Wikipedia

CD4

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

CD4
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген CD4[d][1]
Молекулярная 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], часть мембраны[d][3][3], early endosome[d][3], мембрана[d][3][3], поверхность клетки[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 мембраны[d][3][3][3][…], clathrin-coated vesicle membrane[d][3], часть клеточной мембраны[d][12], наружная сторона клеточной мембраны[d][3][25][22] һәм Липидный рафт[d][3][5][22]
Биологический 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], immune system process[d][3], positive regulation of calcium ion transport into cytosol[d][3], regulation of T cell activation[d][30], иммунный ответ[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]
Изображение Gene Atlas

Искәрмәләр үзгәртү

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,0 2,1 2,2 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; 1550-6606 — PMID:10358157
  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 3,38 3,39 3,40 3,41 3,42 GOA
  4. ↑ 4,0 4,1 Cohen E. A. CD4 dimers constitute the functional component required for T cell activation // J. Immunol. — Baltimore: 2002. — ISSN 0022-1767; 1550-6606 — doi:10.4049/JIMMUNOL.169.11.6261 — PMID:12444132
  5. ↑ 5,0 5,1 5,2 Kwong P. D. Dimeric association and segmental variability in the structure of human CD4 // Nature / M. Skipper — NPG, Springer Science+Business Media, 1997. — ISSN 1476-4687; 0028-0836 — doi:10.1038/387527A0 — PMID: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 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1998. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.273.30.18729 — PMID:9668045
  7. ↑ 7,0 7,1 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 Editors — PLoS, 2009. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0005006 — PMID: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; 1091-6490 — doi:10.1073/PNAS.92.2.349 — PMID: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; 1091-6490 — doi:10.1073/PNAS.97.16.9026 — PMID: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 // Cell — Cell Press, Elsevier BV, 1996. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(00)81314-8 — PMID:8674120
  11. ↑ 11,0 11,1 11,2 11,3 11,4 Miceli M. C., Parnes J. R. Role of CD4 and CD8 in T cell activation and differentiation // Advances in Immunology — Elsevier BV, 1993. — ISSN 0065-2776; 1557-8445 — doi:10.1016/S0065-2776(08)60498-8 — PMID:8512039
  12. ↑ 12,00 12,01 12,02 12,03 12,04 12,05 12,06 12,07 12,08 12,09 12,10 12,11 12,12 12,13 12,14 12,15 Zack J. A. CD4 ligation on human blood monocytes triggers macrophage differentiation and enhances HIV infection // J. Virol. — ASM, 2014. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.00616-14 — PMID:24942581
  13. ↑ Miceli M. C., Parnes J. R. Role of CD4 and CD8 in T cell activation and differentiation // Advances in Immunology — Elsevier BV, 1993. — ISSN 0065-2776; 1557-8445 — doi:10.1016/S0065-2776(08)60498-8 — PMID:8512039
  14. ↑ 14,0 14,1 14,2 Zack J. A. CD4 ligation on human blood monocytes triggers macrophage differentiation and enhances HIV infection // J. Virol. — ASM, 2014. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.00616-14 — PMID:24942581
  15. ↑ Strominger J. L. Interaction between CD4 and class II MHC molecules mediates cell adhesion // Nature / M. Skipper — NPG, Springer Science+Business Media, 1987. — ISSN 1476-4687; 0028-0836 — doi:10.1038/330256A0 — PMID: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 // Cell — Cell Press, Elsevier BV, 1988. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(88)90053-0 — PMID:3262426
  17. ↑ 17,0 17,1 17,2 17,3 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 // Biochemistry / A. Schepartz — ACS, 1999. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI990654O — PMID: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; 1749-6632 — doi:10.1111/J.1749-6632.1995.TB26652.X — PMID:7486703
  20. ↑ Strominger J. L. Interaction between CD4 and class II MHC molecules mediates cell adhesion // Nature / M. Skipper — NPG, Springer Science+Business Media, 1987. — ISSN 1476-4687; 0028-0836 — doi:10.1038/330256A0 — PMID: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 // Cell — Cell Press, Elsevier BV, 1988. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(88)90053-0 — PMID:3262426
  22. ↑ 22,0 22,1 22,2 22,3 22,4 22,5 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
  23. ↑ Kwong P. D. Dimeric association and segmental variability in the structure of human CD4 // Nature / M. Skipper — NPG, Springer Science+Business Media, 1997. — ISSN 1476-4687; 0028-0836 — doi:10.1038/387527A0 — PMID: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 // Blood — American Society of Hematology, Elsevier BV, 2007. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2006-06-030023 — PMID: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 // Blood — American Society of Hematology, Elsevier BV, 2007. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2006-06-030023 — PMID: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; 1067-8824 — doi:10.1128/MCB.10.10.5305 — PMID: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; 1550-6606 — PMID: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; 1550-6606 — PMID: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; 1540-9538 — doi:10.1084/JEM.185.11.2015 — PMID:9166430
  30. ↑ 30,0 30,1 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. Skipper — NPG, Springer Science+Business Media, 1992. — ISSN 1476-4687; 0028-0836 — doi:10.1038/356718A0 — PMID: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; 1550-6606 — PMID: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; 1550-6606 — doi:10.4049/JIMMUNOL.172.10.5887 — PMID:15128768
  33. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  34. ↑ 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.)


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