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Volumn 9, Issue 1, 2009, Pages 76-82

Oculopharyngeal muscular dystrophy: A polyalanine myopathy

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; POLYADENYLIC ACID BINDING PROTEIN; POLYALANINE; UNCLASSIFIED DRUG;

EID: 59149101614     PISSN: 15284042     EISSN: 15346293     Source Type: Journal    
DOI: 10.1007/s11910-009-0012-y     Document Type: Article
Times cited : (69)

References (49)
  • 1
    • 0000232611 scopus 로고
    • Oculopharyngeal muscular dystrophy: A familial disease of late life characterized by dysphagia and progressive ptosis of the eyelids
    • Victor M, Hayes R, Adams RD: Oculopharyngeal muscular dystrophy: a familial disease of late life characterized by dysphagia and progressive ptosis of the eyelids. N Engl J Med 1962, 267:1267-1272.
    • (1962) N Engl J Med , vol.267 , pp. 1267-1272
    • Victor, M.1    Hayes, R.2    Adams, R.D.3
  • 2
    • 0018865908 scopus 로고
    • Nuclear inclusions in oculopharyngeal dystrophy
    • Tomé FM, Fardeau M: Nuclear inclusions in oculopharyngeal muscular dystrophy. Acta Neuropathol 1980, 49:85-87. (Pubitemid 10139969)
    • (1980) Acta Neuropathologica , vol.49 , Issue.1 , pp. 85-87
    • Tome, F.M.S.1    Fardeau, M.2
  • 4
    • 0028915818 scopus 로고
    • The oculopharyngeal muscular dystrophy locus maps to the region of the cardiac alpha and beta myosin heavy chain genes on chromosome 14q11.2-q13
    • Brais B, Xie YG, Sanson M, et al.: The oculopharyngeal muscular dystrophy locus maps to the region of the cardiac alpha and beta myosin heavy chain genes on chromosome 14q11.2-q13. Hum Mol Genet 1995, 4:429-434.
    • (1995) Hum Mol Genet , vol.4 , pp. 429-434
    • Brais, B.1    Xie, Y.G.2    Sanson, M.3
  • 5
    • 0030775367 scopus 로고    scopus 로고
    • Recent studies on oculopharyngeal muscular dystrophy in Quebec
    • Bouchard JP, Brais B, Brunet D, et al.: Recent studies on oculopharyngeal muscular dystrophy in Quebec. Neuromuscul Disord 1997, 7(Suppl 1):S22-S29.
    • (1997) Neuromuscul Disord , vol.7 , Issue.SUPPL. 1
    • Bouchard, J.P.1    Brais, B.2    Brunet, D.3
  • 7
  • 8
    • 0030813827 scopus 로고    scopus 로고
    • Morphological changes in muscle fibers in oculopharyngeal muscular dystrophy
    • Tomé FM, Chateau D, Helbling-Leclerc A, et al.: Morphological changes in muscle fibers in oculopharyngeal muscular dystrophy. Neuromuscul Disord 1997, 7(Suppl 1):S63-S69.
    • (1997) Neuromuscul Disord , vol.7 , Issue.SUPPL. 1
    • Tomé, F.M.1    Chateau, D.2    Helbling-Leclerc, A.3
  • 10
    • 0033920763 scopus 로고    scopus 로고
    • Localization of poly(A)-binding protein 2 (PABP2) in nuclear speckles is independent of import into the nucleus and requires binding to poly(A) RNA
    • Calado A, Carmo-Fonseca M: Localization of poly (A)-binding protein 2(PABP2) in nuclear speckles is independent of import into the nucleus and requires binding to poly (A) RNA. J Cell Sci 2000, 113 (Pt 12):2309-2318. (Pubitemid 30426844)
    • (2000) Journal of Cell Science , vol.113 , Issue.12 , pp. 2309-2318
    • Calado, A.1    Carmo-Fonseca, M.2
  • 11
    • 0033813782 scopus 로고    scopus 로고
    • Nuclear accumulation of expanded PABP2 gene product in oculopharyngeal muscular dystrophy
    • Uyama E, Tsukahara T, Goto K, et al.: Nuclear accumulation of expanded PABP2 gene product in oculopharyngeal muscular dystrophy. Muscle Nerve 2000, 23:1549-1554.
    • (2000) Muscle Nerve , vol.23 , pp. 1549-1554
    • Uyama, E.1    Tsukahara, T.2    Goto, K.3
  • 12
    • 0033764563 scopus 로고    scopus 로고
    • Intranuclear inclusions in oculopharyngeal muscular dystrophy contain poly (A) binding protein 2
    • Becher MW, Kotzuk JA, Davis LE, et al.: Intranuclear inclusions in oculopharyngeal muscular dystrophy contain poly (A) binding protein 2. Ann Neurol 2000, 48:812-815.
    • (2000) Ann Neurol , vol.48 , pp. 812-815
    • Becher, M.W.1    Kotzuk, J.A.2    Davis, L.E.3
  • 13
    • 0142185364 scopus 로고    scopus 로고
    • Involvement of the ubiquitin-proteasome pathway and molecular chaperones in oculopharyngeal muscular dystrophy
    • DOI 10.1093/hmg/ddg293
    • Abu-Baker A, Messaed C, Laganiere J, et al.: Involvement of the ubiquitin-proteasome pathway and molecular chaperones in oculopharyngeal muscular dystrophy. Hum Mol Genet 2003, 12:2609-2623. (Pubitemid 37304684)
    • (2003) Human Molecular Genetics , vol.12 , Issue.20 , pp. 2609-2623
    • Abu-Baker, A.1    Messaed, C.2    Laganiere, J.3    Gaspar, C.4    Brais, B.5    Rouleau, G.A.6
  • 14
    • 0037023781 scopus 로고    scopus 로고
    • Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy
    • DOI 10.1074/jbc.M109633200
    • Bao YP, Cook LJ, O'Donovan D, et al.: Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy. J Biol Chem 2002, 277:12263-12269. (Pubitemid 34952794)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 12263-12269
    • Bao, Y.P.1    Cook, L.J.2    O'Donovan, D.3    Uyama, E.4    Rubinsztein, D.C.5
  • 15
    • 0034703413 scopus 로고    scopus 로고
    • Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly (A) binding protein 2 aggregates which sequester poly (A) RNA
    • Calado A, Tomé FM, Brais B, et al.: Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly (A) binding protein 2 aggregates which sequester poly (A) RNA. Hum Mol Genet 2000, 9:2321-2328.
    • (2000) Hum Mol Genet , vol.9 , pp. 2321-2328
    • Calado, A.1    Tomé, F.M.2    Brais, B.3
  • 16
    • 0035873278 scopus 로고    scopus 로고
    • The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression
    • Kim YJ, Noguchi S, Hayashi YK, et al.: The product of an oculopharyngeal muscular dystrophy gene, poly (A) - binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression. Hum Mol Genet 2001, 10:1129-1139. (Pubitemid 32487536)
    • (2001) Human Molecular Genetics , vol.10 , Issue.11 , pp. 1129-1139
    • Kim, Y.-J.1    Noguchi, S.2    Hayashi, Y.K.3    Tsukahara, T.4    Shimizu, T.5    Arahata, K.6
  • 18
    • 33745940703 scopus 로고    scopus 로고
    • Oculopharyngeal muscular dystrophy: A point mutation which mimics the effect of the PABPN1 gene triplet repeat expansion mutation
    • Robinson DO, Wills AJ, Hammans SR, et al.: Oculopharyngeal muscular dystrophy: a point mutation which mimics the effect of the PABPN1 gene triplet repeat expansion mutation. J Med Genet 2006, 43:267-271.
    • (2006) J Med Genet , vol.43 , pp. 267-271
    • Robinson, D.O.1    Wills, A.J.2    Hammans, S.R.3
  • 19
    • 0036186713 scopus 로고    scopus 로고
    • Unequal crossing-over in unique PABP2 mutations in Japanese patients: A possible cause of oculopharyngeal muscular dystrophy
    • Nakamoto M, Nakano S, Kawashima S, et al.: Unequal crossing-over in unique PABP2 mutations in Japanese patients: a possible cause of oculopharyngeal muscular dystrophy. Arch Neurol 2002, 59:474-477. (Pubitemid 34208160)
    • (2002) Archives of Neurology , vol.59 , Issue.3 , pp. 474-477
    • Nakamoto, M.1    Nakano, S.2    Kawashima, S.3    Ihara, M.4    Nishimura, Y.5    Shinde, A.6    Kakizuka, A.7
  • 20
    • 33645239500 scopus 로고    scopus 로고
    • A de novo PABPN1 germline mutation in a patient with oculopharyngeal muscular dystrophy
    • DOI 10.1097/01.mlg.0000185602.86655.b5, PII 0000553720060100000022
    • Gurtler N, Plasilova M, Podvinec M, et al.: A de novo PABPN1 germline mutation in a patient with oculopharyngeal muscular dystrophy. Laryngoscope 2006, 116:111-114. (Pubitemid 44383973)
    • (2006) Laryngoscope , vol.116 , Issue.1 , pp. 111-114
    • Gurtler, N.1    Plasilova, M.2    Podvinec, M.3    Boesch, N.4    Muller, H.5    Heinimann, K.6
  • 21
    • 38049078661 scopus 로고    scopus 로고
    • An apparently sporadic case of oculopharyngeal muscular dystrophy: The first Italian report
    • Tremolizzo L, Galbussera A, Tagliabue E, et al.: An apparently sporadic case of oculopharyngeal muscular dystrophy: the first Italian report. Neurol Sci 2007, 28:339-341.
    • (2007) Neurol Sci , vol.28 , pp. 339-341
    • Tremolizzo, L.1    Galbussera, A.2    Tagliabue, E.3
  • 22
    • 33947185940 scopus 로고    scopus 로고
    • Siblings with recessive oculopharyngeal muscular dystrophy
    • DOI 10.1016/j.nmd.2006.11.009, PII S0960896606006237
    • Hebbar S, Webberley MJ, Lunt P, et al.: Siblings with recessive oculopharyngeal muscular dystrophy. Neuromuscul Disord 2007, 17:254-257. (Pubitemid 46413754)
    • (2007) Neuromuscular Disorders , vol.17 , Issue.3 , pp. 254-257
    • Hebbar, S.1    Webberley, M.J.2    Lunt, P.3    Robinson, D.O.4
  • 23
    • 34247556900 scopus 로고    scopus 로고
    • Variability of the recessive oculopharyngeal muscular dystrophy phenotype
    • DOI 10.1002/mus.20726
    • Semmler A, Kress W, Vielhaber S, et al.: Variability of the recessive oculopharyngeal muscular dystrophy phenotype. Muscle Nerve 2007, 35:681-684. (Pubitemid 46676860)
    • (2007) Muscle and Nerve , vol.35 , Issue.5 , pp. 681-684
    • Semmler, A.1    Kress, W.2    Vielhaber, S.3    Schroder, R.4    Kornblum, C.5
  • 24
    • 34248995490 scopus 로고    scopus 로고
    • Soluble expanded PABPN1 promotes cell death in oculopharyngeal muscular dystrophy
    • DOI 10.1016/j.nbd.2007.02.004, PII S096999610700040X
    • Messaed C, Dion PA, Abu-Baker A: et al.: Soluble expanded PABPN1 promotes cell death in oculopharyngeal muscular dystrophy. Neurobiol Dis 2007, 26:546-557. This paper is the first to clearly put forward experimental data to suggest that soluble PABPN1 is likely the form responsible for toxicity in OPMD, while the aggregate forms may be protective. (Pubitemid 46778990)
    • (2007) Neurobiology of Disease , vol.26 , Issue.3 , pp. 546-557
    • Messaed, C.1    Dion, P.A.2    Abu-Baker, A.3    Rochefort, D.4    Laganiere, J.5    Brais, B.6    Rouleau, G.A.7
  • 26
    • 0037621980 scopus 로고    scopus 로고
    • Nuclear poly(A)-binding protein PABPN1 is associated with RNA polymerase II during transcription and accompanies the released transcript to the nuclear pore
    • DOI 10.1016/S0014-4827(03)00123-X
    • Bear DG, Fomproix N, Soop T, et al.: Nuclear poly (A) - binding protein PABPN1 is associated with RNA polymerase II during transcription and accompanies the released transcript to the nuclear pore. Exp Cell Res 2003, 286:332-344. (Pubitemid 36566445)
    • (2003) Experimental Cell Research , vol.286 , Issue.2 , pp. 332-344
    • Bear, D.G.1    Fomproix, N.2    Soop, T.3    Bjorkroth, B.4    Masich, S.5    Daneholt, B.6
  • 27
    • 0033951076 scopus 로고    scopus 로고
    • Deciphering the cellular pathway for transport of poly(A)-binding protein II
    • DOI 10.1017/S1355838200991908
    • Calado A, Kutay U, Kuhn U, et al.: Deciphering the cellular pathway for transport of poly (A)-binding protein II. RNA 2000, 6:245-256. (Pubitemid 30091595)
    • (2000) RNA , vol.6 , Issue.2 , pp. 245-256
    • Calado, A.1    Kutay, U.2    Kuhn, U.3    Wahle, E.4    Carmo-Fonseca, M.5
  • 28
    • 33845999251 scopus 로고    scopus 로고
    • Effect of oculopharyngeal muscular dystrophy-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1
    • DOI 10.1111/j.1742-4658.2006.05595.x
    • Lodderstedt G, Hess S, Hause G, et al.: Effect of oculopharyngeal muscular dystrophy-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1. FEBS J 2007, 274:346-355. This paper shows clearly that fibril formation of expanded N-terminal PABPN1 is faster in a concentration-dependent manner than wild-type when placed in the presence of low amounts of fragmented seeds of aggregated protein. Furthermore, fibril morphology was different between the two types of fragments in a way that increased the resistance of the mutated form to a strong solubilization agent. This work is the first to clearly show at the structural level that the polyalanine expansion induces conformational changes that significantly modify the protein's biochemical characteristics. (Pubitemid 46046645)
    • (2007) FEBS Journal , vol.274 , Issue.2 , pp. 346-355
    • Lodderstedt, G.1    Hess, S.2    Hause, G.3    Scheuermann, T.4    Scheibel, T.5    Schwarz, E.6
  • 29
    • 39649092945 scopus 로고    scopus 로고
    • Hofmeister salts and potential therapeutic compounds accelerate in vitro fibril formation of the N-terminal domain of PABPN1 containing a disease-causing alanine extension
    • DOI 10.1021/bi701322g
    • Lodderstedt G, Sachs R, Faust J, et al.: Hofmeister salts and potential therapeutic compounds accelerate in vitro fibril formation of the N-terminal domain of PABPN1 containing a disease-causing alanine extension. Biochemistry 2008, 47:2181-2189. This study describes the influence of various substances on a fibrillar assay of the N-terminal PABPN1 domain. Interestingly, it shows that doxycycline and trehalose, two molecules previously shown to diminish mutated PABPN1 toxicity in a mouse transgenic model, cause an increase in fibril formation. This provides indirect evidence that increased aggregation may in fact be protective or alternatively that these substances, by ensuring a better conformation of the soluble mutated forms, may slow the disease process. (Pubitemid 351287144)
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 2181-2189
    • Lodderstedt, G.1    Sachs, R.2    Faust, J.3    Bordusa, F.4    Kuhn, U.5    Golbik, R.6    Kerth, A.7    Wahle, E.8    Balbach, J.9    Schwarz, E.10
  • 30
    • 43049167415 scopus 로고    scopus 로고
    • Monitoring fibril formation of the N-terminal domain of PABPN1 carrying an alanine repeat by tryptophan fluorescence and real-time NMR
    • Rohrberg J, Sachs R, Lodderstedt G, et al.: Monitoring fibril formation of the N-terminal domain of PABPN1 carrying an alanine repeat by tryptophan fluorescence and real-time NMR. FEBS Lett 2008, 582:1587-1592. This paper shows that interruption of the polyalanine domain by a tryptophan will modify the protein from an insoluble to soluble species, increasing the evidence that the length of noninterrupted polyalanine domain of PABPN1 influences its aggregative properties.
    • (2008) FEBS Lett , vol.582 , pp. 1587-1592
    • Rohrberg, J.1    Sachs, R.2    Lodderstedt, G.3
  • 31
    • 44949250971 scopus 로고    scopus 로고
    • Structural and dynamical characterization of fibrils from a disease-associated alanine expansion domain using proteolysis and solid-state NMR spectroscopy
    • DOI 10.1021/ja800120s
    • Sackewitz M, Scheidt HA, Lodderstedt G, et al.: Structural and dynamical characterization of fibrils from a disease-associated alanine expansion domain using proteolysis and solid-state NMR spectroscopy. J Am Chem Soc 2008, 130:7172-7173. This provides the first structural evidence that the proximity of glycine residues in the N-terminal part of PABPN1 plays a role in the flexibility of the fibril core key for aggregation. (Pubitemid 351813179)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.23 , pp. 7172-7173
    • Sackewitz, M.1    Scheidt, H.A.2    Lodderstedt, G.3    Schierhorn, A.4    Schwarz, E.5    Huster, D.6
  • 32
    • 44349141843 scopus 로고    scopus 로고
    • A folded and functional protein domain in an amyloid-like fibril
    • DOI 10.1110/ps.073276308
    • Sackewitz M, von Einem S, Hause G, et al.: A folded and functional protein domain in an amyloid-like fibril. Protein Sci 2008, 17:1044-1054. This paper surprisingly shows that expansion from 10 to 17 alanines of the N-terminal domain of PABPN1 appears to decrease fibrillar formation, providing structural evidence that the mutated form may in fact have a greater negative impact on physiologic interaction between PABPN1 molecules with itself and other partners. (Pubitemid 351749210)
    • (2008) Protein Science , vol.17 , Issue.6 , pp. 1044-1054
    • Sackewitz, M.1    Von Einem, S.2    Hause, G.3    Wunderlich, M.4    Schmid, F.-X.5    Schwarz, E.6
  • 34
    • 29644437591 scopus 로고    scopus 로고
    • Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy
    • DOI 10.1093/hmg/ddi422
    • Davies JE, Sarkar S, Rubinsztein DC: Treha lose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy. Hum Mol Genet 2006, 15:23-31. (Pubitemid 43020101)
    • (2006) Human Molecular Genetics , vol.15 , Issue.1 , pp. 23-31
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 35
    • 42449108672 scopus 로고    scopus 로고
    • Crystal structure and possible dimerization of the single RRM of human PABPN1
    • DOI 10.1002/prot.21973
    • Ge H, Zhou D, Tong S, et al.:.: Crystal structure and possible dimerization of the single RRM of human PABPN1. Proteins 2008, 71:1539-1545. This paper provides evidence for the structural dimerization of the RNA recognition motif (RRM or RNA-binding domain) of PABPN1. (Pubitemid 351564072)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.3 , pp. 1539-1545
    • Ge, H.1    Zhou, D.2    Tong, S.3    Gao, Y.4    Teng, M.5    Niu, L.6
  • 36
    • 1642451714 scopus 로고    scopus 로고
    • Congo red, doxycycline, and HSP70 overexpression reduce aggregate formation and cell death in cell models of oculopharyngeal muscular dystrophy
    • Bao YP, Sarkar S, Uyama E, et al.: Congo red, doxycycline, and HSP70 overexpression reduce aggregate formation and cell death in cell models of oculopharyngeal muscular dystrophy. J Med Genet 2004, 41:47-51. (Pubitemid 38125688)
    • (2004) Journal of Medical Genetics , vol.41 , Issue.1 , pp. 47-51
    • Bao, Y.P.1    Sarkar, S.2    Uyama, E.3    Rubinsztein, D.C.4
  • 38
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B, Duden R, Rubinsztein DC: Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 2002, 11:1107-1117. (Pubitemid 34521091)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 39
    • 46249124837 scopus 로고    scopus 로고
    • Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1
    • DOI 10.1093/hmg/ddn109
    • Catoire H, Pasco MY, Abu-Baker A, et al.:.: Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1. Hum Mol Genet 2008, 17:2108-2117. This paper describes the first nematode model of OPMD. It provides convincing evidence that inhibition of longevity modulators sirtuins by inhibitors such as sirtinol may favorably diminish the mutated PABPN1 toxicity, and it provides some evidence that soluble PABPN1 in the nematode appears to be the more toxic form. (Pubitemid 351911980)
    • (2008) Human Molecular Genetics , vol.17 , Issue.14 , pp. 2108-2117
    • Catoire, H.1    Pasco, M.Y.2    Abu-Baker, A.3    Holbert, S.4    Tourette, C.5    Brais, B.6    Rouleau, G.A.7    Parker, J.A.8    Neri, C.9
  • 40
    • 33646768641 scopus 로고    scopus 로고
    • A Drosophila model of oculopharyngeal muscular dystrophy reveals intrinsic toxicity of PABPN1
    • Chartier A, Benoit B, Simonelig M: A Drosophila model of oculopharyngeal muscular dystrophy reveals intrinsic toxicity of PABPN1. EMBO J 2006, 25:2253-2262.
    • (2006) EMBO J , vol.25 , pp. 2253-2262
    • Chartier, A.1    Benoit, B.2    Simonelig, M.3
  • 41
    • 28744444484 scopus 로고    scopus 로고
    • Induction of HSP70 expression and recruitment of HSC70 and HSP70 in the nucleus reduce aggregation of a polyalanine expansion mutant of PABPN1 in HeLa cells
    • DOI 10.1093/hmg/ddi395
    • Wang Q, Mosser DD, Bag J: Induction of HSP70 expression and recruitment of HSC70 and HSP70 in the nucleus reduce aggregation of a polyalanine expansion mutant of PABPN1 in HeLa cells. Hum Mol Genet 2005, 14:3673-3684. (Pubitemid 41754667)
    • (2005) Human Molecular Genetics , vol.14 , Issue.23 , pp. 3673-3684
    • Wang, Q.1    Mosser, D.D.2    Bag, J.3
  • 43
    • 1942485876 scopus 로고    scopus 로고
    • Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus
    • DOI 10.1093/hmg/ddh101
    • Berciano MT, Villagra NT, Ojeda JL, et al.: Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus. Hum Mol Genet 2004, 13:829-838. (Pubitemid 38515212)
    • (2004) Human Molecular Genetics , vol.13 , Issue.8 , pp. 829-838
    • Berciano, M.T.1    Villagra, N.T.2    Ojeda, J.L.3    Navascues, J.4    Gomes, A.5    Lafarga, M.6    Carmo-Fonseca, M.7
  • 44
    • 39649096530 scopus 로고    scopus 로고
    • Nuclear compartmentalization and dynamics of the poly (A)-binding protein nuclear 1 (PABPN1) inclusions in supraoptic neurons under physiological and osmotic stress conditions
    • Villagra NT, Bengoechea R, Vaque JP, et al.: Nuclear compartmentalization and dynamics of the poly (A)-binding protein nuclear 1 (PABPN1) inclusions in supraoptic neurons under physiological and osmotic stress conditions. Mol Cell Neurosci 2008, 37:622-633.
    • (2008) Mol Cell Neurosci , vol.37 , pp. 622-633
    • Villagra, N.T.1    Bengoechea, R.2    Vaque, J.P.3
  • 45
    • 41949116233 scopus 로고    scopus 로고
    • Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation
    • DOI 10.1093/hmg/ddm382
    • Davies JE, Sarkar S, Rubinsztein DC: Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation. Hum Mol Genet 2008, 17:1097-1108. This paper on the most studied transgenic mice model of OPMD provides strong evidence that the wild-type PABPN1 can rescue the phenotype to some extent. It demonstrates that knocking down the expression of PABPN1 leads to greater susceptibility to proapoptotic stresses, suggesting that wild-type PABPN1 appears to have an antiapoptotic function that may be mediated in part by the X-linked inhibitor of apoptosis protein. (Pubitemid 351505885)
    • (2008) Human Molecular Genetics , vol.17 , Issue.8 , pp. 1097-1108
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 46
    • 43049151758 scopus 로고    scopus 로고
    • PA BPN1 polya lanine tract deletion and long expansions modify its aggregation pattern and expression
    • Klein AF, Ebihara M, Alexander C, et al.: PA BPN1 polya lanine tract deletion and long expansions modify its aggregation pattern and expression. Exp Cell Res 2008, 314:1652-1666. This paper shows that the polyalanine domain of PABPN1 is not essential for its aggregation but for its proper transport across the nuclear membrane. It also shows that larger-size expansion in the 25-40Ala range leads to more toxicity without a greater formation of aggregates; in fact, with the larger 40Ala construct no clear aggregation was produced despite the higher toxicity.
    • (2008) Exp Cell Res , vol.314 , pp. 1652-1666
    • Klein, A.F.1    Ebihara, M.2    Alexander, C.3
  • 47
    • 34250175866 scopus 로고    scopus 로고
    • Postoperative complications in patients with oculopharyngeal muscular dystrophy: A retrospective study
    • Pellerin HG, Nicole PC, Trepanier CA, et al.: Postoperative complications in patients with oculopharyngeal muscular dystrophy: a retrospective study. Can J Anaesth 2007, 54:361-365. (Pubitemid 46902015)
    • (2007) Canadian Journal of Anesthesia , vol.54 , Issue.5 , pp. 361-365
    • Pellerin, H.G.1    Nicole, P.C.2    Trepanier, C.A.3    Lessard, M.R.4
  • 48
    • 0030728968 scopus 로고    scopus 로고
    • A pilot study on upper esophageal sphincter dilatation for the treatment of dysphagia in patients with oculopharyngeal muscular dystrophy
    • Mathieu J, Lapointe G, Brassard A, et al.: A pilot study on upper esophageal sphincter dilatation for the treatment of dysphagia in patients with oculopharyngeal muscular dystrophy. Neuromuscul Disord 1997, 7:S100-S104.
    • (1997) Neuromuscul Disord , vol.7
    • Mathieu, J.1    Lapointe, G.2    Brassard, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.