NOD2

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/NOD2 latin yazuında])
NOD2
Сурәт
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген NOD2[d][1]
Молекулярная функция Hsp90 protein binding[d][2], нуклеотид-связывающий[d][3], Hsp70 protein binding[d][2], связывание с белками плазмы[d][4][5][6][…], peptidoglycan binding[d][7], enzyme binding[d][8], actin binding[d][2], CARD domain binding[d][9], АТФ-связанные[d][3], protein kinase binding[d][10][11][2], muramyl dipeptide binding[d][3][7] һәм protein-containing complex binding[d][6]
Күзәнәк компоненты Цитоплазма[12][13][13][…], цитозоль[d][13][13][14], Везикула[d][15][7], мембрана[d][3], күзәнәк мембраны[d][3][16][7], поверхность клетки[d][17], basolateral plasma membrane[d][3][18], Сигналосома COP9[d][19], Цитоскелет[d][15], Гольджи аппараты[3], митохондрия[d][3], protein-containing complex[d][15], Цитоплазма[20][3][3][…] һәм цитозоль[d][3][3][7][…]
Биологический процесс positive regulation of prostaglandin-endoperoxide synthase activity[d][3], regulation of apoptotic process[d][3], defense response[d][20], detection of biotic stimulus[d][20], cytokine production involved in immune response[d][21], positive regulation of cytokine production involved in inflammatory response[d][22], intracellular signal transduction[d][23], detection of muramyl dipeptide[d][24][7], positive regulation of interleukin-10 production[d][3], positive regulation of epithelial cell proliferation[d][3], immune system process[d][3], positive regulation of oxidoreductase activity[d][3], response to muramyl dipeptide[d][25][13][14][…], positive regulation of prostaglandin-E synthase activity[d][3], positive regulation of JNK cascade[d][26], positive regulation of nitric-oxide synthase biosynthetic process[d][3], positive regulation of NIK/NF-kappaB signaling[d][16], positive regulation of phosphatidylinositol 3-kinase activity[d][3], positive regulation of gamma-delta T cell activation[d][3], cellular response to muramyl dipeptide[d][27][16][15], JNK cascade[d][3], negative regulation of macrophage apoptotic process[d][3], positive regulation of dendritic cell antigen processing and presentation[d][3], nucleotide-binding oligomerization domain containing 2 signaling pathway[d][28][24], maintenance of gastrointestinal epithelium[d][29], defense response to bacterium[d][23], positive regulation of NF-kappaB transcription factor activity[d][3][18][2][…], positive regulation of interleukin-8 production[d][2], detection of bacterium[d][30], positive regulation of interleukin-1 beta production[d][31], regulation of inflammatory response[d][32], positive regulation of interleukin-6 production[d][33], protein complex oligomerization[d][20], positive regulation of tumor necrosis factor production[d][31][26], positive regulation of ERK1 and ERK2 cascade[d][3], positive regulation of I-kappaB kinase/NF-kappaB signaling[d][34][35], positive regulation of B cell activation[d][36], positive regulation of interleukin-17 production[d][37], positive regulation of type 2 immune response[d][38], nucleotide-binding oligomerization domain containing signaling pathway[d][3], positive regulation of stress-activated MAPK cascade[d][26], positive regulation of Notch signaling pathway[d][3], положительная регуляция транскрипции РНК полимеразой II промотор[d][15], cellular response to organic cyclic compound[d][3], позитивная регуляция пролиферации клеток[d][3], Врождённый иммунитет[d][39][3][28], response to nutrient[d][3], positive regulation of dendritic cell cytokine production[d][3], positive regulation of protein K63-linked ubiquitination[d][11], cellular response to peptidoglycan[d][3], positive regulation of MAP kinase activity[d][3], interleukin-1-mediated signaling pathway[d][3], cellular response to lipopolysaccharide[d][27], response to muramyl dipeptide[d][2][3][7][…], intracellular signal transduction[d][30][40], defense response to bacterium[d][30][40] һәм positive regulation of I-kappaB kinase/NF-kappaB signaling[d][9][24][40]
Изображение Gene Atlas

NOD2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[41][42]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,0 2,1 2,2 2,3 2,4 2,5 2,6 Mohanan V., Grimes C. L. The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2014. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M114.557686 — PMID:24790089
  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 GOA
  4. ↑ Pio F., Godzik A. CLAN, a novel human CED-4-like gene // Genomics / A. Engel — Academic Press, Elsevier BV, 2001. — ISSN 0888-7543; 1089-8646 — doi:10.1006/GENO.2001.6579 — PMID:11472070
  5. ↑ Fillet M., Louis E. The c-Jun N-terminal kinase (JNK)-binding protein (JNKBP1) acts as a negative regulator of NOD2 protein signaling by inhibiting its oligomerization process // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2012. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M112.355545 — PMID:22700971
  6. ↑ 6,0 6,1 Jean da Silva Correia, Miranda Y., Leonard N. et al. The subunit CSN6 of the COP9 signalosome is cleaved during apoptosis // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2007. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M609587200 — PMID:17337451
  7. ↑ 7,0 7,1 7,2 7,3 7,4 7,5 7,6 Barnich N. Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2005. — 6 p. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200502153 — PMID:15998797
  8. ↑ Barnich N. GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2005. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M413776200 — PMID:15753091
  9. ↑ 9,0 9,1 G Nunez Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2001. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M008072200 — PMID:11087742
  10. ↑ Chen C., Gong Y., Zhang M. et al. Reciprocal cross-talk between Nod2 and TAK1 signaling pathways // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M400682200 — PMID:15075345
  11. ↑ 11,0 11,1 Chauhan S., Deretic V. IRGM governs the core autophagy machinery to conduct antimicrobial defense // Mol. Cell — Cell Press, Elsevier BV, 2015. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2015.03.020 — PMID:25891078
  12. ↑ Tschopp J. NLRs join TLRs as innate sensors of pathogens // Trends in Immunology — Elsevier BV, 2005. — ISSN 1471-4906; 1471-4981; 0167-5699 — doi:10.1016/J.IT.2005.06.004 — PMID:15967716
  13. ↑ 13,0 13,1 13,2 13,3 13,4 GOA
  14. ↑ 14,0 14,1 Barnich N. Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2005. — 6 p. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200502153 — PMID:15998797
  15. ↑ 15,0 15,1 15,2 15,3 15,4 Xavier R. Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1 // Inflammatory Bowel Diseases — Lippincott Williams & Wilkins, OUP, 2012. — ISSN 1078-0998; 1536-4844 — doi:10.1002/IBD.21851 — PMID:21887730
  16. ↑ 16,0 16,1 16,2 Monie T. P. Blau syndrome polymorphisms in NOD2 identify nucleotide hydrolysis and helical domain 1 as signalling regulators // FEBS Letters — Elsevier BV, 2014. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2014.07.029 — PMID:25093298
  17. ↑ Kufer T. A. Role for erbin in bacterial activation of Nod2 // Infect. Immun. / A. J. Bäumler — ASM, Hindawi Publishing Corporation, 2006. — ISSN 0019-9567; 1098-5522; 1070-6313 — doi:10.1128/IAI.00035-06 — PMID:16714539
  18. ↑ 18,0 18,1 McDonald C., Chen F. F., Ollendorff V. et al. A role for Erbin in the regulation of Nod2-dependent NF-kappaB signaling // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2005. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M508538200 — PMID:16203728
  19. ↑ Jean da Silva Correia, Miranda Y., Leonard N. et al. The subunit CSN6 of the COP9 signalosome is cleaved during apoptosis // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2007. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M609587200 — PMID:17337451
  20. ↑ 20,0 20,1 20,2 20,3 Tschopp J. NLRs join TLRs as innate sensors of pathogens // Trends in Immunology — Elsevier BV, 2005. — ISSN 1471-4906; 1471-4981; 0167-5699 — doi:10.1016/J.IT.2005.06.004 — PMID:15967716
  21. ↑ Dinarello C. A., Netea M. G., Kim J. IL-32 synergizes with nucleotide oligomerization domain (NOD) 1 and NOD2 ligands for IL-1beta and IL-6 production through a caspase 1-dependent mechanism // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2005. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0508237102 — PMID:16260731
  22. ↑ Kapoor A. Activation of nucleotide oligomerization domain 2 (NOD2) by human cytomegalovirus initiates innate immune responses and restricts virus replication // PLOS ONE / PLOS ONE Editors — PLoS, 2014. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0092704 — PMID:24671169
  23. ↑ 23,0 23,1 Suttorp N., Hippenstiel S., Schmeck B. et al. Nod1-mediated endothelial cell activation by Chlamydophila pneumoniae // Circ. Res. — Lippincott Williams & Wilkins, 2005. — ISSN 0009-7330; 1524-4571 — doi:10.1161/01.RES.0000155721.83594.2C — PMID:15653568
  24. ↑ 24,0 24,1 24,2 Boneca I. G., Chamaillard M., Sansonetti P. J. et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.C200651200 — PMID:12527755
  25. ↑ Mohanan V., Grimes C. L. The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2014. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M114.557686 — PMID:24790089
  26. ↑ 26,0 26,1 26,2 Hsu Y. S., Zhang Y., You Y. et al. The adaptor protein CARD9 is required for innate immune responses to intracellular pathogens // Nat. Immunol. — USA: NPG, 2007. — ISSN 1529-2908; 1529-2916 — doi:10.1038/NI1426 — PMID:17187069
  27. ↑ 27,0 27,1 Lécine P., Perroy J., Borg J. et al. Characterization and Genetic Analyses of New Genes Coding for NOD2 Interacting Proteins // PLOS ONE / PLOS ONE Editors — PLoS, 2016. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0165420 — PMID:27812135
  28. ↑ 28,0 28,1 Komander D., Damgaard R. B., Gyrd-Hansen M. et al. OTULIN restricts Met1-linked ubiquitination to control innate immune signaling // Mol. Cell — Cell Press, Elsevier BV, 2013. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2013.06.004 — PMID:23806334
  29. ↑ Stremmel W., Schmitz G. Aberrant intestinal expression and allelic variants of mucin genes associated with inflammatory bowel disease // J. Mol. Med. — Springer Science+Business Media, 2006. — ISSN 0946-2716; 1432-1440 — doi:10.1007/S00109-006-0100-2 — PMID:17058067
  30. ↑ 30,0 30,1 30,2 Suttorp N., Hippenstiel S., Schmeck B. et al. Nod1-mediated endothelial cell activation by Chlamydophila pneumoniae // Circ. Res. — Lippincott Williams & Wilkins, 2005. — ISSN 0009-7330; 1524-4571 — doi:10.1161/01.RES.0000155721.83594.2C — PMID:15653568
  31. ↑ 31,0 31,1 Núñez G. NOD2 controls the nature of the inflammatory response and subsequent fate of Mycobacterium tuberculosis and M. bovis BCG in human macrophages // Cellular Microbiology — Wiley-Blackwell, 2011. — ISSN 1462-5814; 1462-5822 — doi:10.1111/J.1462-5822.2010.01544.X — PMID:21040358
  32. ↑ Duerr R. H., Brant S. R., Cho J. H. et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease // Nature / M. Skipper — NPG, Springer Science+Business Media, 2001. — ISSN 1476-4687; 0028-0836 — doi:10.1038/35079114 — PMID:11385577
  33. ↑ Zamora D. O. Human endothelial cells express NOD2/CARD15 and increase IL-6 secretion in response to muramyl dipeptide // Microvascular Research — Elsevier BV, 2006. — ISSN 0026-2862; 1095-9319 — doi:10.1016/J.MVR.2005.11.010 — PMID:16414084
  34. ↑ G Nunez Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2001. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M008072200 — PMID:11087742
  35. ↑ Boneca I. G., Chamaillard M., Sansonetti P. J. et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.C200651200 — PMID:12527755
  36. ↑ Riesbeck K., Cardell L. Effects of NOD-like receptors in human B lymphocytes and crosstalk between NOD1/NOD2 and Toll-like receptors // J. Leukoc. Biol. / L. Montaner — Wiley-Blackwell, 2011. — ISSN 0741-5400; 1938-3673 — doi:10.1189/JLB.0210061 — PMID:20844241
  37. ↑ Astrid J van Beelen, Zelinkova Z., Taanman-Kueter E. W. et al. Stimulation of the intracellular bacterial sensor NOD2 programs dendritic cells to promote interleukin-17 production in human memory T cells // Immunity — Cell Press, Elsevier BV, 2007. — ISSN 1074-7613; 1097-4180 — doi:10.1016/J.IMMUNI.2007.08.013 — PMID:17919942
  38. ↑ Chaudhary R., David A van Heel NOD2 activity modulates the phenotype of LPS-stimulated dendritic cells to promote the development of T-helper type 2-like lymphocytes - Possible implications for NOD2-associated Crohn's disease // Journal of Crohn's and Colitis — OUP, 2007. — ISSN 1873-9946; 1876-4479 — doi:10.1016/J.CROHNS.2007.08.006 — PMID:21172192
  39. ↑ Travassos L. H., Carneiro L. A. The Nodosome: Nod1 and Nod2 control bacterial infections and inflammation // Seminars in Immunopathology — Springer Science+Business Media, 2007. — ISSN 1863-2297; 0344-4325; 1863-2300; 1432-2196 — doi:10.1007/S00281-007-0083-2 — PMID:17690884
  40. ↑ 40,0 40,1 40,2 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
  41. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  42. ↑ 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
 Бу — аксым турында мәкалә төпчеге.
Сез мәкаләне үзгәртеп һәм мәгълүмат өстәп, Википедия проектына ярдәм итә аласыз.
Чыганак — https://tt.wikipedia.org/w/index.php?title=NOD2&oldid=4132112