CCR2

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/CCR2 latin yazuında])
CCR2
Сурәт
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген CCR2[d][1]
Молекулярная функция CCR2 chemokine receptor binding[d][2], G protein-coupled receptor activity[d][3][3], гомодимеризация белка[d][3], signal transducer activity[d][4], chemokine receptor activity[d][5][3], C-C chemokine receptor activity[d][4][4], связывание с белками плазмы[d][6], cytokine binding[d][3], chemokine (C-C motif) ligand 2 binding[d][3], chemokine (C-C motif) ligand 12 binding[d][3], chemokine (C-C motif) ligand 7 binding[d][3], C-C chemokine receptor activity[d][3][3][7], chemokine binding[d][7] һәм C-C chemokine binding[d][7]
Күзәнәк компоненты часть мембраны[d][8][3][3], Перикарион[d][3], мембрана[d][3], күзәнәк мембраны[d][3][9][3][…], часть клеточной мембраны[d][10], neuronal cell body[d][3], дендрит[d][3], perinuclear region of cytoplasm[d][3], Цитоплазма[11], цитозоль[d][3], наружная сторона клеточной мембраны[d][4], Цитоплазма[2][7] һәм наружная сторона клеточной мембраны[d][3][7]
Биологический процесс negative regulation of adenylate cyclase activity[d][12], receptor signaling pathway via JAK-STAT[d][13], chemokine-mediated signaling pathway[d][3], cellular calcium ion homeostasis[d][3], positive regulation of monocyte chemotaxis[d][3][3][3][…], dendritic cell chemotaxis[d][14], хемотаксис[d][15][4], blood vessel remodeling[d][3][3], response to wounding[d][10], иммунный ответ[d][16][4][4], воспалительная реакция[d][15][4][4], вирусный процесс[d][3], positive regulation of astrocyte chemotaxis[d][17], передача сигнала[d][3], positive regulation of cytosolic calcium ion concentration[d][18], G protein-coupled receptor signaling pathway[d][3][3][3], monocyte chemotaxis[d][3], positive regulation of T-helper 1 type immune response[d][3][3], negative regulation of type 2 immune response[d][3][3], humoral immune response[d][3], cellular defense response[d][19][3], regulation of vascular endothelial growth factor production[d][3][3], positive regulation of T cell chemotaxis[d][3][3], negative regulation of angiogenesis[d][3][3], ноцицепция[d][4], cellular homeostasis[d][3][3], regulation of cell migration[d][3], positive regulation of interferon-gamma production[d][3][3], positive regulation of interleukin-2 production[d][3][3], T-helper 17 cell chemotaxis[d][3][3], negative regulation of eosinophil degranulation[d][3][3], positive regulation of alpha-beta T cell proliferation[d][3][3], homeostasis of number of cells within a tissue[d][3], positive regulation of inflammatory response[d][3][3], positive regulation of T cell activation[d][3][3], leukocyte adhesion to vascular endothelial cell[d][3], positive regulation of immune complex clearance by monocytes and macrophages[d][3][3], neutrophil clearance[d][3], positive regulation of leukocyte tethering or rolling[d][3], positive regulation of monocyte extravasation[d][3][3], positive regulation of CD8-positive, alpha-beta T cell extravasation[d][3][3], positive regulation of hematopoietic stem cell migration[d][3][3], cytokine-mediated signaling pathway[d][3][2], гемопоэз[d][3], хемотаксис[d][5][3][7], воспалительная реакция[d][5][3][3][…], иммунный ответ[d][20][3][3][…], positive regulation of cytosolic calcium ion concentration[d][21][7], calcium-mediated signaling[d][7], cell chemotaxis[d][7], positive regulation of cold-induced thermogenesis[d][22][3], regulation of T cell cytokine production[d][3][3], ноцицепция[d][3][3], monocyte extravasation[d][3][3], regulation of T cell differentiation[d][3][3], regulation of inflammatory response[d][3][3], positive regulation of synaptic transmission, glutamatergic[d][3][3], inflammatory response to wounding[d][3][3], macrophage migration[d][3][3], positive regulation of thymocyte migration[d][3][3] һәм positive regulation of NMDA glutamate receptor activity[d][3]

CCR2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[23][24]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,0 2,1 2,2 Terashima Y., Kanegasaki S. Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte chemotaxis // Nat. Immunol. — USA: NPG, 2005. — ISSN 1529-2908; 1529-2916 — doi:10.1038/NI1222 — PMID:15995708
  3. ↑ 3,000 3,001 3,002 3,003 3,004 3,005 3,006 3,007 3,008 3,009 3,010 3,011 3,012 3,013 3,014 3,015 3,016 3,017 3,018 3,019 3,020 3,021 3,022 3,023 3,024 3,025 3,026 3,027 3,028 3,029 3,030 3,031 3,032 3,033 3,034 3,035 3,036 3,037 3,038 3,039 3,040 3,041 3,042 3,043 3,044 3,045 3,046 3,047 3,048 3,049 3,050 3,051 3,052 3,053 3,054 3,055 3,056 3,057 3,058 3,059 3,060 3,061 3,062 3,063 3,064 3,065 3,066 3,067 3,068 3,069 3,070 3,071 3,072 3,073 3,074 3,075 3,076 3,077 3,078 3,079 3,080 3,081 3,082 3,083 3,084 3,085 3,086 3,087 3,088 3,089 3,090 3,091 3,092 3,093 3,094 3,095 3,096 3,097 3,098 3,099 3,100 3,101 GOA
  4. ↑ 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 GOA
  5. ↑ 5,0 5,1 5,2 B Bottazzi, F Balkwill, A Mantovani Defective expression of the monocyte chemotactic protein-1 receptor CCR2 in macrophages associated with human ovarian carcinoma // J. Immunol. — Baltimore: 2000. — ISSN 0022-1767; 1550-6606 — doi:10.4049/JIMMUNOL.164.2.733 — PMID:10623817
  6. ↑ Paula V. d., Almeida F. C. L., Valente A. P. Structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor CCR2 and breast cancer microvesicles // Journal of Molecular Biology / P. Wright — Elsevier BV, 2013. — ISSN 0022-2836; 1089-8638 — doi:10.1016/J.JMB.2013.08.001 — PMID:23938203
  7. ↑ 7,0 7,1 7,2 7,3 7,4 7,5 7,6 7,7 7,8 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
  8. ↑ C Combadiere, Ahuja S. K., Damme J. V. et al. Monocyte chemoattractant protein-3 is a functional ligand for CC chemokine receptors 1 and 2B, Monocyte Chemoattractant Protein-3 Is a Functional Ligand for CC Chemokine Receptors 1 and 2B // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1995. — 5 p. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.270.50.29671 — PMID:8530354
  9. ↑ Agace W. W., Roberts A. I., L Wu et al. Human intestinal lamina propria and intraepithelial lymphocytes express receptors specific for chemokines induced by inflammation // Eur. J. Immunol. — Wiley-Blackwell, 2000. — ISSN 0014-2980; 1521-4141 — <819::AID-IMMU819>3.0.CO;2-Y doi:10.1002/1521-4141(200003)30:3<819::AID-IMMU819>3.0.CO;2-Y — PMID:10741397
  10. ↑ 10,0 10,1 Charo I. F., Myers S. J., A Herman et al. Molecular cloning and functional expression of two monocyte chemoattractant protein 1 receptors reveals alternative splicing of the carboxyl-terminal tails // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1994. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.91.7.2752 — PMID:8146186
  11. ↑ Terashima Y., Kanegasaki S. Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte chemotaxis // Nat. Immunol. — USA: NPG, 2005. — ISSN 1529-2908; 1529-2916 — doi:10.1038/NI1222 — PMID:15995708
  12. ↑ Wong L. M., Myers S. J., Tsou C. L. et al. Organization and differential expression of the human monocyte chemoattractant protein 1 receptor gene. Evidence for the role of the carboxyl-terminal tail in receptor trafficking // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1997. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.272.2.1038 — PMID:8995400
  13. ↑ M Mellado, Rodríguez-Frade J. M., A Aragay et al. The chemokine monocyte chemotactic protein 1 triggers Janus kinase 2 activation and tyrosine phosphorylation of the CCR2B receptor // J. Immunol. — Baltimore: 1998. — ISSN 0022-1767; 1550-6606 — PMID:9670957
  14. ↑ Rodríguez-Fernández J. L. The multiple personalities of the chemokine receptor CCR7 in dendritic cells // J. Immunol. — Baltimore: 2006. — ISSN 0022-1767; 1550-6606 — doi:10.4049/JIMMUNOL.176.9.5153 — PMID:16621978
  15. ↑ 15,0 15,1 B Bottazzi, F Balkwill, A Mantovani Defective expression of the monocyte chemotactic protein-1 receptor CCR2 in macrophages associated with human ovarian carcinoma // J. Immunol. — Baltimore: 2000. — ISSN 0022-1767; 1550-6606 — doi:10.4049/JIMMUNOL.164.2.733 — PMID:10623817
  16. ↑ McManus C. M., K Weidenheim, Woodman S. E. et al. Chemokine and chemokine-receptor expression in human glial elements: induction by the HIV protein, Tat, and chemokine autoregulation // Am. J. Pathol. — Elsevier BV, 2000. — ISSN 0002-9440; 1525-2191; 0097-3599 — doi:10.1016/S0002-9440(10)65013-4 — PMID:10751368
  17. ↑ Andjelkovic A. V., Song L., Dzenko K. A. et al. Functional expression of CCR2 by human fetal astrocytes // J. Neurosci. Res. — Wiley, 2002. — ISSN 0360-4012; 1097-4547 — doi:10.1002/JNR.10372 — PMID:12271471
  18. ↑ Frade J. M., M Mellado, Real G. d. et al. Characterization of the CCR2 chemokine receptor: functional CCR2 receptor expression in B cells // J. Immunol. — Baltimore: 1997. — ISSN 0022-1767; 1550-6606 — PMID:9548499
  19. ↑ Rabin R. L., Park M. K., F Liao et al. Chemokine receptor responses on T cells are achieved through regulation of both receptor expression and signaling // J. Immunol. — Baltimore: 1999. — ISSN 0022-1767; 1550-6606 — PMID:10201901
  20. ↑ McManus C. M., K Weidenheim, Woodman S. E. et al. Chemokine and chemokine-receptor expression in human glial elements: induction by the HIV protein, Tat, and chemokine autoregulation // Am. J. Pathol. — Elsevier BV, 2000. — ISSN 0002-9440; 1525-2191; 0097-3599 — doi:10.1016/S0002-9440(10)65013-4 — PMID:10751368
  21. ↑ Frade J. M., M Mellado, Real G. d. et al. Characterization of the CCR2 chemokine receptor: functional CCR2 receptor expression in B cells // J. Immunol. — Baltimore: 1997. — ISSN 0022-1767; 1550-6606 — PMID:9548499
  22. ↑ Qiu Y., Tian X. Y. Eosinophils and type 2 cytokine signaling in macrophages orchestrate development of functional beige fat // Cell — Cell Press, Elsevier BV, 2014. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2014.03.066 — PMID:24906148
  23. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  24. ↑ 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.)


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