Wikipedia

GBA (ген)

GBA (ген) (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[16][17]

GBA
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген GBA[d][1]
Молекулярная функция hydrolase activity, acting on glycosyl bonds[d][2], связывание с белками плазмы[d][3][4], гидролазная активность[d][2][2], signaling receptor binding[d][5][2] һәм glucosylceramidase activity[d][6][7][2][…]
Күзәнәк компоненты мембрана[d][2], Лизосома[d][2][2], экзосома[d][8][9], lysosomal lumen[d][5][2], lysosomal membrane[d][2][5][2][…] һәм внеклеточное пространство[d][2]
Биологический процесс termination of signal transduction[d][10], skin morphogenesis[d][2], glycosphingolipid metabolic process[d][2], positive regulation of protein dephosphorylation[d][10], липидный обмен[d][2], response to testosterone[d][2], cellular response to starvation[d][2], negative regulation of interleukin-6 production[d][10], response to thyroid hormone[d][2], ceramide biosynthetic process[d][11], cellular response to tumor necrosis factor[d][10], sphingosine biosynthetic process[d][11], positive regulation of proteolysis involved in cellular protein catabolic process[d][7][2], regulation of water loss via skin[d][2], response to estrogen[d][2], glucosylceramide catabolic process[d][7][11][2], negative regulation of MAP kinase activity[d][10], response to pH[d][2], Метаболизм[2], negative regulation of inflammatory response[d][10], regulation of macroautophagy[d][12], sphingolipid metabolic process[d][2][2], mitochondrion organization[d][13], neuron projection development[d][13], regulation of cellular protein metabolic process[d][13], positive regulation of proteasomal ubiquitin-dependent protein catabolic process[d][2], negative regulation of protein homooligomerization[d][2][14], cell death in response to oxidative stress[d][13], positive regulation of protein-containing complex disassembly[d][14], regulation of protein metabolic process[d][2], negative regulation of neuron death[d][14], positive regulation of protein lipidation[d][14], positive regulation of neuronal action potential[d][13], positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization[d][2], autophagosome organization[d][2], regulation of lysosomal protein catabolic process[d][13], beta-glucoside catabolic process[d][2] һәм response to dexamethasone[d][2]
Тәэсир итешә афегостат[d][15]
Изображение Gene Atlas

Искәрмәләр 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 GOA
  3. ↑ Dhe-Paganon S., Loppnau P., Schwake M. et al. Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36 // Nature / M. Skipper — NPG, Springer Science+Business Media, 2013. — ISSN 1476-4687; 0028-0836 — doi:10.1038/NATURE12684 — PMID:24162852
  4. ↑ Kaneski C. R., Xu D. S., Hodes R. J. Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2010. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1014376107 — PMID:21098288
  5. ↑ 5,0 5,1 5,2 Schwake M., Saftig P. LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase // Cell — Cell Press, Elsevier BV, 2007. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2007.10.018 — PMID:18022370
  6. ↑ Dermentzaki G., Dimitriou E., Xilouri M. et al. Loss of β-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells // PLOS ONE / PLOS ONE Editors — PLoS, 2013. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0060674 — PMID:23580063
  7. ↑ 7,0 7,1 7,2 Caldwell G. A. Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies // Cell — Cell Press, Elsevier BV, 2011. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2011.06.001 — PMID:21700325
  8. ↑ Sinha A., Kislinger T. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine // Proteomics / L. Stimson — Wiley, 2013. — ISSN 1615-9853; 1615-9861 — doi:10.1002/PMIC.201200561 — PMID:23533145
  9. ↑ Farina A., Lane L., Lescuyer P. et al. Proteomic analysis of podocyte exosome-enriched fraction from normal human urine // Journal of Proteomics — Elsevier BV, 2013. — ISSN 1874-3919; 0165-022X — doi:10.1016/J.JPROT.2013.01.012 — PMID:23376485
  10. ↑ 10,0 10,1 10,2 10,3 10,4 10,5 Kitatani K., Obeid L. M., Hannun Y. A. et al. Acid beta-glucosidase 1 counteracts p38delta-dependent induction of interleukin-6: possible role for ceramide as an anti-inflammatory lipid // 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.M809500200 — PMID:19279008
  11. ↑ 11,0 11,1 11,2 Hannun Y. A., Jenkins R. W. Involvement of acid beta-glucosidase 1 in the salvage pathway of ceramide formation // 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.M802790200 — PMID:19279011
  12. ↑ Gegg M. E., Anthony H V Schapira Mitochondrial dysfunction associated with glucocerebrosidase deficiency // Neurobiol. Dis. — Elsevier BV, 2016. — ISSN 0969-9961; 1095-953X — doi:10.1016/J.NBD.2015.09.006 — PMID:26388395
  13. ↑ 13,0 13,1 13,2 13,3 13,4 13,5 Nirenberg M. J., Kuo S., Rubin L. et al. iPSC-derived dopamine neurons reveal differences between monozygotic twins discordant for Parkinson's disease // Cell Reports — Cell Press, Elsevier BV, 2014. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2014.10.023 — PMID:25456120
  14. ↑ 14,0 14,1 14,2 14,3 Smith G. A., Hallett P. J., Isacson O. Glucocerebrosidase gene therapy prevents α-synucleinopathy of midbrain dopamine neurons // Neurobiol. Dis. — Elsevier BV, 2015. — ISSN 0969-9961; 1095-953X — doi:10.1016/J.NBD.2015.09.009 — PMID:26392287
  15. ↑ Open Targets Platform
  16. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  17. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар 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.)


Бу — аксым турында мәкалә төпчеге.
Сез мәкаләне үзгәртеп һәм мәгълүмат өстәп,   Википедия проектына ярдәм итә аласыз.
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