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FOXO3

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/FOXO3 latin yazuında])
FOXO3
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген FOXO3[d][1]
Молекуляр функция beta-catenin binding[d][2], DNA-binding transcription activator activity, RNA polymerase II-specific[d][3], связывание с белками плазмы[d][4][5][6][…], protein kinase binding[d][7][8][9], chromatin DNA binding[d][3][3], DNA-binding transcription factor activity[d][10][10][11], sequence-specific DNA binding[d][10][10][12], ДНК-связывающий[d][3][3][9], DNA-binding transcription repressor activity, RNA polymerase II-specific[d][3][13], DNA-binding transcription factor activity, RNA polymerase II-specific[d][14][10], mitochondrial transcription factor activity[d][5][3], transcription coregulator binding[d][3], RNA polymerase II cis-regulatory region sequence-specific DNA binding[d][3][3], DNA-binding transcription factor activity, RNA polymerase II-specific[d][15][3][16], DNA-binding transcription factor activity[d][3][3][17][…], transcription factor binding[d][16] һәм sequence-specific DNA binding[d][3][3][18][…]
Күзәнәк компоненты мембрана[d][3][3], нуклеоплазма[d][3][3], цитозоль[d][3][3][3][…], цитоплазма[10][10][19][…], төш[20][10][10][…], митохондрия[3][3][4], mitochondrial outer membrane[d][3][3][5], митохондриальный матрикс[d][3][3][5], protein-containing complex[d][3][4][5], төш[5][3][3][…] һәм цитоплазма[3][3][4][…]
Биологик процесс initiation of primordial ovarian follicle growth[d][3], ovulation from ovarian follicle[d][3], ДНК-зависимая регуляция транскрипции[d][3][3], antral ovarian follicle growth[d][3], positive regulation of erythrocyte differentiation[d][17], glucose homeostasis[d][10], DNA damage response, signal transduction by p53 class mediator[d][3], tumor necrosis factor-mediated signaling pathway[d][21], regulation of reactive oxygen species metabolic process[d][3], transcription by RNA polymerase II[d][10], regulation of neural precursor cell proliferation[d][3], транскрипция, ДНК-зависимая[d][10], neuronal stem cell population maintenance[d][3], positive regulation of neuron apoptotic process[d][18], oocyte maturation[d][3], extrinsic apoptotic signaling pathway in absence of ligand[d][3], positive regulation of apoptotic process[d][13], regulation of translation[d][9], negative regulation of canonical Wnt signaling pathway[d][3], апоптоз[d][3][3], negative regulation of transcription by RNA polymerase II[d][22][23], regulation of transcription by RNA polymerase II[d][3][3], положительная регуляция транскрипции РНК полимеразой II промотор[d][10][12][11], cellular response to oxidative stress[d][3][3], ДНК-зависимая позитивная регуляция транскрипции[d][3][18][21], positive regulation of reactive oxygen species biosynthetic process[d][3], brain morphogenesis[d][3], старение человека[d][3], negative regulation of neuron differentiation[d][3], cellular response to hypoxia[d][3], response to water-immersion restraint stress[d][3], response to nutrient levels[d][3], cellular response to amyloid-beta[d][3], cellular response to corticosterone stimulus[d][3], positive regulation of endothelial cell apoptotic process[d][3], positive regulation of hydrogen peroxide-mediated programmed cell death[d][3], response to dexamethasone[d][3], cellular response to nerve growth factor stimulus[d][3], cellular response to glucose stimulus[d][3], морфогенез анатомической структуры[d][10], cytokine-mediated signaling pathway[d][3], mitochondrial transcription[d][5][3], negative regulation of cell migration[d][24], negative regulation of transcription by RNA polymerase II[d][25][13][16], insulin receptor signaling pathway[d][16], glucose homeostasis[d][3][16], положительная регуляция транскрипции РНК полимеразой II промотор[d][3][18][17][…], positive regulation of autophagy[d][3][3], positive regulation of muscle atrophy[d][3][3] һәм response to starvation[d][3][3]

FOXO3 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[26][27]

Искәрмәләр

[үзгәртү | вики-текстны үзгәртү]
  1. ↑ 1,0 1,1 UniProt
  2. ↑ Essers M. Functional interaction between beta-catenin and FOXO in oxidative stress signaling // Science / H. Thorp — Northern America: AAAS, 2005. — 4 p. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.1109083 — PMID:15905404
  3. ↑ 3,00 3,01 3,02 3,03 3,04 3,05 3,06 3,07 3,08 3,09 3,10 3,11 3,12 3,13 3,14 3,15 3,16 3,17 3,18 3,19 3,20 3,21 3,22 3,23 3,24 3,25 3,26 3,27 3,28 3,29 3,30 3,31 3,32 3,33 3,34 3,35 3,36 3,37 3,38 3,39 3,40 3,41 3,42 3,43 3,44 3,45 3,46 3,47 3,48 3,49 3,50 3,51 3,52 3,53 3,54 3,55 3,56 3,57 3,58 3,59 3,60 3,61 3,62 3,63 3,64 3,65 3,66 3,67 3,68 3,69 3,70 3,71 3,72 3,73 3,74 3,75 GOA
  4. ↑ 4,0 4,1 4,2 4,3 Ryall J. G., Peserico A., Chiacchiera F. et al. A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels // Cell Mol Life Sci — Birkhäuser, Springer Science+Business Media, 2013. — ISSN 1420-9071; 1420-682X — doi:10.1007/S00018-012-1244-6 — PMID:23283301
  5. ↑ 5,0 5,1 5,2 5,3 5,4 5,5 5,6 Tezil T., Fasano C., Peserico A. et al. Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy // Cell Death Dis. — London: Nature Publishing Group, 2018. — ISSN 2041-4889 — doi:10.1038/S41419-018-0336-0 — PMID:29445193
  6. ↑ Kong D. K., Georgescu S. P., Cano C. et al. Deficiency of the transcriptional regulator p8 results in increased autophagy and apoptosis, and causes impaired heart function // Mol. Biol. Cell, — American Society for Cell Biology, 2010. — ISSN 1059-1524; 1939-4586; 1044-2030 — doi:10.1091/MBC.E09-09-0818 — PMID:20181828
  7. ↑ Yang Y., Villén J., Esther B.E. Becker et al. A conserved MST-FOXO signaling pathway mediates oxidative-stress responses and extends life span // Cell — Cell Press, Elsevier BV, 2006. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2006.03.046 — PMID:16751106
  8. ↑ Katayama R. Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2008. — ISSN 0008-5472; 1538-7445 — doi:10.1158/0008-5472.CAN-08-0634 — PMID:18593906
  9. ↑ 9,0 9,1 9,2 Rosenwald A., Gaestel M., Cannell I. G. et al. The MK5/PRAK kinase and Myc form a negative feedback loop that is disrupted during colorectal tumorigenesis // Mol. Cell — Cell Press, Elsevier BV, 2011. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2011.01.023 — PMID:21329882
  10. ↑ 10,00 10,01 10,02 10,03 10,04 10,05 10,06 10,07 10,08 10,09 10,10 10,11 10,12 10,13 GOA
  11. ↑ 11,0 11,1 Löwenberg B. FoxO3a regulates erythroid differentiation and induces BTG1, an activator of protein arginine methyl transferase 1 // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2004. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200307056 — PMID:14734530
  12. ↑ 12,0 12,1 A Brunet, A Bonni, Zigmond M. J. et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor // Cell — Cell Press, Elsevier BV, 1999. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(00)80595-4 — PMID:10102273
  13. ↑ 13,0 13,1 13,2 Wang K., Li P. Foxo3a regulates apoptosis by negatively targeting miR-21 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2010. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M109.093005 — PMID:20371612
  14. ↑ Vaquerizas J. M., Teichmann S., Kummerfeld S. K. A census of human transcription factors: function, expression and evolution // Nature reviews. Genetics — United Kingdom: NPG, 2009. — ISSN 1471-0056; 1471-0064 — doi:10.1038/NRG2538 — PMID:19274049
  15. ↑ Vaquerizas J. M., Teichmann S., Kummerfeld S. K. A census of human transcription factors: function, expression and evolution // Nature reviews. Genetics — United Kingdom: NPG, 2009. — ISSN 1471-0056; 1471-0064 — doi:10.1038/NRG2538 — PMID:19274049
  16. ↑ 16,0 16,1 16,2 16,3 16,4 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform. — OUP, 2011. — ISSN 1467-5463; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
  17. ↑ 17,0 17,1 17,2 Löwenberg B. FoxO3a regulates erythroid differentiation and induces BTG1, an activator of protein arginine methyl transferase 1 // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2004. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200307056 — PMID:14734530
  18. ↑ 18,0 18,1 18,2 18,3 A Brunet, A Bonni, Zigmond M. J. et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor // Cell — Cell Press, Elsevier BV, 1999. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(00)80595-4 — PMID:10102273
  19. ↑ Hung M., Lee D., Xia W. et al. IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a // Cell — Cell Press, Elsevier BV, 2004. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(04)00302-2 — PMID:15084260
  20. ↑ Tezil T., Fasano C., Peserico A. et al. Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy // Cell Death Dis. — London: Nature Publishing Group, 2018. — ISSN 2041-4889 — doi:10.1038/S41419-018-0336-0 — PMID:29445193
  21. ↑ 21,0 21,1 Hung M., Lee D., Xia W. et al. IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a // Cell — Cell Press, Elsevier BV, 2004. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(04)00302-2 — PMID:15084260
  22. ↑ Patterson C., Bode C., Augustin H. BMPER is an endothelial cell regulator and controls bone morphogenetic protein-4-dependent angiogenesis // Circ. Res. — Lippincott Williams & Wilkins, 2008. — ISSN 0009-7330; 1524-4571 — doi:10.1161/CIRCRESAHA.108.178434 — PMID:18787191
  23. ↑ Wang K., Li P. Foxo3a regulates apoptosis by negatively targeting miR-21 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2010. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M109.093005 — PMID:20371612
  24. ↑ Hanniford D., Bhardwaj N. Aberrant miR-182 expression promotes melanoma metastasis by repressing FOXO3 and microphthalmia-associated transcription factor // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2009. — 6 p. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0808263106 — PMID:19188590
  25. ↑ Patterson C., Bode C., Augustin H. BMPER is an endothelial cell regulator and controls bone morphogenetic protein-4-dependent angiogenesis // Circ. Res. — Lippincott Williams & Wilkins, 2008. — ISSN 0009-7330; 1524-4571 — doi:10.1161/CIRCRESAHA.108.178434 — PMID:18787191
  26. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  27. ↑ 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=FOXO3&oldid=4128632