SP100
SP100 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[29][30]
Искәрмәләр
үзгәртү- ↑ 1,0 1,1 UniProt
- ↑ 2,0 2,1 Negorev D. G., Vladimirova O. V., Ivanov A. et al. Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression // J. Virol. — ASM, 2006. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.02164-05 — PMID:16873258
- ↑ Yordy J. S., Li R., Sementchenko V. I. et al. SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion // Oncogene — NPG, 2004. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1207891 — PMID:15247905
- ↑ 4,0 4,1 N Lehming, Saux A. L., J Schüller et al. Chromatin components as part of a putative transcriptional repressing complex // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.13.7322 — PMID:9636147
- ↑ Lechner M. S., Schultz D. C., Negorev D. et al. The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that _targets the chromoshadow domain // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 2005. — ISSN 0006-291X; 1090-2104 — doi:10.1016/J.BBRC.2005.04.016 — PMID:15882967
- ↑ Petsalaki E., Weile J., Jacob Y. et al. Pooled-matrix protein interaction screens using Barcode Fusion Genetics // Mol. Syst. Biol. / R. Aebersold — EMBO, Wiley, 2016. — ISSN 1744-4292 — doi:10.15252/MSB.20156660 — PMID:27107012
- ↑ 7,0 7,1 N Lehming, Saux A. L., J Schüller et al. Chromatin components as part of a putative transcriptional repressing complex // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.13.7322 — PMID:9636147
- ↑ 8,0 8,1 Seeler J. S. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.13.7316 — PMID:9636146
- ↑ 9,0 9,1 9,2 9,3 Möller A., Sirma H., Hofmann T. G. et al. Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression // Oncogene — NPG, 2003. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1207079 — PMID:14647468
- ↑ 10,0 10,1 Bloch D. B., Kieff E. Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100 // EMBO J. — NPG, 2005. — ISSN 0261-4189; 1460-2075 — doi:10.1038/SJ.EMBOJ.7600820 — PMID:16177824
- ↑ 11,0 11,1 Möller A., Sirma H., Hofmann T. G. et al. Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression // Oncogene — NPG, 2003. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1207079 — PMID:14647468
- ↑ 12,00 12,01 12,02 12,03 12,04 12,05 12,06 12,07 12,08 12,09 GOA
- ↑ 13,0 13,1 13,2 Wasylyk C., Schlumberger S. E., Criqui-Filipe P. et al. Sp100 interacts with ETS-1 and stimulates its transcriptional activity // Mol. Cell. Biol. — ASM, 2002. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.22.8.2687-2702.2002 — PMID:11909962
- ↑ 14,0 14,1 Naka K., Ikeda K., Motoyama N. Recruitment of NBS1 into PML oncogenic domains via interaction with SP100 protein // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 2002. — ISSN 0006-291X; 1090-2104 — doi:10.1016/S0006-291X(02)02755-9 — PMID:12470659
- ↑ Liang Y. SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies // Sci. Rep. — Macmillan Publishers, NPG, 2016. — ISSN 2045-2322 — doi:10.1038/SREP26509 — PMID:27211601
- ↑ Vaquerizas J. M., Teichmann S., Kummerfeld S. K. A census of human transcription factors: function, expression and evolution // Nature reviews. Genetics — United Kingdom: NPG, 2009. — ISSN 1471-0056; 1471-0064 — doi:10.1038/NRG2538 — PMID:19274049
- ↑ 17,0 17,1 17,2 17,3 17,4 Yordy J. S., Li R., Sementchenko V. I. et al. SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion // Oncogene — NPG, 2004. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1207891 — PMID:15247905
- ↑ Seeler J. S. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.13.7316 — PMID:9636146
- ↑ 19,0 19,1 19,2 19,3 19,4 Chambon P., Seeler J. S. Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification // Mol. Cell. Biol. — ASM, 2001. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.21.10.3314-3324.2001 — PMID:11313457
- ↑ HH G., Szostecki C, Schröder P et al. Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif // J. Cell Sci. — The Company of Biologists, 1999. — ISSN 0021-9533; 1477-9137 — PMID:9973607
- ↑ 21,0 21,1 21,2 21,3 21,4 Milovic-Holm K., Krieghoff E., Jensen K. et al. FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies // EMBO J. — NPG, 2007. — ISSN 0261-4189; 1460-2075 — doi:10.1038/SJ.EMBOJ.7601504 — PMID:17245429
- ↑ 22,0 22,1 Zinn A. R. Dynamic regulation of p53 subnuclear localization and senescence by MORC3 // Mol. Biol. Cell, — American Society for Cell Biology, 2007. — ISSN 1059-1524; 1939-4586; 1044-2030 — doi:10.1091/MBC.E06-08-0747 — PMID:17332504
- ↑ 23,0 23,1 Henson J. D., Reddel R. Suppression of alternative lengthening of telomeres by Sp100-mediated sequestration of the MRE11/RAD50/NBS1 complex // Mol. Cell. Biol. — ASM, 2005. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.25.7.2708-2721.2005 — PMID:15767676
- ↑ T. Sternsdorf, K. Jensen, H. Will Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1, Evidence for Covalent Modification of the Nuclear Dot–associated Proteins PML and Sp100 by PIC1/SUMO-1 // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 1997. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.139.7.1621 — PMID:9412458
- ↑ 25,0 25,1 25,2 GOA
- ↑ 26,0 26,1 Chaussabel D. SP100 inhibits ETS1 activity in primary endothelial cells // Oncogene — NPG, 2005. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1208245 — PMID:15592518
- ↑ 27,0 27,1 27,2 27,3 T Grötzinger, K Jensen, H Will The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-gamma activation site and an imperfect IFN-stimulated response element which mediate type I IFN inducibility // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1996. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.271.41.25253 — PMID:8810287
- ↑ 28,0 28,1 T. Sternsdorf, K. Jensen, D. Züchner et al. Cellular localization, expression, and structure of the nuclear dot protein 52, Cellular Localization, Expression, and Structure of the Nuclear Dot Protein 52 // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 1997. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.138.2.435 — PMID:9230084
- ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
- ↑ 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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