메뉴 건너뛰기




Volumn 25, Issue 22, 2016, Pages 4920-4938

A small molecule p75NTR ligand normalizes signalling and reduces Huntington's disease phenotypes in R6/2 and BACHD mice

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 3 METHYLPENTANOIC ACID(2 MORPHOLIN 4YL ETHYL)AMIDE; HUNTINGTIN; ISOLEUCINE; NEUROTROPHIN RECEPTOR P75; PHOSPHOPROTEIN DARPP 32; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; LIGAND; LM11A-31; MORPHOLINE DERIVATIVE; NERVE GROWTH FACTOR RECEPTOR; PROTEIN BINDING; TNFRSF16 PROTEIN, MOUSE;

EID: 85015790906     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddw316     Document Type: Article
Times cited : (48)

References (145)
  • 2
    • 33846225133 scopus 로고    scopus 로고
    • Huntington's disease
    • Walker, F.O. (2007) Huntington's disease. Lancet, 369, 218-228.
    • (2007) Lancet , vol.369 , pp. 218-228
    • Walker, F.O.1
  • 3
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Group, HsDCR. (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell, 72, 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 4
    • 34047130812 scopus 로고    scopus 로고
    • Role of brain-derived neurotrophic factor in Huntington's disease
    • Zuccato, C. and Cattaneo, E. (2007) Role of brain-derived neurotrophic factor in Huntington's disease. Prog. Neurobiol., 81, 294-330.
    • (2007) Prog. Neurobiol , vol.81 , pp. 294-330
    • Zuccato, C.1    Cattaneo, E.2
  • 5
    • 41749083721 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor over-expression in the forebrain ameliorates Huntington's disease phenotypes in mice
    • Gharami, K., Xie, Y., An, J.J., Tonegawa, S. and Xu, B. (2008) Brain-derived neurotrophic factor over-expression in the forebrain ameliorates Huntington's disease phenotypes in mice. J. Neurochem., 105, 369-379.
    • (2008) J. Neurochem , vol.105 , pp. 369-379
    • Gharami, K.1    Xie, Y.2    An, J.J.3    Tonegawa, S.4    Xu, B.5
  • 7
    • 0036344505 scopus 로고    scopus 로고
    • Neurotrophin signaling through the p75 neurotrophin receptor
    • Roux, P.P. and Barker, P.A. (2002) Neurotrophin signaling through the p75 neurotrophin receptor. Prog. Neurobiol., 67, 203-233.
    • (2002) Prog. Neurobiol , vol.67 , pp. 203-233
    • Roux, P.P.1    Barker, P.A.2
  • 9
    • 0346849774 scopus 로고    scopus 로고
    • The p75 neurotrophin receptor: multiple interactors and numerous functions
    • Gentry, J.J., Barker, P.A. and Carter, B.D. (2004) The p75 neurotrophin receptor: multiple interactors and numerous functions. Prog. Brain Res., 146, 25-39.
    • (2004) Prog. Brain Res , vol.146 , pp. 25-39
    • Gentry, J.J.1    Barker, P.A.2    Carter, B.D.3
  • 10
    • 84862775324 scopus 로고    scopus 로고
    • p75 neurotrophin receptor signaling in nervous system injury and degeneration: paradox and opportunity
    • Ibanez, C.F. and Simi, A. (2012) p75 neurotrophin receptor signaling in nervous system injury and degeneration: paradox and opportunity. Trends Neurosci., 35, 431-440.
    • (2012) Trends Neurosci , vol.35 , pp. 431-440
    • Ibanez, C.F.1    Simi, A.2
  • 11
    • 84940209789 scopus 로고    scopus 로고
    • Selective reduction of striatal mature BDNF without induction of proBDNF in the zQ175 mouse model of Huntington's disease
    • Ma, Q., Yang, J., Li, T., Milner, T.A. and Hempstead, B.L. (2015) Selective reduction of striatal mature BDNF without induction of proBDNF in the zQ175 mouse model of Huntington's disease. Neurobiol. Dis., 82, 466-477.
    • (2015) Neurobiol. Dis , vol.82 , pp. 466-477
    • Ma, Q.1    Yang, J.2    Li, T.3    Milner, T.A.4    Hempstead, B.L.5
  • 12
    • 84876932695 scopus 로고    scopus 로고
    • Imbalance of p75(NTR)/TrkB protein expression in Huntington's disease: implication for neuroprotective therapies
    • Brito, V., Puigdellivol, M., Giralt, A., Del Toro, D., Alberch, J. and Gines, S. (2013) Imbalance of p75(NTR)/TrkB protein expression in Huntington's disease: implication for neuroprotective therapies. Cell Death Dis., 4, e595.
    • (2013) Cell Death Dis , vol.4
    • Brito, V.1    Puigdellivol, M.2    Giralt, A.3    Del Toro, D.4    Alberch, J.5    Gines, S.6
  • 13
    • 84859269517 scopus 로고    scopus 로고
    • Cholinergic Degeneration and Alterations in the TrkA and p75NTR Balance as a Result of Pro-NGF Injection into Aged Rats
    • Fortress, A.M., Buhusi, M., Helke, K.L. and Granholm, A.C. (2011) Cholinergic Degeneration and Alterations in the TrkA and p75NTR Balance as a Result of Pro-NGF Injection into Aged Rats. J. Aging Res., 2011, 460543.
    • (2011) J. Aging Res , vol.2011
    • Fortress, A.M.1    Buhusi, M.2    Helke, K.L.3    Granholm, A.C.4
  • 14
    • 0000326996 scopus 로고    scopus 로고
    • Competitive signaling between TrkA and p75 nerve growth factor receptors determines cell survival
    • Yoon, S.O., Casaccia-Bonnefil, P., Carter, B. and Chao, M.V. (1998) Competitive signaling between TrkA and p75 nerve growth factor receptors determines cell survival. J. Neurosci., 18, 3273-3281.
    • (1998) J. Neurosci , vol.18 , pp. 3273-3281
    • Yoon, S.O.1    Casaccia-Bonnefil, P.2    Carter, B.3    Chao, M.V.4
  • 15
    • 84941913908 scopus 로고    scopus 로고
    • Fingolimod (FTY720) enhances hippocampal synaptic plasticity and memory in Huntington's disease by preventing p75NTR up-regulation and astrocyte-mediated inflammation
    • Miguez, A., Garcia-Diaz Barriga, G., Brito, V., Straccia, M., Giralt, A., Gines, S., Canals, J.M. and Alberch, J. (2015) Fingolimod (FTY720) enhances hippocampal synaptic plasticity and memory in Huntington's disease by preventing p75NTR up-regulation and astrocyte-mediated inflammation. Hum. Mol. Genet., 24, 4958-4970.
    • (2015) Hum. Mol. Genet , vol.24 , pp. 4958-4970
    • Miguez, A.1    Garcia-Diaz Barriga, G.2    Brito, V.3    Straccia, M.4    Giralt, A.5    Gines, S.6    Canals, J.M.7    Alberch, J.8
  • 16
    • 41149120252 scopus 로고    scopus 로고
    • Systematic assessment of BDNF and its receptor levels in human cortices affected by Huntington's disease
    • Zuccato, C., Marullo, M., Conforti, P., MacDonald, M.E., Tartari, M. and Cattaneo, E. (2008) Systematic assessment of BDNF and its receptor levels in human cortices affected by Huntington's disease. Brain Pathol., 18, 225-238.
    • (2008) Brain Pathol , vol.18 , pp. 225-238
    • Zuccato, C.1    Marullo, M.2    Conforti, P.3    MacDonald, M.E.4    Tartari, M.5    Cattaneo, E.6
  • 18
    • 84888242805 scopus 로고    scopus 로고
    • A small molecule TrkB ligand reduces motor impairment and neuropathology in R6/2 and BACHD mouse models of Huntington's disease
    • Simmons, D.A., Belichenko, N.P., Yang, T., Condon, C., Monbureau, M., Shamloo, M., Jing, D., Massa, S.M. and Longo, F.M. (2013) A small molecule TrkB ligand reduces motor impairment and neuropathology in R6/2 and BACHD mouse models of Huntington's disease. J. Neurosci., 33, 18712-18727.
    • (2013) J. Neurosci , vol.33 , pp. 18712-18727
    • Simmons, D.A.1    Belichenko, N.P.2    Yang, T.3    Condon, C.4    Monbureau, M.5    Shamloo, M.6    Jing, D.7    Massa, S.M.8    Longo, F.M.9
  • 20
    • 84907202379 scopus 로고    scopus 로고
    • Kinase signalling in Huntington's disease
    • Bowles, K.R. and Jones, L. (2014) Kinase signalling in Huntington's disease. J. Huntington's Dis., 3, 89-123.
    • (2014) J. Huntington's Dis , vol.3 , pp. 89-123
    • Bowles, K.R.1    Jones, L.2
  • 21
    • 42049104101 scopus 로고    scopus 로고
    • Small molecule modulation of p75 neurotrophin receptor functions
    • Longo, F.M. and Massa, S.M. (2008) Small molecule modulation of p75 neurotrophin receptor functions. CNS Neurol. Disord. Drug Targets, 7, 63-70.
    • (2008) CNS Neurol. Disord. Drug Targets , vol.7 , pp. 63-70
    • Longo, F.M.1    Massa, S.M.2
  • 22
    • 84879662907 scopus 로고    scopus 로고
    • Small-molecule modulation of neurotrophin receptors: a strategy for the treatment of neurological disease
    • Longo, F.M. and Massa, S.M. (2013) Small-molecule modulation of neurotrophin receptors: a strategy for the treatment of neurological disease. Nat. Rev. Drug Discov., 12, 507-525.
    • (2013) Nat. Rev. Drug Discov , vol.12 , pp. 507-525
    • Longo, F.M.1    Massa, S.M.2
  • 25
    • 84946887711 scopus 로고    scopus 로고
    • Novel p75 neurotrophin receptor ligand stabilizes neuronal calcium, preserves mitochondrial movement and protects against HIV associated neuropathogenesis
    • Meeker, R.B., Poulton, W., Clary, G., Schriver, M. and Longo, F.M. (2016) Novel p75 neurotrophin receptor ligand stabilizes neuronal calcium, preserves mitochondrial movement and protects against HIV associated neuropathogenesis. Exp. Neurol., 275 Pt 1, 182-198.
    • (2016) Exp. Neurol , vol.275 , pp. 182-198
    • Meeker, R.B.1    Poulton, W.2    Clary, G.3    Schriver, M.4    Longo, F.M.5
  • 27
    • 84866506398 scopus 로고    scopus 로고
    • Suppression of Immunodeficiency Virus-Associated Neural Damage by the p75 Neurotrophin Receptor Ligand, LM11A-31, in an In Vitro Feline Model
    • Meeker, R.B., Poulton, W., Feng, W.H., Hudson, L. and Longo, F.M. (2012) Suppression of Immunodeficiency Virus-Associated Neural Damage by the p75 Neurotrophin Receptor Ligand, LM11A-31, in an In Vitro Feline Model. J. Neuroimmune. Pharmacol., 7, 388-400.
    • (2012) J. Neuroimmune. Pharmacol , vol.7 , pp. 388-400
    • Meeker, R.B.1    Poulton, W.2    Feng, W.H.3    Hudson, L.4    Longo, F.M.5
  • 28
    • 46149090787 scopus 로고    scopus 로고
    • Anti-cancer drug induced neurotoxicity and identification of Rho pathway signaling modulators as potential neuroprotectants
    • James, S.E., Burden, H., Burgess, R., Xie, Y., Yang, T., Massa, S.M., Longo, F.M. and Lu, Q. (2008) Anti-cancer drug induced neurotoxicity and identification of Rho pathway signaling modulators as potential neuroprotectants. Neurotoxicology, 29, 605-612.
    • (2008) Neurotoxicology , vol.29 , pp. 605-612
    • James, S.E.1    Burden, H.2    Burgess, R.3    Xie, Y.4    Yang, T.5    Massa, S.M.6    Longo, F.M.7    Lu, Q.8
  • 29
    • 84908340185 scopus 로고    scopus 로고
    • Amelioration of cisplatin-induced experimental peripheral neuropathy by a small molecule targeting p75 NTR
    • Friesland, A., Weng, Z., Duenas, M., Massa, S.M., Longo, F.M. and Lu, Q. (2014) Amelioration of cisplatin-induced experimental peripheral neuropathy by a small molecule targeting p75 NTR. Neurotoxicology, 45, 81-90.
    • (2014) Neurotoxicology , vol.45 , pp. 81-90
    • Friesland, A.1    Weng, Z.2    Duenas, M.3    Massa, S.M.4    Longo, F.M.5    Lu, Q.6
  • 30
    • 84887930062 scopus 로고    scopus 로고
    • A small molecule p75(NTR) ligand protects neurogenesis after traumatic brain injury
    • Shi, J., Longo, F.M. and Massa, S.M. (2013) A small molecule p75(NTR) ligand protects neurogenesis after traumatic brain injury. Stem Cells, 31, 2561-2574.
    • (2013) Stem Cells , vol.31 , pp. 2561-2574
    • Shi, J.1    Longo, F.M.2    Massa, S.M.3
  • 31
    • 84872055368 scopus 로고    scopus 로고
    • Oral administration of a small molecule targeted to block proNGF binding to p75 promotes myelin sparing and functional recovery after spinal cord injury
    • Tep, C., Lim, T.H., Ko, P.O., Getahun, S., Ryu, J.C., Goettl, V.M., Massa, S.M., Basso, M., Longo, F.M. and Yoon, S.O. (2013) Oral administration of a small molecule targeted to block proNGF binding to p75 promotes myelin sparing and functional recovery after spinal cord injury. J. Neurosci., 33, 397-410.
    • (2013) J. Neurosci , vol.33 , pp. 397-410
    • Tep, C.1    Lim, T.H.2    Ko, P.O.3    Getahun, S.4    Ryu, J.C.5    Goettl, V.M.6    Massa, S.M.7    Basso, M.8    Longo, F.M.9    Yoon, S.O.10
  • 33
    • 84908006750 scopus 로고    scopus 로고
    • Small molecule p75NTR ligands reduce pathological phosphorylation and misfolding of tau, inflammatory changes, cholinergic degeneration, and cognitive deficits in AbetaPP(L/S) transgenic mice
    • Nguyen, T.V., Shen, L., Vander Griend, L., Quach, L.N., Belichenko, N.P., Saw, N., Yang, T., Shamloo, M., Wyss-Coray, T., Massa, S.M., et al. (2014) Small molecule p75NTR ligands reduce pathological phosphorylation and misfolding of tau, inflammatory changes, cholinergic degeneration, and cognitive deficits in AbetaPP(L/S) transgenic mice. J. Alzheimer's Dis., 42, 459-483.
    • (2014) J. Alzheimer's Dis , vol.42 , pp. 459-483
    • Nguyen, T.V.1    Shen, L.2    Vander Griend, L.3    Quach, L.N.4    Belichenko, N.P.5    Saw, N.6    Yang, T.7    Shamloo, M.8    Wyss-Coray, T.9    Massa, S.M.10
  • 34
    • 84928919042 scopus 로고    scopus 로고
    • A small molecule p75NTR ligand, LM11A-31, reverses cholinergic neurite dystrophy in Alzheimer's disease mouse models with midto late-stage disease progression
    • Simmons, D.A., Knowles, J.K., Belichenko, N.P., Banerjee, G., Finkle, C., Massa, S.M. and Longo, F.M. (2014) A small molecule p75NTR ligand, LM11A-31, reverses cholinergic neurite dystrophy in Alzheimer's disease mouse models with midto late-stage disease progression. PLoS One, 9, e102136.
    • (2014) PLoS One , vol.9
    • Simmons, D.A.1    Knowles, J.K.2    Belichenko, N.P.3    Banerjee, G.4    Finkle, C.5    Massa, S.M.6    Longo, F.M.7
  • 35
    • 0038045714 scopus 로고    scopus 로고
    • Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability
    • Kanning, K.C., Hudson, M., Amieux, P.S., Wiley, J.C., Bothwell, M. and Schecterson, L.C. (2003) Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability. J. Neurosci., 23, 5425-5436.
    • (2003) J. Neurosci , vol.23 , pp. 5425-5436
    • Kanning, K.C.1    Hudson, M.2    Amieux, P.S.3    Wiley, J.C.4    Bothwell, M.5    Schecterson, L.C.6
  • 36
    • 77954367715 scopus 로고    scopus 로고
    • The p75NTR intracellular domain generated by neurotrophininduced receptor cleavage potentiates Trk signaling
    • Ceni, C., Kommaddi, R.P., Thomas, R., Vereker, E., Liu, X., McPherson, P.S., Ritter, B. and Barker, P.A. (2010) The p75NTR intracellular domain generated by neurotrophininduced receptor cleavage potentiates Trk signaling. J. Cell Sci., 123, 2299-2307.
    • (2010) J. Cell Sci , vol.123 , pp. 2299-2307
    • Ceni, C.1    Kommaddi, R.P.2    Thomas, R.3    Vereker, E.4    Liu, X.5    McPherson, P.S.6    Ritter, B.7    Barker, P.A.8
  • 37
    • 79960455447 scopus 로고    scopus 로고
    • Proteolytic processing of the p75 neurotrophin receptor: A prerequisite for signalling?: Neuronal life, growth and death signalling are crucially regulated by intra-membrane proteolysis and trafficking of p75(NTR)
    • Skeldal, S., Matusica, D., Nykjaer, A. and Coulson, E.J. (2011) Proteolytic processing of the p75 neurotrophin receptor: A prerequisite for signalling?: Neuronal life, growth and death signalling are crucially regulated by intra-membrane proteolysis and trafficking of p75(NTR). Bioessays, 33, 614-625.
    • (2011) Bioessays , vol.33 , pp. 614-625
    • Skeldal, S.1    Matusica, D.2    Nykjaer, A.3    Coulson, E.J.4
  • 38
    • 84928555294 scopus 로고    scopus 로고
    • Neuron-type-specific signaling by the p75NTR death receptor is regulated by differential proteolytic cleavage
    • Vicario, A., Kisiswa, L., Tann, J.Y., Kelly, C.E. and Ibanez, C.F. (2015) Neuron-type-specific signaling by the p75NTR death receptor is regulated by differential proteolytic cleavage. J. Cell Sci., 128, 1507-1517.
    • (2015) J. Cell Sci , vol.128 , pp. 1507-1517
    • Vicario, A.1    Kisiswa, L.2    Tann, J.Y.3    Kelly, C.E.4    Ibanez, C.F.5
  • 39
    • 0035933783 scopus 로고    scopus 로고
    • The p75 neurotrophin receptor activates Akt (protein kinase B) through a phosphatidylinositol 3-kinase-dependent pathway
    • Roux, P.P., Bhakar, A.L., Kennedy, T.E. and Barker, P.A. (2001) The p75 neurotrophin receptor activates Akt (protein kinase B) through a phosphatidylinositol 3-kinase-dependent pathway. J. Biol. Chem., 276, 23097-23104.
    • (2001) J. Biol. Chem , vol.276 , pp. 23097-23104
    • Roux, P.P.1    Bhakar, A.L.2    Kennedy, T.E.3    Barker, P.A.4
  • 41
    • 84856579300 scopus 로고    scopus 로고
    • P38 MAPK is involved in enhanced NMDA receptor-dependent excitotoxicity in YAC transgenic mouse model of Huntington disease
    • Fan, J., Gladding, C.M., Wang, L., Zhang, L.Y., Kaufman, A.M., Milnerwood, A.J. and Raymond, L.A. (2012) P38 MAPK is involved in enhanced NMDA receptor-dependent excitotoxicity in YAC transgenic mouse model of Huntington disease. Neurobiol. Dis., 45, 999-1009.
    • (2012) Neurobiol. Dis , vol.45 , pp. 999-1009
    • Fan, J.1    Gladding, C.M.2    Wang, L.3    Zhang, L.Y.4    Kaufman, A.M.5    Milnerwood, A.J.6    Raymond, L.A.7
  • 42
    • 4444380899 scopus 로고    scopus 로고
    • Adenosine and glutamate extracellular concentrations and mitogen-activated protein kinases in the striatum of Huntington transgenic mice. Selective antagonism of adenosine A2A receptors reduces transmitter outflow
    • Gianfriddo, M., Melani, A., Turchi, D., Giovannini, M.G. and Pedata, F. (2004) Adenosine and glutamate extracellular concentrations and mitogen-activated protein kinases in the striatum of Huntington transgenic mice. Selective antagonism of adenosine A2A receptors reduces transmitter outflow. Neurobiol. Dis., 17, 77-88.
    • (2004) Neurobiol. Dis , vol.17 , pp. 77-88
    • Gianfriddo, M.1    Melani, A.2    Turchi, D.3    Giovannini, M.G.4    Pedata, F.5
  • 44
    • 33646010041 scopus 로고    scopus 로고
    • Roles for NF-kappaB in nerve cell survival, plasticity, and disease
    • Mattson, M.P. and Meffert, M.K. (2006) Roles for NF-kappaB in nerve cell survival, plasticity, and disease. Cell Death Differ., 13, 852-860.
    • (2006) Cell Death Differ , vol.13 , pp. 852-860
    • Mattson, M.P.1    Meffert, M.K.2
  • 45
    • 4644307407 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex and nuclear factor-kappaB contributes to mutant huntingtin neurotoxicity
    • Khoshnan, A., Ko, J., Watkin, E.E., Paige, L.A., Reinhart, P.H. and Patterson, P.H. (2004) Activation of the IkappaB kinase complex and nuclear factor-kappaB contributes to mutant huntingtin neurotoxicity. J. Neurosci., 24, 7999-8008.
    • (2004) J. Neurosci , vol.24 , pp. 7999-8008
    • Khoshnan, A.1    Ko, J.2    Watkin, E.E.3    Paige, L.A.4    Reinhart, P.H.5    Patterson, P.H.6
  • 47
    • 84856641109 scopus 로고    scopus 로고
    • NF-kappaB, the first quarter-century: remarkable progress and outstanding questions
    • Hayden, M.S. and Ghosh, S. (2012) NF-kappaB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev., 26, 203-234.
    • (2012) Genes Dev , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 48
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation
    • Huxford, T., Huang, D.B., Malek, S. and Ghosh, G. (1998) The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. Cell, 95, 759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 49
    • 79958191139 scopus 로고    scopus 로고
    • The role of IkappaB kinase complex in the neurobiology of Huntington's disease
    • Khoshnan, A. and Patterson, P.H. (2011) The role of IkappaB kinase complex in the neurobiology of Huntington's disease. Neurobiol. Dis., 43, 305-311.
    • (2011) Neurobiol. Dis , vol.43 , pp. 305-311
    • Khoshnan, A.1    Patterson, P.H.2
  • 50
    • 0033230625 scopus 로고    scopus 로고
    • Neurotrophin binding to the p75 receptor modulates Rho activity and axonal outgrowth
    • Yamashita, T., Tucker, K.L. and Barde, Y.A. (1999) Neurotrophin binding to the p75 receptor modulates Rho activity and axonal outgrowth. Neuron, 24, 585-593.
    • (1999) Neuron , vol.24 , pp. 585-593
    • Yamashita, T.1    Tucker, K.L.2    Barde, Y.A.3
  • 51
    • 0037408391 scopus 로고    scopus 로고
    • The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI
    • Yamashita, T. and Tohyama, M. (2003) The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI. Nat. Neurosci., 6, 461-467.
    • (2003) Nat. Neurosci , vol.6 , pp. 461-467
    • Yamashita, T.1    Tohyama, M.2
  • 53
    • 70350348368 scopus 로고    scopus 로고
    • Y-27632 improves rotarod performance and reduces huntingtin levels in R6/2 mice
    • Li, M., Huang, Y., Ma, A.A., Lin, E. and Diamond, M.I. (2009) Y-27632 improves rotarod performance and reduces huntingtin levels in R6/2 mice. Neurobiol. Dis., 36, 413-420.
    • (2009) Neurobiol. Dis , vol.36 , pp. 413-420
    • Li, M.1    Huang, Y.2    Ma, A.A.3    Lin, E.4    Diamond, M.I.5
  • 54
    • 84928710726 scopus 로고    scopus 로고
    • Rho Kinase Pathway Alterations in the Brain and Leukocytes in Huntington's Disease
    • Narayanan, K.L., Chopra, V., Rosas, H.D., Malarick, K. and Hersch, S. (2015) Rho Kinase Pathway Alterations in the Brain and Leukocytes in Huntington's Disease. Mol. Neurobiol., 53, 2132-2140.
    • (2015) Mol. Neurobiol , vol.53 , pp. 2132-2140
    • Narayanan, K.L.1    Chopra, V.2    Rosas, H.D.3    Malarick, K.4    Hersch, S.5
  • 55
    • 78449258688 scopus 로고    scopus 로고
    • ProNGF induces PTEN via p75NTR to suppress Trk-mediated survival signaling in brain neurons
    • Song, W., Volosin, M., Cragnolini, A.B., Hempstead, B.L. and Friedman, W.J. (2010) ProNGF induces PTEN via p75NTR to suppress Trk-mediated survival signaling in brain neurons. J. Neurosci., 30, 15608-15615.
    • (2010) J. Neurosci , vol.30 , pp. 15608-15615
    • Song, W.1    Volosin, M.2    Cragnolini, A.B.3    Hempstead, B.L.4    Friedman, W.J.5
  • 56
    • 84862777981 scopus 로고    scopus 로고
    • The RhoA-ROCK-PTEN pathway as a molecular switch for anchorage dependent cell behavior
    • Yang, S. and Kim, H.M. (2012) The RhoA-ROCK-PTEN pathway as a molecular switch for anchorage dependent cell behavior. Biomaterials, 33, 2902-2915.
    • (2012) Biomaterials , vol.33 , pp. 2902-2915
    • Yang, S.1    Kim, H.M.2
  • 58
    • 67650490390 scopus 로고    scopus 로고
    • Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation
    • Rex, C.S., Chen, L.Y., Sharma, A., Liu, J., Babayan, A.H., Gall, C.M. and Lynch, G. (2009) Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation. J. Cell Biol., 186, 85-97.
    • (2009) J. Cell Biol , vol.186 , pp. 85-97
    • Rex, C.S.1    Chen, L.Y.2    Sharma, A.3    Liu, J.4    Babayan, A.H.5    Gall, C.M.6    Lynch, G.7
  • 60
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K., Davies, S., Bates, G., Vonsattel, J. and Aronin, N. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science, 277, 1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.3    Davies, S.4    Bates, G.5    Vonsattel, J.6    Aronin, N.7
  • 61
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • Zuccato, C., Valenza, M. and Cattaneo, E. (2010) Molecular mechanisms and potential therapeutical targets in Huntington's disease. Physiol.Rev., 90, 905-981.
    • (2010) Physiol.Rev , vol.90 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3
  • 62
    • 84884537922 scopus 로고    scopus 로고
    • Choosing an animal model for the study of Huntington's disease
    • Pouladi, M.A., Morton, A.J. and Hayden, M.R. (2013) Choosing an animal model for the study of Huntington's disease. Nat. Rev. Neurosci., 14, 708-721.
    • (2013) Nat. Rev. Neurosci , vol.14 , pp. 708-721
    • Pouladi, M.A.1    Morton, A.J.2    Hayden, M.R.3
  • 63
    • 46749157501 scopus 로고    scopus 로고
    • Full-length human mutant huntingtin with a stable polyglutamine repeat can elicit progressive and selective neuropathogenesis in BACHD mice
    • Gray, M., Shirasaki, D.I., Cepeda, C., Andre, V.M., Wilburn, B., Lu, X.H., Tao, J., Yamazaki, I., Li, S.H., Sun, Y.E., et al. (2008) Full-length human mutant huntingtin with a stable polyglutamine repeat can elicit progressive and selective neuropathogenesis in BACHD mice. J. Neurosci., 28, 6182-6195.
    • (2008) J. Neurosci , vol.28 , pp. 6182-6195
    • Gray, M.1    Shirasaki, D.I.2    Cepeda, C.3    Andre, V.M.4    Wilburn, B.5    Lu, X.H.6    Tao, J.7    Yamazaki, I.8    Li, S.H.9    Sun, Y.E.10
  • 64
    • 84860483495 scopus 로고    scopus 로고
    • Marked differences in neurochemistry and aggregates despite similar behavioural and neuropathological features of Huntington disease in the full-length BACHD and YAC128 mice
    • Pouladi, M.A., Stanek, L.M., Xie, Y., Franciosi, S., Southwell, A.L., Deng, Y., Butland, S., Zhang, W., Cheng, S.H., Shihabuddin, L.S., et al. (2012) Marked differences in neurochemistry and aggregates despite similar behavioural and neuropathological features of Huntington disease in the full-length BACHD and YAC128 mice. Hum. Mol.Genet., 21, 2219-2232.
    • (2012) Hum. Mol.Genet , vol.21 , pp. 2219-2232
    • Pouladi, M.A.1    Stanek, L.M.2    Xie, Y.3    Franciosi, S.4    Southwell, A.L.5    Deng, Y.6    Butland, S.7    Zhang, W.8    Cheng, S.H.9    Shihabuddin, L.S.10
  • 66
    • 34147135990 scopus 로고    scopus 로고
    • AKT and CDK5/p35 mediate brain-derived neurotrophic factor induction of DARPP-32 in medium size spiny neurons in vitro
    • Bogush, A., Pedrini, S., Pelta-Heller, J., Chan, T., Yang, Q., Mao, Z., Sluzas, E., Gieringer, T. and Ehrlich, M.E. (2007) AKT and CDK5/p35 mediate brain-derived neurotrophic factor induction of DARPP-32 in medium size spiny neurons in vitro. J. Biol. Chem., 282, 7352-7359.
    • (2007) J. Biol. Chem , vol.282 , pp. 7352-7359
    • Bogush, A.1    Pedrini, S.2    Pelta-Heller, J.3    Chan, T.4    Yang, Q.5    Mao, Z.6    Sluzas, E.7    Gieringer, T.8    Ehrlich, M.E.9
  • 70
    • 0023227209 scopus 로고
    • Sparing of acetylcholinesterasecontaining striatal neurons in Huntington's disease
    • Ferrante, R.J., Beal, M.F., Kowall, N.W., Richardson, E.P., Jr. and Martin, J.B. (1987) Sparing of acetylcholinesterasecontaining striatal neurons in Huntington's disease. Brain Res., 411, 162-166.
    • (1987) Brain Res , vol.411 , pp. 162-166
    • Ferrante, R.J.1    Beal, M.F.2    Kowall, N.W.3    Richardson, E.P.4    Martin, J.B.5
  • 71
    • 0033736901 scopus 로고    scopus 로고
    • Chemical anatomy of striatal interneurons in normal individuals and in patients with Huntington's disease
    • Cicchetti, F., Prensa, L., Wu, Y. and Parent, A. (2000) Chemical anatomy of striatal interneurons in normal individuals and in patients with Huntington's disease. Brain Res. Brain Res. Rev., 34, 80-101.
    • (2000) Brain Res. Brain Res. Rev , vol.34 , pp. 80-101
    • Cicchetti, F.1    Prensa, L.2    Wu, Y.3    Parent, A.4
  • 72
    • 85046766689 scopus 로고    scopus 로고
    • Enhanced GABAergic Inputs Contribute to Functional Alterations of Cholinergic Interneurons in the R6/2 Mouse Model of Huntington's Disease
    • Holley, S.M., Joshi, P.R., Parievsky, A., Galvan, L., Chen, J.Y., Fisher, Y.E., Huynh, M.N., Cepeda, C. and Levine, M.S. (2015) Enhanced GABAergic Inputs Contribute to Functional Alterations of Cholinergic Interneurons in the R6/2 Mouse Model of Huntington's Disease. eNeuro, 2, pii: e0008.
    • (2015) eNeuro , vol.2
    • Holley, S.M.1    Joshi, P.R.2    Parievsky, A.3    Galvan, L.4    Chen, J.Y.5    Fisher, Y.E.6    Huynh, M.N.7    Cepeda, C.8    Levine, M.S.9
  • 73
    • 84973483653 scopus 로고    scopus 로고
    • Cholinergic interneurons in the Q140 knock-in mouse model of Huntington's disease: Reductions in dendritic branching and thalamostriatal input
    • Deng, Y.P. and Reiner, A. (2016) Cholinergic interneurons in the Q140 knock-in mouse model of Huntington's disease: Reductions in dendritic branching and thalamostriatal input. J Comp. Neurol., Epub ahead of print. doi: 10.1002/cne.24013.
    • (2016) J Comp. Neurol., Epub ahead of print
    • Deng, Y.P.1    Reiner, A.2
  • 74
    • 0037194221 scopus 로고    scopus 로고
    • Cellular localization and development of neuronal intranuclear inclusions in striatal and cortical neurons in R6/2 transgenic mice
    • Meade, C., Deng, Y., Fusco, F., Del Mar, N., Hersch, S., Goldowitz, D. and Reiner, A. (2002) Cellular localization and development of neuronal intranuclear inclusions in striatal and cortical neurons in R6/2 transgenic mice. J. Comp. Neurol., 449, 241-269.
    • (2002) J. Comp. Neurol , vol.449 , pp. 241-269
    • Meade, C.1    Deng, Y.2    Fusco, F.3    Del Mar, N.4    Hersch, S.5    Goldowitz, D.6    Reiner, A.7
  • 75
    • 0033576775 scopus 로고    scopus 로고
    • Intranuclear inclusions in subtypes of striatal neurons in Huntington's disease transgenic mice
    • Kosinski, C.M., Cha, J.H., Young, A.B., Mangiarini, L., Bates, G., Schiefer, J. and Schwarz, M. (1999) Intranuclear inclusions in subtypes of striatal neurons in Huntington's disease transgenic mice. Neuroreport, 10, 3891-3896.
    • (1999) Neuroreport , vol.10 , pp. 3891-3896
    • Kosinski, C.M.1    Cha, J.H.2    Young, A.B.3    Mangiarini, L.4    Bates, G.5    Schiefer, J.6    Schwarz, M.7
  • 76
    • 80054976927 scopus 로고    scopus 로고
    • Reduced striatal acetylcholine efflux in the R6/2 mouse model of Huntington's disease: an examination of the role of altered inhibitory and excitatory mechanisms
    • Farrar, A.M., Callahan, J.W. and Abercrombie, E.D. (2011) Reduced striatal acetylcholine efflux in the R6/2 mouse model of Huntington's disease: an examination of the role of altered inhibitory and excitatory mechanisms. Exp. Neurol., 232, 119-125.
    • (2011) Exp. Neurol , vol.232 , pp. 119-125
    • Farrar, A.M.1    Callahan, J.W.2    Abercrombie, E.D.3
  • 78
    • 0037911453 scopus 로고    scopus 로고
    • Mice transgenic for exon 1 of Huntington's disease: properties of cholinergic and dopaminergic pre-synaptic function in the striatum
    • Vetter, J.M., Jehle, T., Heinemeyer, J., Franz, P., Behrens, P.F., Jackisch, R., Landwehrmeyer, G.B. and Feuerstein, T.J. (2003) Mice transgenic for exon 1 of Huntington's disease: properties of cholinergic and dopaminergic pre-synaptic function in the striatum. J. Neurochem., 85, 1054-1063.
    • (2003) J. Neurochem , vol.85 , pp. 1054-1063
    • Vetter, J.M.1    Jehle, T.2    Heinemeyer, J.3    Franz, P.4    Behrens, P.F.5    Jackisch, R.6    Landwehrmeyer, G.B.7    Feuerstein, T.J.8
  • 80
    • 80052545388 scopus 로고    scopus 로고
    • Pathogenic mechanisms in Huntington's disease
    • Jones, L. and Hughes, A. (2011) Pathogenic mechanisms in Huntington's disease. Int. Rev. Neurobiol., 98, 373-418.
    • (2011) Int. Rev. Neurobiol , vol.98 , pp. 373-418
    • Jones, L.1    Hughes, A.2
  • 81
    • 84898678139 scopus 로고    scopus 로고
    • Extrasynaptic NMDA receptor involvement in central nervous system disorders
    • Parsons, M.P. and Raymond, L.A. (2014) Extrasynaptic NMDA receptor involvement in central nervous system disorders. Neuron, 82, 279-293.
    • (2014) Neuron , vol.82 , pp. 279-293
    • Parsons, M.P.1    Raymond, L.A.2
  • 82
    • 0030601207 scopus 로고    scopus 로고
    • A novel gene iba1 in the major histocompatibility complex class III region encoding an EF hand protein expressed in a monocytic lineage
    • Imai, Y., Ibata, I., Ito, D., Ohsawa, K. and Kohsaka, S. (1996) A novel gene iba1 in the major histocompatibility complex class III region encoding an EF hand protein expressed in a monocytic lineage. Biochem. Biophys. Res. Commun., 224, 855-862.
    • (1996) Biochem. Biophys. Res. Commun , vol.224 , pp. 855-862
    • Imai, Y.1    Ibata, I.2    Ito, D.3    Ohsawa, K.4    Kohsaka, S.5
  • 84
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A., Paterson, H., Johnston, C., Diekmann, D. and Hall, A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell, 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.1    Paterson, H.2    Johnston, C.3    Diekmann, D.4    Hall, A.5
  • 85
    • 34447520021 scopus 로고    scopus 로고
    • Ferritin accumulation in dystrophic microglia is an early event in the development of Huntington's disease
    • Simmons, D.A., Casale, M., Alcon, B., Pham, N., Narayan, N. and Lynch, G. (2007) Ferritin accumulation in dystrophic microglia is an early event in the development of Huntington's disease. Glia, 55, 1074-1084.
    • (2007) Glia , vol.55 , pp. 1074-1084
    • Simmons, D.A.1    Casale, M.2    Alcon, B.3    Pham, N.4    Narayan, N.5    Lynch, G.6
  • 87
    • 81955167911 scopus 로고    scopus 로고
    • Agedependent neurovascular abnormalities and altered microglial morphology in the YAC128 mouse model of Huntington disease
    • Franciosi, S., Ryu, J.K., Shim, Y., Hill, A., Connolly, C., Hayden, M.R., McLarnon, J.G. and Leavitt, B.R. (2012) Agedependent neurovascular abnormalities and altered microglial morphology in the YAC128 mouse model of Huntington disease. Neurobiol. Dis., 45, 438-449.
    • (2012) Neurobiol. Dis , vol.45 , pp. 438-449
    • Franciosi, S.1    Ryu, J.K.2    Shim, Y.3    Hill, A.4    Connolly, C.5    Hayden, M.R.6    McLarnon, J.G.7    Leavitt, B.R.8
  • 88
    • 84991392281 scopus 로고    scopus 로고
    • Motor deficits associated with Huntington's disease occur in the absence of striatal degeneration in BACHD transgenic mice
    • Mantovani, S., Gordon, R., Li, R., Christie, D.C., Kumar, V. and Woodruff, T.M. (2016) Motor deficits associated with Huntington's disease occur in the absence of striatal degeneration in BACHD transgenic mice. Hum. Mol. Genet., 25, 1780-1791.
    • (2016) Hum. Mol. Genet , vol.25 , pp. 1780-1791
    • Mantovani, S.1    Gordon, R.2    Li, R.3    Christie, D.C.4    Kumar, V.5    Woodruff, T.M.6
  • 89
    • 84930822255 scopus 로고    scopus 로고
    • The choreography of neuroinflammation in Huntington's disease
    • Crotti, A. and Glass, C.K. (2015) The choreography of neuroinflammation in Huntington's disease. Trends Immunol., 36, 364-373.
    • (2015) Trends Immunol , vol.36 , pp. 364-373
    • Crotti, A.1    Glass, C.K.2
  • 90
    • 0026320986 scopus 로고
    • Proliferative and degenerative changes in striatal spiny neurons in Huntington's disease: a combined study using the section-Golgi method and calbindin D28k immunocytochemistry
    • Ferrante, R.J., Kowall, N.W. and Richardson, E.P. Jr. (1991) Proliferative and degenerative changes in striatal spiny neurons in Huntington's disease: a combined study using the section-Golgi method and calbindin D28k immunocytochemistry. J. Neurosci., 11, 3877-3887.
    • (1991) J. Neurosci , vol.11 , pp. 3877-3887
    • Ferrante, R.J.1    Kowall, N.W.2    Richardson, E.P.3
  • 91
    • 0021982117 scopus 로고
    • Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease
    • Graveland, G., Williams, R. and DiFiglia, M. (1985) Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease. Science, 227, 770-773.
    • (1985) Science , vol.227 , pp. 770-773
    • Graveland, G.1    Williams, R.2    DiFiglia, M.3
  • 92
    • 84862864841 scopus 로고    scopus 로고
    • A deconvolution method to improve automated 3D-analysis of dendritic spines: application to a mouse model of Huntington's disease
    • Heck, N., Betuing, S., Vanhoutte, P. and Caboche, J. (2012) A deconvolution method to improve automated 3D-analysis of dendritic spines: application to a mouse model of Huntington's disease. Brain Struct. Funct., 217, 421-434.
    • (2012) Brain Struct. Funct , vol.217 , pp. 421-434
    • Heck, N.1    Betuing, S.2    Vanhoutte, P.3    Caboche, J.4
  • 93
    • 0035214922 scopus 로고    scopus 로고
    • Electrophysiological and morphological changes in striatal spiny neurons in R6/2 Huntington's disease transgenic mice
    • Klapstein, G.J., Fisher, R.S., Zanjani, H., Cepeda, C., Jokel, E.S., Chesselet, M.F. and Levine, M.S. (2001) Electrophysiological and morphological changes in striatal spiny neurons in R6/2 Huntington's disease transgenic mice. J. Neurophysiol., 86, 2667-2677.
    • (2001) J. Neurophysiol , vol.86 , pp. 2667-2677
    • Klapstein, G.J.1    Fisher, R.S.2    Zanjani, H.3    Cepeda, C.4    Jokel, E.S.5    Chesselet, M.F.6    Levine, M.S.7
  • 95
    • 0033611825 scopus 로고    scopus 로고
    • p75NTR immunoreactivity in the rat dentate gyrus is mostly within presynaptic profiles but is also found in some astrocytic and postsynaptic profiles
    • Dougherty, K.D. and Milner, T.A. (1999) p75NTR immunoreactivity in the rat dentate gyrus is mostly within presynaptic profiles but is also found in some astrocytic and postsynaptic profiles. J. Comp. Neurol., 407, 77-91.
    • (1999) J. Comp. Neurol , vol.407 , pp. 77-91
    • Dougherty, K.D.1    Milner, T.A.2
  • 97
    • 27344442733 scopus 로고    scopus 로고
    • The p75 neurotrophin receptor negatively modulates dendrite complexity and spine density in hippocampal neurons
    • Zagrebelsky, M., Holz, A., Dechant, G., Barde, Y.A., Bonhoeffer, T. and Korte, M. (2005) The p75 neurotrophin receptor negatively modulates dendrite complexity and spine density in hippocampal neurons. J. Neurosci., 25, 9989-9999.
    • (2005) J. Neurosci , vol.25 , pp. 9989-9999
    • Zagrebelsky, M.1    Holz, A.2    Dechant, G.3    Barde, Y.A.4    Bonhoeffer, T.5    Korte, M.6
  • 98
    • 0347626155 scopus 로고    scopus 로고
    • Exploratory activity and fear conditioning abnormalities develop early in R6/2 Huntington's disease transgenic mice
    • Bolivar, V.J., Manley, K. and Messer, A. (2003) Exploratory activity and fear conditioning abnormalities develop early in R6/2 Huntington's disease transgenic mice. Behav. Neurosci., 117, 1233-1242.
    • (2003) Behav. Neurosci , vol.117 , pp. 1233-1242
    • Bolivar, V.J.1    Manley, K.2    Messer, A.3
  • 99
    • 0033560924 scopus 로고    scopus 로고
    • Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation
    • Carter, R., Lione, L., Humby, T., Mangiarini, L., Mahal, A., Bates, G., Dunnett, S. and Morton, A. (1999) Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation. J. Neurosci., 19, 3248-3257.
    • (1999) J. Neurosci , vol.19 , pp. 3248-3257
    • Carter, R.1    Lione, L.2    Humby, T.3    Mangiarini, L.4    Mahal, A.5    Bates, G.6    Dunnett, S.7    Morton, A.8
  • 100
    • 24044442568 scopus 로고    scopus 로고
    • Early behavioral deficits in R6/2 mice suitable for use in preclinical drug testing
    • Hickey, M.A., Gallant, K., Gross, G.G., Levine, M.S. and Chesselet, M.F. (2005) Early behavioral deficits in R6/2 mice suitable for use in preclinical drug testing. Neurobiol. Dis., 20, 1-11.
    • (2005) Neurobiol. Dis , vol.20 , pp. 1-11
    • Hickey, M.A.1    Gallant, K.2    Gross, G.G.3    Levine, M.S.4    Chesselet, M.F.5
  • 102
    • 84929650469 scopus 로고    scopus 로고
    • Coexistence of Gait Disturbances and Chorea in Experimental Huntington's Disease
    • Casaca-Carreira, J., Temel, Y., van Zelst, M. and Jahanshahi, A. (2015) Coexistence of Gait Disturbances and Chorea in Experimental Huntington's Disease. Behav. Neurol., 2015, 970204.
    • (2015) Behav. Neurol , vol.2015
    • Casaca-Carreira, J.1    Temel, Y.2    van Zelst, M.3    Jahanshahi, A.4
  • 103
    • 84868704750 scopus 로고    scopus 로고
    • Motor, emotional and cognitive deficits in adult BACHD mice: A model for Huntington's disease
    • Abada, Y.S., Schreiber, R. and Ellenbroek, B. (2012) Motor, emotional and cognitive deficits in adult BACHD mice: A model for Huntington's disease. Behav. Brain Res., 238, 243-251.
    • (2012) Behav. Brain Res , vol.238 , pp. 243-251
    • Abada, Y.S.1    Schreiber, R.2    Ellenbroek, B.3
  • 105
    • 0021966828 scopus 로고
    • The gait abnormality of Huntington's disease
    • Koller, W.C. and Trimble, J. (1985) The gait abnormality of Huntington's disease. Neurology, 35, 1450-1454.
    • (1985) Neurology , vol.35 , pp. 1450-1454
    • Koller, W.C.1    Trimble, J.2
  • 106
    • 84949214803 scopus 로고    scopus 로고
    • Update on the role of p75NTR in neurological disorders: A novel therapeutic target
    • Shu, Y.H., Lu, X.M., Wei, J.X., Xiao, L. and Wang, Y.T. (2015) Update on the role of p75NTR in neurological disorders: A novel therapeutic target. Biomed. Pharmacother., 76, 17-23.
    • (2015) Biomed. Pharmacother , vol.76 , pp. 17-23
    • Shu, Y.H.1    Lu, X.M.2    Wei, J.X.3    Xiao, L.4    Wang, Y.T.5
  • 107
    • 0036830562 scopus 로고    scopus 로고
    • The neurotrophin receptor p75(NTR): novel functions and implications for diseases of the nervous system
    • Dechant, G. and Barde, Y.A. (2002) The neurotrophin receptor p75(NTR): novel functions and implications for diseases of the nervous system. Nat. Neurosci., 5, 1131-1136.
    • (2002) Nat. Neurosci , vol.5 , pp. 1131-1136
    • Dechant, G.1    Barde, Y.A.2
  • 108
    • 84930063595 scopus 로고    scopus 로고
    • The p75 neurotrophin receptor: at the crossroad of neural repair and death
    • Meeker, R.B. and Williams, K.S. (2015) The p75 neurotrophin receptor: at the crossroad of neural repair and death. Neural Regen. Res., 10, 721-725.
    • (2015) Neural Regen. Res , vol.10 , pp. 721-725
    • Meeker, R.B.1    Williams, K.S.2
  • 109
    • 13844271798 scopus 로고    scopus 로고
    • Nuclear translocation of the p75 neurotrophin receptor cytoplasmic domain in response to neurotrophin binding
    • Frade, J.M. (2005) Nuclear translocation of the p75 neurotrophin receptor cytoplasmic domain in response to neurotrophin binding. J. Neurosci., 25, 1407-1411.
    • (2005) J. Neurosci , vol.25 , pp. 1407-1411
    • Frade, J.M.1
  • 110
    • 0142242199 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor
    • Jung, K.M., Tan, S., Landman, N., Petrova, K., Murray, S., Lewis, R., Kim, P.K., Kim, D.S., Ryu, S.H., Chao, M.V., et al. (2003) Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor. J. Biol. Chem., 278, 42161-42169.
    • (2003) J. Biol. Chem , vol.278 , pp. 42161-42169
    • Jung, K.M.1    Tan, S.2    Landman, N.3    Petrova, K.4    Murray, S.5    Lewis, R.6    Kim, P.K.7    Kim, D.S.8    Ryu, S.H.9    Chao, M.V.10
  • 112
    • 20444455430 scopus 로고    scopus 로고
    • Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment
    • Rangone, H., Pardo, R., Colin, E., Girault, J.A., Saudou, F. and Humbert, S. (2005) Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment. J. Biol. Chem., 280, 22021-22028.
    • (2005) J. Biol. Chem , vol.280 , pp. 22021-22028
    • Rangone, H.1    Pardo, R.2    Colin, E.3    Girault, J.A.4    Saudou, F.5    Humbert, S.6
  • 113
    • 57049184027 scopus 로고    scopus 로고
    • Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons
    • Zala, D., Colin, E., Rangone, H., Liot, G., Humbert, S. and Saudou, F. (2008) Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons. Hum. Mol. Genet., 17, 3837-3846.
    • (2008) Hum. Mol. Genet , vol.17 , pp. 3837-3846
    • Zala, D.1    Colin, E.2    Rangone, H.3    Liot, G.4    Humbert, S.5    Saudou, F.6
  • 114
    • 84930651058 scopus 로고    scopus 로고
    • Chatting with the neighbors: crosstalk between Rho-kinase (ROCK) and other signaling pathways for treatment of neurological disorders
    • Hensel, N., Rademacher, S. and Claus, P. (2015) Chatting with the neighbors: crosstalk between Rho-kinase (ROCK) and other signaling pathways for treatment of neurological disorders. Front. Neurosci., 9, 198.
    • (2015) Front. Neurosci , vol.9 , pp. 198
    • Hensel, N.1    Rademacher, S.2    Claus, P.3
  • 115
    • 67650258745 scopus 로고    scopus 로고
    • Enhanced degradation of mutant huntingtin by rho kinase inhibition is mediated through activation of proteasome and macroautophagy
    • Bauer, P.O. and Nukina, N. (2009) Enhanced degradation of mutant huntingtin by rho kinase inhibition is mediated through activation of proteasome and macroautophagy. Autophagy, 5, 747-748.
    • (2009) Autophagy , vol.5 , pp. 747-748
    • Bauer, P.O.1    Nukina, N.2
  • 116
    • 50249147874 scopus 로고    scopus 로고
    • Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation
    • Shao, J., Welch, W.J., Diprospero, N.A. and Diamond, M.I. (2008) Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation. Mol. Cell. Cell. Biol., 28, 5196-5208.
    • (2008) Mol. Cell. Cell. Biol , vol.28 , pp. 5196-5208
    • Shao, J.1    Welch, W.J.2    Diprospero, N.A.3    Diamond, M.I.4
  • 118
    • 11844304062 scopus 로고    scopus 로고
    • The role of the Rho GTPases in neuronal development
    • Govek, E., Newey, S. and Van Aelst, L. (2005) The role of the Rho GTPases in neuronal development. Genes Dev., 19, 1-49.
    • (2005) Genes Dev , vol.19 , pp. 1-49
    • Govek, E.1    Newey, S.2    Van Aelst, L.3
  • 119
    • 0034661746 scopus 로고    scopus 로고
    • Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons
    • Nakayama, A.Y., Harms, M.B. and Luo, L. (2000) Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons. J. Neurosci., 20, 5329-5338.
    • (2000) J. Neurosci , vol.20 , pp. 5329-5338
    • Nakayama, A.Y.1    Harms, M.B.2    Luo, L.3
  • 120
    • 84906932529 scopus 로고    scopus 로고
    • NGF rescues hippocampal cholinergic neuronal markers, restores neurogenesis, and improves the spatial working memory in a mouse model of Huntington's Disease
    • Zhang, H., Petit, G.H., Gaughwin, P.M., Hansen, C., Ranganathan, S., Zuo, X., Smith, R., Roybon, L., Brundin, P., Mobley, W.C., et al. (2013) NGF rescues hippocampal cholinergic neuronal markers, restores neurogenesis, and improves the spatial working memory in a mouse model of Huntington's Disease. J. Huntington's Dis., 2, 69-82.
    • (2013) J. Huntington's Dis , vol.2 , pp. 69-82
    • Zhang, H.1    Petit, G.H.2    Gaughwin, P.M.3    Hansen, C.4    Ranganathan, S.5    Zuo, X.6    Smith, R.7    Roybon, L.8    Brundin, P.9    Mobley, W.C.10
  • 123
    • 0037418339 scopus 로고    scopus 로고
    • Dietary restriction normalizes glucose metabolism and BDNF levels, slows disease progression, and increases survival in huntingtin mutant mice
    • Duan, W., Guo, Z., Jiang, H., Ware, M., Li, X. and Mattson, M. (2003) Dietary restriction normalizes glucose metabolism and BDNF levels, slows disease progression, and increases survival in huntingtin mutant mice. Proc. Natl. Acad. Sci. U. S. A, 100, 2911-2916.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 2911-2916
    • Duan, W.1    Guo, Z.2    Jiang, H.3    Ware, M.4    Li, X.5    Mattson, M.6
  • 125
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto, A., Lucas, J.J. and Hen, R. (2000) Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell, 101, 57-66.
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 126
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch, G.M. (2003) Biology of the p21-activated kinases. Annu. Rev. Biochem., 72, 743-781.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 127
    • 84863782433 scopus 로고    scopus 로고
    • Deconstructing signal transduction pathways that regulate the actin cytoskeleton in dendritic spines
    • Penzes, P. and Cahill, M.E. (2012) Deconstructing signal transduction pathways that regulate the actin cytoskeleton in dendritic spines. Cytoskeleton, 69, 426-441.
    • (2012) Cytoskeleton , vol.69 , pp. 426-441
    • Penzes, P.1    Cahill, M.E.2
  • 128
    • 84858116752 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in dendritic spines
    • Penzes, P. and Rafalovich, I. (2012) Regulation of the actin cytoskeleton in dendritic spines. Adv. Exp. Med.Biol., 970, 81-95.
    • (2012) Adv. Exp. Med.Biol , vol.970 , pp. 81-95
    • Penzes, P.1    Rafalovich, I.2
  • 129
    • 79951849928 scopus 로고    scopus 로고
    • An APPL1/Akt signaling complex regulates dendritic spine and synapse formation in hippocampal neurons
    • Majumdar, D., Nebhan, C.A., Hu, L., Anderson, B. and Webb, D.J. (2011) An APPL1/Akt signaling complex regulates dendritic spine and synapse formation in hippocampal neurons. Mol. Cell. Neurosci., 46, 633-644.
    • (2011) Mol. Cell. Neurosci , vol.46 , pp. 633-644
    • Majumdar, D.1    Nebhan, C.A.2    Hu, L.3    Anderson, B.4    Webb, D.J.5
  • 130
    • 45549088610 scopus 로고    scopus 로고
    • Role of Rho GTPases in the morphogenesis and motility of dendritic spines
    • Tashiro, A. and Yuste, R. (2008) Role of Rho GTPases in the morphogenesis and motility of dendritic spines. Methods Enzymol., 439, 285-302.
    • (2008) Methods Enzymol , vol.439 , pp. 285-302
    • Tashiro, A.1    Yuste, R.2
  • 131
    • 84867135617 scopus 로고    scopus 로고
    • Dysfunctional behavioral modulation of corticostriatal communication in the R6/2 mouse model of Huntington's disease
    • Hong, S.L., Cossyleon, D., Hussain, W.A., Walker, L.J., Barton, S.J. and Rebec, G.V. (2012) Dysfunctional behavioral modulation of corticostriatal communication in the R6/2 mouse model of Huntington's disease. PLoS One, 7, e47026.
    • (2012) PLoS One , vol.7
    • Hong, S.L.1    Cossyleon, D.2    Hussain, W.A.3    Walker, L.J.4    Barton, S.J.5    Rebec, G.V.6
  • 132
    • 0028001566 scopus 로고
    • Effect of the nigrostriatal dopamine system on acquired neural responses in the striatum of behaving monkeys
    • Aosaki, T., Graybiel, A.M. and Kimura, M. (1994) Effect of the nigrostriatal dopamine system on acquired neural responses in the striatum of behaving monkeys. Science, 265, 412-415.
    • (1994) Science , vol.265 , pp. 412-415
    • Aosaki, T.1    Graybiel, A.M.2    Kimura, M.3
  • 133
    • 84887918899 scopus 로고    scopus 로고
    • Dopamine imbalance in Huntington's disease: a mechanism for the lack of behavioral flexibility
    • Chen, J.Y., Wang, E.A., Cepeda, C. and Levine, M.S. (2013) Dopamine imbalance in Huntington's disease: a mechanism for the lack of behavioral flexibility. Front. Neurosci., 7, 114.
    • (2013) Front. Neurosci , vol.7 , pp. 114
    • Chen, J.Y.1    Wang, E.A.2    Cepeda, C.3    Levine, M.S.4
  • 136
    • 52649182047 scopus 로고    scopus 로고
    • Spectrum of gait impairments in presymptomatic and symptomatic Huntington's disease
    • Rao, A.K., Muratori, L., Louis, E.D., Moskowitz, C.B. and Marder, K.S. (2008) Spectrum of gait impairments in presymptomatic and symptomatic Huntington's disease. Mov. Disord., 23, 1100-1107.
    • (2008) Mov. Disord , vol.23 , pp. 1100-1107
    • Rao, A.K.1    Muratori, L.2    Louis, E.D.3    Moskowitz, C.B.4    Marder, K.S.5
  • 140
    • 78650599933 scopus 로고    scopus 로고
    • Brief ampakine treatments slow the progression of Huntington's disease phenotypes in R6/2 mice
    • Simmons, D.A., Mehta, R.A., Lauterborn, J.C., Gall, C.M. and Lynch, G. (2011) Brief ampakine treatments slow the progression of Huntington's disease phenotypes in R6/2 mice. Neurobiol. Dis., 41, 436-444.
    • (2011) Neurobiol. Dis , vol.41 , pp. 436-444
    • Simmons, D.A.1    Mehta, R.A.2    Lauterborn, J.C.3    Gall, C.M.4    Lynch, G.5
  • 142
    • 67649635619 scopus 로고    scopus 로고
    • Detection of early behavioral markers of Huntington's disease in R6/2 mice employing an automated social home cage
    • Rudenko, O., Tkach, V., Berezin, V. and Bock, E. (2009) Detection of early behavioral markers of Huntington's disease in R6/2 mice employing an automated social home cage. Behav. Brain Res., 203, 188-199.
    • (2009) Behav. Brain Res , vol.203 , pp. 188-199
    • Rudenko, O.1    Tkach, V.2    Berezin, V.3    Bock, E.4
  • 144
    • 84859158535 scopus 로고    scopus 로고
    • Striatal atrophy and dendritic alterations in a knock-in mouse model of Huntington's disease
    • Lerner, R.P., Trejo Martinez Ldel, C., Zhu, C., Chesselet, M.F. and Hickey, M.A. (2012) Striatal atrophy and dendritic alterations in a knock-in mouse model of Huntington's disease. Brain Res. Bull., 87, 571-578.
    • (2012) Brain Res. Bull , vol.87 , pp. 571-578
    • Lerner, R.P.1    Trejo Martinez Ldel, C.2    Zhu, C.3    Chesselet, M.F.4    Hickey, M.A.5
  • 145
    • 43449117577 scopus 로고    scopus 로고
    • Balancing structure and function at hippocampal dendritic spines
    • Bourne, J.N. and Harris, K.M. (2008) Balancing structure and function at hippocampal dendritic spines. Annu. Rev. Neurosci., 31, 47-67.
    • (2008) Annu. Rev. Neurosci , vol.31 , pp. 47-67
    • Bourne, J.N.1    Harris, K.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.