Degradation or aggregation: the ramifications of post-translational modifications on tau

키워드

참고문헌 (93)

1. Mandelkow EM, "Tau in Alzheimer's disease", Trends Cell Biol, 8, pp.425~427 (1998)[DOI]
2. Andreadis A, "Misregulation of tau alternative splicing in neurodegeneration and dementia", Prog Mol Subcell Biol, 44, pp.89~107 (2006)
3. Goedert M, "Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease", Neuron, 3, pp.519~526 (1989)[DOI]
4. "FEBS Lett", 1992, 95~99, 10.1016[DOI]
5. Kyte J, "A simple method for displaying the hydropathic character of a protein", J Mol Biol, 157, pp.105~132 (1982)[DOI]
6. Alonso AD, "Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein", J Biol Chem, 276, pp.37967~37973 (2001)
7. Wolfe MS, "Tau mutations in neurodegenerative diseases", J Biol Chem, 284, pp.6021~6025 (2009)[DOI]
8. Abraha A, "C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease", J Cell Sci, 113, pp.3737~3745 (2000)
9. Flores-Rodriguez P, "The relationship between truncation and phosphorylation at the C-terminus of tau protein in the paired helical filaments of Alzheimer's disease", Front Neurosci, 9, pp.33~ (2015)
10. Peeraer E, "Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice", Neurobiol Dis, 73, pp.83~95 (2015)[DOI]
11. Guo JL, "Neurofibrillary tangle-like tau pathology induced by synthetic tau fibrils in primary neurons over-expressing mutant tau", FEBS Lett, 587, pp.717~723 (2013)[DOI]
12. Guo JL, "Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles", J Biol Chem, 286, pp.15317~15331 (2011)[DOI]
13. Nubling G, "Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with alpha-synuclein at the single molecule level", Mol Neurodegener, 7, pp.35~ (2012)[DOI]
14. Choi TS, "Supramolecular Modulation of Structural Polymorphism in Pathogenic alpha-Synuclein Fibrils Using Copper(II) Coordination", Angew Chem Int Ed Engl, 57, pp.3099~3103 (2018)[DOI]
15. Wille H, "Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro", J Cell Biol, 118, pp.573~584 (1992)[DOI]
16. Fitzpatrick AWP, "Cryo-EM structures of tau filaments from Alzheimer's disease", Nature, 547, pp.185~190 (2017)[DOI]
17. Giannakopoulos P, "Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer's disease", Neurology, 60, pp.1495~1500 (2003)[DOI]
18. Ethell DW, "An amyloid-notch hypothesis for Alzheimer's disease", Neuroscientist, 16, pp.614~617 (2010)[DOI]
19. Hung SY, "Drug candidates in clinical trials for Alzheimer's disease", J Biomed Sci, 24, pp.47~ (2017)[DOI]
20. Wang Y, "Tau in physiology and pathology", Nat Rev Neurosci, 17, pp.5~21 (2016)[DOI]
21. Min SW, "Acetylation of tau inhibits its degradation and contributes to tauopathy", Neuron, 67, pp.953~966 (2010)[DOI]
22. Roth SY, "Histone acetyltransferases", Annu Rev Biochem, 70, pp.81~120 (2001)[DOI]
23. Liu X, "The structural basis of protein acetylation by the p300", CBP transcriptional coactivator, 2008, pp.451, 846~850
24. Marmorstein R, "Structure of histone acetyltransferases", J Mol Biol, 311, pp.433~444 (2001)[DOI]
25. Cohen TJ, "The acetylation of tau inhibits its function and promotes pathological tau aggregation", Nat Commun, 2, pp.252~ (2011)[DOI]
26. Morris M, "Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice", Nat Neurosci, 18, pp.1183~1189 (2015)[DOI]
27. Cook C, "Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance", Hum Mol Genet, 23, pp.104~116 (2014)[DOI]
28. Ding H, "Histone deacetylase 6 interacts with the microtubule-associated protein tau", J Neurochem, 106, pp.2119~2130 (2008)[DOI]
29. Fan SJ, "The novel histone de acetylase 6 inhibitor, MPT0G211, ameliorates tau phosphorylation and cognitive deficits in an Alzheimer's disease model", Cell Death Dis, 9, pp.655~ (2018)[DOI]
30. Carlomagno Y, "An acetylation-phosphorylation switch that regulates tau aggregation propensity and function", J Biol Chem, 292, pp.15277~15286 (2017)[DOI]
31. Julien C, "Sirtuin 1 reduction parallels the accumulation of tau in Alzheimer disease", J Neuropathol Exp Neurol, 68, pp.48~58 (2009)[DOI]
32. Gorsky MK, "Pseudo-acetylation of multiple sites on human Tau proteins alters Tau phosphorylation and microtubule binding, and ameliorates amyloid beta toxicity", Sci Rep, 7, pp.9984~ (2017)[DOI]
33. Min SW, "Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits", Nat Med, 21, pp.1154~1162 (2015)[DOI]
34. Tracy TE, "Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss", Neuron, 90, pp.245~260 (2016)[DOI]
35. Irwin DJ, "Acetylated tau neuropathology in sporadic and hereditary tauopathies", Am J Pathol, 183, pp.344~351 (2013)[DOI]
36. Trzeciakiewicz H, "A Dual Pathogenic Mechanism Links Tau Acetylation to Sporadic Tauopathy", Sci Rep, 7, pp.44102~ (2017)[DOI]
37. Gorsky MK, "Acetylation mimic of lysine 280 exacerbates human Tau neurotoxicity in vivo", Sci Rep, 6, pp.22685~ (2016)[DOI]
38. Irwin DJ, "Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies", Brain, 135, pp.807~818 (2012)[DOI]
39. Luo Y, "Structural Insight into Tau Protein's Paradox of Intrinsically Disordered Behavior, Self-Acetylation Activity, and Aggregation", J Phys Chem Lett, 5, pp.3026~3031 (2014)[DOI]
40. Santa-Maria I, "Quinones facilitate the self-assembly of the phosphorylated tubulin binding region of tau into fibrillar polymers", Biochemistry, 43, pp.2888~2897 (2004)[DOI]
41. Perez M, "Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model", J Alzheimers Dis, 5, pp.301~308 (2003)[DOI]
42. Noble W, "Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo", Proc Natl Acad Sci U S A, 102, pp.6990~6995 (2005)[DOI]
43. Avila J, "Tau phosphorylation and aggregation in Alzheimer's disease pathology", FEBS Lett, 580, pp.2922~2927 (2006)[DOI]
44. Kopke E, "Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease", J Biol Chem, 268, pp.24374~24384 (1993)
45. Kenessey A, "The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments", Brain Res, 629, pp.40~46 (1993)[DOI]
46. Lee G, "Phosphorylation of tau by fyn: implications for Alzheimer's disease", J Neurosci, 24, pp.2304~2312 (2004)[DOI]
47. Braak E, "A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads", Acta Neuropathol, 87, pp.554~567 (1994)[DOI]
48. Lucas JJ, "Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice", EMBO J, 20, pp.27~39 (2001)[DOI]
49. Forlenza OV, "Lithium, a Therapy for AD: Current Evidence from Clinical Trials of Neurodegenerative Disorders", Curr Alzheimer Res, 13, pp.879~886 (2016)[DOI]
50. King MK, "Glycogen synthase kinase-3 inhibitors: Rescuers of cognitive impairments", Pharmacol Ther, 141, pp.1~12 (2014)[DOI]
51. Matsunaga S, "Lithium as a Treatment for Alzheimer's Disease: A Systematic Review and Meta-Analysis", J Alzheimers Dis, 48, pp.403~410 (2015)[DOI]
52. Yu Y, "Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases", J Neurochem, 108, pp.1480~1494 (2009)[DOI]
53. Noble W, "The importance of tau phosphorylation for neurodegenerative diseases", Front Neurol, 4, pp.83~ (2013)
54. Sontag JM, "Protein phosphatase 2A dysfunction in Alzheimer's disease", Front Mol Neurosci, 7, pp.16~ (2014)
55. Liu F, "Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation", Eur J Neurosci, 22, pp.1942~1950 (2005)[DOI]
56. Gong CX, "Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain", J Neurochem, 65, pp.732~738 (1995)
57. Gong CX, "Phosphoprotein phosphatase activities in Alzheimer disease brain", J Neurochem, 61, pp.921~927 (1993)[DOI]
58. Choi WH, "Open-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation", Nat Commun, 7, pp.10963~ (2016)[DOI]
59. Han DH, "Direct cellular delivery of human proteasomes to delay tau aggregation", Nat Commun, 5, pp.5633~ (2014)[DOI]
60. Jiang Y, "The arginylation branch of the N-end rule pathway positively regulates cellular autophagic flux and clearance of proteotoxic proteins", Autophagy, 12, pp.2197~2212 (2016)[DOI]
61. Kim JH, "Inhibitory RNA Aptamers of Tau Oligomerization and Their Neuroprotective Roles against Proteotoxic Stress", Mol Pharm, 13, pp.2039~2048 (2016)[DOI]
62. Karabiyik C, "Autophagy impairment in Parkinson's disease", Essays Biochem, 61, pp.711~720 (2017)[DOI]
63. Cohen TJ, "The microtubule-associated tau protein has intrinsic acetyltransferase activity", Nat Struct Mol Biol, 20, pp.756~762 (2013)[DOI]
64. Dickey CA, "The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins", J Clin Invest, 117, pp.648~658 (2007)[DOI]
65. Dickey CA, "HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser", Thr sites but not KXGS (MARK) sites, 2006, pp.20, 753~755
66. Liu WK, "Abnormal tau proteins from Alzheimer's disease brains. Purification and amino acid analysis", J Biol Chem, 266, pp.21723~21727 (1991)
67. David DC, "Proteasomal degradation of tau protein", J Neurochem, 83, pp.176~185 (2002)[DOI]
68. Grune T, "Tau protein degradation is catalyzed by the ATP", ubiquitin-independent 20S proteasome under normal cell conditions, 2010, pp.500, 181~188
69. Mori H, "Ubiquitin is a component of paired helical filaments in Alzheimer's disease", Science, 235, pp.1641~1644 (1987)[DOI]
70. Perry G, "Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains", Proc Natl Acad Sci U S A, 84, pp.3033~3036 (1987)[DOI]
71. Cripps D, "Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation", J Biol Chem, 281, pp.10825~10838 (2006)[DOI]
72. Morishima-Kawashima M, "Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments", Neuron, 10, pp.1151~1160 (1993)[DOI]
73. Paine S, "Immunoreactivity to Lys63-linked polyubiquitin is a feature of neurodegeneration", Neurosci Lett, 460, pp.205~208 (2009)[DOI]
74. Tan JM, "Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases", Hum Mol Genet, 17, pp.431~439 (2008)[DOI]
75. Tan Z, "Mutant ubiquitin found in Alzheimer's disease causes neuritic beading of mitochondria in association with neuronal degeneration", Cell Death Differ, 14, pp.1721~1732 (2007)[DOI]
76. Keck S, "Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease", J Neurochem, 85, pp.115~122 (2003)[DOI]
77. Keller JN, "Impaired proteasome function in Alzheimer's disease", J Neurochem, 75, pp.436~439 (2000)
78. Lopez Salon M, "Defective ubiquitination of cerebral proteins in Alzheimer's disease", J Neurosci Res, 62, pp.302~310 (2000)[DOI]
79. Cardozo C, "Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway", Arch Biochem Biophys, 408, pp.103~110 (2002)[DOI]
80. Zhang JY, "Microtubule-associated protein tau is a substrate of ATP", Mg(2+)-dependent proteasome protease system, 2005, pp.112, 547~555
81. de Vrij FM, "Protein quality control in Alzheimer's disease by the ubiquitin proteasome system", Prog Neurobiol, 74, pp.249~270 (2004)[DOI]
82. Lee MJ, "Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system", Prog Neurobiol, 105, pp.49~59 (2013)[DOI]
83. Petrucelli L, "CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation", Hum Mol Genet, 13, pp.703~714 (2004)[DOI]
84. Babu JR, "Sequestosome 1", p62 shuttles polyubiquitinated tau for proteasomal degradation, 2005, pp.94, 192~203
85. Flach K, "Axotrophin", MARCH7 acts as an E3 ubiquitin ligase and ubiquitinates tau protein in vitro impairing microtubule binding, 2014, pp.1842, 1527~1538
86. Shimura H, "CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival", J Biol Chem, 279, pp.4869~4876 (2004)[DOI]
87. Hatakeyama S, "U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy", J Neurochem, 91, pp.299~307 (2004)[DOI]
88. Sahara N, "In vivo evidence of CHIP up-regulation attenuating tau aggregation", J Neurochem, 94, pp.1254~1263 (2005)[DOI]
89. Joshi V, "A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?", Front Mol Neurosci, 9, pp.93~ (2016)
90. Gupta R, "The Proline", Arginine Dipeptide from Hexanucleotide Repeat Expanded C9ORF72 Inhibits the Proteasome, 2017, pp.4, e0249~16
91. 신승균, "Docosahexaenoic acid-mediated protein aggregates may reduce proteasome activity and delay myotube degradation during muscle atrophy in vitro", Experimental and Molecular Medicine, 49, pp.1~11 (2017), 생화학분자생물학회
92. Lee JH, "Facilitated Tau Degradation by USP14 Aptamers via Enhanced Proteasome Activity", Sci Rep, 5, pp.10757~ (2015)[DOI]
93. Wang Y, "Proteolytic processing of tau", Biochem Soc Trans, 38, pp.955~961 (2010)[DOI]

관련 논문AI추천