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Эчтәлеккә күчү

CD4

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/CD4 latin yazuında])
CD4
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген CD4[d][1]
Молекуляр функция transmembrane signaling receptor activity[d][2], virus receptor activity[d][3], гомодимеризация белка[d][4][5], zinc ion binding[d][6], extracellular matrix structural constituent[d][4], enzyme binding[d][7], immunoglobulin binding[d][3], связывание с белками плазмы[d][7][8][9][…], coreceptor activity[d][10][11][3], interleukin-16 binding[d][12], interleukin-16 receptor activity[d][12], MHC class II protein binding[d][13][14][15][…], связывание похожих белков[d][5], protein tyrosine kinase binding[d][16][17], signaling receptor activity[d][18], protein kinase binding[d][19][3], signaling receptor binding[d][3], MHC class II protein binding[d][11][12][20][…] һәм protein tyrosine kinase binding[d][21][3][22]
Күзәнәк компоненты endoplasmic reticulum lumen[d][3], мембрана өлеше[d][3][3], early endosome[d][3], мембрана[d][3][3], күзәнәк өслеге[d][3], endoplasmic reticulum membrane[d][3][3], липидный рафт[d][17][23], T cell receptor complex[d][11], наружная сторона клеточной мембраны[d][17][24], күзәнәк мембранасы[d][3][3][3][…], clathrin-coated vesicle membrane[d][3], күзәнәк мембранасы өлеше[d][12], наружная сторона клеточной мембраны[d][3][25][22] һәм липидный рафт[d][3][5][22]
Биологик процесс transmembrane receptor protein tyrosine kinase signaling pathway[d][11], defense response to Gram-negative bacterium[d][3], positive regulation of protein kinase activity[d][26], mitigation of host defenses by virus[d][3], positive regulation of calcium-mediated signaling[d][3], передача сигнала[d][27][2], helper T cell enhancement of adaptive immune response[d][3], T cell selection[d][28], response to estradiol[d][3], induction by virus of host cell-cell fusion[d][29], adaptive immune response[d][3], response to vitamin D[d][3], T cell differentiation[d][30], cell surface receptor signaling pathway[d][31][3], positive regulation of T cell proliferation[d][3], positive regulation of peptidyl-tyrosine phosphorylation[d][3], enzyme linked receptor protein signaling pathway[d][2], T cell activation[d][17], positive regulation of T cell activation[d][3], maintenance of protein location in cell[d][32], cytokine production[d][3], T cell receptor signaling pathway[d][3], процесс иммунной системы[d][3], positive regulation of calcium ion transport into cytosol[d][3], regulation of T cell activation[d][30], иммун җавап[d][11][3], агрегация клеток[d][3], вирусный процесс[d][3], fusion of virus membrane with host plasma membrane[d][3], membrane organization[d][3], positive regulation of protein phosphorylation[d][12], positive regulation of kinase activity[d][12], interleukin-15-mediated signaling pathway[d][14], positive regulation of I-kappaB kinase/NF-kappaB signaling[d][12], positive regulation of MAPK cascade[d][12], positive regulation of monocyte differentiation[d][12], ДНК-зависимая позитивная регуляция транскрипции[d][12], positive regulation of viral entry into host cell[d][12], regulation of calcium ion transport[d][12], positive regulation of ERK1 and ERK2 cascade[d][14], cellular response to granulocyte macrophage colony-stimulating factor stimulus[d][12], cytokine-mediated signaling pathway[d][3], interleukin-15-mediated signaling pathway[d][12][22], T cell activation[d][3][22], positive regulation of ERK1 and ERK2 cascade[d][12][22] һәм macrophage differentiation[d][12]
Пиктограмма
Изображение Gene Atlas
BERJAYA CD4 Викиҗыентыкта

CD4 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[33][34]

  1. 1 2 UniProt
  2. 1 2 3 Su S. B., W Gong, M Grimm et al. Inhibition of tyrosine kinase activation blocks the down-regulation of CXC chemokine receptor 4 by HIV-1 gp120 in CD4+ T cells // J. Immunol.Baltimore: 1999. — ISSN 0022-1767; 1550-6606PMID:10358157
  3. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 GOA
  4. 1 2 Cohen E. A. CD4 dimers constitute the functional component required for T cell activation // J. Immunol.Baltimore: 2002. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.169.11.6261PMID:12444132
  5. 1 2 3 Kwong P. D. Dimeric association and segmental variability in the structure of human CD4 // Nature / M. SkipperNPG, (untranslated), 1997. — ISSN 1476-4687; 0028-0836doi:10.1038/387527A0PMID:9168119
  6. M. Huse, Eck M. J., Harrison S. C. A Zn2+ ion links the cytoplasmic tail of CD4 and the N-terminal region of Lck, A Zn2+ Ion Links the Cytoplasmic Tail of CD4 and the N-terminal Region of Lck // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1998. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.273.30.18729PMID:9668045
  7. 1 2 Benichou S., Py B., Basmaciogullari S. et al. The phospholipid scramblases 1 and 4 are cellular receptors for the secretory leukocyte protease inhibitor and interact with CD4 at the plasma membrane // PLOS ONE / PLOS ONE EditorsPLoS, 2009. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0005006PMID:19333378
  8. S Salghetti, R Mariani, J Skowronski Human immunodeficiency virus type 1 Nef and p56lck protein-tyrosine kinase interact with a common element in CD4 cytoplasmic tail // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 1995. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.92.2.349PMID:7831289
  9. J Sodroski, R Wyatt, Kwong P. D. Energetics of the HIV gp120-CD4 binding reaction // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2000. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.97.16.9026PMID:10922058
  10. M. Parmentier A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors // CellCell Press, Elsevier, 1996. — ISSN 0092-8674; 1097-4172doi:10.1016/S0092-8674(00)81314-8PMID:8674120
  11. 1 2 3 4 5 Miceli M. C., Parnes J. R. Role of CD4 and CD8 in T cell activation and differentiation // Advances in ImmunologyElsevier, 1993. — ISSN 0065-2776; 1557-8445doi:10.1016/S0065-2776(08)60498-8PMID:8512039
  12. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 Zack J. A. CD4 ligation on human blood monocytes triggers macrophage differentiation and enhances HIV infection, CD4 Ligation on Human Blood Monocytes Triggers Macrophage Differentiation and Enhances HIV Infection // J. Virol.ASM, 2014. — ISSN 0022-538X; 1098-5514; 1070-6321doi:10.1128/JVI.00616-14PMID:24942581
  13. Miceli M. C., Parnes J. R. Role of CD4 and CD8 in T cell activation and differentiation // Advances in ImmunologyElsevier, 1993. — ISSN 0065-2776; 1557-8445doi:10.1016/S0065-2776(08)60498-8PMID:8512039
  14. 1 2 3 Zack J. A. CD4 ligation on human blood monocytes triggers macrophage differentiation and enhances HIV infection, CD4 Ligation on Human Blood Monocytes Triggers Macrophage Differentiation and Enhances HIV Infection // J. Virol.ASM, 2014. — ISSN 0022-538X; 1098-5514; 1070-6321doi:10.1128/JVI.00616-14PMID:24942581
  15. Strominger J. L. Interaction between CD4 and class II MHC molecules mediates cell adhesion // Nature / M. SkipperNPG, (untranslated), 1987. — ISSN 1476-4687; 0028-0836doi:10.1038/330256A0PMID:2823150
  16. A. Veillette, Bookman M. A., Horak E. M. et al. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck // CellCell Press, Elsevier, 1988. — ISSN 0092-8674; 1097-4172doi:10.1016/0092-8674(88)90053-0PMID:3262426
  17. 1 2 3 4 GOA
  18. J Sodroski, R Wyatt, P Kwong Conformational changes of gp120 in epitopes near the CCR5 binding site are induced by CD4 and a CD4 miniprotein mimetic // BiochemistryACS, 1999. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI990654OPMID:10413516
  19. Campbell K. S., A Buder, U Deuschle Interaction of p56lck with CD4 in the yeast two-hybrid system // Ann. New York Acad. Sci.New York: Wiley-Blackwell, 1995. — ISSN 0077-8923; 1749-6632doi:10.1111/J.1749-6632.1995.TB26652.XPMID:7486703
  20. Strominger J. L. Interaction between CD4 and class II MHC molecules mediates cell adhesion // Nature / M. SkipperNPG, (untranslated), 1987. — ISSN 1476-4687; 0028-0836doi:10.1038/330256A0PMID:2823150
  21. A. Veillette, Bookman M. A., Horak E. M. et al. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck // CellCell Press, Elsevier, 1988. — ISSN 0092-8674; 1097-4172doi:10.1016/0092-8674(88)90053-0PMID:3262426
  22. 1 2 3 4 5 6 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
  23. Kwong P. D. Dimeric association and segmental variability in the structure of human CD4 // Nature / M. SkipperNPG, (untranslated), 1997. — ISSN 1476-4687; 0028-0836doi:10.1038/387527A0PMID:9168119
  24. Wilson T. J., Presti R. M., Cella M. et al. FcRL6, a new ITIM-bearing receptor on cytolytic cells, is broadly expressed by lymphocytes following HIV-1 infection // BloodAmerican Society of Hematology, Elsevier, 2007. — ISSN 0006-4971; 1528-0020doi:10.1182/BLOOD-2006-06-030023PMID:17213291
  25. Wilson T. J., Presti R. M., Cella M. et al. FcRL6, a new ITIM-bearing receptor on cytolytic cells, is broadly expressed by lymphocytes following HIV-1 infection // BloodAmerican Society of Hematology, Elsevier, 2007. — ISSN 0006-4971; 1528-0020doi:10.1182/BLOOD-2006-06-030023PMID:17213291
  26. Luo K. X., Sefton B. M. Cross-linking of T-cell surface molecules CD4 and CD8 stimulates phosphorylation of the lck tyrosine protein kinase at the autophosphorylation site // Mol. Cell. Biol.ASM, 1990. — ISSN 0270-7306; 1098-5549; 1067-8824doi:10.1128/MCB.10.10.5305PMID:2118992
  27. Fauci A. S., M Dybul, AS F. et al. Dendritic cells express multiple chemokine receptors used as coreceptors for HIV entry // J. Immunol.Baltimore: 1998. — ISSN 0022-1767; 1550-6606PMID:9558100
  28. Frank G. D., Parnes J. R. The level of CD4 surface protein influences T cell selection in the thymus // J. Immunol.Baltimore: 1998. — ISSN 0022-1767; 1550-6606PMID:9551897
  29. F Liao, G Alkhatib, Peden K. W. et al. STRL33, A novel chemokine receptor-like protein, functions as a fusion cofactor for both macrophage-tropic and T cell line-tropic HIV-1 // J. Exp. Med.Rockefeller University Press, 1997. — ISSN 0022-1007; 1540-9538doi:10.1084/JEM.185.11.2015PMID:9166430
  30. 1 2 Seong R. H., Chamberlain J. W., Parnes J. R. Signal for T-cell differentiation to a CD4 cell lineage is delivered by CD4 transmembrane region and/or cytoplasmic tail // Nature / M. SkipperNPG, (untranslated), 1992. — ISSN 1476-4687; 0028-0836doi:10.1038/356718A0PMID:1533274
  31. FW R. HIV-1 envelope gp120 inhibits the monocyte response to chemokines through CD4 signal-dependent chemokine receptor down-regulation // J. Immunol.Baltimore: 1998. — ISSN 0022-1767; 1550-6606PMID:9780207
  32. Balamuth F., Brogdon J. L., Bottomly K. CD4 raft association and signaling regulate molecular clustering at the immunological synapse site // J. Immunol.Baltimore: 2004. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.172.10.5887PMID:15128768
  33. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  34. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.
  • 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.)