LRP1
Внешний вид
LRP1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[34][35]
Искәрмәләр
[үзгәртү | вики-текстны үзгәртү]- ↑ 1,0 1,1 UniProt
- ↑ 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 2,37 2,38 2,39 2,40 2,41 2,42 2,43 2,44 2,45 2,46 2,47 2,48 2,49 2,50 2,51 2,52 2,53 2,54 2,55 2,56 2,57 2,58 2,59 2,60 2,61 2,62 2,63 2,64 2,65 2,66 2,67 2,68 GOA
- ↑ 3,0 3,1 Dichlberger A., Schaap F. G., Lins L. et al. Effects of six APOA5 variants, identified in patients with severe hypertriglyceridemia, on in vitro lipoprotein lipase activity and receptor binding // Arteriosclerosis, Thrombosis, and Vascular Biology — Lippincott Williams & Wilkins, 2008. — ISSN 1079-5642; 1524-4636 — doi:10.1161/ATVBAHA.108.172866 — PMID:18635818
- ↑ U Beisiegel, W Weber, G Ihrke et al. The LDL-receptor-related protein, LRP, is an apolipoprotein E-binding protein // Nature / M. Skipper — NPG, Springer Science+Business Media, 1989. — ISSN 1476-4687; 0028-0836 — doi:10.1038/341162A0 — PMID:2779654
- ↑ S Stefansson, Lawrence D. A., Argraves W. S. Plasminogen activator inhibitor-1 and vitronectin promote the cellular clearance of thrombin by low density lipoprotein receptor-related proteins 1 and 2 // 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.271.14.8215 — PMID:8626514
- ↑ S Stefansson, Lawrence D. A., Argraves W. S. Plasminogen activator inhibitor-1 and vitronectin promote the cellular clearance of thrombin by low density lipoprotein receptor-related proteins 1 and 2 // 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.271.14.8215 — PMID:8626514
- ↑ H Muramatsu, K Zou, N Sakaguchi et al. LDL receptor-related protein as a component of the midkine receptor // Biochem. Biophys. Res. Commun. — Academic Press, Elsevier BV, 2000. — ISSN 0006-291X; 1090-2104 — doi:10.1006/BBRC.2000.2549 — PMID:10772929
- ↑ Sinning I., Wild K. Phosphorylation of LRP1 regulates the interaction with Fe65 // FEBS Letters — Elsevier BV, 2011. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2011.09.028 — PMID:21968187
- ↑ Eugenin E. A., King J. E., Nath A. et al. HIV-tat induces formation of an LRP-PSD-95- NMDAR-nNOS complex that promotes apoptosis in neurons and astrocytes // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2007. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0611699104 — PMID:17360663
- ↑ Kim J., Castellano J. M., Holtzman D. M. Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular A beta clearance // Neuron / K. Brose — Cell Press, Elsevier BV, 2009. — 13 p. — ISSN 0896-6273; 1097-4199 — doi:10.1016/J.NEURON.2009.11.013 — PMID:20005821
- ↑ 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
- ↑ 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
- ↑ Husemann J, JD L., Kodama T et al. Scavenger receptor class B type I (SR-BI) mediates adhesion of neonatal murine microglia to fibrillar beta-amyloid // J. Neuroimmunol. — Elsevier BV, 2001. — ISSN 0165-5728; 1872-8421 — doi:10.1016/S0165-5728(01)00239-9 — PMID:11240025
- ↑ 14,0 14,1 14,2 14,3 14,4 Kanekiyo T., Zhang J., Liu Q. et al. Heparan sulphate proteoglycan and the low-density lipoprotein receptor-related protein 1 constitute major pathways for neuronal amyloid-beta uptake // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2011. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.5491-10.2011 — PMID:21289173
- ↑ Forsberg L., Baig S. M. Whole exome sequencing identifies LRP1 as a pathogenic gene in autosomal recessive keratosis pilaris atrophicans // J. Med. Genet. — BMJ, 2015. — ISSN 0022-2593; 1468-6244 — doi:10.1136/JMEDGENET-2014-102931 — PMID:26142438
- ↑ 16,0 16,1 16,2 16,3 Ma Q., Kisler K., Zhu D. et al. Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance // Nat. Neurosci. — NPG, 2015. — 10 p. — ISSN 1097-6256; 1546-1726 — doi:10.1038/NN.4025 — PMID:26005850
- ↑ A Kurdowska, Alden S. M., Noble J. M. et al. Involvement of alpha-2-macroglobulin receptor in clearance of interleukin 8-alpha-2-macroglobulin complexes by human alveolar macrophages // Cytokine — Elsevier BV, 2000. — ISSN 1043-4666; 1096-0023 — doi:10.1006/CYTO.1999.0640 — PMID:10880251
- ↑ 18,0 18,1 Holtzman D. M. Neuronal clearance of amyloid-β by endocytic receptor LRP1. // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2013. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.3487-13.2013 — PMID:24305823
- ↑ 19,0 19,1 19,2 19,3 19,4 19,5 Kanekiyo T., Liu C., Shinohara M. et al. LRP1 in brain vascular smooth muscle cells mediates local clearance of Alzheimer's amyloid-β. // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2012. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.3987-12.2012 — PMID:23152628
- ↑ 20,0 20,1 S Rogne, O Myklebost, S. Rogne et al. Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor // EMBO J. — NPG, 1988. — ISSN 0261-4189; 1460-2075 — doi:10.1002/J.1460-2075.1988.TB03306.X — PMID:3266596
- ↑ 21,0 21,1 21,2 21,3 GOA
- ↑ 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
- ↑ Ghai R., Coulson E. J., Collins B. M. et al. Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2013. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1216229110 — PMID:23382219
- ↑ 24,0 24,1 Rozanov D. V., Hahn-Dantona E., Strickland D. K. et al. The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells // 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.M311569200 — PMID:14645246
- ↑ Schröder B., Wrocklage C., Pan C. et al. Integral and associated lysosomal membrane proteins // Traffic — Wiley-Blackwell, 2007. — ISSN 1398-9219; 1600-0854 — doi:10.1111/J.1600-0854.2007.00643.X — PMID:17897319
- ↑ Schröder B., Wrocklage C., Pan C. et al. Integral and associated lysosomal membrane proteins // Traffic — Wiley-Blackwell, 2007. — ISSN 1398-9219; 1600-0854 — doi:10.1111/J.1600-0854.2007.00643.X — PMID:17897319
- ↑ 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
- ↑ 28,0 28,1 28,2 28,3 28,4 Hooper N. M. Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1 // 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.M112.400358 — PMID:23386614
- ↑ Deane R. SRF and myocardin regulate LRP-mediated amyloid-beta clearance in brain vascular cells // Nat. Cell Biol. — NPG, 2009. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB1819 — PMID:19098903
- ↑ 30,0 30,1 Choucair-Jaafar N., Laporte V., Levy R. et al. Complement receptor 3 (CD11b/CD18) is implicated in the elimination of β-amyloid peptides // Fundamental and Clinical Pharmacology — Wiley-Blackwell, 2011. — ISSN 0767-3981; 1472-8206 — doi:10.1111/J.1472-8206.2010.00811.X — PMID:20199584
- ↑ 31,0 31,1 Pflanzner T., Petsch B., André-Dohmen B. et al. Cellular prion protein participates in amyloid-β transcytosis across the blood-brain barrier // J. Cereb. Blood Flow Metab. / International Society for Cerebral Blood Flow and Metabolism — NPG, 2012. — ISSN 0271-678X; 1559-7016 — doi:10.1038/JCBFM.2012.7 — PMID:22293988
- ↑ Deane R. SRF and myocardin regulate LRP-mediated amyloid-beta clearance in brain vascular cells // Nat. Cell Biol. — NPG, 2009. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB1819 — PMID:19098903
- ↑ Holtzman D. M. Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Aβ uptake and degradation by astrocytes // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2012. — 13 p. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M111.288746 — PMID:22383525
- ↑ 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 | 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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