Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M. Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase. Biochemistry. December 2012, 51 (51): 10197–207. PMID 23231058. doi:10.1021/bi301194t.Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M (December 2012). "Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase". Biochemistry. 51 (51): 10197–207. doi:10.1021/bi301194t. PMID23231058 (页面存档备份,存于互联网档案馆).
Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP. Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis. Journal of the American Chemical Society. May 2010, 132 (18): 6507–16. PMID 20397725. doi:10.1021/ja100974t.Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP (May 2010). "Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis". Journal of the American Chemical Society. 132 (18): 6507–16. doi:10.1021/ja100974t. PMID20397725 (页面存档备份,存于互联网档案馆).
Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M. Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues. Molecular BioSystems. June 2011, 7 (6): 1863–73. PMID 21505655. doi:10.1039/c1mb05051f.Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M (June 2011). "Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Molecular BioSystems. 7 (6): 1863–73. doi:10.1039/c1mb05051f. PMID21505655 (页面存档备份,存于互联网档案馆).
Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M. Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs. Biochemical Pharmacology. November 2004, 68 (9): 1749–56. PMID 15450940. doi:10.1016/j.bcp.2004.06.012.Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M (November 2004). "Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology. 68 (9): 1749–56. doi:10.1016/j.bcp.2004.06.012. PMID15450940 (页面存档备份,存于互联网档案馆).
Bernstein BE, Hol WG. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry. March 1998, 37 (13): 4429–36. PMID 9521762. doi:10.1021/bi9724117.Bernstein BE, Hol WG (March 1998). "Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry. 37 (13): 4429–36. doi:10.1021/bi9724117. PMID9521762 (页面存档备份,存于互联网档案馆).
Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M. Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase. Biochemistry. December 2012, 51 (51): 10197–207. PMID 23231058. doi:10.1021/bi301194t.Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M (December 2012). "Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase". Biochemistry. 51 (51): 10197–207. doi:10.1021/bi301194t. PMID23231058 (页面存档备份,存于互联网档案馆).
Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP. Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis. Journal of the American Chemical Society. May 2010, 132 (18): 6507–16. PMID 20397725. doi:10.1021/ja100974t.Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP (May 2010). "Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis". Journal of the American Chemical Society. 132 (18): 6507–16. doi:10.1021/ja100974t. PMID20397725 (页面存档备份,存于互联网档案馆).
Yoshida A, Tani K. Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects. Biomedica Biochimica Acta. 1983, 42 (11–12): S263-7. PMID 6689547.Yoshida A, Tani K (1983). "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects". Biomedica Biochimica Acta. 42 (11–12): S263-7. PMID6689547 (页面存档备份,存于互联网档案馆).
Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M. Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues. Molecular BioSystems. June 2011, 7 (6): 1863–73. PMID 21505655. doi:10.1039/c1mb05051f.Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M (June 2011). "Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Molecular BioSystems. 7 (6): 1863–73. doi:10.1039/c1mb05051f. PMID21505655 (页面存档备份,存于互联网档案馆).
Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M. Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs. Biochemical Pharmacology. November 2004, 68 (9): 1749–56. PMID 15450940. doi:10.1016/j.bcp.2004.06.012.Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M (November 2004). "Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology. 68 (9): 1749–56. doi:10.1016/j.bcp.2004.06.012. PMID15450940 (页面存档备份,存于互联网档案馆).
Bernstein BE, Hol WG. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry. March 1998, 37 (13): 4429–36. PMID 9521762. doi:10.1021/bi9724117.Bernstein BE, Hol WG (March 1998). "Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry. 37 (13): 4429–36. doi:10.1021/bi9724117. PMID9521762 (页面存档备份,存于互联网档案馆).
Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M. Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase. Biochemistry. December 2012, 51 (51): 10197–207. PMID 23231058. doi:10.1021/bi301194t.Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M (December 2012). "Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase". Biochemistry. 51 (51): 10197–207. doi:10.1021/bi301194t. PMID23231058 (页面存档备份,存于互联网档案馆).
Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP. Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis. Journal of the American Chemical Society. May 2010, 132 (18): 6507–16. PMID 20397725. doi:10.1021/ja100974t.Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP (May 2010). "Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis". Journal of the American Chemical Society. 132 (18): 6507–16. doi:10.1021/ja100974t. PMID20397725 (页面存档备份,存于互联网档案馆).
Yoshida A, Tani K. Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects. Biomedica Biochimica Acta. 1983, 42 (11–12): S263-7. PMID 6689547.Yoshida A, Tani K (1983). "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects". Biomedica Biochimica Acta. 42 (11–12): S263-7. PMID6689547 (页面存档备份,存于互联网档案馆).
Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M. Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues. Molecular BioSystems. June 2011, 7 (6): 1863–73. PMID 21505655. doi:10.1039/c1mb05051f.Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M (June 2011). "Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Molecular BioSystems. 7 (6): 1863–73. doi:10.1039/c1mb05051f. PMID21505655 (页面存档备份,存于互联网档案馆).
Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M. Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs. Biochemical Pharmacology. November 2004, 68 (9): 1749–56. PMID 15450940. doi:10.1016/j.bcp.2004.06.012.Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M (November 2004). "Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology. 68 (9): 1749–56. doi:10.1016/j.bcp.2004.06.012. PMID15450940 (页面存档备份,存于互联网档案馆).
Bernstein BE, Hol WG. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry. March 1998, 37 (13): 4429–36. PMID 9521762. doi:10.1021/bi9724117.Bernstein BE, Hol WG (March 1998). "Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry. 37 (13): 4429–36. doi:10.1021/bi9724117. PMID9521762 (页面存档备份,存于互联网档案馆).
Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M. Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase. Biochemistry. December 2012, 51 (51): 10197–207. PMID 23231058. doi:10.1021/bi301194t.Varga A, Palmai Z, Gugolya Z, Gráczer É, Vonderviszt F, Závodszky P, Balog E, Vas M (December 2012). "Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase". Biochemistry. 51 (51): 10197–207. doi:10.1021/bi301194t. PMID23231058 (页面存档备份,存于互联网档案馆).
Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP. Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis. Journal of the American Chemical Society. May 2010, 132 (18): 6507–16. PMID 20397725. doi:10.1021/ja100974t.Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M, Waltho JP (May 2010). "Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis". Journal of the American Chemical Society. 132 (18): 6507–16. doi:10.1021/ja100974t. PMID20397725 (页面存档备份,存于互联网档案馆).
Yoshida A, Tani K. Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects. Biomedica Biochimica Acta. 1983, 42 (11–12): S263-7. PMID 6689547.Yoshida A, Tani K (1983). "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects". Biomedica Biochimica Acta. 42 (11–12): S263-7. PMID6689547 (页面存档备份,存于互联网档案馆).
Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M. Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues. Molecular BioSystems. June 2011, 7 (6): 1863–73. PMID 21505655. doi:10.1039/c1mb05051f.Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C, Vas M (June 2011). "Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Molecular BioSystems. 7 (6): 1863–73. doi:10.1039/c1mb05051f. PMID21505655 (页面存档备份,存于互联网档案馆).
Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M. Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs. Biochemical Pharmacology. November 2004, 68 (9): 1749–56. PMID 15450940. doi:10.1016/j.bcp.2004.06.012.Gallois-Montbrun S, Faraj A, Seclaman E, Sommadossi JP, Deville-Bonne D, Véron M (November 2004). "Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology. 68 (9): 1749–56. doi:10.1016/j.bcp.2004.06.012. PMID15450940 (页面存档备份,存于互联网档案馆).
Bernstein BE, Hol WG. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry. March 1998, 37 (13): 4429–36. PMID 9521762. doi:10.1021/bi9724117.Bernstein BE, Hol WG (March 1998). "Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry. 37 (13): 4429–36. doi:10.1021/bi9724117. PMID9521762 (页面存档备份,存于互联网档案馆).