MAPT

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Время, выделенное для выполнения скриптов, истекло.

MAPT (ингл. Время, выделенное для выполнения скриптов, истекло.) — Время, выделенное для выполнения скриптов, истекло. аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[54][55]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. 1,0 1,1 UniProt
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  5. A Takashima, M Murayama, O Murayama et al. Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau // Proc. Natl. Acad. Sci. U.S.A. / M. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.95.16.9637PMID:9689133
  6. Geetha T. Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation // J. Neurochem.Wiley-Blackwell, 2005. — ISSN 0022-3042; 1471-4159doi:10.1111/J.1471-4159.2005.03181.XPMID:15953362
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  8. Strittmatter W. J., Saunders A. M., M Goedert et al. Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease // Proc. Natl. Acad. Sci. U.S.A. / M. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 1994. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.91.23.11183PMID:7972031
  9. Chambraud B., Sardin E., Giustiniani J. et al. A role for FKBP52 in Tau protein function // Proc. Natl. Acad. Sci. U.S.A. / M. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2010. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.0914957107PMID:20133804
  10. Gamblin T. C., Chen F., Zambrano A. et al. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease // Proc. Natl. Acad. Sci. U.S.A. / M. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2003. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.1630428100PMID:12888622
  11. Brancolini C. Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis // J. Neurosci. / M. PicciottoSociety for Neuroscience, 1998. — ISSN 0270-6474; 1529-2401doi:10.1523/JNEUROSCI.18-18-07061.1998PMID:9736630
  12. 12,00 12,01 12,02 12,03 12,04 12,05 12,06 12,07 12,08 12,09 12,10 12,11 12,12 UniProt-GOA
  13. Bodea L., Eckert A., Götz J. et al. Tau physiology and pathomechanisms in frontotemporal lobar degeneration // J. Neurochem.Wiley-Blackwell, 2016. — ISSN 0022-3042; 1471-4159doi:10.1111/JNC.13600PMID:27306859
  14. Götz J. Tau promotes neurodegeneration via DRP1 mislocalization in vivo // Neuron / K. BroseCell Press, Elsevier BV, 2012. — ISSN 0896-6273; 1097-4199doi:10.1016/J.NEURON.2012.06.026PMID:22920254
  15. 15,00 15,01 15,02 15,03 15,04 15,05 15,06 15,07 15,08 15,09 15,10 15,11 15,12 15,13 15,14 15,15 15,16 15,17 15,18 15,19 15,20 Guo T., Noble W., Hanger D. P. Roles of tau protein in health and disease. // Acta Neuropathol. (Berl)Springer, 2017. — ISSN 0001-6322; 1432-0533doi:10.1007/S00401-017-1707-9PMID:28386764
  16. 16,0 16,1 16,2 16,3 Yu J., Tan L. The Role of MAPT in Neurodegenerative Diseases: Genetics, Mechanisms and Therapy // Mol. Neurobiol.Springer, 2016. — ISSN 0893-7648; 1559-1182doi:10.1007/S12035-015-9415-8PMID:26363795
  17. Butner K. A., Kirschner M. W. Tau protein binds to microtubules through a flexible array of distributed weak sites // J. Cell Biol. / J. NunnariRockefeller University Press, 1991. — ISSN 0021-9525; 1540-8140doi:10.1083/JCB.115.3.717PMID:1918161
  18. 18,0 18,1 18,2 18,3 18,4 Yu J., Tan L. The Role of MAPT in Neurodegenerative Diseases: Genetics, Mechanisms and Therapy // Mol. Neurobiol.Springer, 2016. — ISSN 0893-7648; 1559-1182doi:10.1007/S12035-015-9415-8PMID:26363795
  19. Diaz-Hernandez M., María Teresa Miras Portugal Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells // Mol. Cell. Neurosci.Elsevier BV, 2007. — ISSN 1044-7431; 1095-9327doi:10.1016/J.MCN.2007.12.010PMID:18272392
  20. Atapour N., Hensch T. K., Hirokawa N. Defects in Synaptic Plasticity, Reduced NMDA-Receptor Transport, and Instability of Postsynaptic Density Proteins in Mice Lacking Microtubule-Associated Protein 1A // J. Neurosci. / M. PicciottoSociety for Neuroscience, 2015. — ISSN 0270-6474; 1529-2401doi:10.1523/JNEUROSCI.2671-15.2015PMID:26609151
  21. Plattner F. Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites. // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2013. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M112.433326PMID:23362255
  22. Gamblin T. C., Chen F., Zambrano A. et al. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease // Proc. Natl. Acad. Sci. U.S.A. / M. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2003. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.1630428100PMID:12888622
  23. Brancolini C. Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis // J. Neurosci. / M. PicciottoSociety for Neuroscience, 1998. — ISSN 0270-6474; 1529-2401doi:10.1523/JNEUROSCI.18-18-07061.1998PMID:9736630
  24. Ryoo S., Jeong H. K., Radnaabazar C. et al. DYRK1A-mediated hyperphosphorylation of Tau. A functional link between Down syndrome and Alzheimer disease. // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2007. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M707358200PMID:17906291
  25. Zweckstetter M., Mandelkow E. Phosphorylation of human Tau protein by microtubule affinity-regulating kinase 2. // Biochemistry / A. SchepartzAmerican Chemical Society, 2013. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI401266NPMID:24251416
  26. O. Schweers, E. Schönbrunn-Hanebeck, A. Marx et al. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1994. — ISSN 0021-9258; 1083-351X; 1067-8816PMID:7929085
  27. Mandelkow E. Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain // Biochemistry / A. SchepartzAmerican Chemical Society, 2004. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI0357006PMID:14769047
  28. Eliezer D., Barré P., Kobaslija M. et al. Residual structure in the repeat domain of tau: echoes of microtubule binding and paired helical filament formation // Biochemistry / A. SchepartzAmerican Chemical Society, 2005. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI048953NPMID:15654759
  29. Diaz-Hernandez M., María Teresa Miras Portugal Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells // Mol. Cell. Neurosci.Elsevier BV, 2007. — ISSN 1044-7431; 1095-9327doi:10.1016/J.MCN.2007.12.010PMID:18272392
  30. Zhou Y., Hayashi I., Wong J. et al. Intracellular clusterin interacts with brain isoforms of the bridging integrator 1 and with the microtubule-associated protein Tau in Alzheimer's disease // PLOS ONE / PLOS ONE EditorsPLoS, 2014. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0103187PMID:25051234
  31. Chiosis G., Greengard P. Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies // Proc. Natl. Acad. Sci. U.S.A. / M. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2007. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.0701055104PMID:17517623
  32. Mandelkow E., Hoenger A., Skiniotis G. Surface-decoration of microtubules by human tau // Journal of Molecular Biology / P. WrightElsevier BV, 2004. — ISSN 0022-2836; 1089-8638doi:10.1016/J.JMB.2004.04.008PMID:15147841
  33. 33,0 33,1 33,2 Cummings D. M., Muzammil A Nahaboo Solim, Moens T. G. et al. A genome-wide gene-expression analysis and database in transgenic mice during development of amyloid or tau pathology // Cell ReportsCell Press, Elsevier BV, 2015. — ISSN 2211-1247; 2639-1856doi:10.1016/J.CELREP.2014.12.041PMID:25620700
  34. Dinh K., Poindexter B. J., Barnes J. L. et al. Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells // CytokineElsevier BV, 2009. — ISSN 1043-4666; 1096-0023doi:10.1016/J.CYTO.2008.12.004PMID:19157893
  35. 35,0 35,1 Black M. M., T Slaughter, S Moshiach et al. Tau is enriched on dynamic microtubules in the distal region of growing axons // J. Neurosci. / M. PicciottoSociety for Neuroscience, 1996. — ISSN 0270-6474; 1529-2401doi:10.1523/JNEUROSCI.16-11-03601.1996PMID:8642405
  36. Lee G. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain // J. Cell Biol. / J. NunnariRockefeller University Press, 1995. — ISSN 0021-9525; 1540-8140doi:10.1083/JCB.131.5.1327PMID:8522593
  37. Villacé P., Marión R. M., Ortín J. The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs // Nucleic Acids Res.OUP, University of Oxford, 2004. — ISSN 0305-1048; 1362-4962; 1362-4954doi:10.1093/NAR/GKH552PMID:15121898
  38. 38,0 38,1 38,2 Ittner L. M., Ke Y. D., Delerue F. et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models // CellCell Press, Elsevier BV, 2010. — ISSN 0092-8674; 1097-4172doi:10.1016/J.CELL.2010.06.036PMID:20655099
  39. Black M. M., T Slaughter, S Moshiach et al. Tau is enriched on dynamic microtubules in the distal region of growing axons // J. Neurosci. / M. PicciottoSociety for Neuroscience, 1996. — ISSN 0270-6474; 1529-2401doi:10.1523/JNEUROSCI.16-11-03601.1996PMID:8642405
  40. Ittner L. M., Ke Y. D., Delerue F. et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models // CellCell Press, Elsevier BV, 2010. — ISSN 0092-8674; 1097-4172doi:10.1016/J.CELL.2010.06.036PMID:20655099
  41. Deaconescu A. M., Kutter S. Regulation of Microtubule Assembly by Tau and not by Pin1. // Journal of Molecular Biology / P. WrightElsevier BV, 2016. — ISSN 0022-2836; 1089-8638doi:10.1016/J.JMB.2016.03.010PMID:26996940
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  43. Miller B. L., Seeley W. W. Acetylated tau destabilizes the cytoskeleton in the axon initial segment and is mislocalized to the somatodendritic compartment // Mol. Neurodegener.BMC, Springer, 2016. — ISSN 1750-1326doi:10.1186/S13024-016-0109-0PMID:27356871
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  50. Weingarten M. D., Lockwood A. H., Hwo S. Y. et al. A protein factor essential for microtubule assembly // Proc. Natl. Acad. Sci. U.S.A. / M. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 1975. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.72.5.1858PMID:1057175
  51. Drechsel D. N., Hyman A. A., Cobb M. H. et al. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau // Mol. Biol. Cell,American Society for Cell Biology, 1992. — ISSN 1059-1524; 1939-4586; 1044-2030doi:10.1091/MBC.3.10.1141PMID:1421571
  52. Mandelkow E., Mandelkow E., G Drewes et al. Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262 // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1995. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.270.13.7679PMID:7706316
  53. A Caceres, J Mautino, Kosik K. S. Suppression of MAP2 in cultured cerebellar macroneurons inhibits minor neurite formation // Neuron / K. BroseCell Press, Elsevier BV, 1992. — ISSN 0896-6273; 1097-4199doi:10.1016/0896-6273(92)90025-9PMID:1389180
  54. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). 18 сентябрь, 2017 тикшерелде.
  55. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелде.

Время, выделенное для выполнения скриптов, истекло.

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.)