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Phosphoglyceratkinase (German Wikipedia)

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

refsWebsite
Global rank German rank
18nih.gov
4th place
7th place
17doi.org
2nd place
3rd place
2omim.org
4,380th place
781st place
1uniprot.org
5,673rd place
995th place

doi.org

  • A. Dhar, A. Samiotakis, S. Ebbinghaus, L. Nienhaus, D. Homouz, M. Gruebele, M. S. Cheung: Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding. In: Proceedings of the National Academy of Sciences. Band 107, Nummer 41, Oktober 2010, S. 17586–17591, doi:10.1073/pnas.1006760107, PMID 20921368, PMC 2955104 (freier Volltext).
  • S. Kumar, B. Ma, C. J. Tsai, H. Wolfson, R. Nussinov: Folding funnels and conformational transitions via hinge-bending motions. In: Cell biochemistry and biophysics. Band 31, Nummer 2, 1999, S. 141–164, doi:10.1007/BF02738169, PMID 10593256 (Review).
  • L. R. Chiarelli, S. M. Morera, P. Bianchi, E. Fermo, A. Zanella, A. Galizzi, G. Valentini: Molecular insights on pathogenic effects of mutations causing phosphoglycerate kinase deficiency. In: PLOS ONE. Band 7, Nummer 2, 2012, S. e32065, doi:10.1371/journal.pone.0032065, PMID 22348148, PMC 3279470 (freier Volltext).
  • J. M. Yon, M. Desmadril, J. M. Betton, P. Minard, N. Ballery, D. Missiakas, S. Gaillard-Miran, D. Perahia, L. Mouawad: Flexibility and folding of phosphoglycerate kinase. In: Biochimie. Band 72, Nummer 6–7, 1990 Jun-Jul, S. 417–429, doi:10.1016/0300-9084(90)90066-p, PMID 2124145 (Review).
  • L. Zerrad, A. Merli, G. F. Schröder, A. Varga,.. Gráczer, P. Pernot, A. Round, M. Vas, M. W. Bo: A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase. In: Journal of Biological Chemistry. Band 286, Nummer 16, April 2011, S. 14040–14048, doi:10.1074/jbc.M110.206813, PMID 21349853, PMC 3077604 (freier Volltext).
  • A. Varga, Z. Palmai, Z. Gugolya,.. Gráczer, F. Vonderviszt, P. Závodszky, E. Balog, M.: Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase. In: Biochemistry. Band 51, Nummer 51, Dezember 2012, S. 10197–10207, doi:10.1021/bi301194t, PMID 23231058.
  • M. J. Cliff, M. W. Bowler, A. Varga, J. P. Marston, J. Szabó, A. M. Hounslow, N. J. Baxter, G. M. Blackburn, M. Vas, J. P. Waltho: Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis. In: Journal of the American Chemical Society. Band 132, Nummer 18, Mai 2010, S. 6507–6516, doi:10.1021/ja100974t, PMID 20397725.
  • R. D. Banks, C. C. F. Blake, P. R. Evans, R. Haser, D. W. Rice, G. W. Hardy, M. Merrett, A. W. Phillips: Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme. In: Nature. 279, 1979, S. 773, doi:10.1038/279773a0.
  • B. E. Bernstein, W. G. Hol: Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. In: Biochemistry. Band 37, Nummer 13, März 1998, S. 4429–4436, doi:10.1021/bi9724117, PMID 9521762.
  • M. Larsson-Raźnikiewicz: Kinetic studies on the reaction catalyzed by phosphoglycerate kinase. II. The kinetic relationships between 3-phosphoglycerate, MgATP2-and activating metal ion. In: Biochimica et Biophysica Acta. Band 132, Nummer 1, Januar 1967, S. 33–40, doi:10.1016/0005-2744(67)90189-1, PMID 6030358.
  • A. Varga, L. Chaloin, G. Sági, R. Sendula, E. Gráczer, K. Liliom, P. Závodszky, C. Lionne, M. Vas: Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues. In: Molecular bioSystems. Band 7, Nummer 6, Juni 2011, S. 1863–1873, doi:10.1039/c1mb05051f, PMID 21505655.
  • Märtha Larsson-Raźnikiewicz, Eva Wiksell: Inhibition of phosphoglycerate kinase by salicylates. In: Biochimica et Biophysica Acta - Enzymology. 523, 1978, S. 94, doi:10.1016/0005-2744(78)90012-8.
  • E. Beutler: PGK deficiency. In: British Journal of Haematology. Band 136, Nummer 1, Januar 2007, S. 3–11, doi:10.1111/j.1365-2141.2006.06351.x, PMID 17222195 (Review).
  • M. Rhodes, L. Ashford, B. Manes, C. Calder, J. Domm, H. Frangoul: Bone marrow transplantation in phosphoglycerate kinase (PGK) deficiency. In: British Journal of Haematology. Band 152, Nummer 4, Februar 2011, S. 500–502, doi:10.1111/j.1365-2141.2010.08474.x, PMID 21223252.
  • D. Zieker, I. Königsrainer, I. Tritschler, M. Löffler, S. Beckert, F. Traub, K. Nieselt, S. Bühler, M. Weller, J. Gaedcke, R. S. Taichman, H. Northoff, B. L. Brücher, A. Königsrainer: Phosphoglycerate kinase 1 a promoting enzyme for peritoneal dissemination in gastric cancer. In: International Journal of Cancer. Band 126, Nummer 6, März 2010, S. 1513–1520, doi:10.1002/ijc.24835, PMID 19688824, PMC 2811232 (freier Volltext).
  • A. J. Lay, X. M. Jiang, O. Kisker, E. Flynn, A. Underwood, R. Condron, P. J. Hogg: Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. In: Nature. Band 408, Nummer 6814, Dezember 2000, S. 869–873, doi:10.1038/35048596, PMID 11130727.
  • S. Gallois-Montbrun, A. Faraj, E. Seclaman, J. P. Sommadossi, D. Deville-Bonne, M. Véron: Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs. In: Biochemical pharmacology. Band 68, Nummer 9, November 2004, S. 1749–1756, doi:10.1016/j.bcp.2004.06.012, PMID 15450940.

nih.gov

ncbi.nlm.nih.gov

  • J. Wang et al.: A glycolytic mechanism regulating an angiogenic switch in prostate cancer. Cancer Res. 67/1/2007: 149–159; PMID 17210694.
  • A. Dhar, A. Samiotakis, S. Ebbinghaus, L. Nienhaus, D. Homouz, M. Gruebele, M. S. Cheung: Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding. In: Proceedings of the National Academy of Sciences. Band 107, Nummer 41, Oktober 2010, S. 17586–17591, doi:10.1073/pnas.1006760107, PMID 20921368, PMC 2955104 (freier Volltext).
  • S. Kumar, B. Ma, C. J. Tsai, H. Wolfson, R. Nussinov: Folding funnels and conformational transitions via hinge-bending motions. In: Cell biochemistry and biophysics. Band 31, Nummer 2, 1999, S. 141–164, doi:10.1007/BF02738169, PMID 10593256 (Review).
  • L. R. Chiarelli, S. M. Morera, P. Bianchi, E. Fermo, A. Zanella, A. Galizzi, G. Valentini: Molecular insights on pathogenic effects of mutations causing phosphoglycerate kinase deficiency. In: PLOS ONE. Band 7, Nummer 2, 2012, S. e32065, doi:10.1371/journal.pone.0032065, PMID 22348148, PMC 3279470 (freier Volltext).
  • J. M. Yon, M. Desmadril, J. M. Betton, P. Minard, N. Ballery, D. Missiakas, S. Gaillard-Miran, D. Perahia, L. Mouawad: Flexibility and folding of phosphoglycerate kinase. In: Biochimie. Band 72, Nummer 6–7, 1990 Jun-Jul, S. 417–429, doi:10.1016/0300-9084(90)90066-p, PMID 2124145 (Review).
  • L. Zerrad, A. Merli, G. F. Schröder, A. Varga,.. Gráczer, P. Pernot, A. Round, M. Vas, M. W. Bo: A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase. In: Journal of Biological Chemistry. Band 286, Nummer 16, April 2011, S. 14040–14048, doi:10.1074/jbc.M110.206813, PMID 21349853, PMC 3077604 (freier Volltext).
  • A. Varga, Z. Palmai, Z. Gugolya,.. Gráczer, F. Vonderviszt, P. Závodszky, E. Balog, M.: Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase. In: Biochemistry. Band 51, Nummer 51, Dezember 2012, S. 10197–10207, doi:10.1021/bi301194t, PMID 23231058.
  • M. J. Cliff, M. W. Bowler, A. Varga, J. P. Marston, J. Szabó, A. M. Hounslow, N. J. Baxter, G. M. Blackburn, M. Vas, J. P. Waltho: Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis. In: Journal of the American Chemical Society. Band 132, Nummer 18, Mai 2010, S. 6507–6516, doi:10.1021/ja100974t, PMID 20397725.
  • B. E. Bernstein, W. G. Hol: Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. In: Biochemistry. Band 37, Nummer 13, März 1998, S. 4429–4436, doi:10.1021/bi9724117, PMID 9521762.
  • M. Larsson-Raźnikiewicz: Kinetic studies on the reaction catalyzed by phosphoglycerate kinase. II. The kinetic relationships between 3-phosphoglycerate, MgATP2-and activating metal ion. In: Biochimica et Biophysica Acta. Band 132, Nummer 1, Januar 1967, S. 33–40, doi:10.1016/0005-2744(67)90189-1, PMID 6030358.
  • A. Varga, L. Chaloin, G. Sági, R. Sendula, E. Gráczer, K. Liliom, P. Závodszky, C. Lionne, M. Vas: Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues. In: Molecular bioSystems. Band 7, Nummer 6, Juni 2011, S. 1863–1873, doi:10.1039/c1mb05051f, PMID 21505655.
  • A. Yoshida, K. Tani: Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects. In: Biomedica biochimica acta. Band 42, Nummer 11–12, 1983, S. S263–S267, PMID 6689547.
  • E. Beutler: PGK deficiency. In: British Journal of Haematology. Band 136, Nummer 1, Januar 2007, S. 3–11, doi:10.1111/j.1365-2141.2006.06351.x, PMID 17222195 (Review).
  • M. Rhodes, L. Ashford, B. Manes, C. Calder, J. Domm, H. Frangoul: Bone marrow transplantation in phosphoglycerate kinase (PGK) deficiency. In: British Journal of Haematology. Band 152, Nummer 4, Februar 2011, S. 500–502, doi:10.1111/j.1365-2141.2010.08474.x, PMID 21223252.
  • D. Zieker, I. Königsrainer, I. Tritschler, M. Löffler, S. Beckert, F. Traub, K. Nieselt, S. Bühler, M. Weller, J. Gaedcke, R. S. Taichman, H. Northoff, B. L. Brücher, A. Königsrainer: Phosphoglycerate kinase 1 a promoting enzyme for peritoneal dissemination in gastric cancer. In: International Journal of Cancer. Band 126, Nummer 6, März 2010, S. 1513–1520, doi:10.1002/ijc.24835, PMID 19688824, PMC 2811232 (freier Volltext).
  • A. J. Lay, X. M. Jiang, O. Kisker, E. Flynn, A. Underwood, R. Condron, P. J. Hogg: Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. In: Nature. Band 408, Nummer 6814, Dezember 2000, S. 869–873, doi:10.1038/35048596, PMID 11130727.
  • S. Gallois-Montbrun, A. Faraj, E. Seclaman, J. P. Sommadossi, D. Deville-Bonne, M. Véron: Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs. In: Biochemical pharmacology. Band 68, Nummer 9, November 2004, S. 1749–1756, doi:10.1016/j.bcp.2004.06.012, PMID 15450940.

ghr.nlm.nih.gov

omim.org

uniprot.org