Эчтәлеккә күчү

ITGA6

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/ITGA6 latin yazuında])
ITGA6
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген Интегрин альфа-6[d][1]
Молекуляр функция связывание с ионом металла[d][2], integrin binding[d][3], связывание с белками плазмы[d][4][5][6][…], laminin binding[d][2], neuregulin binding[d][7], protein-containing complex binding[d][3][2], insulin-like growth factor I binding[d][8], cadherin binding[d][9] һәм cadherin binding[d][10]
Күзәнәк компоненты мембрана өлеше[d][2], мембрана[d][2], фокальные контакты[d][11], basal part of cell[d][2], күзәнәк мембранасы[d][2][2][2][…], Гемидесмосома[d][2], базаль мембрана[d][2], күзәнәк өслеге[d][3][12][13][…], integrin complex[d][2][2], basal plasma membrane[d][2], basolateral plasma membrane[d][2], наружная сторона клеточной мембраны[d][2], integrin alpha6-beta4 complex[d][2], filopodium[d][2], фокальные контакты[d][14] һәм күзәнәк өслеге[d][2][15][16][…]
Биологик процесс cellular response to extracellular stimulus[d][2], hemidesmosome assembly[d][2], развитие почечной системы[d][17], nail development[d][17], positive regulation of cell-cell adhesion[d][2], filopodium assembly[d][2], negative regulation of extrinsic apoptotic signaling pathway[d][18], extracellular matrix organization[d][2], odontogenesis of dentin-containing tooth[d][2], cell-substrate adhesion[d][15], positive regulation of GTPase activity[d][19], агрегация клеток[d][2][2], cell adhesion mediated by integrin[d][3], brown fat cell differentiation[d][2], positive regulation of apoptotic process[d][20], cell-substrate junction assembly[d][21], integrin-mediated signaling pathway[d][2], positive regulation of phosphorylation[d][18], cell-matrix adhesion[d][2], digestive tract development[d][17], ectodermal cell differentiation[d][16], leukocyte migration[d][2][2], развитие кожи[d][17], положительная регуляция транскрипции РНК полимеразой II промотор[d][18], amelogenesis[d][17], cellular response to organic cyclic compound[d][2], positive regulation of cell-substrate adhesion[d][2], positive regulation of cell migration[d][22], cell-cell adhesion[d][2] һәм positive regulation of neuron projection development[d][2][2]

ITGA6 (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. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 2,33 2,34 2,35 2,36 GOA
  3. ↑ 3,0 3,1 3,2 3,3 GOA
  4. ↑ Takada Y., Noda M. alpha4beta1- and alpha6beta1-integrins are functional receptors for midkine, a heparin-binding growth factor // J. Cell Sci. — The Company of Biologists, 2004. — ISSN 0021-9533; 1477-9137 — doi:10.1242/JCS.01423 — PMID:15466886
  5. ↑ I. Tachibana, J. Bodorova, F. Berditchevski et al. NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins, NAG-2, a Novel Transmembrane-4 Superfamily (TM4SF) Protein That Complexes with Integrins and Other TM4SF Proteins // 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.272.46.29181 — PMID:9360996
  6. ↑ ME H., Crouse C, Sonnenberg A Association of the VLA alpha 6 subunit with a novel protein. A possible alternative to the common VLA beta 1 subunit on certain cell lines // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1989. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:2649503
  7. ↑ Taniguchi Y., Takada Y. Direct binding of the EGF-like domain of neuregulin-1 to integrins ({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB signaling // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2010. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M110.113878 — PMID:20682778
  8. ↑ Taniguchi Y., Takada Y. Cross-talk between integrin α6β4 and insulin-like growth factor-1 receptor (IGF1R) through direct α6β4 binding to IGF1 and subsequent α6β4-IGF1-IGF1R ternary complex formation in anchorage-independent conditions // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2012. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M111.304170 — PMID:22351760
  9. ↑ Zanivan S., Zaidel-Bar R. E-cadherin interactome complexity and robustness resolved by quantitative proteomics // Sci. Signal. — AAAS, 2014. — ISSN 1945-0877; 1937-9145 — doi:10.1126/SCISIGNAL.2005473 — PMID:25468996
  10. ↑ Zanivan S., Zaidel-Bar R. E-cadherin interactome complexity and robustness resolved by quantitative proteomics // Sci. Signal. — AAAS, 2014. — ISSN 1945-0877; 1937-9145 — doi:10.1126/SCISIGNAL.2005473 — PMID:25468996
  11. ↑ Waterman C. 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. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  12. ↑ Brafman D. A., C Phung, N Kumar et al. Regulation of endodermal differentiation of human embryonic stem cells through integrin-ECM interactions // Cell Death & Differentiation — NPG, 2013. — ISSN 1350-9047; 1476-5403 — doi:10.1038/CDD.2012.138 — PMID:23154389
  13. ↑ Prockop D. J. Integrin expression and integrin-mediated adhesion in vitro of human multipotent stromal cells (MSCs) to endothelial cells from various blood vessels // Cell and Tissue Research — Springer Science+Business Media, 2010. — ISSN 0302-766X; 1432-0878 — doi:10.1007/S00441-010-0994-4 — PMID:20563599
  14. ↑ Waterman C. 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. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  15. ↑ 15,0 15,1 Schaffer D. V. Characterization of integrin engagement during defined human embryonic stem cell culture // FASEB J. — FASEB, 2010. — ISSN 0892-6638; 1530-6860 — doi:10.1096/FJ.08-126821 — PMID:19933311
  16. ↑ 16,0 16,1 Brafman D. A., C Phung, N Kumar et al. Regulation of endodermal differentiation of human embryonic stem cells through integrin-ECM interactions // Cell Death & Differentiation — NPG, 2013. — ISSN 1350-9047; 1476-5403 — doi:10.1038/CDD.2012.138 — PMID:23154389
  17. ↑ 17,0 17,1 17,2 17,3 17,4 D Kiritsi, L Hyla-Klekot, C Has Phenotypic spectrum of epidermolysis bullosa associated with α6β4 integrin mutations // Br. J. Dermatol. — Wiley-Blackwell, 2013. — ISSN 0007-0963; 1365-2133 — doi:10.1111/BJD.12317 — PMID:23496044
  18. ↑ 18,0 18,1 18,2 Lamb L. E., Zarif J. C., Miranti C. K. The androgen receptor induces integrin α6β1 to promote prostate tumor cell survival via NF-κB and Bcl-xL Independently of PI3K signaling, The Androgen Receptor Induces Integrin α6β1 to Promote Prostate Tumor Cell Survival via NF-κB and Bcl-xL Independently of PI3K Signaling // Cancer Res. / G. C. Prendergast — American Association for Cancer Research, 2011. — ISSN 0008-5472; 1538-7445 — doi:10.1158/0008-5472.CAN-10-2745 — PMID:21310825
  19. ↑ Lee H., Ji S., Park S. et al. Odontogenic Ameloblast-associated Protein (ODAM) Mediates Junctional Epithelium Attachment to Teeth via Integrin-ODAM-Rho Guanine Nucleotide Exchange Factor 5 (ARHGEF5)-RhoA Signaling // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2015. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M115.648022 — PMID:25911094
  20. ↑ Juric V., Chen C., Lau L. F. Fas-mediated apoptosis is regulated by the extracellular matrix protein CCN1 (CYR61) in vitro and in vivo // Mol. Cell. Biol. — ASM, 2009. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.00064-09 — PMID:19364818
  21. ↑ L Ruzzi, L Gagnoux-Palacios, M Pinola et al. A homozygous mutation in the integrin alpha6 gene in junctional epidermolysis bullosa with pyloric atresia // J. Clin. Invest. / R. S. Ahima — American Society for Clinical Investigation, 1997. — ISSN 0021-9738; 1558-8238 — doi:10.1172/JCI119474 — PMID:9185503
  22. ↑ Nohata N. Tumour-suppressive microRNA-29s inhibit cancer cell migration and invasion by targeting laminin-integrin signalling in head and neck squamous cell carcinoma // Br. J. Cancer, BJC — NPG, 2013. — ISSN 0007-0920; 1532-1827 — doi:10.1038/BJC.2013.607 — PMID:24091622
  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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