Эчтәлеккә күчү

HMGB1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/HMGB1 latin yazuında])
HMGB1
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген HMGB1[d][1]
Молекуляр функция DNA-binding transcription factor activity[d][2], bubble DNA binding[d][3], DNA polymerase binding[d][4], C-X-C chemokine binding[d][5], transcription factor binding[d][2], phosphatidylserine binding[d][6], lipopolysaccharide binding[d][7], активность лиазы[d][4], single-stranded DNA binding[d][3], damaged DNA binding[d][3][4], связывание с белками плазмы[d][8][9][10][…], DNA binding, bending[d][11][11][2], supercoiled DNA binding[d][3], ДНК-связывающий[d][3][3], four-way junction DNA binding[d][3], RAGE receptor binding[d][3], chemoattractant activity[d][3], RNA binding[d][12][13], double-stranded DNA binding[d][11][11], double-stranded RNA binding[d][11], single-stranded RNA binding[d][11], cytokine activity[d][11][11], calcium-dependent protein kinase regulator activity[d][11], protein kinase activator activity[d][11], double-stranded DNA binding[d][3], transcription coactivator activity[d][14], RNA binding[d][15][16], cytokine activity[d][3], integrin binding[d][17], transcription factor binding[d][14][18] һәм DNA binding, bending[d][3][3][14][…]
Күзәнәк компоненты цитоплазма[11][11], эндосома[d][3], мембрана[d][3], transcription repressor complex[d][19], күзәнәк тышындагы өлкә[d][3][3], төш[11][11][11][…], күзәнәк өслеге[d][20], күзәнәк мембранасы[d][3], нуклеоплазма[d][3], Хромосома[3], condensed chromosome[d][21], endoplasmic reticulum-Golgi intermediate compartment[d][3], secretory granule lumen[d][3], ficolin-1-rich granule lumen[d][3], күзәнәк тышындагы мохит[d][11][22], early endosome[d][11], neuron projection[d][11], күзәнәк тышындагы мохит[d][3][20], төш[3][3][3][…], цитоплазма[3][18] һәм alphav-beta3 integrin-HMGB1 complex[d][17]
Биологик процесс T-helper 1 cell activation[d][23], apoptotic DNA fragmentation[d][3], adaptive immune response[d][3], regulation of transcription by RNA polymerase II[d][24], positive regulation of DNA ligation[d][3], positive regulation of JNK cascade[d][25], cellular response to DNA damage stimulus[d][3], apoptotic cell clearance[d][6], positive regulation of cysteine-type endopeptidase activity involved in apoptotic process[d][26], positive regulation of toll-like receptor 9 signaling pathway[d][3], negative regulation of RNA polymerase II transcription preinitiation complex assembly[d][27], positive regulation of dendritic cell differentiation[d][28], positive regulation of DNA binding[d][14][9], neuron projection development[d][3], negative regulation of blood vessel endothelial cell migration[d][29], positive regulation of interleukin-12 production[d][28], positive regulation of monocyte chemotaxis[d][5], activation of innate immune response[d][30], DNA ligation involved in DNA repair[d][3], врождённый иммунитет[d][3][3], воспалительная реакция[d][3][31], репарация ДНК[d][3], positive regulation of MAPK cascade[d][25], positive regulation of activated T cell proliferation[d][28], DNA geometric change[d][3], DNA recombination[d][11][11], inflammatory response to antigenic stimulus[d][20], positive regulation of interleukin-10 production[d][23], immune system process[d][3], negative regulation of transcription by RNA polymerase II[d][32], regulation of restriction endodeoxyribonuclease activity[d][4], хемотаксис[d][3], positive regulation of mismatch repair[d][33], negative regulation of CD4-positive, alpha-beta T cell differentiation[d][23], positive regulation of cytosolic calcium ion concentration[d][5], T-helper 1 cell differentiation[d][28], dendritic cell chemotaxis[d][3], аутофагия[d][3], neutrophil clearance[d][6], V(D)J-рекомбинация[d][34], positive regulation of apoptotic process[d][26], DNA topological change[d][3], positive chemotaxis[d][3], toll-like receptor signaling pathway[d][3], neutrophil degranulation[d][3], күз үсеше[d][11], myeloid dendritic cell activation[d][11][11], positive regulation of protein phosphorylation[d][11], endothelial cell proliferation[d][11], plasmacytoid dendritic cell activation[d][11], macrophage activation involved in immune response[d][11], regulation of tolerance induction[d][11][35], regulation of T cell mediated immune response to tumor cell[d][11][11], base-excision repair[d][11], regulation of autophagy[d][36][11], үпкәләр үсеше[d][11], activation of protein kinase activity[d][11], positive regulation of interferon-alpha production[d][11], positive regulation of interferon-beta production[d][11], positive regulation of interleukin-6 production[d][11], positive regulation of tumor necrosis factor production[d][11], positive regulation of toll-like receptor 2 signaling pathway[d][11], positive regulation of toll-like receptor 4 signaling pathway[d][11], endothelial cell chemotaxis[d][11], positive regulation of innate immune response[d][11], positive regulation of myeloid cell differentiation[d][11], positive regulation of glycogen catabolic process[d][11], regulation of protein kinase activity[d][11], положительная регуляция транскрипции РНК полимеразой II промотор[d][11][2], response to glucocorticoid[d][11], positive regulation of ERK1 and ERK2 cascade[d][11][37], positive regulation of wound healing[d][11], positive regulation of NIK/NF-kappaB signaling[d][11], positive regulation of sprouting angiogenesis[d][11], negative regulation of apoptotic cell clearance[d][11], regulation of nucleotide-excision repair[d][11], regulation of signaling receptor activity[d][11], negative regulation of transcription by RNA polymerase II[d][19][19], myeloid dendritic cell activation[d][3], activation of innate immune response[d][38][18], regulation of tolerance induction[d][39], regulation of T cell mediated immune response to tumor cell[d][3], DNA recombination[d][3][3][18], ремоделирование хроматина[d][18], regulation of transcription by RNA polymerase II[d][9][18], regulation of signaling receptor activity[d][18], regulation of autophagy[d][40], positive regulation of autophagy[d][18], үсеш процессы[d][18], positive regulation of interleukin-6 production[d][18], positive regulation of tumor necrosis factor production[d][18], positive regulation of blood vessel endothelial cell migration[d][41], positive regulation of innate immune response[d][18], положительная регуляция транскрипции РНК полимеразой II промотор[d][14][18], cell chemotaxis[d][18], positive regulation of ERK1 and ERK2 cascade[d][5][18], cellular response to lipopolysaccharide[d][3], positive regulation of NIK/NF-kappaB signaling[d][18], positive regulation of vascular endothelial cell proliferation[d][41], negative regulation of apoptotic cell clearance[d][17] һәм negative regulation of interferon-gamma production[d][23]

HMGB1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[42][43]

Искәрмәләр

[үзгәртү | вики-текстны үзгәртү]
  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,0 2,1 2,2 2,3 Stros M., Polanská E., Struncová S. et al. HMGB1 and HMGB2 proteins up-regulate cellular expression of human topoisomerase IIalpha // Nucleic Acids Res. — OUP, University of Oxford, 2009. — ISSN 0305-1048; 1362-4962; 1362-4954 — doi:10.1093/NAR/GKP067 — PMID:19223331
  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 3,43 3,44 3,45 3,46 3,47 3,48 3,49 3,50 3,51 3,52 GOA
  4. ↑ 4,0 4,1 4,2 4,3 Wilson S. H. HMGB1 is a cofactor in mammalian base excision repair // Mol. Cell — Cell Press, Elsevier BV, 2007. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2007.06.029 — PMID:17803946
  5. ↑ 5,0 5,1 5,2 5,3 Venereau E., Apuzzo T., Marchis F. D. et al. HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4 // J. Exp. Med. — Rockefeller University Press, 2012. — ISSN 0022-1007; 1540-9538 — doi:10.1084/JEM.20111739 — PMID:22370717
  6. ↑ 6,0 6,1 6,2 Liu G., Lorne E. High mobility group protein-1 inhibits phagocytosis of apoptotic neutrophils through binding to phosphatidylserine // J. Immunol. — Baltimore: 2008. — ISSN 0022-1767; 1550-6606 — doi:10.4049/JIMMUNOL.181.6.4240 — PMID:18768881
  7. ↑ Youn J. H., Kwak M. S., Wu J. et al. Identification of lipopolysaccharide-binding peptide regions within HMGB1 and their effects on subclinical endotoxemia in a mouse model // Eur. J. Immunol. — Wiley-Blackwell, 2011. — ISSN 0014-2980; 1521-4141 — doi:10.1002/EJI.201141391 — PMID:21660935
  8. ↑ Ku W., Chiu S., Chen Y. et al. Complementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2 // Mol. Cell. Proteomics — American Society for Biochemistry and Molecular Biology, 2009. — ISSN 1535-9476; 1535-9484 — doi:10.1074/MCP.M900013-MCP200 — PMID:19505873
  9. ↑ 9,0 9,1 9,2 Stros M., Ozaki T., Bacikova A. et al. HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2002. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M110233200 — PMID:11748232
  10. ↑ L Jayaraman, Moorthy N. C., Murthy K. G. et al. High mobility group protein-1 (HMG-1) is a unique activator of p53 // Genes Dev. — Cold Spring Harbor Laboratory Press, 1998. — ISSN 0890-9369; 1549-5477 — doi:10.1101/GAD.12.4.462 — PMID:9472015
  11. ↑ 11,00 11,01 11,02 11,03 11,04 11,05 11,06 11,07 11,08 11,09 11,10 11,11 11,12 11,13 11,14 11,15 11,16 11,17 11,18 11,19 11,20 11,21 11,22 11,23 11,24 11,25 11,26 11,27 11,28 11,29 11,30 11,31 11,32 11,33 11,34 11,35 11,36 11,37 11,38 11,39 11,40 11,41 11,42 11,43 11,44 11,45 11,46 11,47 11,48 11,49 11,50 11,51 11,52 11,53 GOA
  12. ↑ Preiss T., Beckmann B. M., Humphreys D. T. et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins // Cell — Cell Press, Elsevier BV, 2012. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2012.04.031 — PMID:22658674
  13. ↑ Bonneau R. The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts // Mol. Cell — Cell Press, Elsevier BV, 2012. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2012.05.021 — PMID:22681889
  14. ↑ 14,0 14,1 14,2 14,3 14,4 Stros M., Polanská E., Struncová S. et al. HMGB1 and HMGB2 proteins up-regulate cellular expression of human topoisomerase IIalpha // Nucleic Acids Res. — OUP, University of Oxford, 2009. — ISSN 0305-1048; 1362-4962; 1362-4954 — doi:10.1093/NAR/GKP067 — PMID:19223331
  15. ↑ Bonneau R. The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts // Mol. Cell — Cell Press, Elsevier BV, 2012. — ISSN 1097-2765; 1097-4164 — doi:10.1016/J.MOLCEL.2012.05.021 — PMID:22681889
  16. ↑ Preiss T., Beckmann B. M., Humphreys D. T. et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins // Cell — Cell Press, Elsevier BV, 2012. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2012.04.031 — PMID:22658674
  17. ↑ 17,0 17,1 17,2 Friggeri A. HMGB1 inhibits macrophage activity in efferocytosis through binding to the alphavbeta3-integrin // American Journal of Physiology: Cell Physiology — 2010. — ISSN 0363-6143; 1522-1563 — doi:10.1152/AJPCELL.00152.2010 — PMID:20826760
  18. ↑ 18,00 18,01 18,02 18,03 18,04 18,05 18,06 18,07 18,08 18,09 18,10 18,11 18,12 18,13 18,14 18,15 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
  19. ↑ 19,0 19,1 19,2 Gazzar M. E., Yoza B. K., Chen X. et al. Chromatin-specific remodeling by HMGB1 and linker histone H1 silences proinflammatory genes during endotoxin tolerance // Mol. Cell. Biol. — ASM, 2009. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.01862-08 — PMID:19158276
  20. ↑ 20,0 20,1 20,2 Kalyan S., Chow A. W. Linking innate and adaptive immunity: human Vgamma9Vdelta2 T cells enhance CD40 expression and HMGB-1 secretion // Mediators of Inflammation — Hindawi Publishing Corporation, 2009. — ISSN 0962-9351; 1466-1861 — doi:10.1155/2009/819408 — PMID:19841752
  21. ↑ Agresti A., Bianchi M. E., Nordmann P. Association of chromatin proteins high mobility group box (HMGB) 1 and HMGB2 with mitotic chromosomes // Mol. Biol. Cell, — American Society for Cell Biology, 2003. — ISSN 1059-1524; 1939-4586; 1044-2030 — doi:10.1091/MBC.E02-09-0581 — PMID:12925773
  22. ↑ Kalyan S., Chow A. W. Linking innate and adaptive immunity: human Vgamma9Vdelta2 T cells enhance CD40 expression and HMGB-1 secretion // Mediators of Inflammation — Hindawi Publishing Corporation, 2009. — ISSN 0962-9351; 1466-1861 — doi:10.1155/2009/819408 — PMID:19841752
  23. ↑ 23,0 23,1 23,2 23,3 Wild C. A., Bergmann C., Fritz G. et al. HMGB1 conveys immunosuppressive characteristics on regulatory and conventional T cells // Int. Immunol. — OUP, 2012. — ISSN 0953-8178; 1460-2377 — doi:10.1093/INTIMM/DXS051 — PMID:22473704
  24. ↑ Stros M., Ozaki T., Bacikova A. et al. HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2002. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M110233200 — PMID:11748232
  25. ↑ 25,0 25,1 Andersson U., Moldawer L. L. Structural basis for the proinflammatory cytokine activity of high mobility group box 1 // Mol. Med. — The Feinstein Institute for Medical Research, BMC, Springer Science+Business Media, 2003. — ISSN 1076-1551; 1528-3658 — PMID:12765338
  26. ↑ 26,0 26,1 Zhu X., Yao Y., Liang H. et al. Effect of high mobility group box-1 protein on apoptosis of peritoneal macrophages // Arch. Biochem. Biophys. — Academic Press, Elsevier BV, 2009. — ISSN 0003-9861; 1096-0384 — doi:10.1016/J.ABB.2009.09.016 — PMID:19800306
  27. ↑ Ge H, RG R. The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1994. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:8006019
  28. ↑ 28,0 28,1 28,2 28,3 Rovere-Querini P., Nawroth P. P. Release of high mobility group box 1 by dendritic cells controls T cell activation via the receptor for advanced glycation end products // J. Immunol. — Baltimore: 2005. — ISSN 0022-1767; 1550-6606 — doi:10.4049/JIMMUNOL.174.12.7506 — PMID:15944249
  29. ↑ Billiar T. R. High mobility group Box 1 inhibits human pulmonary artery endothelial cell migration via a Toll-like receptor 4- and interferon response factor 3-dependent mechanism(s) // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2013. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M112.434142 — PMID:23148224
  30. ↑ Wang H. HMGB1-DNA complex-induced autophagy limits AIM2 inflammasome activation through RAGE // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 2014. — ISSN 0006-291X; 1090-2104 — doi:10.1016/J.BBRC.2014.06.074 — PMID:24971542
  31. ↑ Lee W., Ku S., Kim T. H. et al. Emodin-6-O-β-D-glucoside inhibits HMGB1-induced inflammatory responses in vitro and in vivo // Food Chem. Toxicol. / J. L. Domingo — Elsevier BV, 2013. — ISSN 0278-6915; 1873-6351 — doi:10.1016/J.FCT.2012.10.061 — PMID:23146691
  32. ↑ Gazzar M. E., Yoza B. K., Chen X. et al. Chromatin-specific remodeling by HMGB1 and linker histone H1 silences proinflammatory genes during endotoxin tolerance // Mol. Cell. Biol. — ASM, 2009. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.01862-08 — PMID:19158276
  33. ↑ Li G. Evidence for involvement of HMGB1 protein in human DNA mismatch repair // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M401931200 — PMID:15014079
  34. ↑ Nussenzweig M. C. V(D)J recombination: modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins // J. Exp. Med. — Rockefeller University Press, 1997. — ISSN 0022-1007; 1540-9538 — doi:10.1084/JEM.185.11.2025 — PMID:9166431
  35. ↑ Green D. R. Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein // Immunity — Cell Press, Elsevier BV, 2008. — ISSN 1074-7613; 1097-4180 — doi:10.1016/J.IMMUNI.2008.05.013 — PMID:18631454
  36. ↑ Bianchi M. E., Tracey K. J., Zeh H. J. et al. Endogenous HMGB1 regulates autophagy // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2010. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200911078 — PMID:20819940
  37. ↑ Venereau E., Apuzzo T., Marchis F. D. et al. HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4 // J. Exp. Med. — Rockefeller University Press, 2012. — ISSN 0022-1007; 1540-9538 — doi:10.1084/JEM.20111739 — PMID:22370717
  38. ↑ Wang H. HMGB1-DNA complex-induced autophagy limits AIM2 inflammasome activation through RAGE // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 2014. — ISSN 0006-291X; 1090-2104 — doi:10.1016/J.BBRC.2014.06.074 — PMID:24971542
  39. ↑ Green D. R. Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein // Immunity — Cell Press, Elsevier BV, 2008. — ISSN 1074-7613; 1097-4180 — doi:10.1016/J.IMMUNI.2008.05.013 — PMID:18631454
  40. ↑ Bianchi M. E., Tracey K. J., Zeh H. J. et al. Endogenous HMGB1 regulates autophagy // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2010. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200911078 — PMID:20819940
  41. ↑ 41,0 41,1 Kessler B., Harris A. L. miR-193a-3p interaction with HMGB1 downregulates human endothelial cell proliferation and migration // Sci. Rep. — Macmillan Publishers, NPG, 2017. — ISSN 2045-2322 — doi:10.1038/SREP44137 — PMID:28276476
  42. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  43. ↑ 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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