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

NCR3
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген NCR3[d][1]
Молекуляр функция signaling receptor binding[d][2], гомодимеризация белка[d][2], cell adhesion molecule binding[d][2], связывание с белками плазмы[d][3][4][5][…] һәм связывание похожих белков[d][6][7][8]
Күзәнәк компоненты мембрана өлеше[d][9], күзәнәк мембранасы[d][9][9], күзәнәк мембранасы өлеше[d][10] һәм мембрана[d][9]
Биологик процесс susceptibility 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] һәм positive regulation of natural killer cell mediated cytotoxicity[d][12][15]

Искәрмәләр

үзгәртү
  1. 1,0 1,1 UniProt
  2. 2,0 2,1 2,2 2,3 2,4 2,5 2,6 2,7 GOA
  3. 3,0 3,1 3,2 Engert A., Elke Pogge von Strandmann Dendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function // PLOS ONE / PLOS ONE EditorsPLoS, 2008. — ISSN 1932-6203doi: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. — ISSN 0021-9258; 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. — ISSN 0021-9258; 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. — ISSN 0021-9258; 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. — ISSN 0027-8424; 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. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M111.304238PMID:22807449
  9. 9,0 9,1 9,2 9,3 9,4 9,5 GOA
  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. — ISSN 0093-7711; 1432-1211doi:10.1007/BF00179392PMID:7590964
  11. 11,0 11,1 R 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. — ISSN 0093-7711; 1432-1211doi:10.1007/S002510000192PMID:10941844
  12. 12,0 12,1 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. — ISSN 0006-4971; 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. — ISSN 0006-4971; 1528-0020doi:10.1182/BLOOD-2005-07-2696PMID:16304049
  14. 14,0 14,1 Engert A., Elke Pogge von Strandmann Dendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function // PLOS ONE / PLOS ONE EditorsPLoS, 2008. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0003377PMID:18852879
  15. 15,0 15,1 15,2 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; 1477-4054doi: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
  • 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.)