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Sérotonine N-acétyltransférase (French Wikipedia)

Analysis of information sources in references of the Wikipedia article "Sérotonine N-acétyltransférase" in French language version.

refsWebsite
Global rank French rank
24nih.gov
4th place
12th place
22doi.org
2nd place
3rd place
3semanticscholar.org
11th place
325th place
1qmul.ac.uk
1,735th place
168th place
1brenda-enzymes.org
low place
low place
1rcsb.org
8,838th place
low place
1harvard.edu
18th place
118th place

brenda-enzymes.org

doi.org

dx.doi.org

  • « The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression », Genomics, vol. 34, no 1,‎ , p. 76–84 (PMID 8661026, DOI 10.1006/geno.1996.0243)
  • « Serotonin N-acetyltransferase: mechanism and inhibition », Curr. Med. Chem., vol. 9, no 12,‎ , p. 1187–99 (PMID 12052171, DOI 10.2174/0929867023370013)
  • J. De Angelis, J. Gastel, D. C. Klein et P. A. Cole, « Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87) », The Journal of Biological Chemistry, vol. 273, no 5,‎ , p. 3045–3050 (PMID 9446620, DOI 10.1074/jbc.273.5.3045)
  • « The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog », Cell, vol. 97, no 3,‎ , p. 361–9 (PMID 10319816, DOI 10.1016/S0092-8674(00)80745-X, S2CID 18272015)
  • « Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism », Mol. Cell, vol. 3, no 1,‎ , p. 23–32 (PMID 10024876, DOI 10.1016/S1097-2765(00)80171-9)
  • « Investigation of the roles of catalytic residues in serotonin N-acetyltransferase », J. Biol. Chem., vol. 277, no 20,‎ , p. 18118–26 (PMID 11884405, DOI 10.1074/jbc.M200595200).
  • « Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation », Cell, vol. 105, no 2,‎ , p. 257–67 (PMID 11336675, DOI 10.1016/S0092-8674(01)00316-6, S2CID 9564413)
  • Matthew W. Vetting, Luiz Pedro S. de Carvalho, Michael Yu et Subray S. Hegde, « Structure and functions of the GNAT superfamily of acetyltransferases », Archives of Biochemistry and Biophysics, vol. 433, no 1,‎ , p. 212–226 (PMID 15581578, DOI 10.1016/j.abb.2004.09.003)
  • « cAmp regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation », J. Biol. Chem., vol. 276, no 26,‎ , p. 24097–107 (PMID 11313340, DOI 10.1074/jbc.M011298200)
  • « Rhythmic serotonin N-acetyltransferase mRNA degradation is essential for the maintenance of its circadian oscillation », Mol. Cell. Biol., vol. 25, no 8,‎ , p. 3232–46 (PMID 15798208, PMCID 1069600, DOI 10.1128/MCB.25.8.3232-3246.2005)
  • « Analysis of serotonin N-acetyltransferase regulation in vitro and in live cells using protein semisynthesis », Biochemistry, vol. 47, no 39,‎ , p. 10407–19 (PMID 18771288, PMCID 2682328, DOI 10.1021/bi801189d)
  • « Protein kinase C regulates the activity and stability of serotonin N-acetyltransferase », J. Neurochem., vol. 90, no 2,‎ , p. 442–54 (PMID 15228600, DOI 10.1111/j.1471-4159.2004.02495.x, S2CID 42638894)
  • « An intramolecular disulfide bridge as a catalytic switch for serotonin N-acetyltransferase », J. Biol. Chem., vol. 277, no 46,‎ , p. 44229–35 (PMID 12215431, DOI 10.1074/jbc.M203305200)
  • Lawrence M. Szewczuk, S. Adrian Saldanha, Surajit Ganguly et Erin M. Bowers, « De novo discovery of serotonin N-acetyltransferase inhibitors », Journal of Medicinal Chemistry, vol. 50, no 22,‎ , p. 5330–5338 (PMID 17924613, PMCID 2531295, DOI 10.1021/jm0706463)
  • « New substrate analogues of human serotonin N-acetyltransferase produce in situ specific and potent inhibitors », Eur. J. Biochem., vol. 271, no 2,‎ , p. 418–28 (PMID 14717709, DOI 10.1046/j.1432-1033.2003.03942.x)
  • « Novel bisubstrate analog inhibitors of serotonin N-acetyltransferase: the importance of being neutral », Bioorg. Chem., vol. 31, no 5,‎ , p. 398–411 (PMID 12941292, DOI 10.1016/S0045-2068(03)00081-6)
  • « Receptor- and ligand-based study on novel 2,2'-bithienyl derivatives as non-peptidic AANAT inhibitors », J Chem Inf Model, vol. 50, no 3,‎ , p. 446–60 (PMID 20196559, DOI 10.1021/ci9004805)
  • « Structure-activity relationships for substrates and inhibitors of pineal 5-hydroxytryptamine-N-acetyltransferase: preliminary studies », Eur. J. Pharmacol., vol. 307, no 2,‎ , p. 133–40 (PMID 8832214, DOI 10.1016/0014-2999(96)00228-2)
  • « Substrate specificity and inhibition studies of human serotonin N-acetyltransferase », J. Biol. Chem., vol. 275, no 12,‎ , p. 8794–805 (PMID 10722724, DOI 10.1074/jbc.275.12.8794)
  • Khalil et Philip A. Cole, « A Potent Inhibitor of the Melatonin Rhythm Enzyme », J. Am. Chem. Soc., vol. 120, no 24,‎ , p. 6195–6196 (DOI 10.1021/ja981365a)
  • « Mechanism-based inhibition of the melatonin rhythm enzyme: pharmacologic exploitation of active site functional plasticity », Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no 22,‎ , p. 12418–12423 (PMID 10535937, PMCID 22936, DOI 10.1073/pnas.96.22.12418, Bibcode 1999PNAS...9612418K)
  • « Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase », Chemistry & Biology, vol. 8, no 4,‎ , p. 379–389 (PMID 11325593, DOI 10.1016/s1074-5521(01)00020-5)

harvard.edu

ui.adsabs.harvard.edu

nih.gov

ncbi.nlm.nih.gov

  • « Entrez Gene: arylalkylamine N-acetyltransferase »
  • « The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression », Genomics, vol. 34, no 1,‎ , p. 76–84 (PMID 8661026, DOI 10.1006/geno.1996.0243)
  • « Serotonin N-acetyltransferase: mechanism and inhibition », Curr. Med. Chem., vol. 9, no 12,‎ , p. 1187–99 (PMID 12052171, DOI 10.2174/0929867023370013)
  • J. De Angelis, J. Gastel, D. C. Klein et P. A. Cole, « Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87) », The Journal of Biological Chemistry, vol. 273, no 5,‎ , p. 3045–3050 (PMID 9446620, DOI 10.1074/jbc.273.5.3045)
  • « The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog », Cell, vol. 97, no 3,‎ , p. 361–9 (PMID 10319816, DOI 10.1016/S0092-8674(00)80745-X, S2CID 18272015)
  • « Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism », Mol. Cell, vol. 3, no 1,‎ , p. 23–32 (PMID 10024876, DOI 10.1016/S1097-2765(00)80171-9)
  • « Investigation of the roles of catalytic residues in serotonin N-acetyltransferase », J. Biol. Chem., vol. 277, no 20,‎ , p. 18118–26 (PMID 11884405, DOI 10.1074/jbc.M200595200).
  • « Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation », Cell, vol. 105, no 2,‎ , p. 257–67 (PMID 11336675, DOI 10.1016/S0092-8674(01)00316-6, S2CID 9564413)
  • Matthew W. Vetting, Luiz Pedro S. de Carvalho, Michael Yu et Subray S. Hegde, « Structure and functions of the GNAT superfamily of acetyltransferases », Archives of Biochemistry and Biophysics, vol. 433, no 1,‎ , p. 212–226 (PMID 15581578, DOI 10.1016/j.abb.2004.09.003)
  • Klein, Coon, Roseboom et Weller, « The melatonin rhythm-generating enzyme: Molecular regulation of serotonin N-acetyltransferase in the pineal gland », Recent Progress in Hormone Research, vol. 52,‎ , p. 307–357; discussion 357–8 (PMID 9238858)
  • « cAmp regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation », J. Biol. Chem., vol. 276, no 26,‎ , p. 24097–107 (PMID 11313340, DOI 10.1074/jbc.M011298200)
  • « Rhythmic serotonin N-acetyltransferase mRNA degradation is essential for the maintenance of its circadian oscillation », Mol. Cell. Biol., vol. 25, no 8,‎ , p. 3232–46 (PMID 15798208, PMCID 1069600, DOI 10.1128/MCB.25.8.3232-3246.2005)
  • « Analysis of serotonin N-acetyltransferase regulation in vitro and in live cells using protein semisynthesis », Biochemistry, vol. 47, no 39,‎ , p. 10407–19 (PMID 18771288, PMCID 2682328, DOI 10.1021/bi801189d)
  • « Protein kinase C regulates the activity and stability of serotonin N-acetyltransferase », J. Neurochem., vol. 90, no 2,‎ , p. 442–54 (PMID 15228600, DOI 10.1111/j.1471-4159.2004.02495.x, S2CID 42638894)
  • « An intramolecular disulfide bridge as a catalytic switch for serotonin N-acetyltransferase », J. Biol. Chem., vol. 277, no 46,‎ , p. 44229–35 (PMID 12215431, DOI 10.1074/jbc.M203305200)
  • Lawrence M. Szewczuk, S. Adrian Saldanha, Surajit Ganguly et Erin M. Bowers, « De novo discovery of serotonin N-acetyltransferase inhibitors », Journal of Medicinal Chemistry, vol. 50, no 22,‎ , p. 5330–5338 (PMID 17924613, PMCID 2531295, DOI 10.1021/jm0706463)
  • « New substrate analogues of human serotonin N-acetyltransferase produce in situ specific and potent inhibitors », Eur. J. Biochem., vol. 271, no 2,‎ , p. 418–28 (PMID 14717709, DOI 10.1046/j.1432-1033.2003.03942.x)
  • « Novel bisubstrate analog inhibitors of serotonin N-acetyltransferase: the importance of being neutral », Bioorg. Chem., vol. 31, no 5,‎ , p. 398–411 (PMID 12941292, DOI 10.1016/S0045-2068(03)00081-6)
  • « Receptor- and ligand-based study on novel 2,2'-bithienyl derivatives as non-peptidic AANAT inhibitors », J Chem Inf Model, vol. 50, no 3,‎ , p. 446–60 (PMID 20196559, DOI 10.1021/ci9004805)
  • « Structure-activity relationships for substrates and inhibitors of pineal 5-hydroxytryptamine-N-acetyltransferase: preliminary studies », Eur. J. Pharmacol., vol. 307, no 2,‎ , p. 133–40 (PMID 8832214, DOI 10.1016/0014-2999(96)00228-2)
  • « Substrate specificity and inhibition studies of human serotonin N-acetyltransferase », J. Biol. Chem., vol. 275, no 12,‎ , p. 8794–805 (PMID 10722724, DOI 10.1074/jbc.275.12.8794)
  • « Mechanism-based inhibition of the melatonin rhythm enzyme: pharmacologic exploitation of active site functional plasticity », Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no 22,‎ , p. 12418–12423 (PMID 10535937, PMCID 22936, DOI 10.1073/pnas.96.22.12418, Bibcode 1999PNAS...9612418K)
  • « Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase », Chemistry & Biology, vol. 8, no 4,‎ , p. 379–389 (PMID 11325593, DOI 10.1016/s1074-5521(01)00020-5)
  • « N-bromoacetyltryptamine strongly and reversibly inhibits in vitro melatonin secretion from mammalian pinealocytes », Neuroendocrinology Letters, vol. 26, no 5,‎ , p. 581–592 (PMID 16264397)

qmul.ac.uk

chem.qmul.ac.uk

rcsb.org

semanticscholar.org

api.semanticscholar.org