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Wikipedia
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NCR3

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/NCR3 latin yazuında])
NCR3
Нинди таксонда барH. sapiens[d][1]
Кодлаучы генNCR3[d][1]
Молекуляр функцияsignaling receptor binding[d][2],гомодимеризация белка[d][2],cell adhesion molecule binding[d][2],связывание с белками плазмы[d][3][4][5][…] һәмсвязывание похожих белков[d][6][7][8]
Күзәнәк компонентымембрана өлеше[d][9],күзәнәк мембранасы[d][9][9],күзәнәк мембранасы өлеше[d][10] һәммембрана[d][9]
Биологик процессsusceptibility to T cell mediated cytotoxicity[d][2],heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules[d][2],воспалительная реакция[d][11],cell recognition[d][12],positive regulation of natural killer cell mediated cytotoxicity[d][13],positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target[d][2],иммун җавап[d][11],susceptibility to natural killer cell mediated cytotoxicity[d][2],homophilic cell adhesion via plasma membrane adhesion molecules[d][2],regulation of immune response[d][9],immune response-activating cell surface receptor signaling pathway[d][14],natural killer cell activation[d][14],immune system process[d][9],immune response-activating cell surface receptor signaling pathway[d][3][15],natural killer cell activation[d][3][15] һәмpositive regulation of natural killer cell mediated cytotoxicity[d][12][15]

NCR3 (ингл. ) —аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[16][17]

Искәрмәләр

[үзгәртү |вики-текстны үзгәртү]
  1. 1,01,1UniProt
  2. 2,02,12,22,32,42,52,62,7GOA
  3. 3,03,13,2Engert A.,Elke Pogge von StrandmannDendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function //PLOS ONE /PLOS ONE EditorsPLoS, 2008. — ISSN1932-6203doi:10.1371/JOURNAL.PONE.0003377PMID:18852879
  4. Steinle A.,Hartmann J.The Stalk Domain of NKp30 Contributes to Ligand Binding and Signaling of a Preassembled NKp30-CD3ζ Complex //J. Biol. Chem. /L. M. GieraschBaltimore [etc.]:American Society for Biochemistry and Molecular Biology, 2016. — 12 p. — ISSN0021-9258;1083-351X;1067-8816doi:10.1074/JBC.M116.742981PMID:27754869
  5. Geng J.Tumor-released Galectin-3, a soluble inhibitory ligand of human NKp30, plays an important role in tumor escape from NK cell attack //J. Biol. Chem. /L. M. GieraschBaltimore [etc.]:American Society for Biochemistry and Molecular Biology, 2014. — ISSN0021-9258;1083-351X;1067-8816doi:10.1074/JBC.M114.603464PMID:25315772
  6. Hartmann J.,Davies K.Homo-oligomerization of the activating natural killer cell receptor NKp30 ectodomain increases its binding affinity for cellular ligands //J. Biol. Chem. /L. M. GieraschBaltimore [etc.]:American Society for Biochemistry and Molecular Biology, 2013. — ISSN0021-9258;1083-351X;1067-8816doi:10.1074/JBC.M113.514786PMID:24275655
  7. Colonna M.,Joyce M. G.Crystal structure of human natural cytotoxicity receptor NKp30 and identification of its ligand binding site //Proc. Natl. Acad. Sci. U.S.A. /M. R. Berenbaum[Washington, etc.],USA:National Academy of Sciences [etc.], 2011. — ISSN0027-8424;1091-6490doi:10.1073/PNAS.1100622108PMID:21444796
  8. Tampé R.,Diefenbach A.The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding //J. Biol. Chem. /L. M. GieraschBaltimore [etc.]:American Society for Biochemistry and Molecular Biology, 2012. — ISSN0021-9258;1083-351X;1067-8816doi:10.1074/JBC.M111.304238PMID:22807449
  9. 9,09,19,29,39,49,5GOA
  10. I. Holzinger, Baey A. d., G. Messer et al.Cloning and genomic characterization of LST1: a new gene in the human TNF region //ImmunogeneticsSpringer Science+Business Media, 1995. — ISSN0093-7711;1432-1211doi:10.1007/BF00179392PMID:7590964
  11. 11,011,1R Sivakamasundari, A Raghunathan, Zhang C. Y. et al.Expression and cellular localization of the protein encoded by the 1C7 gene: a recently described component of the MHC //ImmunogeneticsSpringer Science+Business Media, 2000. — ISSN0093-7711;1432-1211doi:10.1007/S002510000192PMID:10941844
  12. 12,012,1Romagnani P.,Marcenaro S.,Lazzeri E. et al.Expression of the DNAM-1 ligands, Nectin-2 (CD112) and poliovirus receptor (CD155), on dendritic cells: relevance for natural killer-dendritic cell interaction //BloodAmerican Society of Hematology,Elsevier BV, 2005. — 7 p. — ISSN0006-4971;1528-0020doi:10.1182/BLOOD-2005-07-2696PMID:16304049
  13. Romagnani P.,Marcenaro S.,Lazzeri E. et al.Expression of the DNAM-1 ligands, Nectin-2 (CD112) and poliovirus receptor (CD155), on dendritic cells: relevance for natural killer-dendritic cell interaction //BloodAmerican Society of Hematology,Elsevier BV, 2005. — 7 p. — ISSN0006-4971;1528-0020doi:10.1182/BLOOD-2005-07-2696PMID:16304049
  14. 14,014,1Engert A.,Elke Pogge von StrandmannDendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function //PLOS ONE /PLOS ONE EditorsPLoS, 2008. — ISSN1932-6203doi:10.1371/JOURNAL.PONE.0003377PMID:18852879
  15. 15,015,115,2Livstone 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. — ISSN1467-5463;1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  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 |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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