메뉴 건너뛰기




Volumn 21, Issue 10, 2015, Pages 1154-1162

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

(22)  Min, Sang Won a,b   Chen, Xu a,b   Tracy, Tara E a,b   Li, Yaqiao a   Zhou, Yungui a   Wang, Chao a,b   Shirakawa, Kotaro a   Minami, S Sakura a,b   Defensor, Erwin c   Mok, Sue Ann d   Sohn, Peter Dongmin a,d   Schilling, Birgit e   Cong, Xin e   Ellerby, Lisa e   Gibson, Bradford W e   Johnson, Jeffrey f   Krogan, Nevan f   Shamloo, Mehrdad c   Gestwicki, Jason d   Masliah, Eliezer g   more..


Author keywords

[No Author keywords available]

Indexed keywords

E1A ASSOCIATED P300 PROTEIN; SALICYLIC ACID; SALSALATE; TAU PROTEIN;

EID: 84943637753     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.3951     Document Type: Article
Times cited : (385)

References (59)
  • 1
    • 60049091402 scopus 로고    scopus 로고
    • Tauopathies with parkinsonism: Clinical spectrum, neuropathologic basis, biological markers, and treatment options
    • Ludolph, A. C. et al. Tauopathies with parkinsonism: clinical spectrum, neuropathologic basis, biological markers, and treatment options. Eur. J. Neurol. 16, 297-309 (2009).
    • (2009) Eur. J. Neurol , vol.16 , pp. 297-309
    • Ludolph, A.C.1
  • 2
    • 34447096691 scopus 로고    scopus 로고
    • Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: Consensus of the Consortium for Frontotemporal Lobar Degeneration
    • Cairns, N. J. et al. Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol. 114, 5-22 (2007).
    • (2007) Acta Neuropathol , vol.114 , pp. 5-22
    • Cairns, N.J.1
  • 3
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H. & Braak, E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82, 239-259 (1991).
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 4
    • 84858965241 scopus 로고    scopus 로고
    • Identification of oligomers at early stages of tau aggregation in Alzheimers disease
    • Lasagna-Reeves, C. A. et al. Identification of oligomers at early stages of tau aggregation in Alzheimers disease. FASEB J. 26, 1946-1959 (2012).
    • (2012) FASEB J , vol.26 , pp. 1946-1959
    • Lasagna-Reeves, C.A.1
  • 5
    • 84883517948 scopus 로고    scopus 로고
    • Characteristics of tau oligomers
    • Ren, Y. & Sahara, N. Characteristics of tau oligomers. Frontiers Neurol. 4, 102 (2013).
    • (2013) Frontiers Neurol , vol.4 , pp. 102
    • Ren, Y.1    Sahara, N.2
  • 6
    • 33244456786 scopus 로고    scopus 로고
    • Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimers disease
    • Maeda, S. et al. Increased levels of granular tau oligomers: an early sign of brain aging and Alzheimers disease. Neurosci. Res. 54, 197-201 (2006).
    • (2006) Neurosci. Res , vol.54 , pp. 197-201
    • Maeda, S.1
  • 7
    • 79957913270 scopus 로고    scopus 로고
    • Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
    • Lasagna-Reeves, C. A. et al. Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice. Mol. Neurodegener. 6, 39 (2011).
    • (2011) Mol. Neurodegener , vol.6 , pp. 39
    • Lasagna-Reeves, C.A.1
  • 8
    • 34147125835 scopus 로고    scopus 로고
    • Accumulation of pathological tau species and memory loss in a conditional model of tauopathy
    • Berger, Z. et al. Accumulation of pathological tau species and memory loss in a conditional model of tauopathy. J. Neurosci. 27, 3650-3662 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 3650-3662
    • Berger, Z.1
  • 9
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz, K. et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481 (2005).
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1
  • 10
    • 80855138109 scopus 로고    scopus 로고
    • Reversibility of Tau-related cognitive defects in a regulatable FTD mouse model
    • Sydow, A. et al. Reversibility of Tau-related cognitive defects in a regulatable FTD mouse model. J. Mol. Neurosci. 45, 432-437 (2011).
    • (2011) J. Mol. Neurosci , vol.45 , pp. 432-437
    • Sydow, A.1
  • 11
    • 84864389698 scopus 로고    scopus 로고
    • Degradation of tau protein by autophagy and proteasomal pathways
    • Wang, Y. & Mandelkow, E. Degradation of tau protein by autophagy and proteasomal pathways. Biochem. Soc. Trans. 40, 644-652 (2012).
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 644-652
    • Wang, Y.1    Mandelkow, E.2
  • 12
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee, B. H. et al. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184 (2010).
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1
  • 13
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • Tai, H. C. et al. The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am. J. Pathol. 181, 1426-1435 (2012).
    • (2012) Am. J. Pathol , vol.181 , pp. 1426-1435
    • Tai, H.C.1
  • 14
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • Min, S. W. et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67, 953-966 (2010).
    • (2010) Neuron , vol.67 , pp. 953-966
    • Min, S.W.1
  • 15
    • 79953087890 scopus 로고    scopus 로고
    • The acetylation of tau inhibits its function and promotes pathological tau aggregation
    • Cohen, T. J. et al. The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat. Commun. 2, 252 (2011).
    • (2011) Nat. Commun , vol.2 , pp. 252
    • Cohen, T.J.1
  • 16
    • 79954415619 scopus 로고    scopus 로고
    • Comprehensive lysine acetylomes emerging from bacteria to humans
    • Kim, G. W. & Yang, X. J. Comprehensive lysine acetylomes emerging from bacteria to humans. Trends Biochem. Sci. 36, 211-220 (2011).
    • (2011) Trends Biochem. Sci , vol.36 , pp. 211-220
    • Kim, G.W.1    Yang, X.J.2
  • 17
    • 84868677556 scopus 로고    scopus 로고
    • Biochemistry and cell biology of tau protein in neurofibrillary degeneration
    • Mandelkow, E. M. & Mandelkow, E. Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb. Perspect. Med. 2, a006247 (2012).
    • (2012) Cold Spring Harb. Perspect. Med , vol.2 , pp. a006247
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 18
    • 84890357149 scopus 로고    scopus 로고
    • Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance
    • Cook, C. et al. Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance. Hum. Mol. Genet. 23, 104-116 (2014).
    • (2014) Hum. Mol. Genet , vol.23 , pp. 104-116
    • Cook, C.1
  • 19
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • Yoshiyama, Y. et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron 53, 337-351 (2007).
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1
  • 20
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha, G. A. , Bowser, R. , Kazam, I. G. & Davies, P. Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J. Neurosci. Res. 48, 128-132 (1997).
    • (1997) J. Neurosci. Res , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 21
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimers disease
    • Weaver, C. L. , Espinoza, M. , Kress, Y. & Davies, P. Conformational change as one of the earliest alterations of tau in Alzheimers disease. Neurobiol. Aging 21, 719-727 (2000).
    • (2000) Neurobiol. Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3    Davies, P.4
  • 22
    • 84896690531 scopus 로고    scopus 로고
    • Regulation of the mitogen-activated protein kinase kinase (MEK)-1 by NAD-dependent deacetylases
    • Yeung, F. et al. Regulation of the mitogen-activated protein kinase kinase (MEK)-1 by NAD-dependent deacetylases. Oncogene 34, 798-804 (2015).
    • (2015) Oncogene , vol.34 , pp. 798-804
    • Yeung, F.1
  • 23
    • 84896532784 scopus 로고    scopus 로고
    • Microtubule acetylation amplifies p38 kinase signalling and anti-inflammatory IL-10 production
    • Wang, B. et al. Microtubule acetylation amplifies p38 kinase signalling and anti-inflammatory IL-10 production. Nat. Commun. 5, 3479 (2014).
    • (2014) Nat. Commun , vol.5 , pp. 3479
    • Wang, B.1
  • 24
    • 84892455332 scopus 로고    scopus 로고
    • P300-dependent acetylation of activating transcription factor 5 enhances C/EBPβ transactivation of C/EBPα during 3T3-L1 differentiation
    • Zhao, Y. et al. p300-dependent acetylation of activating transcription factor 5 enhances C/EBPβ transactivation of C/EBPα during 3T3-L1 differentiation. Mol. Cell. Biol. 34, 315-324 (2014).
    • (2014) Mol. Cell. Biol , vol.34 , pp. 315-324
    • Zhao, Y.1
  • 25
    • 70349705552 scopus 로고    scopus 로고
    • AAV-tau mediates pyramidal neurodegeneration by cell-cycle re-entry without neurofibrillary tangle formation in wild-type mice
    • Jaworski, T. et al. AAV-tau mediates pyramidal neurodegeneration by cell-cycle re-entry without neurofibrillary tangle formation in wild-type mice. PLoS ONE 4, e7280 (2009).
    • (2009) PLoS ONE , vol.4 , pp. e7280
    • Jaworski, T.1
  • 26
    • 84858439334 scopus 로고    scopus 로고
    • Intact neurobehavioral development and dramatic impairments of procedural-like memory following neonatal ventral hippocampal lesion in rats
    • Lecourtier, L. et al. Intact neurobehavioral development and dramatic impairments of procedural-like memory following neonatal ventral hippocampal lesion in rats. Neuroscience 207, 110-123 (2012).
    • (2012) Neuroscience , vol.207 , pp. 110-123
    • Lecourtier, L.1
  • 27
    • 79958829010 scopus 로고    scopus 로고
    • P301S mutant human tau transgenic mice manifest early symptoms of human tauopathies with dementia and altered sensorimotor gating
    • Takeuchi, H. et al. P301S mutant human tau transgenic mice manifest early symptoms of human tauopathies with dementia and altered sensorimotor gating. PLoS ONE 6, e21050 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e21050
    • Takeuchi, H.1
  • 28
    • 78149285661 scopus 로고    scopus 로고
    • CBP/p300 double null cells reveal effect of coactivator level and diversity on CREB transactivation
    • Kasper, L. H. et al. CBP/p300 double null cells reveal effect of coactivator level and diversity on CREB transactivation. EMBO J. 29, 3660-3672 (2010).
    • (2010) EMBO J , vol.29 , pp. 3660-3672
    • Kasper, L.H.1
  • 29
    • 84922363112 scopus 로고    scopus 로고
    • Genome-wide and single-cell analyses reveal a context dependent relationship between CBP recruitment and gene expression
    • Kasper, L. H. , Qu, C. , Obenauer, J. C. , McGoldrick, D. J. & Brindle, P. K. Genome-wide and single-cell analyses reveal a context dependent relationship between CBP recruitment and gene expression. Nucleic Acids Res. 42, 11363-11382 (2014).
    • (2014) Nucleic Acids Res , vol.42 , pp. 11363-11382
    • Kasper, L.H.1    Qu, C.2    Obenauer, J.C.3    McGoldrick, D.J.4    Brindle, P.K.5
  • 30
    • 78751611793 scopus 로고    scopus 로고
    • Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation
    • Jin, Q. et al. Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation. EMBO J. 30, 249-262 (2011).
    • (2011) EMBO J , vol.30 , pp. 249-262
    • Jin, Q.1
  • 31
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function. Cell 128, 693-705 (2007).
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 32
    • 78650653951 scopus 로고    scopus 로고
    • Anti-inflammatory action of donepezil ameliorates tau pathology, synaptic loss, and neurodegeneration in a tauopathy mouse model
    • Yoshiyama, Y. , Kojima, A. , Ishikawa, C. & Arai, K. Anti-inflammatory action of donepezil ameliorates tau pathology, synaptic loss, and neurodegeneration in a tauopathy mouse model. J. Alzheimers Dis. 22, 295-306 (2010).
    • (2010) J. Alzheimers Dis , vol.22 , pp. 295-306
    • Yoshiyama, Y.1    Kojima, A.2    Ishikawa, C.3    Arai, K.4
  • 33
    • 84875233425 scopus 로고    scopus 로고
    • Thy1-hAPPLond/Swe+ mouse model of Alzheimers disease displays broad behavioral deficits in sensorimotor, cognitive and social function
    • Faizi, M. et al. Thy1-hAPPLond/Swe+ mouse model of Alzheimers disease displays broad behavioral deficits in sensorimotor, cognitive and social function. Brain Behav. 2, 142-154 (2012).
    • (2012) Brain Behav , vol.2 , pp. 142-154
    • Faizi, M.1
  • 34
    • 84876695265 scopus 로고    scopus 로고
    • Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation
    • Grinberg, L. T. et al. Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation. Acta Neuropathol. 125, 581-593 (2013).
    • (2013) Acta Neuropathol , vol.125 , pp. 581-593
    • Grinberg, L.T.1
  • 35
    • 84880638106 scopus 로고    scopus 로고
    • Acetylated tau neuropathology in sporadic and hereditary tauopathies
    • Irwin, D. J. et al. Acetylated tau neuropathology in sporadic and hereditary tauopathies. Am. J. Pathol. 183, 344-351 (2013).
    • (2013) Am. J. Pathol. , vol.183 , pp. 344-351
    • Irwin, D.J.1
  • 36
    • 84857620173 scopus 로고    scopus 로고
    • Acetylated tau, a novel pathological signature in Alzheimers disease and other tauopathies
    • Irwin, D. J. et al. Acetylated tau, a novel pathological signature in Alzheimers disease and other tauopathies. Brain 135, 807-818 (2012).
    • (2012) Brain , vol.135 , pp. 807-818
    • Irwin, D.J.1
  • 38
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: Structural, cellular, and molecular biology
    • Smith, W. L. , DeWitt, D. L. & Garavito, R. M. Cyclooxygenases: structural, cellular, and molecular biology. Annu. Rev. Biochem. 69, 145-182 (2000).
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 145-182
    • Smith, W.L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 39
    • 0035936004 scopus 로고    scopus 로고
    • Nonsteroidal antiinflammatory drugs and the risk of Alzheimers disease
    • in t Veld, B. A. et al. Nonsteroidal antiinflammatory drugs and the risk of Alzheimers disease. N. Engl. J. Med. 345, 1515-1521 (2001).
    • (2001) N. Engl. J. Med , vol.345 , pp. 1515-1521
    • In Tveld, B.A.1
  • 40
    • 84924975742 scopus 로고    scopus 로고
    • Assembly and interrogation of Alzheimers disease genetic networks reveal novel regulators of progression
    • Aubry, S. et al. Assembly and interrogation of Alzheimers disease genetic networks reveal novel regulators of progression. PLoS ONE 10, e0120352 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0120352
    • Aubry, S.1
  • 41
    • 84861222690 scopus 로고    scopus 로고
    • The ancient drug salicylate directly activates AMP-activated protein kinase
    • Hawley, S. A. et al. The ancient drug salicylate directly activates AMP-activated protein kinase. Science 336, 918-922 (2012).
    • (2012) Science , vol.336 , pp. 918-922
    • Hawley, S.A.1
  • 42
    • 81755174323 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses endothelial cell inflammation through phosphorylation of transcriptional coactivator p300
    • Zhang, Y. , Qiu, J. , Wang, X. , Zhang, Y. & Xia, M. AMP-activated protein kinase suppresses endothelial cell inflammation through phosphorylation of transcriptional coactivator p300. Arterioscler. Thromb. Vasc. Biol. 31, 2897-2908 (2011).
    • (2011) Arterioscler. Thromb. Vasc. Biol , vol.31 , pp. 2897-2908
    • Zhang, Y.1    Qiu, J.2    Wang, X.3    Zhang, Y.4    Xia, M.5
  • 43
    • 84155184239 scopus 로고    scopus 로고
    • AMP-activated protein kinase inhibits TGF-β-induced fibrogenic responses of hepatic stellate cells by targeting transcriptional coactivator p300
    • Lim, J. Y. , Oh, M. A. , Kim, W. H. , Sohn, H. Y. & Park, S. I. AMP-activated protein kinase inhibits TGF-β-induced fibrogenic responses of hepatic stellate cells by targeting transcriptional coactivator p300. J. Cell. Physiol. 227, 1081-1089 (2012).
    • (2012) J. Cell. Physiol , vol.227 , pp. 1081-1089
    • Lim, J.Y.1    Oh, M.A.2    Kim, W.H.3    Sohn, H.Y.4    Park, S.I.5
  • 44
    • 2942752412 scopus 로고    scopus 로고
    • Regulation of NF-κB action by reversible acetylation
    • discussion 218-225
    • Greene, W. C. & Chen, L. F. Regulation of NF-κB action by reversible acetylation. Novartis Found. Symp. 259, 208-217 discussion 218-225 (2004).
    • (2004) Novartis Found. Symp , vol.259 , pp. 208-217
    • Greene, W.C.1    Chen, L.F.2
  • 45
    • 4644353149 scopus 로고    scopus 로고
    • Ethanol selectively modulates inflammatory activation signaling of brain microglia
    • Lee, H. et al. Ethanol selectively modulates inflammatory activation signaling of brain microglia. J. Neuroimmunol. 156, 88-95 (2004).
    • (2004) J. Neuroimmunol , vol.156 , pp. 88-95
    • Lee, H.1
  • 46
    • 33646418394 scopus 로고    scopus 로고
    • Conversion of mild cognitive impairment to Alzheimer disease predicted by hippocampal atrophy maps
    • Apostolova, L. G. et al. Conversion of mild cognitive impairment to Alzheimer disease predicted by hippocampal atrophy maps. Arch. Neurol. 63, 693-699 (2006).
    • (2006) Arch. Neurol , vol.63 , pp. 693-699
    • Apostolova, L.G.1
  • 47
    • 77958522371 scopus 로고    scopus 로고
    • Hippocampal CA1 apical neuropil atrophy in mild Alzheimer disease visualized with 7-T MRI
    • Kerchner, G. A. et al. Hippocampal CA1 apical neuropil atrophy in mild Alzheimer disease visualized with 7-T MRI. Neurology 75, 1381-1387 (2010).
    • (2010) Neurology , vol.75 , pp. 1381-1387
    • Kerchner, G.A.1
  • 48
    • 84875867608 scopus 로고    scopus 로고
    • Cerebral atrophy in mild cognitive impairment and Alzheimer disease: Rates and acceleration
    • Leung, K. K. et al. Cerebral atrophy in mild cognitive impairment and Alzheimer disease: rates and acceleration. Neurology 80, 648-654 (2013).
    • (2013) Neurology , vol.80 , pp. 648-654
    • Leung, K.K.1
  • 49
    • 40449086665 scopus 로고    scopus 로고
    • Dose translation from animal to human studies revisited
    • Reagan-Shaw, S. , Nihal, M. & Ahmad, N. Dose translation from animal to human studies revisited. FASEB J. 22, 659-661 (2008).
    • (2008) FASEB J , vol.22 , pp. 659-661
    • Reagan-Shaw, S.1    Nihal, M.2    Ahmad, N.3
  • 50
    • 84861178173 scopus 로고    scopus 로고
    • Platform-independent and label-free quantitation of proteomic data using MS1 extracted ion chromatograms in skyline: Application to protein acetylation and phosphorylation
    • Schilling, B. et al. Platform-independent and label-free quantitation of proteomic data using MS1 extracted ion chromatograms in skyline: application to protein acetylation and phosphorylation. Mol. Cell. Proteomics 11, 202-214 (2012).
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 202-214
    • Schilling, B.1
  • 51
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov, I. V. et al. The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 6, 1638-1655 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1
  • 52
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N. , Pappin, D. J. , Creasy, D. M. & Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 53
    • 20144372893 scopus 로고    scopus 로고
    • SIRT1 regulates HIV transcription via Tat deacetylation
    • Pagans, S. et al. SIRT1 regulates HIV transcription via Tat deacetylation. PLoS Biol. 3, e41 (2005).
    • (2005) PLoS Biol , vol.3 , pp. e41
    • Pagans, S.1
  • 54
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 Protects against microglia-dependent amyloid-β toxicity through inhibiting NF-κB signaling
    • Chen, J. et al. SIRT1 Protects against microglia-dependent amyloid-β toxicity through inhibiting NF-κB signaling. J. Biol. Chem. 280, 40364-40374 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 40364-40374
    • Chen, J.1
  • 55
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S. et al. Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39, 11714-11721 (2000).
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1
  • 56
    • 83455171054 scopus 로고    scopus 로고
    • Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation
    • Moore, C. L. et al. Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation. Biochemistry 50, 10876-10886 (2011).
    • (2011) Biochemistry , vol.50 , pp. 10876-10886
    • Moore, C.L.1
  • 57
    • 0002587798 scopus 로고
    • The Gompertz curve as a growth curve
    • Winsor, C. P. The Gompertz curve as a growth curve. Proc. Natl. Acad. Sci. USA 18, 1-8 (1932).
    • (1932) Proc. Natl. Acad. Sci. USA , vol.18 , pp. 1-8
    • Winsor, C.P.1
  • 58
    • 0036193799 scopus 로고    scopus 로고
    • Comparative analysis of an improved thioflavin-s stain, Gallyas silver stain, and immunohistochemistry for neurofibrillary tangle demonstration on the same sections
    • Sun, A. , Nguyen, X. V. & Bing, G. Comparative analysis of an improved thioflavin-s stain, Gallyas silver stain, and immunohistochemistry for neurofibrillary tangle demonstration on the same sections. J. Histochem. Cytochem. 50, 463-472 (2002).
    • (2002) J. Histochem. Cytochem , vol.50 , pp. 463-472
    • Sun, A.1    Nguyen, X.V.2    Bing, G.3
  • 59
    • 78751487447 scopus 로고    scopus 로고
    • Robust protective effects of a novel multimodal neuroprotectant oxopropanoyloxy benzoic acid (a salicylic acid/pyruvate ester) in the postischemic brain
    • Kim, S. W. et al. Robust protective effects of a novel multimodal neuroprotectant oxopropanoyloxy benzoic acid (a salicylic acid/pyruvate ester) in the postischemic brain. Mol. Pharmacol. 79, 220-228 (2011).
    • (2011) Mol. Pharmacol , vol.79 , pp. 220-228
    • Kim, S.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.