(en) « Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase », Biochemistry, vol. 51, no 51, , p. 10197-10207 (PMID23231058, DOI10.1021/bi301194t, lire en ligne)
(en) Matthew J. Cliff, Matthew W. Bowler, Andrea Varga, James P. Marston, Judit Szabó, Andrea M. Hounslow, Nicola J. Baxter, G. Michael Blackburn, Mária Vas et Jonathan P. Waltho, « Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis », Journal of the American Chemical Society, vol. 132, no 18, , p. 6507-6516 (PMID20397725, DOI10.1021/ja100974t, lire en ligne)
doi.org
dx.doi.org
(en) Laurent R. Chiarelli, Simone M. Morera, Paola Bianchi, Elisa Fermo, Alberto Zanella, Alessandro Galizzi et Giovanna Valentini, « Molecular Insights on Pathogenic Effects of Mutations Causing Phosphoglycerate Kinase Deficiency », PLoS One, vol. 7, no 2, , e32065 (PMID22348148, PMCID3279470, DOI10.1371/journal.pone.0032065, lire en ligne)
(en) Apratim Dhar, Antonios Samiotakis, Simon Ebbinghaus, Lea Nienhaus, Dirar Homouz, Martin Gruebele et Margaret S. Cheung, « Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 41, , p. 17586-17591 (PMID20921368, PMCID2955104, DOI10.1073/pnas.1006760107, JSTOR20780502, lire en ligne)
(en) Sandeep Kumar, Buyong Ma, Chung-Jung Tsai, Haim Wolfson et Ruth Nussinov, « Folding funnels and conformational transitions via hinge-bending motions », Cell Biochemistry and Biophysics, vol. 31, no 2, , p. 141-164 (PMID10593256, DOI10.1007/BF02738169, lire en ligne)
(en) J. M. Yon, M. Desmadril, J. M. Betton, P. Minard, N. Ballery, D. Missiakas, Gaillard-Miran S., D. Perahia et L. Mouawad, « Flexibility and folding of phosphoglycerate kinase », Biochimie, vol. 72, nos 6-7, , p. 417-429 (PMID2124145, DOI10.1016/0300-9084(90)90066-P, lire en ligne)
(en) Louiza Zerrad, Angelo Merli, Gunnar F. Schröder, Andrea Varga, Éva Gráczer, Petra Pernot, Adam Round, Mária Vas et Matthew W. Bowler, « A Spring-loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase », Journal of Biological Chemistry, vol. 286, no 16, , p. 14040-14048 (PMID21349853, DOI10.1074/jbc.M110.206813, lire en ligne)
(en) « Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase », Biochemistry, vol. 51, no 51, , p. 10197-10207 (PMID23231058, DOI10.1021/bi301194t, lire en ligne)
(en) Matthew J. Cliff, Matthew W. Bowler, Andrea Varga, James P. Marston, Judit Szabó, Andrea M. Hounslow, Nicola J. Baxter, G. Michael Blackburn, Mária Vas et Jonathan P. Waltho, « Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis », Journal of the American Chemical Society, vol. 132, no 18, , p. 6507-6516 (PMID20397725, DOI10.1021/ja100974t, lire en ligne)
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jbc.org
(en) Louiza Zerrad, Angelo Merli, Gunnar F. Schröder, Andrea Varga, Éva Gráczer, Petra Pernot, Adam Round, Mária Vas et Matthew W. Bowler, « A Spring-loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase », Journal of Biological Chemistry, vol. 286, no 16, , p. 14040-14048 (PMID21349853, DOI10.1074/jbc.M110.206813, lire en ligne)
jstor.org
(en) Apratim Dhar, Antonios Samiotakis, Simon Ebbinghaus, Lea Nienhaus, Dirar Homouz, Martin Gruebele et Margaret S. Cheung, « Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 41, , p. 17586-17591 (PMID20921368, PMCID2955104, DOI10.1073/pnas.1006760107, JSTOR20780502, lire en ligne)
nih.gov
ncbi.nlm.nih.gov
(en) H. C. Watson, N. P. Walker, P. J. Shaw, T. N. Bryant, P. L. Wendell, L. A. Fothergill, R. E. Perkins, S. C. Conroy, M. J. Dobson et M. F. Tuite, « Sequence and structure of yeast phosphoglycerate kinase », The EMBO Journal, vol. 1, no 12, , p. 1635-1640 (PMID6765200, PMCID553262, lire en ligne)
(en) Laurent R. Chiarelli, Simone M. Morera, Paola Bianchi, Elisa Fermo, Alberto Zanella, Alessandro Galizzi et Giovanna Valentini, « Molecular Insights on Pathogenic Effects of Mutations Causing Phosphoglycerate Kinase Deficiency », PLoS One, vol. 7, no 2, , e32065 (PMID22348148, PMCID3279470, DOI10.1371/journal.pone.0032065, lire en ligne)
(en) Apratim Dhar, Antonios Samiotakis, Simon Ebbinghaus, Lea Nienhaus, Dirar Homouz, Martin Gruebele et Margaret S. Cheung, « Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 41, , p. 17586-17591 (PMID20921368, PMCID2955104, DOI10.1073/pnas.1006760107, JSTOR20780502, lire en ligne)
(en) Sandeep Kumar, Buyong Ma, Chung-Jung Tsai, Haim Wolfson et Ruth Nussinov, « Folding funnels and conformational transitions via hinge-bending motions », Cell Biochemistry and Biophysics, vol. 31, no 2, , p. 141-164 (PMID10593256, DOI10.1007/BF02738169, lire en ligne)
(en) J. M. Yon, M. Desmadril, J. M. Betton, P. Minard, N. Ballery, D. Missiakas, Gaillard-Miran S., D. Perahia et L. Mouawad, « Flexibility and folding of phosphoglycerate kinase », Biochimie, vol. 72, nos 6-7, , p. 417-429 (PMID2124145, DOI10.1016/0300-9084(90)90066-P, lire en ligne)
(en) Louiza Zerrad, Angelo Merli, Gunnar F. Schröder, Andrea Varga, Éva Gráczer, Petra Pernot, Adam Round, Mária Vas et Matthew W. Bowler, « A Spring-loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase », Journal of Biological Chemistry, vol. 286, no 16, , p. 14040-14048 (PMID21349853, DOI10.1074/jbc.M110.206813, lire en ligne)
(en) « Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase », Biochemistry, vol. 51, no 51, , p. 10197-10207 (PMID23231058, DOI10.1021/bi301194t, lire en ligne)
(en) Matthew J. Cliff, Matthew W. Bowler, Andrea Varga, James P. Marston, Judit Szabó, Andrea M. Hounslow, Nicola J. Baxter, G. Michael Blackburn, Mária Vas et Jonathan P. Waltho, « Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis », Journal of the American Chemical Society, vol. 132, no 18, , p. 6507-6516 (PMID20397725, DOI10.1021/ja100974t, lire en ligne)
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plos.org
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(en) Laurent R. Chiarelli, Simone M. Morera, Paola Bianchi, Elisa Fermo, Alberto Zanella, Alessandro Galizzi et Giovanna Valentini, « Molecular Insights on Pathogenic Effects of Mutations Causing Phosphoglycerate Kinase Deficiency », PLoS One, vol. 7, no 2, , e32065 (PMID22348148, PMCID3279470, DOI10.1371/journal.pone.0032065, lire en ligne)
pnas.org
(en) Apratim Dhar, Antonios Samiotakis, Simon Ebbinghaus, Lea Nienhaus, Dirar Homouz, Martin Gruebele et Margaret S. Cheung, « Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 41, , p. 17586-17591 (PMID20921368, PMCID2955104, DOI10.1073/pnas.1006760107, JSTOR20780502, lire en ligne)
sciencedirect.com
(en) J. M. Yon, M. Desmadril, J. M. Betton, P. Minard, N. Ballery, D. Missiakas, Gaillard-Miran S., D. Perahia et L. Mouawad, « Flexibility and folding of phosphoglycerate kinase », Biochimie, vol. 72, nos 6-7, , p. 417-429 (PMID2124145, DOI10.1016/0300-9084(90)90066-P, lire en ligne)
springer.com
link.springer.com
(en) Sandeep Kumar, Buyong Ma, Chung-Jung Tsai, Haim Wolfson et Ruth Nussinov, « Folding funnels and conformational transitions via hinge-bending motions », Cell Biochemistry and Biophysics, vol. 31, no 2, , p. 141-164 (PMID10593256, DOI10.1007/BF02738169, lire en ligne)