HFE

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/HFE latin yazuında])
HFE
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген HFE[d][1]
Молекулярная функция peptide antigen binding[d][2][3], beta-2-microglobulin binding[d][3][4][5], co-receptor binding[d][6], связывание с белками плазмы[d][7][8][9], transferrin receptor binding[d][10][11][12][…], signaling receptor binding[d][13][14], natural killer cell lectin-like receptor binding[d][15] һәм transferrin receptor binding[d][4][3][16][…]
Күзәнәк компоненты часть мембраны[d][17], recycling endosome[d][7], HFE-transferrin receptor complex[d][17][17][18][…], мембрана[d][17], basal part of cell[d][7], күзәнәк мембраны[d][19][20][19], apical part of cell[d][17][7], часть клеточной мембраны[d][13], terminal web[d][17], early endosome[d][7], MHC class I protein complex[d][2][3], perinuclear region of cytoplasm[d][7][5], цитоплазматическая везикула[d][7][18], наружная сторона клеточной мембраны[d][21], внеклеточное пространство[d][22], күзәнәк мембраны[d][17][13][17][…], внеклеточное пространство[d][23][24] һәм наружная сторона клеточной мембраны[d][14][24]
Биологический процесс negative regulation of T cell antigen processing and presentation[d][17], positive regulation of peptide hormone secretion[d][23], positive regulation of receptor-mediated endocytosis[d][16], cellular response to iron ion[d][16], antigen processing and presentation[d][3], negative regulation of receptor binding[d][4], regulation of protein localization to cell surface[d][18], antigen processing and presentation of peptide antigen via MHC class I[d][2], женская беременность[d][17], positive regulation of pathway-restricted SMAD protein phosphorylation[d][14], response to iron ion starvation[d][19], iron ion homeostasis[d][23][17][17][…], negative regulation of antigen processing and presentation of endogenous peptide antigen via MHC class I[d][25], ion transport[d][17], BMP signaling pathway[d][14], cellular response to iron ion starvation[d][17], response to iron ion[d][23], multicellular organismal iron ion homeostasis[d][17], positive regulation of ferrous iron binding[d][16], positive regulation of transferrin receptor binding[d][16], positive regulation of signaling receptor activity[d][16], регенерация печени[d][17], positive regulation of gene expression[d][17][17], negative regulation of T cell cytokine production[d][25], acute-phase response[d][17], negative regulation of proteasomal ubiquitin-dependent protein catabolic process[d][14], negative regulation of ubiquitin-dependent protein catabolic process[d][14], positive regulation of receptor binding[d][16], negative regulation of signaling receptor activity[d][4], positive regulation of protein binding[d][16], hormone biosynthetic process[d][17], negative regulation of CD8-positive, alpha-beta T cell activation[d][25], cellular iron ion homeostasis[d][20][19], iron ion import across plasma membrane[d][19][19][26], transferrin transport[d][17], protein-containing complex assembly[d][13], T cell mediated cytotoxicity[d][15], иммунный ответ[d][15], natural killer cell activation[d][15], natural killer cell mediated cytotoxicity[d][15], susceptibility to natural killer cell mediated cytotoxicity[d][15], iron ion import across plasma membrane[d][19][19][26][…], regulation of iron ion transport[d][16], cellular iron ion homeostasis[d][17][27], iron ion import across plasma membrane[d][17][24], response to iron ion starvation[d][17][24] һәм iron ion import across plasma membrane[d][17]
Изображение Gene Atlas

HFE (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[28][29]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,0 2,1 2,2 Feder J. N., A Gnirke, W Thomas et al. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis // Nature Genetics / M. Axton, T. Faial — NPG, 1996. — ISSN 1061-4036; 1546-1718 — doi:10.1038/NG0896-399 — PMID:8696333
  3. ↑ 3,0 3,1 3,2 3,3 3,4 Lebrón J. A., Bennett M. J., Vaughn D. E. et al. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor // Cell — Cell Press, Elsevier BV, 1998. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(00)81151-4 — PMID:9546397
  4. ↑ 4,0 4,1 4,2 4,3 Feder J. N., Penny D. M., A Irrinki et al. The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding // 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.95.4.1472 — PMID:9465039
  5. ↑ 5,0 5,1 A Waheed, S Parkkila, J Saarnio et al. Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1999. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.96.4.1579 — PMID:9990067
  6. ↑ Hentze M. W., Muckenthaler M. U. The hemochromatosis proteins HFE, TfR2, and HJV form a membrane-associated protein complex for hepcidin regulation // Journal of Hepatology — Elsevier BV, 2012. — ISSN 0168-8278; 1600-0641 — doi:10.1016/J.JHEP.2012.06.015 — PMID:22728873
  7. ↑ 7,0 7,1 7,2 7,3 7,4 7,5 7,6 Bacharach E. Transferrin receptor co-localizes and interacts with the hemochromatosis factor (HFE) and the divalent metal transporter-1 (DMT1) in trophoblast cells // J. Cell. Physio. — Wiley, 2005. — ISSN 0021-9541; 1097-4652 — doi:10.1002/JCP.20349 — PMID:15880641
  8. ↑ Ka C., Gac G. L., Dupradeau F. et al. The Q283P amino-acid change in HFE leads to structural and functional consequences similar to those described for the mutated 282Y HFE protein // Hum. Genet. — Springer Science+Business Media, 2005. — ISSN 0340-6717; 1432-1203 — doi:10.1007/S00439-005-1307-Y — PMID:15965644
  9. ↑ Liam S O'Driscoll, Carmo-Fonseca M. N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding // FEBS J. — Wiley-Blackwell, 2010. — ISSN 1742-464X; 0014-2956; 1742-4658; 1432-1033 — doi:10.1111/J.1742-4658.2010.07727.X — PMID:20618438
  10. ↑ A Waheed, S Parkkila, J Saarnio et al. Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1999. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.96.4.1579 — PMID:9990067
  11. ↑ Hentze M. W., Muckenthaler M. U. The hemochromatosis proteins HFE, TfR2, and HJV form a membrane-associated protein complex for hepcidin regulation // Journal of Hepatology — Elsevier BV, 2012. — ISSN 0168-8278; 1600-0641 — doi:10.1016/J.JHEP.2012.06.015 — PMID:22728873
  12. ↑ Lebrón J. A., Bennett M. J., Vaughn D. E. et al. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor // Cell — Cell Press, Elsevier BV, 1998. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(00)81151-4 — PMID:9546397
  13. ↑ 13,0 13,1 13,2 13,3 Bennett M. J., Lebrón J. A., Bjorkman P. J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor // Nature / M. Skipper — NPG, Springer Science+Business Media, 2000. — ISSN 1476-4687; 0028-0836 — doi:10.1038/47417 — PMID:10638746
  14. ↑ 14,0 14,1 14,2 14,3 14,4 14,5 Cheng W. H., Zhao Y., Yu P. B. et al. HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression // Blood — American Society of Hematology, Elsevier BV, 2014. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2014-01-552281 — PMID:24904118
  15. ↑ 15,0 15,1 15,2 15,3 15,4 15,5 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
  16. ↑ 16,0 16,1 16,2 16,3 16,4 16,5 16,6 16,7 16,8 Waheed A., Britton R. S., Grubb J. H. et al. HFE association with transferrin receptor 2 increases cellular uptake of transferrin-bound iron // Arch. Biochem. Biophys. — Academic Press, Elsevier BV, 2008. — ISSN 0003-9861; 1096-0384 — doi:10.1016/J.ABB.2008.02.041 — PMID:18353247
  17. ↑ 17,00 17,01 17,02 17,03 17,04 17,05 17,06 17,07 17,08 17,09 17,10 17,11 17,12 17,13 17,14 17,15 17,16 17,17 17,18 17,19 17,20 17,21 17,22 17,23 17,24 GOA
  18. ↑ 18,0 18,1 18,2 William J H Griffiths, Cox T. M. Co-localization of the mammalian hemochromatosis gene product (HFE) and a newly identified transferrin receptor (TfR2) in intestinal tissue and cells // J. Histochem. Cytochem. — SAGE Publishing, 2003. — ISSN 0022-1554; 1551-5044 — doi:10.1177/002215540305100507 — PMID:12704209
  19. ↑ 19,0 19,1 19,2 19,3 19,4 19,5 19,6 19,7 GOA
  20. ↑ 20,0 20,1 Bennett M. J., Lebrón J. A., Bjorkman P. J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor // Nature / M. Skipper — NPG, Springer Science+Business Media, 2000. — ISSN 1476-4687; 0028-0836 — doi:10.1038/47417 — PMID:10638746
  21. ↑ Cheng W. H., Zhao Y., Yu P. B. et al. HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression // Blood — American Society of Hematology, Elsevier BV, 2014. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2014-01-552281 — PMID:24904118
  22. ↑ Camaschella C., Girelli D., Ganz T. A time course of hepcidin response to iron challenge in patients with HFE and TFR2 hemochromatosis // Haematologica — Ferrata Storti Foundation, 2011. — ISSN 0390-6078; 1592-8721; 1138-0381 — doi:10.3324/HAEMATOL.2010.033449 — PMID:21173098
  23. ↑ 23,0 23,1 23,2 23,3 Camaschella C., Girelli D., Ganz T. A time course of hepcidin response to iron challenge in patients with HFE and TFR2 hemochromatosis // Haematologica — Ferrata Storti Foundation, 2011. — ISSN 0390-6078; 1592-8721; 1138-0381 — doi:10.3324/HAEMATOL.2010.033449 — PMID:21173098
  24. ↑ 24,0 24,1 24,2 24,3 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
  25. ↑ 25,0 25,1 25,2 Lapointe R. The WT hemochromatosis protein HFE inhibits CD8⁺ T-lymphocyte activation // Eur. J. Immunol. — Wiley-Blackwell, 2014. — ISSN 0014-2980; 1521-4141 — doi:10.1002/EJI.201343955 — PMID:24643698
  26. ↑ 26,0 26,1 Roy C. N., Penny D. M., Feder J. N. et al. The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1999. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.274.13.9022 — PMID:10085150
  27. ↑ Roy C. N., Penny D. M., Feder J. N. et al. The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1999. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.274.13.9022 — PMID:10085150
  28. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  29. ↑ 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.)


Миоглобин молекуласы
 Бу — аксым турында мәкалә төпчеге.
Сез мәкаләне үзгәртеп һәм мәгълүмат өстәп, Википедия проектына ярдәм итә аласыз.
Чыганак — https://tt.wikipedia.org/w/index.php?title=HFE&oldid=4129482