BST2 |
|
Нинди таксонда бар |
H. sapiens[d][1] |
Кодлаучы ген |
Тетерин[d][1] |
Молекуляр функция |
гомодимеризация белка[d][2], signal transducer activity[d][3], связывание с белками плазмы[d][4][5][6][…], metalloendopeptidase inhibitor activity[d][5], RNA binding[d][7] һәм связывание похожих белков[d][8][9][10] |
Күзәнәк компоненты |
цитоплазма[11][5], мембрана өлеше[d][11], multivesicular body[d][12], эндосома[d][11], late endosome[d][11], Гольджи аппараты[11][11], мембрана[d][11][13], күзәнәк мембранасы[d][11][11][14][…], күзәнәк мембранасы өлеше[d][15], күзәнәк өслеге[d][11][12][11], apical plasma membrane[d][11][11], липидный рафт[d][11], anchored component of membrane[d][11], экзосома[d][16][17][18], цитозоль[d][11] һәм azurophil granule membrane[d][11] |
Биологик процесс |
negative regulation of intracellular transport of viral material[d][11][14][19][…], regulation of actin cytoskeleton organization[d][11], response to interferon-gamma[d][11][11], immune system process[d][11], передача сигнала между клетками[d][15], response to virus[d][11][14][19][…], response to interferon-beta[d][11][11], развитие многоклеточного организма[d][15], B cell activation[d][11], negative regulation of viral genome replication[d][11][19], negative regulation of cell migration[d][5], humoral immune response[d][15], defense response to virus[d][11][11][2], type I interferon signaling pathway[d][11], negative regulation of cell growth[d][5], negative regulation of plasmacytoid dendritic cell cytokine production[d][4], response to interferon-alpha[d][11][11], positive regulation of I-kappaB kinase/NF-kappaB signaling[d][3], пролиферация[d][15], врождённый иммунитет[d][11][11][20], negative regulation of endopeptidase activity[d][11] һәм neutrophil degranulation[d][11] |
BST2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[21][22]
- ↑ 1,0 1,1 UniProt
- ↑ 2,0 2,1 Hinz A., Miguet N., Natrajan G. et al. Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain // Cell Host & Microbe — Cell Press, Elsevier BV, 2010. — ISSN 1931-3128; 1934-6069 — doi:10.1016/J.CHOM.2010.03.005 — PMID:20399176
- ↑ 3,0 3,1 Sugano S., Doi T. Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways // Oncogene — NPG, 2003. — ISSN 0950-9232; 1476-5594 — doi:10.1038/SJ.ONC.1206406 — PMID:12761501
- ↑ 4,0 4,1 Cao W., Bover L., Cho M. et al. Regulation of TLR7/9 responses in plasmacytoid dendritic cells by BST2 and ILT7 receptor interaction // J. Exp. Med. — Rockefeller University Press, 2009. — ISSN 0022-1007; 1540-9538 — doi:10.1084/JEM.20090547 — PMID:19564354
- ↑ 5,0 5,1 5,2 5,3 5,4 Gu G., Zhao D., Yin Z. et al. BST-2 binding with cellular MT1-MMP blocks cell growth and migration via decreasing MMP2 activity // J. Cell. Biochem. — Wiley, 2012. — ISSN 0730-2312; 1097-4644; 0733-1959 — doi:10.1002/JCB.23433 — PMID:22065321
- ↑ Opella S. J. HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions // 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.M111.296772 — PMID:22072710
- ↑ 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
- ↑ Schubert H. L., Zhai Q., Sandrin V. et al. Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2010. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1008206107 — PMID:20880831
- ↑ Yang H., Bieniasz P. D. Structural insight into the mechanisms of enveloped virus tethering by tetherin // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2010. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1011485107 — PMID:20940320
- ↑ Bieniasz P. D., Johnson M. C. Tetherin inhibits HIV-1 release by directly tethering virions to cells // Cell — Cell Press, Elsevier BV, 2009. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2009.08.039 — PMID:19879838
- ↑ 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 GOA
- ↑ 12,0 12,1 Marsh M., Janvier K. Rab7A is required for efficient production of infectious HIV-1 // PLoS Pathog. — PLoS, 2011. — ISSN 1553-7366; 1553-7374 — doi:10.1371/JOURNAL.PPAT.1002347 — PMID:22072966
- ↑ Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom. — Wiley, 2010. — ISSN 1076-5174; 1096-9888 — doi:10.1002/JMS.1696 — PMID:19946888
- ↑ 14,0 14,1 14,2 Bavari S., Kuhn J. H., Radoshitzky S. R. et al. Infectious Lassa virus, but not filoviruses, is restricted by BST-2/tetherin // J. Virol. — ASM, 2010. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.00103-10 — PMID:20686043
- ↑ 15,0 15,1 15,2 15,3 15,4 J. Ishikawa, T. Kaisho, H. Tomizawa et al. Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth // Genomics / A. Engel — Academic Press, Elsevier BV, 1995. — ISSN 0888-7543; 1089-8646 — doi:10.1016/0888-7543(95)80171-H — PMID:7607676
- ↑ Pisitkun T., Tchapyjnikov D., Knepper M. A. Large-scale proteomics and phosphoproteomics of urinary exosomes // Journal of the American Society of Nephrology / J. Briggs — American Society of Nephrology, 2008. — ISSN 1046-6673; 1533-3450 — doi:10.1681/ASN.2008040406 — PMID:19056867
- ↑ 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 Biology — Wiley, 2010. — ISSN 0818-9641; 1440-1711 — doi:10.1038/ICB.2010.64 — PMID:20458337
- ↑ Farina A., Lane L., Lescuyer P. et al. Proteomic analysis of podocyte exosome-enriched fraction from normal human urine // Journal of Proteomics — Elsevier BV, 2013. — ISSN 1874-3919; 0165-022X — doi:10.1016/J.JPROT.2013.01.012 — PMID:23376485
- ↑ 19,0 19,1 19,2 Weidner J. M., Jiang D., Pan X. et al. Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms // J. Virol. — ASM, 2010. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.01328-10 — PMID:20943977
- ↑ Jouvenet N., Bieniasz P. D., Neil S. Broad-spectrum inhibition of retroviral and filoviral particle release by tetherin // J. Virol. — ASM, 2009. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.02211-08 — PMID:19036818
- ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
- ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.
- 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.)