"Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase". Biochemistry. 51 (51): 10197–207. December 2012. doi:10.1021/bi301194t. PMID23231058.
"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. May 2010. doi:10.1021/ja100974t. PMID20397725.
Banks, R. D.; Blake, C. C. F.; Evans, P. R.; Haser, R.; Rice, D. W.; Hardy, G. W.; Merrett, M.; Phillips, A. W. (28 June 1979). "Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme". Nature. 279 (5716): 773–777. Bibcode:1979Natur.279..773B. doi:10.1038/279773a0. PMID450128.
"Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry. 37 (13): 4429–36. March 1998. doi:10.1021/bi9724117. PMID9521762.
"Kinetic studies on the reaction catalyzed by phosphoglycerate kinase. II. The kinetic relationships between 3-phosphoglycerate, MgATP2-and activating metal ion". Biochimica et Biophysica Acta (BBA) - Enzymology. 132 (1): 33–40. Jan 1967. doi:10.1016/0005-2744(67)90189-1. PMID6030358.
"Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Molecular BioSystems. 7 (6): 1863–73. June 2011. doi:10.1039/c1mb05051f. PMID21505655.
Larsson-Raźnikiewicz, Märtha; Wiksell, Eva (1 March 1978). "Inhibition of phosphoglycerate kinase by salicylates". Biochimica et Biophysica Acta (BBA) - Enzymology. 523 (1): 94–100. doi:10.1016/0005-2744(78)90012-8. PMID343818.
"Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology. 68 (9): 1749–56. November 2004. doi:10.1016/j.bcp.2004.06.012. PMID15450940.
Banks, R. D.; Blake, C. C. F.; Evans, P. R.; Haser, R.; Rice, D. W.; Hardy, G. W.; Merrett, M.; Phillips, A. W. (28 June 1979). "Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme". Nature. 279 (5716): 773–777. Bibcode:1979Natur.279..773B. doi:10.1038/279773a0. PMID450128.
"Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase". Biochemistry. 51 (51): 10197–207. December 2012. doi:10.1021/bi301194t. PMID23231058.
"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. May 2010. doi:10.1021/ja100974t. PMID20397725.
Banks, R. D.; Blake, C. C. F.; Evans, P. R.; Haser, R.; Rice, D. W.; Hardy, G. W.; Merrett, M.; Phillips, A. W. (28 June 1979). "Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme". Nature. 279 (5716): 773–777. Bibcode:1979Natur.279..773B. doi:10.1038/279773a0. PMID450128.
"Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry. 37 (13): 4429–36. March 1998. doi:10.1021/bi9724117. PMID9521762.
"Kinetic studies on the reaction catalyzed by phosphoglycerate kinase. II. The kinetic relationships between 3-phosphoglycerate, MgATP2-and activating metal ion". Biochimica et Biophysica Acta (BBA) - Enzymology. 132 (1): 33–40. Jan 1967. doi:10.1016/0005-2744(67)90189-1. PMID6030358.
"Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Molecular BioSystems. 7 (6): 1863–73. June 2011. doi:10.1039/c1mb05051f. PMID21505655.
Larsson-Raźnikiewicz, Märtha; Wiksell, Eva (1 March 1978). "Inhibition of phosphoglycerate kinase by salicylates". Biochimica et Biophysica Acta (BBA) - Enzymology. 523 (1): 94–100. doi:10.1016/0005-2744(78)90012-8. PMID343818.
"Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology. 68 (9): 1749–56. November 2004. doi:10.1016/j.bcp.2004.06.012. PMID15450940.