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Énolase (French Wikipedia)

Analysis of information sources in references of the Wikipedia article "Énolase" in French language version.

refsWebsite
Global rank French rank
15nih.gov
4th place
12th place
12doi.org
2nd place
3rd place
1acs.org
1,248th place
778th place
1springer.de
low place
8,714th place
1elsevier.com
610th place
265th place
1asm.org
3,555th place
1,209th place

acs.org

pubs.acs.org

  • (en) Todd M. Larsen, Joseph E. Wedekind, Ivan Rayment et George H. Reed, « A Carboxylate Oxygen of the Substrate Bridges the Magnesium Ions at the Active Site of Enolase:  Structure of the Yeast Enzyme Complexed with the Equilibrium Mixture of 2-Phosphoglycerate and Phosphoenolpyruvate at 1.8 Å Resolution », Biochemistry, vol. 35, no 14,‎ , p. 4349-4358 (PMID 8605183, DOI 10.1021/bi952859c, lire en ligne)

asm.org

iai.asm.org

  • (en) Hüther FJ, Psarros N, Duschner H, « Isolation, characterization, and inhibition kinetics of enolase from Streptococcus rattus FA-1 », Infect Immun., vol. 58, no 4,‎ , p. 1043–7 (PMID 2318530, PMCID 258580, lire en ligne)

doi.org

dx.doi.org

  • (en) Todd M. Larsen, Joseph E. Wedekind, Ivan Rayment et George H. Reed, « A Carboxylate Oxygen of the Substrate Bridges the Magnesium Ions at the Active Site of Enolase:  Structure of the Yeast Enzyme Complexed with the Equilibrium Mixture of 2-Phosphoglycerate and Phosphoenolpyruvate at 1.8 Å Resolution », Biochemistry, vol. 35, no 14,‎ , p. 4349-4358 (PMID 8605183, DOI 10.1021/bi952859c, lire en ligne)
  • (en) Pancholi V, « Multifunctional α-enolase: its role in diseases », Cell Mol Life Sci., vol. 58, no 7,‎ , p. 902–20 (PMID 11497239, DOI 10.1007/PL00000910, lire en ligne)
  • (en) Hoorn RK, Flickweert JP, Staal GE, « Purification and properties of enolase of human erythroctyes », Int J Biochem, vol. 5, nos 11–12,‎ , p. 845–52 (DOI 10.1016/0020-711X(74)90119-0)
  • (en) Poyner RR, Laughlin LT, Sowa GA, Reed GH, « Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants », Biochemistry, vol. 35, no 5,‎ , p. 1692–9 (PMID 8634301, DOI 10.1021/bi952186y)
  • (en) Reed GH, Poyner RR, Larsen TM, Wedekind JE, Rayment I, « Structural and mechanistic studies of enolase », Curr Opin Struct Biol., vol. 6, no 6,‎ , p. 736–43 (PMID 8994873, DOI 10.1016/S0959-440X(96)80002-9, lire en ligne)
  • (en) Wedekind JE, Reed GH, Rayment I, « Octahedral coordination at the high-affinity metal site in enolase: crystallographic analysis of the MgII—enzyme complex from yeast at 1.9 Å resolution », Biochemistry, vol. 34, no 13,‎ , p. 4325–30 (PMID 7703246, DOI 10.1021/bi00013a022)
  • (en) Wedekind JE, Poyner RR, Reed GH, Rayment I, « Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-Å resolution », Biochemistry, vol. 33, no 31,‎ , p. 9333–42 (PMID 8049235, DOI 10.1021/bi00197a038)
  • (en) Larsen TM, Wedekind JE, Rayment I, Reed GH, « A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 Å resolution », Biochemistry, vol. 35, no 14,‎ , p. 4349–58 (PMID 8605183, DOI 10.1021/bi952859c)
  • (en) Duquerroy S, Camus C, Janin J, « X-ray structure and catalytic mechanism of lobster enolase », Biochemistry, vol. 34, no 39,‎ , p. 12513–23 (PMID 7547999, DOI 10.1021/bi00039a005)
  • (en) Royds JA, Timperley WR, Taylor CB, « Levels of enolase and other enzymes in the cerebrospinal fluid as indices of pathological change », J Neurol Neurosurg Psychiatr., vol. 44, no 12,‎ , p. 1129–35 (PMID 7334408, PMCID 491233, DOI 10.1136/jnnp.44.12.1129)
  • (en) Hay E, Royds JA, Davies-Jones GA, Lewtas NA, Timperley WR, Taylor CB, « Cerebrospinal fluid enolase in stroke », J Neurol Neurosurg Psychiatr., vol. 47, no 7,‎ , p. 724–9 (PMID 6747647, PMCID 1027902, DOI 10.1136/jnnp.47.7.724)
  • (en) Fujii A, Yoneda M, Ito T, Yamamura O, Satomi S, Higa H, Kimura A, Suzuki M, Yamashita M, Yuasa T, Suzuki H, Kuriyama M, « Autoantibodies against the amino terminal of alpha-enolase are a useful diagnostic marker of Hashimoto's encephalopathy », J. Neuroimmunol., vol. 162, nos 1–2,‎ , p. 130–6 (PMID 15833368, DOI 10.1016/j.jneuroim.2005.02.004)

elsevier.com

linkinghub.elsevier.com

nih.gov

ncbi.nlm.nih.gov

  • (en) Todd M. Larsen, Joseph E. Wedekind, Ivan Rayment et George H. Reed, « A Carboxylate Oxygen of the Substrate Bridges the Magnesium Ions at the Active Site of Enolase:  Structure of the Yeast Enzyme Complexed with the Equilibrium Mixture of 2-Phosphoglycerate and Phosphoenolpyruvate at 1.8 Å Resolution », Biochemistry, vol. 35, no 14,‎ , p. 4349-4358 (PMID 8605183, DOI 10.1021/bi952859c, lire en ligne)
  • (en) Pancholi V, « Multifunctional α-enolase: its role in diseases », Cell Mol Life Sci., vol. 58, no 7,‎ , p. 902–20 (PMID 11497239, DOI 10.1007/PL00000910, lire en ligne)
  • (en) Peshavaria M, Day IN, « Molecular structure of the human muscle-specific enolase gene (ENO3) », Biochem J., vol. 275 (Pt 2), no Pt 2,‎ , p. 427–33 (PMID 1840492, PMCID 1150071)
  • (en) Poyner RR, Laughlin LT, Sowa GA, Reed GH, « Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants », Biochemistry, vol. 35, no 5,‎ , p. 1692–9 (PMID 8634301, DOI 10.1021/bi952186y)
  • (en) Reed GH, Poyner RR, Larsen TM, Wedekind JE, Rayment I, « Structural and mechanistic studies of enolase », Curr Opin Struct Biol., vol. 6, no 6,‎ , p. 736–43 (PMID 8994873, DOI 10.1016/S0959-440X(96)80002-9, lire en ligne)
  • (en) Wedekind JE, Reed GH, Rayment I, « Octahedral coordination at the high-affinity metal site in enolase: crystallographic analysis of the MgII—enzyme complex from yeast at 1.9 Å resolution », Biochemistry, vol. 34, no 13,‎ , p. 4325–30 (PMID 7703246, DOI 10.1021/bi00013a022)
  • (en) Wedekind JE, Poyner RR, Reed GH, Rayment I, « Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-Å resolution », Biochemistry, vol. 33, no 31,‎ , p. 9333–42 (PMID 8049235, DOI 10.1021/bi00197a038)
  • (en) Larsen TM, Wedekind JE, Rayment I, Reed GH, « A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 Å resolution », Biochemistry, vol. 35, no 14,‎ , p. 4349–58 (PMID 8605183, DOI 10.1021/bi952859c)
  • (en) Duquerroy S, Camus C, Janin J, « X-ray structure and catalytic mechanism of lobster enolase », Biochemistry, vol. 34, no 39,‎ , p. 12513–23 (PMID 7547999, DOI 10.1021/bi00039a005)
  • (en) Royds JA, Timperley WR, Taylor CB, « Levels of enolase and other enzymes in the cerebrospinal fluid as indices of pathological change », J Neurol Neurosurg Psychiatr., vol. 44, no 12,‎ , p. 1129–35 (PMID 7334408, PMCID 491233, DOI 10.1136/jnnp.44.12.1129)
  • (en) Roine RO, Somer H, Kaste M, Viinikka L, Karonen SL, « Neurological outcome after out-of-hospital cardiac arrest. Prediction by cerebrospinal fluid enzyme analysis », Arch Neurol., vol. 46, no 7,‎ , p. 753–6 (PMID 2742544)
  • (en) Hay E, Royds JA, Davies-Jones GA, Lewtas NA, Timperley WR, Taylor CB, « Cerebrospinal fluid enolase in stroke », J Neurol Neurosurg Psychiatr., vol. 47, no 7,‎ , p. 724–9 (PMID 6747647, PMCID 1027902, DOI 10.1136/jnnp.47.7.724)
  • (en) Fujii A, Yoneda M, Ito T, Yamamura O, Satomi S, Higa H, Kimura A, Suzuki M, Yamashita M, Yuasa T, Suzuki H, Kuriyama M, « Autoantibodies against the amino terminal of alpha-enolase are a useful diagnostic marker of Hashimoto's encephalopathy », J. Neuroimmunol., vol. 162, nos 1–2,‎ , p. 130–6 (PMID 15833368, DOI 10.1016/j.jneuroim.2005.02.004)
  • (en) Centers For Disease Control, « Populations receiving optimally fluoridated public drinking water—United States, 2000 », MMWR Morb Mortal Wkly Rep., vol. 51, no 7,‎ , p. 144–7 (PMID 11905481)
  • (en) Hüther FJ, Psarros N, Duschner H, « Isolation, characterization, and inhibition kinetics of enolase from Streptococcus rattus FA-1 », Infect Immun., vol. 58, no 4,‎ , p. 1043–7 (PMID 2318530, PMCID 258580, lire en ligne)

springer.de

link.springer.de