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ICAM1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/ICAM1 latin yazuında])
ICAM1
Сурәт
Нинди таксонда барH. sapiens[1]
Кодлаучы генICAM-1[d][1]
Молекуляр функцияvirus receptor activity[d][2],protein-containing complex binding[d][3][2],integrin binding[d][4][3][5],связывание с белками плазмы[d][6][7][8][…],transmembrane signaling receptor activity[d][9],integrin binding[d][10][2][11][…] һәмsignaling receptor activity[d][9]
Күзәнәк компонентымембрана өлеше[d][2],мембрана[d][3][3][12],фокальные контакты[d][13],күзәнәк мембранасы[d][2][14][2],күзәнәк мембранасы өлеше[d][15],күзәнәк өслеге[d][3][16][17],иммунологик синапс[d][2],липидный рафт[d][2],экзосома[d][18][19][20],наружная сторона клеточной мембраны[d][2],күзәнәк тышындагы мохит[d][2][21],внеклеточный матрикс[d][22],күзәнәк мембранасы өлеше[d][9][23],фокальные контакты[d][24],күзәнәк өслеге[d][2][25][26],мембрана[d][2][2][27],collagen-containing extracellular matrix[d][28] һәмэкзосома[d][29][30][31]
Биологик процессleukocyte cell-cell adhesion[d][32][2],response to ionizing radiation[d][2],establishment of endothelial barrier[d][33],negative regulation of endothelial cell apoptotic process[d][34],cellular response to organic substance[d][2],heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules[d][32],response to amino acid[d][2],response to hypoxia[d][2],positive regulation of actin filament polymerization[d][2],response to organic cyclic compound[d][2],T cell antigen processing and presentation[d][2],establishment of Sertoli cell barrier[d][2],response to sulfur dioxide[d][2],response to copper ion[d][2],interferon-gamma-mediated signaling pathway[d][2],positive regulation of nitric oxide biosynthetic process[d][2],response to amphetamine[d][2],cellular response to tumor necrosis factor[d][2],regulation of leukocyte mediated cytotoxicity[d][35],T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell[d][32],extracellular matrix organization[d][2],acute inflammatory response to antigenic stimulus[d][2],ишетү[d][2],cellular response to alkaloid[d][2],response to gonadotropin[d][2],positive regulation of cellular extravasation[d][36],positive regulation of GTPase activity[d][2],response to lipopolysaccharide[d][2],regulation of cell adhesion[d][2],агрегация клеток[d][3][3][37],cell adhesion mediated by integrin[d][2],positive regulation of NF-kappaB transcription factor activity[d][2],negative regulation of extrinsic apoptotic signaling pathway via death domain receptors[d][34],positive regulation of vasoconstriction[d][2],cellular response to interleukin-1[d][2],cellular response to nutrient levels[d][2],negative regulation of calcium ion transport[d][2],regulation of cell shape[d][2],membrane to membrane docking[d][38],positive regulation of peptidyl-tyrosine phosphorylation[d][2],ovarian follicle development[d][2],regulation of immune response[d][2],positive regulation of ERK1 and ERK2 cascade[d][34],regulation of ruffle assembly[d][2],viral entry into host cell[d][2],response to ethanol[d][2],вирусный процесс[d][2],cellular response to lipopolysaccharide[d][2],cellular response to hypoxia[d][2],leukocyte migration[d][38],cellular response to glucose stimulus[d][2],response to insulin[d][2],cellular response to interferon-gamma[d][2],cellular response to interleukin-6[d][2],cellular response to dexamethasone stimulus[d][2],establishment of endothelial intestinal barrier[d][2],positive regulation of leukocyte adhesion to vascular endothelial cell[d][2],cellular response to leukemia inhibitory factor[d][2],cell-cell adhesion[d][2][2],агрегация клеток[d][2][2][39][…],cytokine-mediated signaling pathway[d][2],T cell extravasation[d][2] һәмcellular response to amyloid-beta[d][40]
Изображение Gene Atlas
 ICAM1 Викиҗыентыкта

ICAM1 (ингл. ) —аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[41][42]

Искәрмәләр

[үзгәртү |вики-текстны үзгәрт]
  1. 12UniProt
  2. 123456789101112131415161718192021222324252627282930313233343536373839404142434445464748495051525354555657585960616263646566GOA
  3. 1234567GOA
  4. Holness C. L., Needham L. A., Gatter K. C. et al.Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively expressed on resting leukocytes //Nature /M. SkipperNPG,Springer Science+Business Media, 1992. — ISSN1476-4687;0028-0836doi:10.1038/360481A0PMID:1448173
  5. Chiang Y.,Lee F. S.CBAP functions as a novel component in chemokine-induced ZAP70-mediated T-cell adhesion and migration //PLOS ONE /PLOS ONE EditorsPLoS, 2013. — ISSN1932-6203doi:10.1371/JOURNAL.PONE.0061761PMID:23620790
  6. Madrid F. S.,Rocha-Perugini V.,Gonzalez-Granado J. M. et al.CD81 controls sustained T cell activation signaling and defines the maturation stages of cognate immunological synapses //Mol. Cell. Biol.ASM, 2013. — ISSN0270-7306;1098-5549;1067-8824doi:10.1128/MCB.00302-13PMID:23858057
  7. Gewirtz A.CD98 and intracellular adhesion molecule I regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia, CD98 and Intracellular Adhesion Molecule I Regulate the Activity of Amino Acid Transporter LAT-2 in Polarized Intestinal Epithelia //J. Biol. Chem. /L. M. GieraschBaltimore [etc.]:American Society for Biochemistry and Molecular Biology, 2003. — ISSN0021-9258;1083-351X;1067-8816doi:10.1074/JBC.M302777200PMID:12716892
  8. Joachimiak A.Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation //CellCell Press,Elsevier, 2003. — ISSN0092-8674;1097-4172doi:10.1016/S0092-8674(02)01257-6PMID:12526797
  9. 123McClelland A.The major human rhinovirus receptor is ICAM-1 //CellCell Press,Elsevier, 1989. — ISSN0092-8674;1097-4172doi:10.1016/0092-8674(89)90688-0PMID:2538243
  10. Holness C. L., Needham L. A., Gatter K. C. et al.Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively expressed on resting leukocytes //Nature /M. SkipperNPG,Springer Science+Business Media, 1992. — ISSN1476-4687;0028-0836doi:10.1038/360481A0PMID:1448173
  11. Chiang Y.,Lee F. S.CBAP functions as a novel component in chemokine-induced ZAP70-mediated T-cell adhesion and migration //PLOS ONE /PLOS ONE EditorsPLoS, 2013. — ISSN1932-6203doi:10.1371/JOURNAL.PONE.0061761PMID:23620790
  12. Lippert D.Defining the membrane proteome of NK cells //J. Mass Spectrom.Wiley, 2010. — ISSN1076-5174;1096-9888doi:10.1002/JMS.1696PMID:19946888
  13. Waterman C.,Yates J. R.Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation //Nat. Cell Biol.NPG, 2011. — ISSN1465-7392;1476-4679doi:10.1038/NCB2216PMID:21423176
  14. Dustin M. L.Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families //CellCell Press,Elsevier, 1988. — ISSN0092-8674;1097-4172doi:10.1016/0092-8674(88)90434-5PMID:3349522
  15. McClelland A.The major human rhinovirus receptor is ICAM-1 //CellCell Press,Elsevier, 1989. — ISSN0092-8674;1097-4172doi:10.1016/0092-8674(89)90688-0PMID:2538243
  16. Robinson C. M.Mycobacterium tuberculosis infection of human dendritic cells decreases integrin expression, adhesion and migration to chemokines //ImmunologyWiley-Blackwell,Wiley, 2014. — ISSN0019-2805;1365-2567doi:10.1111/IMM.12164PMID:23981064
  17. Teckchandani A., Toida N., Goodchild J. et al.Quantitative proteomics identifies a Dab2/integrin module regulating cell migration //J. Cell Biol. /J. NunnariRockefeller University Press, 2009. — ISSN0021-9525;1540-8140doi:10.1083/JCB.200812160PMID:19581412
  18. Atay S.Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells //Exp. Cell. Res.Academic Press,Elsevier, 2011. — ISSN0014-4827;1090-2422doi:10.1016/J.YEXCR.2011.01.014PMID:21276792
  19. Buschow S. I.,Stoorvogel W.,Wauben M.MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis //Immunology & Cell BiologyWiley, 2010. — ISSN0818-9641;1440-1711doi:10.1038/ICB.2010.64PMID:20458337
  20. Pisitkun T.,Tchapyjnikov D.,Knepper M. A.Large-scale proteomics and phosphoproteomics of urinary exosomes //Journal of the American Society of Nephrology /J. BriggsAmerican Society of Nephrology, 2008. — ISSN1046-6673;1533-3450doi:10.1681/ASN.2008040406PMID:19056867
  21. Augustin H. G.Circulating endothelial cell adhesion molecules as diagnostic markers for the early identification of pregnant women at risk for development of preeclampsia //American Journal of Obstetrics and GynecologyElsevier, 1997. — ISSN0002-9378;1097-6868;1085-8709doi:10.1016/S0002-9378(97)70213-8PMID:9290466
  22. Mayr M.,Iozzo R. V.,Barallobre-Barreiro J. et al.Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation //CirculationLippincott Williams & Wilkins, 2016. — ISSN0009-7322;1524-4539doi:10.1161/CIRCULATIONAHA.115.016423PMID:27559042
  23. 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. — ISSN1467-5463;1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  24. Waterman C.,Yates J. R.Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation //Nat. Cell Biol.NPG, 2011. — ISSN1465-7392;1476-4679doi:10.1038/NCB2216PMID:21423176
  25. Robinson C. M.Mycobacterium tuberculosis infection of human dendritic cells decreases integrin expression, adhesion and migration to chemokines //ImmunologyWiley-Blackwell,Wiley, 2014. — ISSN0019-2805;1365-2567doi:10.1111/IMM.12164PMID:23981064
  26. Teckchandani A., Toida N., Goodchild J. et al.Quantitative proteomics identifies a Dab2/integrin module regulating cell migration //J. Cell Biol. /J. NunnariRockefeller University Press, 2009. — ISSN0021-9525;1540-8140doi:10.1083/JCB.200812160PMID:19581412
  27. Lippert D.Defining the membrane proteome of NK cells //J. Mass Spectrom.Wiley, 2010. — ISSN1076-5174;1096-9888doi:10.1002/JMS.1696PMID:19946888
  28. Mayr M.,Iozzo R. V.,Barallobre-Barreiro J. et al.Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation //CirculationLippincott Williams & Wilkins, 2016. — ISSN0009-7322;1524-4539doi:10.1161/CIRCULATIONAHA.115.016423PMID:27559042
  29. Atay S.Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells //Exp. Cell. Res.Academic Press,Elsevier, 2011. — ISSN0014-4827;1090-2422doi:10.1016/J.YEXCR.2011.01.014PMID:21276792
  30. Buschow S. I.,Stoorvogel W.,Wauben M.MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis //Immunology & Cell BiologyWiley, 2010. — ISSN0818-9641;1440-1711doi:10.1038/ICB.2010.64PMID:20458337
  31. Pisitkun T.,Tchapyjnikov D.,Knepper M. A.Large-scale proteomics and phosphoproteomics of urinary exosomes //Journal of the American Society of Nephrology /J. BriggsAmerican Society of Nephrology, 2008. — ISSN1046-6673;1533-3450doi:10.1681/ASN.2008040406PMID:19056867
  32. 123Dustin M. L.T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1 //Nature /M. SkipperNPG,Springer Science+Business Media, 1989. — ISSN1476-4687;0028-0836doi:10.1038/341619A0PMID:2477710
  33. Aranda J. F.,Millán J.,Kremer L. et al.MYADM controls endothelial barrier function through ERM-dependent regulation of ICAM-1 expression //Mol. Biol. Cell,American Society for Cell Biology, 2013. — ISSN1059-1524;1939-4586;1044-2030doi:10.1091/MBC.E11-11-0914PMID:23264465
  34. 123E Pluskota, S E D'SouzaFibrinogen interactions with ICAM-1 (CD54) regulate endothelial cell survival //FEBS J.Wiley-Blackwell, 2000. — ISSN1742-464X;1742-4658doi:10.1046/J.1432-1327.2000.01520.XPMID:10903502
  35. Yokomori H.Expression of adhesion molecules on mature cholangiocytes in canal of Hering and bile ductules in wedge biopsy samples of primary biliary cirrhosis //World J. Gastroenterol.Baishideng Publishing Group, 2005. — ISSN1007-9327;2219-2840doi:10.3748/WJG.V11.I28.4382PMID:16038038
  36. Greenwood J.,Couraud P.,Lyck R. et al.Intracellular domain of brain endothelial intercellular adhesion molecule-1 is essential for T lymphocyte-mediated signaling and migration //J. Immunol.Baltimore: 2003. — ISSN0022-1767;1550-6606doi:10.4049/JIMMUNOL.171.4.2099PMID:12902516
  37. Ottoboni L.,Meregalli M.,Torrente Y. et al.VCAM-1 expression on dystrophic muscle vessels has a critical role in the recruitment of human blood-derived CD133+ stem cells after intra-arterial transplantation //BloodAmerican Society of Hematology,Elsevier, 2006. — ISSN0006-4971;1528-0020doi:10.1182/BLOOD-2006-04-018564PMID:16809613
  38. 12Yáñez-Mó M.,Serrador J. M.,Montoya M. C. et al.Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes //J. Cell Biol. /J. NunnariRockefeller University Press, 2002. — 13 p. — ISSN0021-9525;1540-8140doi:10.1083/JCB.200112126PMID:12082081
  39. Ottoboni L.,Meregalli M.,Torrente Y. et al.VCAM-1 expression on dystrophic muscle vessels has a critical role in the recruitment of human blood-derived CD133+ stem cells after intra-arterial transplantation //BloodAmerican Society of Hematology,Elsevier, 2006. — ISSN0006-4971;1528-0020doi:10.1182/BLOOD-2006-04-018564PMID:16809613
  40. R Giri, Y Shen, M Stins et al.beta-amyloid-induced migration of monocytes across human brain endothelial cells involves RAGE and PECAM-1. //American Journal of Physiology-Cell Physiology:Cell Physiology — 2000. — ISSN0363-6143;1522-1563doi:10.1152/AJPCELL.2000.279.6.C1772PMID:11078691
  41. HUGO Gene Nomenclature Commitee, HGNC:29223(ингл.).әлеге чыганактан 2015-10-25 архивланды.18 сентябрь, 2017 тикшерелгән.
  42. UniProt, Q9ULJ7(ингл.).18 сентябрь, 2017 тикшерелгән.

Чыганаклар

[үзгәртү |вики-текстны үзгәрт]
  • 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
Чыганак —https://tt.wikipedia.org/w/index.php?title=ICAM1&oldid=4129674
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