메뉴 건너뛰기




Volumn 13, Issue 7, 2017, Pages

Elimination of huntingtin in the adult mouse leads to progressive behavioral deficits, bilateral thalamic calcification, and altered brain iron homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

HUNTINGTIN; IRON; RNA 18S;

EID: 85026661643     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1006846     Document Type: Article
Times cited : (72)

References (78)
  • 1
    • 33846225133 scopus 로고    scopus 로고
    • Huntington’s disease
    • 17240289
    • Walker FO, Huntington’s disease. Lancet. 2007;369(9557): 218–228. doi: 10.1016/S0140-6736(07)60111-1 17240289
    • (2007) Lancet , vol.369 , Issue.9557 , pp. 218-228
    • Walker, F.O.1
  • 2
    • 80052533413 scopus 로고    scopus 로고
    • Genetics and neuropathology of Huntington’s disease
    • 21907094
    • Reiner A, Dragatsis I, Dietrich P, Genetics and neuropathology of Huntington’s disease. Int Rev Neurobiol. 2011;98: 325–372. doi: 10.1016/B978-0-12-381328-2.00014-6 21907094
    • (2011) Int Rev Neurobiol , vol.98 , pp. 325-372
    • Reiner, A.1    Dragatsis, I.2    Dietrich, P.3
  • 3
    • 84907660103 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system involvement in Huntington’s disease
    • 25324717
    • Ortega Z, Lucas JJ, Ubiquitin-proteasome system involvement in Huntington’s disease. Front Mol Neurosci. 2014;7: 77. doi: 10.3389/fnmol.2014.00077 25324717
    • (2014) Front Mol Neurosci , vol.7 , pp. 77
    • Ortega, Z.1    Lucas, J.J.2
  • 4
    • 0034491812 scopus 로고    scopus 로고
    • Pathology of CAG repeat diseases
    • 11211058
    • Yamada M, Tsuji S, Takahashi H, Pathology of CAG repeat diseases. Neuropathology. 2000;20(4): 319–325. 11211058
    • (2000) Neuropathology , vol.20 , Issue.4 , pp. 319-325
    • Yamada, M.1    Tsuji, S.2    Takahashi, H.3
  • 6
    • 84941569159 scopus 로고    scopus 로고
    • Therapeutic advances in Huntington’s Disease
    • 26226924
    • Shannon KM, Fraint A, Therapeutic advances in Huntington’s Disease. Mov Disord. 2015;30(11): 1539–1546. doi: 10.1002/mds.26331 26226924
    • (2015) Mov Disord , vol.30 , Issue.11 , pp. 1539-1546
    • Shannon, K.M.1    Fraint, A.2
  • 7
    • 83255177161 scopus 로고    scopus 로고
    • Using non-coding small RNAs to develop therapies for Huntington’s disease
    • 22158031
    • Zhang Y, Friedlander RM, Using non-coding small RNAs to develop therapies for Huntington’s disease. Gene Ther. 2011;18(12): 1139–1149. doi: 10.1038/gt.2011.170 22158031
    • (2011) Gene Ther , vol.18 , Issue.12 , pp. 1139-1149
    • Zhang, Y.1    Friedlander, R.M.2
  • 8
    • 84907924586 scopus 로고    scopus 로고
    • Targets for future clinical trials in Huntington’s disease: what’s in the pipeline?
    • 25155142
    • Wild EJ, Tabrizi SJ, Targets for future clinical trials in Huntington’s disease: what’s in the pipeline?Mov Disord. 2014;29(11): 1434–1445. doi: 10.1002/mds.26007 25155142
    • (2014) Mov Disord , vol.29 , Issue.11 , pp. 1434-1445
    • Wild, E.J.1    Tabrizi, S.J.2
  • 9
    • 65249131740 scopus 로고    scopus 로고
    • Sustained effects of nonallele-specific Huntingtin silencing
    • 19334076
    • Drouet V, Perrin V, Hassig R, Dufour N, Auregan G, Alves S, et al. Sustained effects of nonallele-specific Huntingtin silencing. Ann Neurol. 2009;65(3): 276–285. doi: 10.1002/ana.21569 19334076
    • (2009) Ann Neurol , vol.65 , Issue.3 , pp. 276-285
    • Drouet, V.1    Perrin, V.2    Hassig, R.3    Dufour, N.4    Auregan, G.5    Alves, S.6
  • 10
    • 67349100160 scopus 로고    scopus 로고
    • Nonallele-specific silencing of mutant and wild-type huntingtin demonstrates therapeutic efficacy in Huntington’s disease mice
    • 19240687
    • Boudreau RL, McBride JL, Martins I, Shen S, Xing Y, Carter BJ, et al. Nonallele-specific silencing of mutant and wild-type huntingtin demonstrates therapeutic efficacy in Huntington’s disease mice. Mol Ther. 2009; 17(6): 1053–1063. doi: 10.1038/mt.2009.17 19240687
    • (2009) Mol Ther , vol.17 , Issue.6 , pp. 1053-1063
    • Boudreau, R.L.1    McBride, J.L.2    Martins, I.3    Shen, S.4    Xing, Y.5    Carter, B.J.6
  • 11
    • 82955199935 scopus 로고    scopus 로고
    • Preclinical safety of RNAi-mediated HTT suppression in the rhesus macaque as a potential therapy for Huntington’s disease
    • 22031240
    • McBride JL, Pitzer MR, Boudreau RL, Dufour B, Hobbs T, Ojeda SR, et al. Preclinical safety of RNAi-mediated HTT suppression in the rhesus macaque as a potential therapy for Huntington’s disease. Mol Ther. 2011;19(12): 2152–2162. doi: 10.1038/mt.2011.219 22031240
    • (2011) Mol Ther , vol.19 , Issue.12 , pp. 2152-2162
    • McBride, J.L.1    Pitzer, M.R.2    Boudreau, R.L.3    Dufour, B.4    Hobbs, T.5    Ojeda, S.R.6
  • 12
    • 84860192454 scopus 로고    scopus 로고
    • Six-month partial suppression of Huntingtin is well tolerated in the adult rhesus striatum
    • Grondin R, Kaytor MD, Ai Y, Nelson PT, Thakker DR, Heisel J, et al. Six-month partial suppression of Huntingtin is well tolerated in the adult rhesus striatum. Brain. 2012;135(Pt4): 1197–1209.
    • (2012) Brain , vol.135 , Issue.Pt4 , pp. 1197-1209
    • Grondin, R.1    Kaytor, M.D.2    Ai, Y.3    Nelson, P.T.4    Thakker, D.R.5    Heisel, J.6
  • 13
    • 0035282594 scopus 로고    scopus 로고
    • Loss of normal huntingtin function: new developments in Huntington’s disease research
    • 11182459
    • Cattaneo E, Rigamonti D, Goffredo D, Zuccato C, Squitieri F, Sipione S, Loss of normal huntingtin function: new developments in Huntington’s disease research. Trends Neurosci. 2001;24(3): 182–188. 11182459
    • (2001) Trends Neurosci , vol.24 , Issue.3 , pp. 182-188
    • Cattaneo, E.1    Rigamonti, D.2    Goffredo, D.3    Zuccato, C.4    Squitieri, F.5    Sipione, S.6
  • 14
    • 84943264955 scopus 로고    scopus 로고
    • . In:,.:;. pp. –. San Diego Elsevier Academic Press
    • Dietrich P, Dragatsis I, LeDoux M, Use of Genetically engineered mice to study the biology of huntingtin. In: Movement Disorders: Genetics and Models, 2nd ed. San Diego: Elsevier Academic Press; 2015. pp. 547–555.
    • (2015) Movement Disorders: Genetics and Models , pp. 547-555
    • Dietrich, P.1    Dragatsis, I.2    LeDoux, M.3
  • 15
    • 84960441124 scopus 로고    scopus 로고
    • The Biology of Huntingtin
    • 26938440
    • Saudou F, Humbert S, The Biology of Huntingtin. Neuron. 2016;89(5): 910–926. doi: 10.1016/j.neuron.2016.02.003 26938440
    • (2016) Neuron , vol.89 , Issue.5 , pp. 910-926
    • Saudou, F.1    Humbert, S.2
  • 16
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • 11062468
    • Dragatsis I, Levine MS, Zeitlin S, Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat Genet. 2000;26(3): 300–306. doi: 10.1038/81593 11062468
    • (2000) Nat Genet , vol.26 , Issue.3 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 17
    • 85009060712 scopus 로고    scopus 로고
    • Huntingtin-mediated multipolar-bipolar transition of newborn cortical neurons is critical for their postnatal neuronal morphology
    • 28017473
    • Barnat M, Le Friec J, Benstaali C, Humbert S, Huntingtin-mediated multipolar-bipolar transition of newborn cortical neurons is critical for their postnatal neuronal morphology. Neuron. 2017; 93(1): 99–114. doi: 10.1016/j.neuron.2016.11.035 28017473
    • (2017) Neuron , vol.93 , Issue.1 , pp. 99-114
    • Barnat, M.1    Le Friec, J.2    Benstaali, C.3    Humbert, S.4
  • 18
    • 0037090881 scopus 로고    scopus 로고
    • Efficient recombination in diverse tissues by a tamoxifen-inducible form of Cre: a tool for temporally regulated gene activation/inactivation in the mouse
    • 11944939
    • Hayashi S, McMahon AP, Efficient recombination in diverse tissues by a tamoxifen-inducible form of Cre: a tool for temporally regulated gene activation/inactivation in the mouse. Dev Biol. 2002;244(2): 305–318. doi: 10.1006/dbio.2002.0597 11944939
    • (2002) Dev Biol , vol.244 , Issue.2 , pp. 305-318
    • Hayashi, S.1    McMahon, A.P.2
  • 19
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic leathlity in mice nullizygous for the Huntington’s disease gene homologue
    • 7550343
    • Zeitlin S, Liu JP, Chapman DL, Papaioannou VE, Efstratiadis A, Increased apoptosis and early embryonic leathlity in mice nullizygous for the Huntington’s disease gene homologue. Nat Genet. 1995;11(2): 155–163. doi: 10.1038/ng1095-155 7550343
    • (1995) Nat Genet , vol.11 , Issue.2 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 20
    • 0141618325 scopus 로고    scopus 로고
    • Complexin II is essential for normal neurological function in mice
    • 12915444
    • Glynn D, Bortnick RA, Morton AJ, Complexin II is essential for normal neurological function in mice. Hum Mol Genet. 2003;12(19): 2431–2448. doi: 10.1093/hmg/ddg249 12915444
    • (2003) Hum Mol Genet , vol.12 , Issue.19 , pp. 2431-2448
    • Glynn, D.1    Bortnick, R.A.2    Morton, A.J.3
  • 21
    • 0021020947 scopus 로고
    • Spontaneous eye lesions in laboratory animals: incidence in relation to age
    • 6368130
    • Taradach C, Greaves P, Spontaneous eye lesions in laboratory animals: incidence in relation to age. Crit Rev Toxicol. 1984;12(2): 121–147. doi: 10.3109/10408448409023759 6368130
    • (1984) Crit Rev Toxicol , vol.12 , Issue.2 , pp. 121-147
    • Taradach, C.1    Greaves, P.2
  • 22
    • 0021261133 scopus 로고
    • Cataract and other ophthalmic lesions in senescence accelerated mouse (SAM). Morphology and Incidence of senescence associated ophthalmic changes in mice
    • 6714329
    • Hosokawa M, Takeshita S, Higuchi K, Shimizu K, Irino M, Toda K, et al. Cataract and other ophthalmic lesions in senescence accelerated mouse (SAM). Morphology and Incidence of senescence associated ophthalmic changes in mice. Exp Eye Res. 1984;38(2): 105–114. 6714329
    • (1984) Exp Eye Res , vol.38 , Issue.2 , pp. 105-114
    • Hosokawa, M.1    Takeshita, S.2    Higuchi, K.3    Shimizu, K.4    Irino, M.5    Toda, K.6
  • 23
    • 84957686701 scopus 로고    scopus 로고
    • Germline deletion of huntingtin causes male infertility and arrested spermiogenesis in mice
    • 26659666
    • Yan J, Zhang H, Liu Y, Zhao F, Zhu S, Xie C, et al. Germline deletion of huntingtin causes male infertility and arrested spermiogenesis in mice. J Cell Sci. 2016;129(3): 492–501. doi: 10.1242/jcs.173666 26659666
    • (2016) J Cell Sci , vol.129 , Issue.3 , pp. 492-501
    • Yan, J.1    Zhang, H.2    Liu, Y.3    Zhao, F.4    Zhu, S.5    Xie, C.6
  • 24
    • 9444286388 scopus 로고    scopus 로고
    • Expression of normal and mutant huntingtin in the developing brain
    • 8757264
    • Bhide PG, Day M, Sapp E, Schwarz C, Sheth A, Kim J, et al. Expression of normal and mutant huntingtin in the developing brain. J Neurosci. 1996;16(17): 5523–5535. 8757264
    • (1996) J Neurosci , vol.16 , Issue.17 , pp. 5523-5535
    • Bhide, P.G.1    Day, M.2    Sapp, E.3    Schwarz, C.4    Sheth, A.5    Kim, J.6
  • 25
    • 0030771894 scopus 로고    scopus 로고
    • Huntingtin localization in brains of normal and Huntington’s disease patients
    • 9382472
    • Sapp E, Schwarz C, Chase K, Bhide PG, Young AB, Penney J, et al. Huntingtin localization in brains of normal and Huntington’s disease patients. Ann Neurol. 1997;42(4): 604–612. doi: 10.1002/ana.410420411 9382472
    • (1997) Ann Neurol , vol.42 , Issue.4 , pp. 604-612
    • Sapp, E.1    Schwarz, C.2    Chase, K.3    Bhide, P.G.4    Young, A.B.5    Penney, J.6
  • 26
    • 59749097196 scopus 로고    scopus 로고
    • Medium spiny neurons for transplantation in Huntington’s disease
    • Kelly CM, Dunnett SB, Rosser AE, Medium spiny neurons for transplantation in Huntington’s disease. Biochem Soc Trans. 2009;37(Pt1): 323–328.
    • (2009) Biochem Soc Trans , vol.37 , Issue.Pt1 , pp. 323-328
    • Kelly, C.M.1    Dunnett, S.B.2    Rosser, A.E.3
  • 28
    • 84908010890 scopus 로고    scopus 로고
    • Activation of Nrf2 by dimethyl fumarate improves vascular calcification
    • 25135648
    • Ha CM, Park S, Choi YK, Jeong JY, Oh CJ, Bae KH, et al. Activation of Nrf2 by dimethyl fumarate improves vascular calcification. Vascul Pharmacol. 2014;63(1):29–36. doi: 10.1016/j.vph.2014.06.007 25135648
    • (2014) Vascul Pharmacol , vol.63 , Issue.1 , pp. 29-36
    • Ha, C.M.1    Park, S.2    Choi, Y.K.3    Jeong, J.Y.4    Oh, C.J.5    Bae, K.H.6
  • 30
    • 84964678895 scopus 로고    scopus 로고
    • Osteopontin protects against high phosphate-induced nephrocalcinosis and vascular calcification
    • 27083280
    • Paloian NJ, Leaf EM, Giachelli CM, Osteopontin protects against high phosphate-induced nephrocalcinosis and vascular calcification. Kidney Int. 2016;89(5):1027–1036. doi: 10.1016/j.kint.2015.12.046 27083280
    • (2016) Kidney Int , vol.89 , Issue.5 , pp. 1027-1036
    • Paloian, N.J.1    Leaf, E.M.2    Giachelli, C.M.3
  • 31
    • 0014471460 scopus 로고
    • Idiopathic familial cerebrovascular ferrocalcinosis (Fahr’s disease) and review of differential diagnosis of intracranial calcification in children
    • 4179335
    • Babbitt DP, Tang T, Dobbs J, Berk R, Idiopathic familial cerebrovascular ferrocalcinosis (Fahr’s disease) and review of differential diagnosis of intracranial calcification in children. Am J Roentgenol Radium Ther Nucl Med. 1969;105(2): 352–358. 4179335
    • (1969) Am J Roentgenol Radium Ther Nucl Med , vol.105 , Issue.2 , pp. 352-358
    • Babbitt, D.P.1    Tang, T.2    Dobbs, J.3    Berk, R.4
  • 32
    • 0024448236 scopus 로고
    • Abnormal systemic metabolism of iron, porphyrin, and calcium in Fahr's syndrome
    • 2817830
    • Beall SS, Patten BM, Mallette JL, Jankovic J, Abnormal systemic metabolism of iron, porphyrin, and calcium in Fahr's syndrome. Ann Neurol. 1989;26(4): 569–575. doi: 10.1002/ana.410260412 2817830
    • (1989) Ann Neurol , vol.26 , Issue.4 , pp. 569-575
    • Beall, S.S.1    Patten, B.M.2    Mallette, J.L.3    Jankovic, J.4
  • 33
    • 14044252284 scopus 로고    scopus 로고
    • What is and is not Fahr’s disease
    • 15734663
    • Manyam BV, What is and is not Fahr’s disease. Parkinsonism Relat Disord. 2005;11(2): 73–80. doi: 10.1016/j.parkreldis.2004.12.001 15734663
    • (2005) Parkinsonism Relat Disord , vol.11 , Issue.2 , pp. 73-80
    • Manyam, B.V.1
  • 35
    • 78650125646 scopus 로고    scopus 로고
    • Intracranial calcifications on CT
    • 20027545
    • Kıroğlu Y, Callı C, Karabulut N, Oncel C, Intracranial calcifications on CT. Diagn Interv Radiol. 2010;16(4): 263–269. doi: 10.4261/1305-3825.DIR.2626-09.1 20027545
    • (2010) Diagn Interv Radiol , vol.16 , Issue.4 , pp. 263-269
    • Kıroğlu, Y.1    Callı, C.2    Karabulut, N.3    Oncel, C.4
  • 36
    • 2642646258 scopus 로고    scopus 로고
    • Mouse mutant embryos lacking huntingtin are rescued from lethality by wild-type extraembryonic tissues
    • 9502734
    • Dragatsis I, Efstratiadis A, Zeitlin S, Mouse mutant embryos lacking huntingtin are rescued from lethality by wild-type extraembryonic tissues. Development. 1998;125(8): 1529–1539. 9502734
    • (1998) Development , vol.125 , Issue.8 , pp. 1529-1539
    • Dragatsis, I.1    Efstratiadis, A.2    Zeitlin, S.3
  • 37
    • 34548406422 scopus 로고    scopus 로고
    • Huntingtin-deficient zebrafish exhibit defects in iron utilization and development
    • 17567778
    • Lumsden AL, Henshall TL, Dayan S, Lardelli MT, Richards RI, Huntingtin-deficient zebrafish exhibit defects in iron utilization and development. Hum Mol Genet. 2007;16(16): 1905–1920. doi: 10.1093/hmg/ddm138 17567778
    • (2007) Hum Mol Genet , vol.16 , Issue.16 , pp. 1905-1920
    • Lumsden, A.L.1    Henshall, T.L.2    Dayan, S.3    Lardelli, M.T.4    Richards, R.I.5
  • 39
    • 84856489978 scopus 로고    scopus 로고
    • Regulation of brain iron and copper homeostasis by brain barrier systems: implication in neurodegenerative diseases
    • 22115751
    • Zheng W, Monnot AD, Regulation of brain iron and copper homeostasis by brain barrier systems: implication in neurodegenerative diseases. Pharmacol Ther. 2012;133(2): 177–188. doi: 10.1016/j.pharmthera.2011.10.006 22115751
    • (2012) Pharmacol Ther , vol.133 , Issue.2 , pp. 177-188
    • Zheng, W.1    Monnot, A.D.2
  • 40
    • 84894475785 scopus 로고    scopus 로고
    • Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities
    • 23815406
    • Singh N, Haldar S, Tripathi AK, Horback K, Wong J, Sharma D, et al. Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities. Antioxid Redox Signal. 2014;20(8): 1324–1363. doi: 10.1089/ars.2012.4931 23815406
    • (2014) Antioxid Redox Signal , vol.20 , Issue.8 , pp. 1324-1363
    • Singh, N.1    Haldar, S.2    Tripathi, A.K.3    Horback, K.4    Wong, J.5    Sharma, D.6
  • 41
    • 84877741258 scopus 로고    scopus 로고
    • Mammalian iron homeostasis in health and disease: uptake, storage, transport, and molecular mechanisms of action
    • 23199217
    • Lawen A, Lane DJ, Mammalian iron homeostasis in health and disease: uptake, storage, transport, and molecular mechanisms of action. Antioxid Redox Signal. 2013;18(18):2473–5207. doi: 10.1089/ars.2011.4271 23199217
    • (2013) Antioxid Redox Signal , vol.18 , Issue.18 , pp. 2473-5207
    • Lawen, A.1    Lane, D.J.2
  • 42
    • 85019633961 scopus 로고    scopus 로고
    • The regulation of iron absorbtion and homeostasis
    • 28303071
    • Wallace DF, The regulation of iron absorbtion and homeostasis. Clin Biochem Rev. 2016;37(2):51–62. 28303071
    • (2016) Clin Biochem Rev , vol.37 , Issue.2 , pp. 51-62
    • Wallace, D.F.1
  • 43
    • 84962327593 scopus 로고    scopus 로고
    • Ablation of huntingtin in adult neurons is non-deleterious but its depletion in young mice causes acute pancreatitis
    • 26951659
    • Wang G, Liu X, Gaertig MA, Li S, Li XJ, Ablation of huntingtin in adult neurons is non-deleterious but its depletion in young mice causes acute pancreatitis. Proc Natl Acad Sci U S A. 2016;113(12): 3359–3364. doi: 10.1073/pnas.1524575113 26951659
    • (2016) Proc Natl Acad Sci U S A , vol.113 , Issue.12 , pp. 3359-3364
    • Wang, G.1    Liu, X.2    Gaertig, M.A.3    Li, S.4    Li, X.J.5
  • 44
    • 84883328825 scopus 로고    scopus 로고
    • Huntingtin acts non cell-autonomously on hippocampal neurogenesis and controls anxiety-related behaviors in adult mouse
    • 24019939
    • Pla P, Orvoen S, Benstaali C, Dodier S, Gardier AM, David DJ, et al. Huntingtin acts non cell-autonomously on hippocampal neurogenesis and controls anxiety-related behaviors in adult mouse. PLoS One. 2013;8(9): e73902. doi: 10.1371/journal.pone.0073902 24019939
    • (2013) PLoS One , vol.8 , Issue.9 , pp. e73902
    • Pla, P.1    Orvoen, S.2    Benstaali, C.3    Dodier, S.4    Gardier, A.M.5    David, D.J.6
  • 45
    • 0018955015 scopus 로고
    • Bilateral basal ganglia calcifications visualized on CT scan
    • 7420090
    • Brannan TS, Burger AA, Chaudhary MY, Bilateral basal ganglia calcifications visualized on CT scan. J Neurol Neurosurg Psychiatry. 1980;43(5): 403–406. 7420090
    • (1980) J Neurol Neurosurg Psychiatry , vol.43 , Issue.5 , pp. 403-406
    • Brannan, T.S.1    Burger, A.A.2    Chaudhary, M.Y.3
  • 46
  • 47
    • 0142219729 scopus 로고    scopus 로고
    • Mineralization of the basal ganglia: implications for neuropsychiatry, pathology and neuroimaging
    • 14572624
    • Casanova MF, Araque JM, Mineralization of the basal ganglia: implications for neuropsychiatry, pathology and neuroimaging. Psychiatry Res. 2003;121(1): 59–87. 14572624
    • (2003) Psychiatry Res , vol.121 , Issue.1 , pp. 59-87
    • Casanova, M.F.1    Araque, J.M.2
  • 48
    • 0014307789 scopus 로고
    • Bilateral thalamic calcification in ageing mice
    • 5691245
    • Fraser H, Bilateral thalamic calcification in ageing mice. J Pathol Bacteriol. 1968;96(1): 220–222. doi: 10.1002/path.1700960124 5691245
    • (1968) J Pathol Bacteriol , vol.96 , Issue.1 , pp. 220-222
    • Fraser, H.1
  • 49
    • 0018839829 scopus 로고
    • Spontaneous lesions in control and BALB/C female mice
    • 7365377
    • Sheldon WG, Greenman DL, Spontaneous lesions in control and BALB/C female mice. J Environ Pathol Toxicol. 1980;3(3 Spec No): 155–167. 7365377
    • (1980) J Environ Pathol Toxicol , vol.3 , Issue.3 Spec No , pp. 155-167
    • Sheldon, W.G.1    Greenman, D.L.2
  • 50
    • 0019936435 scopus 로고
    • An ultrastructural study of spontaneous mineralization in the brains of aging mice
    • 7180386
    • Morgan KT, Johnson BP, Frith CH, Townsend J, An ultrastructural study of spontaneous mineralization in the brains of aging mice. Acta Neuropathol. 1982;58(2): 120–124. 7180386
    • (1982) Acta Neuropathol , vol.58 , Issue.2 , pp. 120-124
    • Morgan, K.T.1    Johnson, B.P.2    Frith, C.H.3    Townsend, J.4
  • 51
    • 33745464027 scopus 로고    scopus 로고
    • Thalamic calcification in vitamin D receptor knockout mice
    • 16641675
    • Kalueff A, Loseva E, Haapasalo H, Rantala I, Keranen J, Lou YR, et al. Thalamic calcification in vitamin D receptor knockout mice. Neuroreport. 2006;17(7): 717–721. doi: 10.1097/01.wnr.0000215770.79281.e4 16641675
    • (2006) Neuroreport , vol.17 , Issue.7 , pp. 717-721
    • Kalueff, A.1    Loseva, E.2    Haapasalo, H.3    Rantala, I.4    Keranen, J.5    Lou, Y.R.6
  • 52
    • 10444289094 scopus 로고    scopus 로고
    • Genetic heterogeneity in familial idiopathic basal ganglia calcification (Fahr disease)
    • 15596772
    • Oliveira JR, Spiteri E, Sobrido MJ, Hopfer S, Klepper J, Voit T, et al. Genetic heterogeneity in familial idiopathic basal ganglia calcification (Fahr disease). Neurology. 2004;63(11): 2165–2167. 15596772
    • (2004) Neurology , vol.63 , Issue.11 , pp. 2165-2167
    • Oliveira, J.R.1    Spiteri, E.2    Sobrido, M.J.3    Hopfer, S.4    Klepper, J.5    Voit, T.6
  • 53
    • 84928208407 scopus 로고    scopus 로고
    • Update and mutational analysys of Slc20a2: a major cause of primary familial brain calcification
    • 25726928
    • Lemos RR, Ramos EM, Legati A, Nicolas G, Jenkinson EM, Livingston JH, et al. Update and mutational analysys of Slc20a2: a major cause of primary familial brain calcification. Hum. Mutat. 2015;36(5): 489–495. doi: 10.1002/humu.22778 25726928
    • (2015) Hum. Mutat , vol.36 , Issue.5 , pp. 489-495
    • Lemos, R.R.1    Ramos, E.M.2    Legati, A.3    Nicolas, G.4    Jenkinson, E.M.5    Livingston, J.H.6
  • 54
    • 84885948431 scopus 로고    scopus 로고
    • Loss of function of Slc20a2 associated with familial idiopathic basal ganglia calcification in humans causes brain calcifications in mice
    • 23934451
    • Jensen N, Schrøder HD, Hejbøl EK, Füchtbauer EM, de Oliveira JR, Pedersen L, Loss of function of Slc20a2 associated with familial idiopathic basal ganglia calcification in humans causes brain calcifications in mice. J Mol Neurosci. 2013;51(3): 994–949. doi: 10.1007/s12031-013-0085-6 23934451
    • (2013) J Mol Neurosci , vol.51 , Issue.3 , pp. 949-994
    • Jensen, N.1    Schrøder, H.D.2    Hejbøl, E.K.3    Füchtbauer, E.M.4    de Oliveira, J.R.5    Pedersen, L.6
  • 55
    • 84873693930 scopus 로고    scopus 로고
    • Mutation of the PDGFRB gene as a cause of idiopathic basal ganglia calcification
    • 23255827
    • Nicolas G, Pottier C, Maltête D, Coutant S, Rovelet-Lecrux A, Legallic S, et al. Mutation of the PDGFRB gene as a cause of idiopathic basal ganglia calcification. Neurology. 2013;80(2): 181–187. doi: 10.1212/WNL.0b013e31827ccf34 23255827
    • (2013) Neurology , vol.80 , Issue.2 , pp. 181-187
    • Nicolas, G.1    Pottier, C.2    Maltête, D.3    Coutant, S.4    Rovelet-Lecrux, A.5    Legallic, S.6
  • 56
    • 84883463387 scopus 로고    scopus 로고
    • Mutations in the gene encoding PDGF-B cause brain calcifications in humans and mice
    • 23913003
    • Keller A, Westenberger A, Sobrido MJ, García-Murias M, Domingo A, Sears RL, et al. Mutations in the gene encoding PDGF-B cause brain calcifications in humans and mice. Nat Genet. 2013;45(9): 1077–1082. doi: 10.1038/ng.2723 23913003
    • (2013) Nat Genet , vol.45 , Issue.9 , pp. 1077-1082
    • Keller, A.1    Westenberger, A.2    Sobrido, M.J.3    García-Murias, M.4    Domingo, A.5    Sears, R.L.6
  • 58
    • 84904697923 scopus 로고    scopus 로고
    • Thalamostriatal synapses-another substrate for dopamine action?
    • 24968774
    • Arbuthnott GW, Thalamostriatal synapses-another substrate for dopamine action?Prog Brain Res. 2014;211:1–11. doi: 10.1016/B978-0-444-63425-2.00001-5 24968774
    • (2014) Prog Brain Res , vol.211 , pp. 1-11
    • Arbuthnott, G.W.1
  • 59
    • 0034838768 scopus 로고    scopus 로고
    • Iron and iron management proteins in neurobiology
    • 11551742
    • Connor JR, Menzies SL, Burdo JR, Boyer PJ, Iron and iron management proteins in neurobiology. Pediatr Neurol. 2001;25(2): 118–129. 11551742
    • (2001) Pediatr Neurol , vol.25 , Issue.2 , pp. 118-129
    • Connor, J.R.1    Menzies, S.L.2    Burdo, J.R.3    Boyer, P.J.4
  • 60
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • 11175792
    • LaVaute T, Smith S, Cooperman S, Iwai K, Land W, Meyron-Holtz E, et al. Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice. Nat Genet. 2001;27(2): 209–214. doi: 10.1038/84859 11175792
    • (2001) Nat Genet , vol.27 , Issue.2 , pp. 209-214
    • LaVaute, T.1    Smith, S.2    Cooperman, S.3    Iwai, K.4    Land, W.5    Meyron-Holtz, E.6
  • 61
    • 80053902000 scopus 로고    scopus 로고
    • Iron insufficiency compromises motor neurons and their mitochondrial function in Irp2-null mice
    • 22003390
    • Jeong SY, Crooks DR, Wilson-Ollivierre H, Ghosh MC, Sougrat R, Lee J, et al. Iron insufficiency compromises motor neurons and their mitochondrial function in Irp2-null mice. PLoS One. 2011;6(10): e25404. doi: 10.1371/journal.pone.0025404 22003390
    • (2011) PLoS One , vol.6 , Issue.10 , pp. e25404
    • Jeong, S.Y.1    Crooks, D.R.2    Wilson-Ollivierre, H.3    Ghosh, M.C.4    Sougrat, R.5    Lee, J.6
  • 62
    • 55349084412 scopus 로고    scopus 로고
    • A function of huntingtin in the guanine nucleotide exchange of Rab11
    • 18845944
    • Li X, Sapp E, Valencia A, Kegel KB, Qin ZH, Alexander J, et al. A function of huntingtin in the guanine nucleotide exchange of Rab11. Neuroreport. 2008;19(16):1643–1647. doi: 10.1097/WNR.0b013e328315cd4c 18845944
    • (2008) Neuroreport , vol.19 , Issue.16 , pp. 1643-1647
    • Li, X.1    Sapp, E.2    Valencia, A.3    Kegel, K.B.4    Qin, Z.H.5    Alexander, J.6
  • 63
    • 84867169653 scopus 로고    scopus 로고
    • In-vivo evidence for the disruption of Rab11 vesicle transport by loss of huntingtin
    • 23032403
    • Power D, Srinivasan S, Gunawardena S, In-vivo evidence for the disruption of Rab11 vesicle transport by loss of huntingtin. Neuroreport. 2012;23(16):970–977. doi: 10.1097/WNR.0b013e328359d990 23032403
    • (2012) Neuroreport , vol.23 , Issue.16 , pp. 970-977
    • Power, D.1    Srinivasan, S.2    Gunawardena, S.3
  • 64
    • 0034638828 scopus 로고    scopus 로고
    • Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network
    • 11121436
    • Wilcke M, Johannes L, Galli T, Mayau V, Goud B, Salamero J, Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network. J Cell Biol. 2000;151(6):1207–1220. 11121436
    • (2000) J Cell Biol , vol.151 , Issue.6 , pp. 1207-1220
    • Wilcke, M.1    Johannes, L.2    Galli, T.3    Mayau, V.4    Goud, B.5    Salamero, J.6
  • 65
    • 84884678807 scopus 로고    scopus 로고
    • Arf6, Rab11 and transferrin receptor define distinct populations of recycling endosomes
    • 24255739
    • Kobayashi H, Fukuda M, Arf6, Rab11 and transferrin receptor define distinct populations of recycling endosomes. Commun Integr Biol. 2013; 6(5): e25036. doi: 10.4161/cib.25036 24255739
    • (2013) Commun Integr Biol , vol.6 , Issue.5 , pp. e25036
    • Kobayashi, H.1    Fukuda, M.2
  • 66
    • 84871650414 scopus 로고    scopus 로고
    • Expression and function of ferroportin in O-2A progenitor cells
    • Lin Q, Feng J, Zhao X, Zhang G, Wang W, Expression and function of ferroportin in O-2A progenitor cells. Anat Rec. (Hoboken). 2013;296(1): 108–116.
    • (2013) Anat Rec. (Hoboken) , vol.296 , Issue.1 , pp. 108-116
    • Lin, Q.1    Feng, J.2    Zhao, X.3    Zhang, G.4    Wang, W.5
  • 67
    • 84876883321 scopus 로고    scopus 로고
    • Iron-responsive miR-485-3p regulates cellular iron homeostasis by targeting ferroportin
    • 23593016
    • Sangokoya C, Doss JF, Chi JT, Iron-responsive miR-485-3p regulates cellular iron homeostasis by targeting ferroportin. PLoS Genet. 2013;9(4): e1003408. doi: 10.1371/journal.pgen.1003408 23593016
    • (2013) PLoS Genet , vol.9 , Issue.4 , pp. e1003408
    • Sangokoya, C.1    Doss, J.F.2    Chi, J.T.3
  • 68
    • 57249086448 scopus 로고    scopus 로고
    • Allele-specific silencing of mutant Huntington’s disease gene
    • 19094060
    • Zhang Y, Engelman J, Friedlander RM, Allele-specific silencing of mutant Huntington’s disease gene. J Neurochem. 2009;108(1): 82–90. doi: 10.1111/j.1471-4159.2008.05734.x 19094060
    • (2009) J Neurochem , vol.108 , Issue.1 , pp. 82-90
    • Zhang, Y.1    Engelman, J.2    Friedlander, R.M.3
  • 69
    • 84901688904 scopus 로고    scopus 로고
    • Personalized gene silencing therapeutics for Huntington disease
    • 24646433
    • Kay C, Skotte NH, Southwell AL, Hayden MR, Personalized gene silencing therapeutics for Huntington disease. Clin Genet. 2014;86(1): 29–36. doi: 10.1111/cge.12385 24646433
    • (2014) Clin Genet , vol.86 , Issue.1 , pp. 29-36
    • Kay, C.1    Skotte, N.H.2    Southwell, A.L.3    Hayden, M.R.4
  • 70
    • 84927177598 scopus 로고    scopus 로고
    • In vivo evaluation of candidate allele-specific mutant huntingtin gene silencing antisense oligonucleotides
    • 25101598
    • Southwell AL, Skotte NH, Kordasiewicz HB, Østergaard ME, Watt AT, Carroll JB, et al. In vivo evaluation of candidate allele-specific mutant huntingtin gene silencing antisense oligonucleotides. Mol Ther. 2014;22(12): 2093–2106. doi: 10.1038/mt.2014.153 25101598
    • (2014) Mol Ther , vol.22 , Issue.12 , pp. 2093-2106
    • Southwell, A.L.1    Skotte, N.H.2    Kordasiewicz, H.B.3    Østergaard, M.E.4    Watt, A.T.5    Carroll, J.B.6
  • 71
    • 84926664315 scopus 로고    scopus 로고
    • Artificial mRNAs targeting mutant huntingtin show preferential silencing in vitro and in vivo
    • 25849618
    • Monteys AM, Wilson MJ, Boudreau RL, Spengler RM, Davidson BL, Artificial mRNAs targeting mutant huntingtin show preferential silencing in vitro and in vivo. Mol Ther Nucleic Acids. 2015;4: e234. doi: 10.1038/mtna.2015.7 25849618
    • (2015) Mol Ther Nucleic Acids , vol.4 , pp. e234
    • Monteys, A.M.1    Wilson, M.J.2    Boudreau, R.L.3    Spengler, R.M.4    Davidson, B.L.5
  • 72
    • 11044228787 scopus 로고    scopus 로고
    • Huntingtin-associated protein 1 (Hap1) mutant mice bypassing the early postnatal lethality are neuroanatomically normal and fertile but display growth retardation
    • 15496430
    • Dragatsis I, Zeitlin S, Dietrich P, Huntingtin-associated protein 1 (Hap1) mutant mice bypassing the early postnatal lethality are neuroanatomically normal and fertile but display growth retardation. Hum Mol Genet. 2004;13(24): 3115–3125. doi: 10.1093/hmg/ddh328 15496430
    • (2004) Hum Mol Genet , vol.13 , Issue.24 , pp. 3115-3125
    • Dragatsis, I.1    Zeitlin, S.2    Dietrich, P.3
  • 73
    • 57649228989 scopus 로고    scopus 로고
    • Congenital hydrocephalus associated with abnormal subcommissural organ in mice lacking huntingtin in Wnt1 lineages
    • 18838463
    • Dietrich P, Shanmugasundaram R, Shuyu E, Dragatsis I, Congenital hydrocephalus associated with abnormal subcommissural organ in mice lacking huntingtin in Wnt1 lineages. Hum Mol Genet. 2009;18(1): 142–150. doi: 10.1093/hmg/ddn324 18838463
    • (2009) Hum Mol Genet , vol.18 , Issue.1 , pp. 142-150
    • Dietrich, P.1    Shanmugasundaram, R.2    Shuyu, E.3    Dragatsis, I.4
  • 74
    • 84901217827 scopus 로고    scopus 로고
    • Quantification assays for total and polyglutamine-expanded huntingtin proteins
    • 24816435
    • Macdonald D, Tessari MA, Boogaard I, Smith M, Pulli K, Szynol A, et al. Quantification assays for total and polyglutamine-expanded huntingtin proteins. PLoS One. 2014;9(5): e96854. doi: 10.1371/journal.pone.0096854 24816435
    • (2014) PLoS One , vol.9 , Issue.5 , pp. e96854
    • Macdonald, D.1    Tessari, M.A.2    Boogaard, I.3    Smith, M.4    Pulli, K.5    Szynol, A.6
  • 75
    • 84861228589 scopus 로고    scopus 로고
    • The group 2 metabotropic glutamate receptor agonist LY379268 rescues neuronal, neurochemical and motor abnormalities in R6/2 Huntington’s disease mice
    • 22472187
    • Reiner A, Lafferty DC, Wang HB, Del Mar N, Deng YP, The group 2 metabotropic glutamate receptor agonist LY379268 rescues neuronal, neurochemical and motor abnormalities in R6/2 Huntington’s disease mice. Neurobiol Dis. 2012;47(1): 75–91. doi: 10.1016/j.nbd.2012.03.025 22472187
    • (2012) Neurobiol Dis , vol.47 , Issue.1 , pp. 75-91
    • Reiner, A.1    Lafferty, D.C.2    Wang, H.B.3    Del Mar, N.4    Deng, Y.P.5
  • 76
    • 0037444445 scopus 로고    scopus 로고
    • Mutant huntingtin causes context-dependent neurodegeneration in mice with Huntington’s disease
    • 12657678
    • Yu ZX, Li SH, Evans J, Pillarisetti A, Li H, Li XJ, Mutant huntingtin causes context-dependent neurodegeneration in mice with Huntington’s disease. J Neurosci. 2003;23(6): 2193–2202. 12657678
    • (2003) J Neurosci , vol.23 , Issue.6 , pp. 2193-2202
    • Yu, Z.X.1    Li, S.H.2    Evans, J.3    Pillarisetti, A.4    Li, H.5    Li, X.J.6
  • 77
    • 85009275008 scopus 로고    scopus 로고
    • Enhanced histochemical detection of iron in paraffin sections of mouse central nervous system tissue: application in the APP/PS1 mouse model of Alzheimer’s disease
    • Sands SA, Leung-Toung R, Wang Y, Connelly J, LeVine SM, Enhanced histochemical detection of iron in paraffin sections of mouse central nervous system tissue: application in the APP/PS1 mouse model of Alzheimer’s disease. ASN Neuro. 2016;8(5).
    • (2016) ASN Neuro , vol.8 , Issue.5
    • Sands, S.A.1    Leung-Toung, R.2    Wang, Y.3    Connelly, J.4    LeVine, S.M.5
  • 78
    • 84952772333 scopus 로고    scopus 로고
    • Impaired myelination and reduced brain ferric iron in the mouse model of mucolipidosis IV
    • 26398942
    • Grishchuk Y, Peña KA, Coblentz J, King VE, Humphrey DM, Wang SL, et al. Impaired myelination and reduced brain ferric iron in the mouse model of mucolipidosis IV. Dis Model Mech. 2015;8(12): 1591–1601. doi: 10.1242/dmm.021154 26398942
    • (2015) Dis Model Mech , vol.8 , Issue.12 , pp. 1591-1601
    • Grishchuk, Y.1    Peña, K.A.2    Coblentz, J.3    King, V.E.4    Humphrey, D.M.5    Wang, S.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.