Эчтәлеккә күчү

GCH1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/GCH1 latin yazuında])
GCH1
Сурәт
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген GCH1[d][1]
Молекуляр функция нуклеотид-связывающий[d][2], calcium ion binding[d][2], гомодимеризация белка[d][3], zinc ion binding[d][4][5][6], GTP binding[d][4][4][5][…], связывание с ионом металла[d][2], связывание с белками плазмы[d][3][7][8][…], активность катализатора[d][2], гидролазная активность[d][2], GTP cyclohydrolase I activity[d][4][4][4][…], mitogen-activated protein kinase binding[d][8], GTPase activity[d][9], GTP-dependent protein binding[d][2], translation initiation factor binding[d][2], GTP cyclohydrolase I activity[d][4][4][4][…], GTP binding[d][2][2][10][…], zinc ion binding[d][2][11][12][…] һәм GTP cyclohydrolase I activity[d][2][2][2][…]
Күзәнәк компоненты цитоплазма[4][4][13], цитозоль[d][2][14][9][…], ядерная мембрана[d][2], нуклеоплазма[d][2], цитоплазматическая везикула[d][14], төш[2][15], neuron projection terminus[d][16], protein-containing complex[d][2][17] һәм цитоплазма[2][2][18][…]
Биологик процесс nitric oxide biosynthetic process[d][19], response to interferon-gamma[d][19][20][21], neuromuscular process controlling posture[d][22], protein heterooligomerization[d][2], negative regulation of blood pressure[d][2], dopamine biosynthetic process[d][23], regulation of lung blood pressure[d][2], вазодилатация[d][2], pteridine-containing compound biosynthetic process[d][10][9][24], 7,8-dihydroneopterin 3'-triphosphate biosynthetic process[d][2], dihydrobiopterin metabolic process[d][2], regulation of blood pressure[d][25][2], response to tumor necrosis factor[d][19], tetrahydrofolate biosynthetic process[d][2], response to lipopolysaccharide[d][26][19][20], positive regulation of nitric-oxide synthase activity[d][25][27][24][…], response to pain[d][2][2], tetrahydrobiopterin biosynthetic process[d][28][29][4][…], Метаболизм[2], protein homooligomerization[d][2][12], regulation of removal of superoxide radicals[d][27], positive regulation of heart rate[d][2], protein-containing complex assembly[d][2] һәм tetrahydrobiopterin biosynthetic process[d][30][27][2][…]
Изображение Gene Atlas

GCH1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[31][32]

Искәрмәләр

[үзгәртү | вики-текстны үзгәртү]
  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 2,33 2,34 GOA
  3. ↑ 3,0 3,1 Swick L., Kapatos G. A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions // J. Neurochem. — Wiley-Blackwell, 2006. — ISSN 0022-3042; 1471-4159 — doi:10.1111/J.1471-4159.2006.03836.X — PMID:16696853
  4. ↑ 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 4,10 4,11 GOA
  5. ↑ 5,0 5,1 Ichinose H., Suzuki T. GTP cyclohydrolase I utilizes metal-free GTP as its substrate // FEBS J. — Wiley-Blackwell, 2004. — ISSN 1742-464X; 0014-2956; 1742-4658; 1432-1033 — doi:10.1046/J.1432-1033.2003.03933.X — PMID:14717702
  6. ↑ G Auerbach, A Herrmann, A Bracher et al. Zinc plays a key role in human and bacterial GTP cyclohydrolase I // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2000. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.240463497 — PMID:11087827
  7. ↑ T Yoneyama, Brewer J. M., K Hatakeyama GTP cyclohydrolase I feedback regulatory protein is a pentamer of identical subunits. Purification, cDNA cloning, and bacterial expression // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1997. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.272.15.9690 — PMID:9092499
  8. ↑ 8,0 8,1 Chiarini A., Armato U., Pacchiana R. et al. Proteomic analysis of GTP cyclohydrolase 1 multiprotein complexes in cultured normal adult human astrocytes under both basal and cytokine-activated conditions // Proteomics / L. Stimson — Wiley, 2009. — ISSN 1615-9853; 1615-9861 — doi:10.1002/PMIC.200800561 — PMID:19294699
  9. ↑ 9,0 9,1 9,2 G Schoedon, U Redweik, Curtius H. C. Purification of GTP cyclohydrolase I from human liver and production of specific monoclonal antibodies // FEBS J. — Wiley-Blackwell, 1989. — ISSN 1742-464X; 0014-2956; 1742-4658; 1432-1033 — doi:10.1111/J.1432-1033.1989.TB14491.X — PMID:2463916
  10. ↑ 10,0 10,1 Blau N. The application of 8-aminoguanosine triphosphate, a new inhibitor of GTP cyclohydrolase I, to the purification of the enzyme from human liver // Biochim. Biophys. Acta — Elsevier BV, 1986. — ISSN 0006-3002; 1878-2434 — doi:10.1016/0304-4165(86)90115-7 — PMID:3753653
  11. ↑ Ichinose H., Suzuki T. GTP cyclohydrolase I utilizes metal-free GTP as its substrate // FEBS J. — Wiley-Blackwell, 2004. — ISSN 1742-464X; 0014-2956; 1742-4658; 1432-1033 — doi:10.1046/J.1432-1033.2003.03933.X — PMID:14717702
  12. ↑ 12,0 12,1 G Auerbach, A Herrmann, A Bracher et al. Zinc plays a key role in human and bacterial GTP cyclohydrolase I // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2000. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.240463497 — PMID:11087827
  13. ↑ I Nagatsu, K Ikemoto, K Kitahama et al. Specific localization of the guanosine triphosphate (GTP) cyclohydrolase I-immunoreactivity in the human brain // Journal of Neural Transmission / P. Riederer — Springer Science+Business Media, 1999. — ISSN 0300-9564; 1435-1463 — doi:10.1007/S007020050183 — PMID:10907721
  14. ↑ 14,0 14,1 G Schoedon, Curtis H. C., A Niederwieser Localization of GTP cyclohydrolase I in human peripheral blood smears using a specific monoclonal antibody and an immune-alkaline phosphatase labeling technique // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 1987. — ISSN 0006-291X; 1090-2104 — doi:10.1016/S0006-291X(87)80264-4 — PMID:3318829
  15. ↑ Chavan B., Gillbro J. M., Rokos H. et al. GTP cyclohydrolase feedback regulatory protein controls cofactor 6-tetrahydrobiopterin synthesis in the cytosol and in the nucleus of epidermal keratinocytes and melanocytes // J. Invest. Dermatol. / M. C. Udey — NPG, Elsevier BV, 2006. — ISSN 0022-202X; 1523-1747 — doi:10.1038/SJ.JID.5700425 — PMID:16778797
  16. ↑ Kapatos G. The neurobiology of tetrahydrobiopterin biosynthesis: a model for regulation of GTP cyclohydrolase I gene transcription within nigrostriatal dopamine neurons // IUBMB Life — Wiley-Blackwell, IUBMB, 2013. — ISSN 1521-6543; 1521-6551 — doi:10.1002/IUB.1140 — PMID:23457032
  17. ↑ Lauderdale J. D., Wilensky J. S., Oliver E. R. et al. 3' deletions cause aniridia by preventing PAX6 gene expression // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2000. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.240398797 — PMID:11087823
  18. ↑ I Nagatsu, K Ikemoto, K Kitahama et al. Specific localization of the guanosine triphosphate (GTP) cyclohydrolase I-immunoreactivity in the human brain // Journal of Neural Transmission / P. Riederer — Springer Science+Business Media, 1999. — ISSN 0300-9564; 1435-1463 — doi:10.1007/S007020050183 — PMID:10907721
  19. ↑ 19,0 19,1 19,2 19,3 Katusic Z. S., A. Stelter, S. Milstien Cytokines stimulate GTP cyclohydrolase I gene expression in cultured human umbilical vein endothelial cells, Cytokines Stimulate GTP Cyclohydrolase I Gene Expression in Cultured Human Umbilical Vein Endothelial Cells // Arteriosclerosis, Thrombosis, and Vascular Biology — Lippincott Williams & Wilkins, 1998. — ISSN 1079-5642; 1524-4636 — doi:10.1161/01.ATV.18.1.27 — PMID:9445252
  20. ↑ 20,0 20,1 G Weiss, Werner E. R. Pteridine biosynthesis in human endothelial cells. Impact on nitric oxide-mediated formation of cyclic GMP // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1993. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:7678411
  21. ↑ A Gesierich, F Niroomand, Tiefenbacher C. P. Role of human GTP cyclohydrolase I and its regulatory protein in tetrahydrobiopterin metabolism // Basic Research in Cardiology — Springer Berlin Heidelberg, Springer Science+Business Media, 2003. — ISSN 0300-8428; 1435-1803 — doi:10.1007/S00395-003-0394-Y — PMID:12607127
  22. ↑ H Ichinose Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations in the GTP cyclohydrolase I gene // Nature Genetics / M. Axton, T. Faial — NPG, 1994. — ISSN 1061-4036; 1546-1718 — doi:10.1038/NG1194-236 — PMID:7874165
  23. ↑ Duan C., Su Y., Zhao C. et al. The assays of activities and function of TH, AADC, and GCH1 and their potential use in ex vivo gene therapy of PD // Brain Research Protocols — 2005. — ISSN 1385-299X; 1872-809X — doi:10.1016/J.BRAINRESPROT.2005.10.005 — PMID:16338639
  24. ↑ 24,0 24,1 Channon K. M. Augmented BH4 by gene transfer restores nitric oxide synthase function in hyperglycemic human endothelial cells // Cardiovascular Research — OUP, 2005. — ISSN 0008-6363; 1755-3245 — doi:10.1016/J.CARDIORES.2004.10.040 — PMID:15721862
  25. ↑ 25,0 25,1 Wessel J., Salem R. M., Rodriguez-Flores J. L. et al. Discovery of common human genetic variants of GTP cyclohydrolase 1 (GCH1) governing nitric oxide, autonomic activity, and cardiovascular risk // J. Clin. Invest. / R. S. Ahima — American Society for Clinical Investigation, 2007. — ISSN 0021-9738; 1558-8238 — doi:10.1172/JCI31093 — PMID:17717598
  26. ↑ Huang A., Zhang Y., Chen K. et al. Cytokine-stimulated GTP cyclohydrolase I expression in endothelial cells requires coordinated activation of nuclear factor-kappaB and Stat1/Stat3 // Circ. Res. — Lippincott Williams & Wilkins, 2005. — ISSN 0009-7330; 1524-4571 — doi:10.1161/01.RES.0000153669.24827.DF — PMID:15604419
  27. ↑ 27,0 27,1 27,2 Crabtree M. J., Channon K. M. Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M109.041483 — PMID:19666465
  28. ↑ Funayama M., Ichinose H. Novel mutations in the guanosine triphosphate cyclohydrolase 1 gene associated with DYT5 dystonia // Archives of Neurology — American Medical Association, 2006. — ISSN 0003-9942; 1538-3687 — doi:10.1001/ARCHNEUR.63.11.1605 — PMID:17101830
  29. ↑ Crabtree M. J., Channon K. M. Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2009. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M109.041483 — PMID:19666465
  30. ↑ Funayama M., Ichinose H. Novel mutations in the guanosine triphosphate cyclohydrolase 1 gene associated with DYT5 dystonia // Archives of Neurology — American Medical Association, 2006. — ISSN 0003-9942; 1538-3687 — doi:10.1001/ARCHNEUR.63.11.1605 — PMID:17101830
  31. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  32. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

[үзгәртү | вики-текстны үзгәртү]
  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)


Миоглобин молекуласы
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Чыганак — https://tt.wikipedia.org/w/index.php?title=GCH1&oldid=4252760