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Syntáza mastných kyselín (Slovak Wikipedia)

Analysis of information sources in references of the Wikipedia article "Syntáza mastných kyselín" in Slovak language version.

refsWebsite
Global rank Slovak rank
41nih.gov
4th place
21st place
40doi.org
2nd place
7th place
1acs.org
1,248th place
598th place
1worldcat.org
5th place
1st place
1sciencedirect.com
149th place
118th place
1web.archive.org
1st place
8th place
1oncotherapynetwork.com
low place
low place

acs.org

pubs.acs.org

doi.org

dx.doi.org

  • Animal Fatty Acid Synthase: A Chemical Nanofactory. Chemical Reviews, 2021-08-11, s. 9502–9553. Dostupné online. ISSN 0009-2665. DOI: 10.1021/acs.chemrev.1c00147. PMID 34156235. (po anglicky)
  • Regulation of synthesis of hepatic fatty acid synthetase: binding of fatty acid synthetase antibodies to polysomes. Proceedings of the National Academy of Sciences of the United States of America, October 1975, s. 3956–3960. DOI: 10.1073/pnas.72.10.3956. PMID 1060077.
  • Presence of two polypeptide chains comprising fatty acid synthetase. Proceedings of the National Academy of Sciences of the United States of America, May 1975, s. 1940–1944. DOI: 10.1073/pnas.72.5.1940. PMID 1098047.
  • Specific release of the thioesterase component of the fatty acid synthetase multienzyme complex by limited trypsinization. Proceedings of the National Academy of Sciences of the United States of America, April 1976, s. 1184–1188. DOI: 10.1073/pnas.73.4.1184. PMID 1063400.
  • Structural and functional organization of the animal fatty acid synthase. Progress in Lipid Research, July 2003, s. 289–317. DOI: 10.1016/S0163-7827(02)00067-X. PMID 12689621.
  • Isolation and chromosomal mapping of genomic clones encoding the human fatty acid synthase gene. Genomics, February 1995, s. 420–424. DOI: 10.1006/geno.1994.1518. PMID 7835891.
  • Human fatty acid synthase: properties and molecular cloning. Proceedings of the National Academy of Sciences of the United States of America, Oct 1995, s. 8695–8699. DOI: 10.1073/pnas.92.19.8695. PMID 7567999.
  • The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chemico-Biological Interactions, Feb 2009, s. 94–98. DOI: 10.1016/j.cbi.2008.10.040. PMID 19027726.
  • Evolutionary implications of bacterial polyketide synthases. Molecular Biology and Evolution, October 2005, s. 2027–2039. DOI: 10.1093/molbev/msi193. PMID 15958783.
  • Fulmer T. Not so FAS. Science-Business EXchange, March 2009, s. 430. DOI: 10.1038/scibx.2009.430.
  • Human fatty acid synthase: role of interdomain in the formation of catalytically active synthase dimer. Proceedings of the National Academy of Sciences of the United States of America, March 2001, s. 3104–3108. DOI: 10.1073/pnas.051635998. PMID 11248039.
  • Smith S. The animal fatty acid synthase: one gene, one polypeptide, seven enzymes. FASEB Journal, December 1994, s. 1248–1259. DOI: 10.1096/fasebj.8.15.8001737. PMID 8001737.
  • Animal fatty acid synthetase. A novel arrangement of the beta-ketoacyl synthetase sites comprising domains of the two subunits. Journal of Biological Chemistry, May 1981, s. 5128–5133. DOI: 10.1016/S0021-9258(19)69376-2. PMID 6112225.
  • Animal fatty acid synthetase. Identification of the residues comprising the novel arrangement of the beta-ketoacyl synthetase site and their role in its cold inactivation. Journal of Biological Chemistry, March 1982, s. 3230–3235. DOI: 10.1016/S0021-9258(19)81100-6. PMID 7061475.
  • Differential affinity labeling of the two subunits of the homodimeric animal fatty acid synthase allows isolation of heterodimers consisting of subunits that have been independently modified. Journal of Biological Chemistry, February 1998, s. 4937–4943. DOI: 10.1074/jbc.273.9.4937. PMID 9478938.
  • Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry, September 2001, s. 10792–18799. DOI: 10.1021/bi015535z. PMID 11535054.
  • Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model. Journal of Biological Chemistry, April 1999, s. 11557–11563. DOI: 10.1074/jbc.274.17.11557. PMID 10206962.
  • Engineering of an active animal fatty acid synthase dimer with only one competent subunit. Chemistry and Biology, February 2003, s. 169–173. DOI: 10.1016/S1074-5521(03)00023-1. PMID 12618189.
  • Structure and molecular organization of mammalian fatty acid synthase. Nature Structural and Molecular Biology, March 2005, s. 225–232. DOI: 10.1038/nsmb899. PMID 15711565.
  • The crystal structure of a mammalian fatty acid synthase. Science, September 2008, s. 1315–1322. DOI: 10.1126/science.1161269. PMID 18772430.
  • The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell, April 2007, s. 319–332. DOI: 10.1016/j.cell.2007.03.013. PMID 17448991.
  • Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy. Proceedings of the National Academy of Sciences of the United States of America, May 2010, s. 9164–9169. DOI: 10.1073/pnas.0913547107. PMID 20231485.
  • Mechanism of substrate shuttling by the acyl-carrier protein within the fatty acid mega-synthase. Journal of the American Chemical Society, September 2010, s. 12357–12364. DOI: 10.1021/ja103354w. PMID 20704262.
  • Hormonal regulation of mouse fatty acid synthase gene transcription in liver. Journal of Biological Chemistry, January 1989, s. 574–577. DOI: 10.1016/S0021-9258(17)31298-X. PMID 2535847.
  • Occupancy and function of the -150 sterol regulatory element and -65 E-box in nutritional regulation of the fatty acid synthase gene in living animals. Molecular and Cellular Biology, August 2003, s. 5896–5907. DOI: 10.1128/MCB.23.16.5896-5907.2003. PMID 12897158.
  • Direct interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoter. Journal of Biological Chemistry, February 2007, s. 5453–5467. DOI: 10.1074/jbc.M610566200. PMID 17197698.
  • Identification of liver X receptor-retinoid X receptor as an activator of the sterol regulatory element-binding protein 1c gene promoter. Molecular and Cellular Biology, May 2001, s. 2991–3000. DOI: 10.1128/MCB.21.9.2991-3000.2001. PMID 11287605.
  • Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta. Genes & Development, November 2000, s. 2819–2830. DOI: 10.1101/gad.844900. PMID 11090130.
  • Fatty acid synthase inhibitory activity of acylphloroglucinols isolated from Dryopteris crassirhizoma. Bioorganic & Medicinal Chemistry Letters, September 2006, s. 4738–4742. DOI: 10.1016/j.bmcl.2006.07.018. PMID 16870425.
  • Fatty acid synthase: a metabolic oncogene in prostate cancer?. Journal of Cellular Biochemistry, January 2004, s. 47–53. DOI: 10.1002/jcb.10708. PMID 14689581.
  • Increased expression of fatty acid synthase (OA-519) in ovarian neoplasms predicts shorter survival. Human Pathology, June 1997, s. 686–692. DOI: 10.1016/S0046-8177(97)90177-5. PMID 9191002.
  • Clinical importance of FASN in relation to HIF-1α and SREBP-1c in gastric adenocarcinoma. Life Sciences, May 2019, s. 169–176. Dostupné online. DOI: 10.1016/j.lfs.2019.03.056. PMID 30914315.
  • Design and synthesis of a series of bioavailable fatty acid synthase (FASN) KR domain inhibitors for cancer therapy. Bioorganic & Medicinal Chemistry Letters, May 2018, s. 2159–2164. DOI: 10.1016/j.bmcl.2018.05.014. PMID 29779975.
  • A human fatty acid synthase inhibitor binds β-ketoacyl reductase in the keto-substrate site. Nature Chemical Biology, September 2014, s. 774–779. DOI: 10.1038/nchembio.1603. PMID 25086508.
  • Understanding the Intersections between Metabolism and Cancer Biology. Cell, February 2017, s. 657–669. DOI: 10.1016/j.cell.2016.12.039. PMID 28187287.
  • Identification of a physiologically relevant endogenous ligand for PPARalpha in liver.. Cell, August 2009, s. 476–488. DOI: 10.1016/j.cell.2009.05.036. PMID 19646743.
  • Antidiabetic and antisteatotic effects of the selective fatty acid synthase (FAS) inhibitor platensimycin in mouse models of diabetes.. Proceedings of the National Academy of Sciences of the United States of America, March 2011, s. 5378–5383. DOI: 10.1073/pnas.1002588108. PMID 21389266.
  • Fatty acid synthase as a potential therapeutic target in cancer. Future Oncology, April 2010, s. 551–562. DOI: 10.2217/fon.10.11. PMID 20373869.
  • Synthesis of novel beta-lactone inhibitors of fatty acid synthase. Journal of Medicinal Chemistry, September 2008, s. 5285–5296. DOI: 10.1021/jm800321h. PMID 18710210.
  • Genome-wide linkage and association analyses implicate FASN in predisposition to uterine leiomyomata. American Journal of Human Genetics, 2012, s. 621–628. DOI: 10.1016/j.ajhg.2012.08.009. PMID 23040493.

nih.gov

ncbi.nlm.nih.gov

  • Animal Fatty Acid Synthase: A Chemical Nanofactory. Chemical Reviews, 2021-08-11, s. 9502–9553. Dostupné online. ISSN 0009-2665. DOI: 10.1021/acs.chemrev.1c00147. PMID 34156235. (po anglicky)
  • Regulation of synthesis of hepatic fatty acid synthetase: binding of fatty acid synthetase antibodies to polysomes. Proceedings of the National Academy of Sciences of the United States of America, October 1975, s. 3956–3960. DOI: 10.1073/pnas.72.10.3956. PMID 1060077.
  • Presence of two polypeptide chains comprising fatty acid synthetase. Proceedings of the National Academy of Sciences of the United States of America, May 1975, s. 1940–1944. DOI: 10.1073/pnas.72.5.1940. PMID 1098047.
  • Specific release of the thioesterase component of the fatty acid synthetase multienzyme complex by limited trypsinization. Proceedings of the National Academy of Sciences of the United States of America, April 1976, s. 1184–1188. DOI: 10.1073/pnas.73.4.1184. PMID 1063400.
  • Structural and functional organization of the animal fatty acid synthase. Progress in Lipid Research, July 2003, s. 289–317. DOI: 10.1016/S0163-7827(02)00067-X. PMID 12689621.
  • Entrez Gene: FASN fatty acid synthase [online]. . Dostupné online.
  • Isolation and chromosomal mapping of genomic clones encoding the human fatty acid synthase gene. Genomics, February 1995, s. 420–424. DOI: 10.1006/geno.1994.1518. PMID 7835891.
  • Human fatty acid synthase: properties and molecular cloning. Proceedings of the National Academy of Sciences of the United States of America, Oct 1995, s. 8695–8699. DOI: 10.1073/pnas.92.19.8695. PMID 7567999.
  • The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chemico-Biological Interactions, Feb 2009, s. 94–98. DOI: 10.1016/j.cbi.2008.10.040. PMID 19027726.
  • Evolutionary implications of bacterial polyketide synthases. Molecular Biology and Evolution, October 2005, s. 2027–2039. DOI: 10.1093/molbev/msi193. PMID 15958783.
  • Human fatty acid synthase: role of interdomain in the formation of catalytically active synthase dimer. Proceedings of the National Academy of Sciences of the United States of America, March 2001, s. 3104–3108. DOI: 10.1073/pnas.051635998. PMID 11248039.
  • Smith S. The animal fatty acid synthase: one gene, one polypeptide, seven enzymes. FASEB Journal, December 1994, s. 1248–1259. DOI: 10.1096/fasebj.8.15.8001737. PMID 8001737.
  • Animal fatty acid synthetase. A novel arrangement of the beta-ketoacyl synthetase sites comprising domains of the two subunits. Journal of Biological Chemistry, May 1981, s. 5128–5133. DOI: 10.1016/S0021-9258(19)69376-2. PMID 6112225.
  • Animal fatty acid synthetase. Identification of the residues comprising the novel arrangement of the beta-ketoacyl synthetase site and their role in its cold inactivation. Journal of Biological Chemistry, March 1982, s. 3230–3235. DOI: 10.1016/S0021-9258(19)81100-6. PMID 7061475.
  • Differential affinity labeling of the two subunits of the homodimeric animal fatty acid synthase allows isolation of heterodimers consisting of subunits that have been independently modified. Journal of Biological Chemistry, February 1998, s. 4937–4943. DOI: 10.1074/jbc.273.9.4937. PMID 9478938.
  • Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry, September 2001, s. 10792–18799. DOI: 10.1021/bi015535z. PMID 11535054.
  • Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit. Reevaluation of the side-by-side, antiparallel subunit model. Journal of Biological Chemistry, April 1999, s. 11557–11563. DOI: 10.1074/jbc.274.17.11557. PMID 10206962.
  • Engineering of an active animal fatty acid synthase dimer with only one competent subunit. Chemistry and Biology, February 2003, s. 169–173. DOI: 10.1016/S1074-5521(03)00023-1. PMID 12618189.
  • Structure and molecular organization of mammalian fatty acid synthase. Nature Structural and Molecular Biology, March 2005, s. 225–232. DOI: 10.1038/nsmb899. PMID 15711565.
  • The crystal structure of a mammalian fatty acid synthase. Science, September 2008, s. 1315–1322. DOI: 10.1126/science.1161269. PMID 18772430.
  • The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell, April 2007, s. 319–332. DOI: 10.1016/j.cell.2007.03.013. PMID 17448991.
  • Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy. Proceedings of the National Academy of Sciences of the United States of America, May 2010, s. 9164–9169. DOI: 10.1073/pnas.0913547107. PMID 20231485.
  • Mechanism of substrate shuttling by the acyl-carrier protein within the fatty acid mega-synthase. Journal of the American Chemical Society, September 2010, s. 12357–12364. DOI: 10.1021/ja103354w. PMID 20704262.
  • Hormonal regulation of mouse fatty acid synthase gene transcription in liver. Journal of Biological Chemistry, January 1989, s. 574–577. DOI: 10.1016/S0021-9258(17)31298-X. PMID 2535847.
  • Occupancy and function of the -150 sterol regulatory element and -65 E-box in nutritional regulation of the fatty acid synthase gene in living animals. Molecular and Cellular Biology, August 2003, s. 5896–5907. DOI: 10.1128/MCB.23.16.5896-5907.2003. PMID 12897158.
  • Direct interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoter. Journal of Biological Chemistry, February 2007, s. 5453–5467. DOI: 10.1074/jbc.M610566200. PMID 17197698.
  • Identification of liver X receptor-retinoid X receptor as an activator of the sterol regulatory element-binding protein 1c gene promoter. Molecular and Cellular Biology, May 2001, s. 2991–3000. DOI: 10.1128/MCB.21.9.2991-3000.2001. PMID 11287605.
  • Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta. Genes & Development, November 2000, s. 2819–2830. DOI: 10.1101/gad.844900. PMID 11090130.
  • Fatty acid synthase inhibitory activity of acylphloroglucinols isolated from Dryopteris crassirhizoma. Bioorganic & Medicinal Chemistry Letters, September 2006, s. 4738–4742. DOI: 10.1016/j.bmcl.2006.07.018. PMID 16870425.
  • Fatty acid synthase: a metabolic oncogene in prostate cancer?. Journal of Cellular Biochemistry, January 2004, s. 47–53. DOI: 10.1002/jcb.10708. PMID 14689581.
  • MRNA stability and overexpression of fatty acid synthase in human breast cancer cell lines. Anticancer Research, 2007, s. 27–34. PMID 17352212.
  • Increased expression of fatty acid synthase (OA-519) in ovarian neoplasms predicts shorter survival. Human Pathology, June 1997, s. 686–692. DOI: 10.1016/S0046-8177(97)90177-5. PMID 9191002.
  • Clinical importance of FASN in relation to HIF-1α and SREBP-1c in gastric adenocarcinoma. Life Sciences, May 2019, s. 169–176. Dostupné online. DOI: 10.1016/j.lfs.2019.03.056. PMID 30914315.
  • Design and synthesis of a series of bioavailable fatty acid synthase (FASN) KR domain inhibitors for cancer therapy. Bioorganic & Medicinal Chemistry Letters, May 2018, s. 2159–2164. DOI: 10.1016/j.bmcl.2018.05.014. PMID 29779975.
  • A human fatty acid synthase inhibitor binds β-ketoacyl reductase in the keto-substrate site. Nature Chemical Biology, September 2014, s. 774–779. DOI: 10.1038/nchembio.1603. PMID 25086508.
  • Understanding the Intersections between Metabolism and Cancer Biology. Cell, February 2017, s. 657–669. DOI: 10.1016/j.cell.2016.12.039. PMID 28187287.
  • Identification of a physiologically relevant endogenous ligand for PPARalpha in liver.. Cell, August 2009, s. 476–488. DOI: 10.1016/j.cell.2009.05.036. PMID 19646743.
  • Antidiabetic and antisteatotic effects of the selective fatty acid synthase (FAS) inhibitor platensimycin in mouse models of diabetes.. Proceedings of the National Academy of Sciences of the United States of America, March 2011, s. 5378–5383. DOI: 10.1073/pnas.1002588108. PMID 21389266.
  • Fatty acid synthase as a potential therapeutic target in cancer. Future Oncology, April 2010, s. 551–562. DOI: 10.2217/fon.10.11. PMID 20373869.
  • Synthesis of novel beta-lactone inhibitors of fatty acid synthase. Journal of Medicinal Chemistry, September 2008, s. 5285–5296. DOI: 10.1021/jm800321h. PMID 18710210.
  • Genome-wide linkage and association analyses implicate FASN in predisposition to uterine leiomyomata. American Journal of Human Genetics, 2012, s. 621–628. DOI: 10.1016/j.ajhg.2012.08.009. PMID 23040493.

oncotherapynetwork.com

  • First Human Study Taking Place With Fatty Acid Synthase Inhibitor [online]. oncotherapynetwork.com, April 7, 2017, [cit. 2023-10-29]. Dostupné online. Archivované 2019-04-15 z originálu.

sciencedirect.com

web.archive.org

  • First Human Study Taking Place With Fatty Acid Synthase Inhibitor [online]. oncotherapynetwork.com, April 7, 2017, [cit. 2023-10-29]. Dostupné online. Archivované 2019-04-15 z originálu.

worldcat.org