”. The Biochemical Journal 81: 503–13. (December 1961). doi:10.1042/bj0810503. PMC 1243371. PMID 14458448.
“C2 metabolism in Euglena”. Advances in Experimental Medicine and Biology 979: 39–45. (2017). doi:10.1007/978-3-319-54910-1_3. ISBN 978-3-319-54908-8. PMID 28429316.
“Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants. A case study of endosymbiotic gene transfer”. European Journal of Biochemistry 269 (3): 868–83. (February 2002). doi:10.1046/j.0014-2956.2001.02722.x. PMID 11846788.
“CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activity”. Human Molecular Genetics 23 (9): 2313–23. (May 2014). doi:10.1093/hmg/ddt624. PMC 3976331. PMID 24334609.
“The Human Knockout Gene CLYBL Connects Itaconate to Vitamin B12”. Cell 171 (4): 771–782.e11. (November 2017). doi:10.1016/j.cell.2017.09.051. PMC 5827971. PMID 29056341.
“A Missing Link to Vitamin B12 Metabolism”. Cell 171 (4): 736–737. (November 2017). doi:10.1016/j.cell.2017.10.030. PMID 29100069.
“Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis”. Microbiology 155 (Pt 10): 3166–75. (October 2009). doi:10.1099/mic.0.030858-0. PMID 19684068.
“Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis”. Journal of Bacteriology 181 (23): 7161–7. (December 1999). PMC 103675. PMID 10572116.
“Kinetic and chemical mechanism of malate synthase from Mycobacterium tuberculosis”. Biochemistry 50 (32): 6879–87. (August 2011). doi:10.1021/bi2007299. PMC 3153559. PMID 21728344.
“Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation in Mycobacterium tuberculosis”. Proceedings of the National Academy of Sciences of the United States of America 114 (11): E2225–E2232. (March 2017). doi:10.1073/pnas.1617655114. PMC 5358392. PMID 28265055.
“Down-regulation of malate synthase in Mycobacterium tuberculosis H37Ra leads to reduced stress tolerance, persistence and survival in macrophages”. Tuberculosis 106: 73–81. (September 2017). doi:10.1016/j.tube.2017.07.006. PMID 28802408.
“A systems chemical biology study of malate synthase and isocitrate lyase inhibition in Mycobacterium tuberculosis during active and NRP growth”. Computational Biology and Chemistry 47: 167–80. (December 2013). doi:10.1016/j.compbiolchem.2013.07.002. PMC 4010430. PMID 24121675.
“Structural and Functional Characterization of Malate Synthase G from Opportunistic Pathogen Pseudomonas aeruginosa”. Biochemistry 56 (41): 5539–5549. (October 2017). doi:10.1021/acs.biochem.7b00852. PMID 28985053.
“Modeling, molecular docking, probing catalytic binding mode of acetyl-CoA malate synthase G in Brucella melitensis 16M”. Biochemistry and Biophysics Reports 8: 192–199. (December 2016). doi:10.1016/j.bbrep.2016.08.020. PMC 5613768. PMID 28955956.
“Utilization of acetate in Escherichia coli: structural organization and differential expression of the ace operon”. Biochimie 71 (9–10): 1043–9. (September 1989). doi:10.1016/0300-9084(89)90109-0. PMID 2512996.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

rcsb.org

PDB: 5T8G; “Mycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product Exchange”. The Journal of Biological Chemistry 291 (53): 27421–32. (December 2016). doi:10.1074/jbc.m116.750877. PMC 5207166. PMID 27738104.
Bank, RCSB Protein Data. “RCSB PDB: Homepage” (英語). www.rcsb.org. 2018年3月5日閲覧。

worldcat.org

search.worldcat.org

Kumar, Ranjeet; Bhakuni, Vinod (2010-10). “A functionally active dimer of mycobacterium tuberculosis malate synthase G”. European biophysics journal: EBJ 39 (11): 1557–1562. doi:10.1007/s00249-010-0598-7. ISSN 1432-1017. PMID 20306314.

worldcat.org

Stryer, Lubert; Berg, Jeremy M.; Tymoczko, John L. (2003). Biochemistry (fifth ed.). New York: Freeman. ISBN 978-0-7167-4684-3. OCLC 48055706