메뉴 건너뛰기




Volumn 280, Issue 17, 2013, Pages 4230-4250

PABPN1: Molecular function and muscle disease

Author keywords

alternative cleavage polyadenylation; muscle disease; nuclear aggregates; oculopharyngeal muscular dystrophy; PABPN1; poly(A) RNA binding protein; polyadenylation; RNA processing

Indexed keywords

POLYADENOSINE RNA BINDING PROTEIN POLYADENYLATE BINDING NUCLEAR PROTEIN 1; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84882714408     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12294     Document Type: Review
Times cited : (94)

References (120)
  • 2
    • 84861911071 scopus 로고    scopus 로고
    • Translational control by changes in poly(A) tail length: Recycling mRNAs
    • Weill L, Belloc E, Bava FA, &, Mendez R, (2012) Translational control by changes in poly(A) tail length: recycling mRNAs. Nat Struct Mol Biol 19, 577-585.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 577-585
    • Weill, L.1    Belloc, E.2    Bava, F.A.3    Mendez, R.4
  • 3
    • 2442482777 scopus 로고    scopus 로고
    • Structure and function of poly(A) binding proteins
    • Kuhn U, &, Wahle E, (2004) Structure and function of poly(A) binding proteins. Biochim Biophys Acta 1678, 67-84.
    • (2004) Biochim Biophys Acta , vol.1678 , pp. 67-84
    • Kuhn, U.1    Wahle, E.2
  • 4
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus DA, Evans MC, &, Jacobson A, (2003) Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol 4, 223.
    • (2003) Genome Biol , vol.4 , pp. 223
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 5
    • 0035823036 scopus 로고    scopus 로고
    • Evidence for a pioneer round of mRNA translation: MRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20
    • Ishigaki Y, Li X, Serin G, &, Maquat LE, (2001) Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell 106, 607-617.
    • (2001) Cell , vol.106 , pp. 607-617
    • Ishigaki, Y.1    Li, X.2    Serin, G.3    Maquat, L.E.4
  • 6
    • 0025817865 scopus 로고
    • A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation
    • Wahle E, (1991) A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation. Cell 66, 759-768.
    • (1991) Cell , vol.66 , pp. 759-768
    • Wahle, E.1
  • 7
    • 0028015909 scopus 로고
    • Immunodetection of poly(A) binding protein II in the cell nucleus
    • Krause S, Fakan S, Weis K, &, Wahle E, (1994) Immunodetection of poly(A) binding protein II in the cell nucleus. Exp Cell Res 214, 75-82.
    • (1994) Exp Cell Res , vol.214 , pp. 75-82
    • Krause, S.1    Fakan, S.2    Weis, K.3    Wahle, E.4
  • 8
    • 0033951076 scopus 로고    scopus 로고
    • Deciphering the cellular pathway for transport of poly(A)-binding protein II
    • Calado A, Kutay U, Kuhn U, Wahle E, &, Carmo-Fonseca M, (2000) Deciphering the cellular pathway for transport of poly(A)-binding protein II. RNA 6, 245-256.
    • (2000) RNA , vol.6 , pp. 245-256
    • Calado, A.1    Kutay, U.2    Kuhn, U.3    Wahle, E.4    Carmo-Fonseca, M.5
  • 9
    • 0041312652 scopus 로고    scopus 로고
    • Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA
    • Kerwitz Y, Kuhn U, Lilie H, Knoth A, Scheuermann T, Friedrich H, Schwarz E, &, Wahle E, (2003) Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA. EMBO J 22, 3705-3714.
    • (2003) EMBO J , vol.22 , pp. 3705-3714
    • Kerwitz, Y.1    Kuhn, U.2    Lilie, H.3    Knoth, A.4    Scheuermann, T.5    Friedrich, H.6    Schwarz, E.7    Wahle, E.8
  • 10
    • 69249151288 scopus 로고    scopus 로고
    • Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor
    • Kuhn U, Gundel M, Knoth A, Kerwitz Y, Rudel S, &, Wahle E, (2009) Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor. J Biol Chem 284, 22803-22814.
    • (2009) J Biol Chem , vol.284 , pp. 22803-22814
    • Kuhn, U.1    Gundel, M.2    Knoth, A.3    Kerwitz, Y.4    Rudel, S.5    Wahle, E.6
  • 13
    • 84870669335 scopus 로고    scopus 로고
    • Polyadenylation-dependent control of long noncoding RNA expression by the poly(A)-binding protein nuclear 1
    • Beaulieu YB, Kleinman CL, Landry-Voyer AM, Majewski J, &, Bachand F, (2012) Polyadenylation-dependent control of long noncoding RNA expression by the poly(A)-binding protein nuclear 1. PLoS Gene 8, e1003078.
    • (2012) PLoS Gene , vol.8
    • Beaulieu, Y.B.1    Kleinman, C.L.2    Landry-Voyer, A.M.3    Majewski, J.4    Bachand, F.5
  • 15
    • 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, (1962) Oculopharyngeal muscular dystrophy. A familial disease of late life characterized by dysphagia and progressive ptosis of the eyelids. N Eng J Med 267, 1267-1272.
    • (1962) N Eng J Med , vol.267 , pp. 1267-1272
    • Victor, M.1    Hayes, R.2    Adams, R.D.3
  • 21
    • 0038607076 scopus 로고    scopus 로고
    • The RNA binding domains of the nuclear poly(A)-binding protein
    • Kuhn U, Nemeth A, Meyer S, &, Wahle E, (2003) The RNA binding domains of the nuclear poly(A)-binding protein. J Biol Chem 278, 16916-16925.
    • (2003) J Biol Chem , vol.278 , pp. 16916-16925
    • Kuhn, U.1    Nemeth, A.2    Meyer, S.3    Wahle, E.4
  • 22
    • 42449108672 scopus 로고    scopus 로고
    • Crystal structure and possible dimerization of the single RRM of human PABPN1
    • Ge H, Zhou D, Tong S, Gao Y, Teng M, &, Niu L, (2008) Crystal structure and possible dimerization of the single RRM of human PABPN1. Proteins 71, 1539-1545.
    • (2008) Proteins , vol.71 , pp. 1539-1545
    • Ge, H.1    Zhou, D.2    Tong, S.3    Gao, Y.4    Teng, M.5    Niu, L.6
  • 23
    • 2342512885 scopus 로고    scopus 로고
    • Xenopus embryonic poly(A) binding protein 2 (ePABP2) defines a new family of cytoplasmic poly(A) binding proteins expressed during the early stages of vertebrate development
    • Good PJ, Abler L, Herring D, &, Sheets MD, (2004) Xenopus embryonic poly(A) binding protein 2 (ePABP2) defines a new family of cytoplasmic poly(A) binding proteins expressed during the early stages of vertebrate development. Genesis 38, 166-175.
    • (2004) Genesis , vol.38 , pp. 166-175
    • Good, P.J.1    Abler, L.2    Herring, D.3    Sheets, M.D.4
  • 25
    • 0035504113 scopus 로고    scopus 로고
    • Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death
    • Fan X, Dion P, Laganiere J, Brais B, &, Rouleau GA, (2001) Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death. Human Mol Genet 10, 2341-2351.
    • (2001) Human Mol Genet , vol.10 , pp. 2341-2351
    • Fan, X.1    Dion, P.2    Laganiere, J.3    Brais, B.4    Rouleau, G.A.5
  • 26
    • 0039374447 scopus 로고    scopus 로고
    • Unusual sites of arginine methylation in poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3
    • Smith JJ, Rucknagel KP, Schierhorn A, Tang J, Nemeth A, Linder M, Herschman HR, &, Wahle E, (1999) Unusual sites of arginine methylation in poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. J Biol Chem 274, 13229-13234.
    • (1999) J Biol Chem , vol.274 , pp. 13229-13234
    • Smith, J.J.1    Rucknagel, K.P.2    Schierhorn, A.3    Tang, J.4    Nemeth, A.5    Linder, M.6    Herschman, H.R.7    Wahle, E.8
  • 27
    • 50649114242 scopus 로고    scopus 로고
    • Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behavior
    • Fronz K, Otto S, Kolbel K, Kuhn U, Friedrich H, Schierhorn A, Beck-Sickinger AG, Ostareck-Lederer A, &, Wahle E, (2008) Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behavior. J Biol Chem 283, 20408-20420.
    • (2008) J Biol Chem , vol.283 , pp. 20408-20420
    • Fronz, K.1    Otto, S.2    Kolbel, K.3    Kuhn, U.4    Friedrich, H.5    Schierhorn, A.6    Beck-Sickinger, A.G.7    Ostareck-Lederer, A.8    Wahle, E.9
  • 28
    • 80053046235 scopus 로고    scopus 로고
    • Arginine methylation of the nuclear poly(A) binding protein weakens the interaction with its nuclear import receptor, transportin
    • Fronz K, Guttinger S, Burkert K, Kuhn U, Stohr N, Schierhorn A, &, Wahle E, (2011) Arginine methylation of the nuclear poly(A) binding protein weakens the interaction with its nuclear import receptor, transportin. J Biol Chem 286, 32986-32994.
    • (2011) J Biol Chem , vol.286 , pp. 32986-32994
    • Fronz, K.1    Guttinger, S.2    Burkert, K.3    Kuhn, U.4    Stohr, N.5    Schierhorn, A.6    Wahle, E.7
  • 29
    • 84881631563 scopus 로고    scopus 로고
    • Methylation of the nuclear poly(A) binding protein by type i protein arginine methyltransferases - How and why
    • in press. doi: 10.1515/hsz-2013-0121
    • Wahle E, &, Moritz B, (2013) Methylation of the nuclear poly(A) binding protein by type I protein arginine methyltransferases-how and why. Biol Chem.in press. doi: 10.1515/hsz-2013-0121
    • (2013) Biol Chem
    • Wahle, E.1    Moritz, B.2
  • 30
    • 0034737319 scopus 로고    scopus 로고
    • The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail
    • Keller RW, Kuhn U, Aragon M, Bornikova L, Wahle E, &, Bear DG, (2000) The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail. J Mol Biol 297, 569-583.
    • (2000) J Mol Biol , vol.297 , pp. 569-583
    • Keller, R.W.1    Kuhn, U.2    Aragon, M.3    Bornikova, L.4    Wahle, E.5    Bear, D.G.6
  • 31
    • 80052979140 scopus 로고    scopus 로고
    • Mechanisms and consequences of alternative polyadenylation
    • Di Giammartino DC, Nishida K, &, Manley JL, (2011) Mechanisms and consequences of alternative polyadenylation. Mol Cell 43, 853-866.
    • (2011) Mol Cell , vol.43 , pp. 853-866
    • Di Giammartino, D.C.1    Nishida, K.2    Manley, J.L.3
  • 34
    • 66049104920 scopus 로고    scopus 로고
    • Progressive lengthening of 3′ untranslated regions of mRNAs by alternative polyadenylation during mouse embryonic development
    • Ji Z, Lee JY, Pan Z, Jiang B, &, Tian B, (2009) Progressive lengthening of 3′ untranslated regions of mRNAs by alternative polyadenylation during mouse embryonic development. Proc Natl Acad Sci U S A 106, 7028-7033.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7028-7033
    • Ji, Z.1    Lee, J.Y.2    Pan, Z.3    Jiang, B.4    Tian, B.5
  • 35
    • 68749113985 scopus 로고    scopus 로고
    • Widespread shortening of 3′UTRs by alternative cleavage and polyadenylation activates oncogenes in cancer cells
    • Mayr C, &, Bartel DP, (2009) Widespread shortening of 3′UTRs by alternative cleavage and polyadenylation activates oncogenes in cancer cells. Cell 138, 673-684.
    • (2009) Cell , vol.138 , pp. 673-684
    • Mayr, C.1    Bartel, D.P.2
  • 39
    • 84871764494 scopus 로고    scopus 로고
    • Depletion of nuclear poly(A) binding protein PABPN1 produces a compensatory response by cytoplasmic PABP4 and PABP5 in cultured human cells
    • Bhattacharjee RB, &, Bag J, (2012) Depletion of nuclear poly(A) binding protein PABPN1 produces a compensatory response by cytoplasmic PABP4 and PABP5 in cultured human cells. PLoS ONE 7, e53036.
    • (2012) PLoS ONE , vol.7
    • Bhattacharjee, R.B.1    Bag, J.2
  • 40
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases
    • Mitchell P, Petfalski E, Shevchenko A, Mann M, &, Tollervey D, (1997) The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases. Cell 91, 457-466.
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 41
    • 26444460263 scopus 로고    scopus 로고
    • An essential cytoplasmic function for the nuclear poly(A) binding protein, PABP2, in poly(A) tail length control and early development in Drosophila
    • Benoit B, Mitou G, Chartier A, Temme C, Zaessinger S, Wahle E, Busseau I, &, Simonelig M, (2005) An essential cytoplasmic function for the nuclear poly(A) binding protein, PABP2, in poly(A) tail length control and early development in Drosophila. Develop Cell 9, 511-522.
    • (2005) Develop Cell , vol.9 , pp. 511-522
    • Benoit, B.1    Mitou, G.2    Chartier, A.3    Temme, C.4    Zaessinger, S.5    Wahle, E.6    Busseau, I.7    Simonelig, M.8
  • 42
    • 77953284100 scopus 로고    scopus 로고
    • Molecular mechanisms of eukaryotic pre-mRNA 3′ end processing regulation
    • Millevoi S, &, Vagner S, (2010) Molecular mechanisms of eukaryotic pre-mRNA 3′ end processing regulation. Nucleic Acids Res 38, 2757-2774.
    • (2010) Nucleic Acids Res , vol.38 , pp. 2757-2774
    • Millevoi, S.1    Vagner, S.2
  • 43
    • 42449084129 scopus 로고    scopus 로고
    • Protein factors in pre-mRNA 3′-end processing
    • Mandel CR, Bai Y, &, Tong L, (2008) Protein factors in pre-mRNA 3′-end processing. Cell Mol Life Sci 65, 1099-1122.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1099-1122
    • Mandel, C.R.1    Bai, Y.2    Tong, L.3
  • 44
    • 67249129775 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the nuclear poly(A)-binding protein Pab2 to nascent transcripts and association with translating mRNPs
    • Lemieux C, &, Bachand F, (2009) Cotranscriptional recruitment of the nuclear poly(A)-binding protein Pab2 to nascent transcripts and association with translating mRNPs. Nucleic Acids Res 37, 3418-3430.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3418-3430
    • Lemieux, C.1    Bachand, F.2
  • 45
    • 34147145820 scopus 로고    scopus 로고
    • Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast
    • Perreault A, Lemieux C, &, Bachand F, (2007) Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast. J Biol Chem 282, 7552-7562.
    • (2007) J Biol Chem , vol.282 , pp. 7552-7562
    • Perreault, A.1    Lemieux, C.2    Bachand, F.3
  • 46
    • 73649112807 scopus 로고    scopus 로고
    • The nuclear poly(A)-binding protein interacts with the exosome to promote synthesis of noncoding small nucleolar RNAs
    • Lemay JF, D'Amours A, Lemieux C, Lackner DH, St-Sauveur VG, Bahler J, &, Bachand F, (2010) The nuclear poly(A)-binding protein interacts with the exosome to promote synthesis of noncoding small nucleolar RNAs. Mol Cell 37, 34-45.
    • (2010) Mol Cell , vol.37 , pp. 34-45
    • Lemay, J.F.1    D'Amours, A.2    Lemieux, C.3    Lackner, D.H.4    St-Sauveur, V.G.5    Bahler, J.6    Bachand, F.7
  • 47
    • 84873424140 scopus 로고    scopus 로고
    • A proline-tyrosine nuclear localization signal (Py-Nls) is required for the nuclear import of fission yeast pab2, but not of human pabpn1
    • Mallet PL, &, Bachand F, (2012) A proline-tyrosine nuclear localization signal (Py-Nls) is required for the nuclear import of fission yeast pab2, but not of human pabpn1. Traffic 14, 282-294.
    • (2012) Traffic , vol.14 , pp. 282-294
    • Mallet, P.L.1    Bachand, F.2
  • 48
    • 80053597137 scopus 로고    scopus 로고
    • A pre-mRNA degradation pathway that selectively targets intron-containing genes requires the nuclear poly(A)-binding protein
    • Lemieux C, Marguerat S, Lafontaine J, Barbezier N, Bahler J, &, Bachand F, (2011) A pre-mRNA degradation pathway that selectively targets intron-containing genes requires the nuclear poly(A)-binding protein. Mol Cell 44, 108-119.
    • (2011) Mol Cell , vol.44 , pp. 108-119
    • Lemieux, C.1    Marguerat, S.2    Lafontaine, J.3    Barbezier, N.4    Bahler, J.5    Bachand, F.6
  • 49
    • 77956248052 scopus 로고    scopus 로고
    • Negative regulation of meiotic gene expression by the nuclear poly(A)-binding protein in fission yeast
    • St-Andre O, Lemieux C, Perreault A, Lackner DH, Bahler J, &, Bachand F, (2010) Negative regulation of meiotic gene expression by the nuclear poly(A)-binding protein in fission yeast. J Biol Chem 285, 27859-27868.
    • (2010) J Biol Chem , vol.285 , pp. 27859-27868
    • St-Andre, O.1    Lemieux, C.2    Perreault, A.3    Lackner, D.H.4    Bahler, J.5    Bachand, F.6
  • 50
    • 77954959806 scopus 로고    scopus 로고
    • Importance of polyadenylation in the selective elimination of meiotic mRNAs in growing S. Pombe cells
    • Yamanaka S, Yamashita A, Harigaya Y, Iwata R, &, Yamamoto M, (2010) Importance of polyadenylation in the selective elimination of meiotic mRNAs in growing S. pombe cells. EMBO J 29, 2173-2181.
    • (2010) EMBO J , vol.29 , pp. 2173-2181
    • Yamanaka, S.1    Yamashita, A.2    Harigaya, Y.3    Iwata, R.4    Yamamoto, M.5
  • 52
    • 79952514373 scopus 로고    scopus 로고
    • The type II poly(A)-binding protein PABP-2 genetically interacts with the let-7 miRNA and elicits heterochronic phenotypes in Caenorhabditis elegans
    • Hurschler BA, Harris DT, &, Grosshans H, (2011) The type II poly(A)-binding protein PABP-2 genetically interacts with the let-7 miRNA and elicits heterochronic phenotypes in Caenorhabditis elegans. Nucleic Acids Res 39, 5647-5657.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5647-5657
    • Hurschler, B.A.1    Harris, D.T.2    Grosshans, H.3
  • 53
    • 0033214213 scopus 로고    scopus 로고
    • The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitro
    • Benoit B, Nemeth A, Aulner N, Kuhn U, Simonelig M, Wahle E, &, Bourbon HM, (1999) The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitro. Nucleic Acids Res 27, 3771-3778.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3771-3778
    • Benoit, B.1    Nemeth, A.2    Aulner, N.3    Kuhn, U.4    Simonelig, M.5    Wahle, E.6    Bourbon, H.M.7
  • 54
    • 0018865908 scopus 로고
    • Nuclear inclusions in oculopharyngeal dystrophy
    • Tome FM, &, Fardeau M, (1980) Nuclear inclusions in oculopharyngeal dystrophy. Acta Neuropathol 49, 85-87.
    • (1980) Acta Neuropathol , vol.49 , pp. 85-87
    • Tome, F.M.1    Fardeau, M.2
  • 55
    • 0032824836 scopus 로고    scopus 로고
    • Polyglutamine diseases: Protein cleavage and aggregation
    • Zoghbi HY, &, Orr HT, (1999) Polyglutamine diseases: protein cleavage and aggregation. Curr Opin Neurobiol 9, 566-570.
    • (1999) Curr Opin Neurobiol , vol.9 , pp. 566-570
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 56
    • 8444221584 scopus 로고    scopus 로고
    • A polyalanine tract expansion in Arx forms intranuclear inclusions and results in increased cell death
    • Nasrallah IM, Minarcik JC, &, Golden JA, (2004) A polyalanine tract expansion in Arx forms intranuclear inclusions and results in increased cell death. J Cell Biol 167, 411-416.
    • (2004) J Cell Biol , vol.167 , pp. 411-416
    • Nasrallah, I.M.1    Minarcik, J.C.2    Golden, J.A.3
  • 57
    • 10844222804 scopus 로고    scopus 로고
    • A recurrent polyalanine expansion in the transcription factor FOXL2 induces extensive nuclear and cytoplasmic protein aggregation
    • Caburet S, Demarez A, Moumne L, Fellous M, De Baere E, &, Veitia RA, (2004) A recurrent polyalanine expansion in the transcription factor FOXL2 induces extensive nuclear and cytoplasmic protein aggregation. J Med Gene 41, 932-936.
    • (2004) J Med Gene , vol.41 , pp. 932-936
    • Caburet, S.1    Demarez, A.2    Moumne, L.3    Fellous, M.4    De Baere, E.5    Veitia, R.A.6
  • 58
    • 0344845146 scopus 로고    scopus 로고
    • Trinucleotide expansions leading to an extended poly-L-alanine segment in the poly (A) binding protein PABPN1 cause fibril formation
    • Scheuermann T, Schulz B, Blume A, Wahle E, Rudolph R, &, Schwarz E, (2003) Trinucleotide expansions leading to an extended poly-L-alanine segment in the poly (A) binding protein PABPN1 cause fibril formation. Protein Sci 12, 2685-2692.
    • (2003) Protein Sci , vol.12 , pp. 2685-2692
    • Scheuermann, T.1    Schulz, B.2    Blume, A.3    Wahle, E.4    Rudolph, R.5    Schwarz, E.6
  • 59
    • 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
    • Lodderstedt G, Hess S, Hause G, Scheuermann T, Scheibel T, &, Schwarz E, (2007) Effect of oculopharyngeal muscular dystrophy-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1. FEBS J 274, 346-355.
    • (2007) FEBS J , vol.274 , pp. 346-355
    • Lodderstedt, G.1    Hess, S.2    Hause, G.3    Scheuermann, T.4    Scheibel, T.5    Schwarz, E.6
  • 60
    • 84863306240 scopus 로고    scopus 로고
    • Polyalanine-independent conformational conversion of nuclear poly(A)-binding protein 1 (PABPN1)
    • Winter R, Kuhn U, Hause G, &, Schwarz E, (2012) Polyalanine- independent conformational conversion of nuclear poly(A)-binding protein 1 (PABPN1). J Biol Chem 287, 22662-22671.
    • (2012) J Biol Chem , vol.287 , pp. 22662-22671
    • Winter, R.1    Kuhn, U.2    Hause, G.3    Schwarz, E.4
  • 61
    • 17844369724 scopus 로고    scopus 로고
    • In vivo aggregation properties of the nuclear poly(A)-binding protein PABPN1
    • Tavanez JP, Calado P, Braga J, Lafarga M, &, Carmo-Fonseca M, (2005) In vivo aggregation properties of the nuclear poly(A)-binding protein PABPN1. RNA 11, 752-762.
    • (2005) RNA , vol.11 , pp. 752-762
    • Tavanez, J.P.1    Calado, P.2    Braga, J.3    Lafarga, M.4    Carmo-Fonseca, M.5
  • 62
    • 0033768247 scopus 로고    scopus 로고
    • PABP2 polyalanine tract expansion causes intranuclear inclusions in oculopharyngeal muscular dystrophy
    • Shanmugam V, Dion P, Rochefort D, Laganiere J, Brais B, &, Rouleau GA, (2000) PABP2 polyalanine tract expansion causes intranuclear inclusions in oculopharyngeal muscular dystrophy. Ann Neurol 48, 798-802.
    • (2000) Ann Neurol , vol.48 , pp. 798-802
    • Shanmugam, V.1    Dion, P.2    Rochefort, D.3    Laganiere, J.4    Brais, B.5    Rouleau, G.A.6
  • 63
    • 0142185364 scopus 로고    scopus 로고
    • Involvement of the ubiquitin-proteasome pathway and molecular chaperones in oculopharyngeal muscular dystrophy
    • Abu-Baker A, Messaed C, Laganiere J, Gaspar C, Brais B, &, Rouleau GA, (2003) Involvement of the ubiquitin-proteasome pathway and molecular chaperones in oculopharyngeal muscular dystrophy. Human Mol Genet 12, 2609-2623.
    • (2003) Human Mol Genet , vol.12 , pp. 2609-2623
    • Abu-Baker, A.1    Messaed, C.2    Laganiere, J.3    Gaspar, C.4    Brais, B.5    Rouleau, G.A.6
  • 64
    • 30144442961 scopus 로고    scopus 로고
    • Ectopic expression of a polyalanine expansion mutant of poly(A)-binding protein N1 in muscle cells in culture inhibits myogenesis
    • Wang Q, &, Bag J, (2006) Ectopic expression of a polyalanine expansion mutant of poly(A)-binding protein N1 in muscle cells in culture inhibits myogenesis. Biochem Biophys Res Commun 340, 815-822.
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 815-822
    • Wang, Q.1    Bag, J.2
  • 65
    • 68149091769 scopus 로고    scopus 로고
    • Hsp70 chaperones and type i PRMTs are sequestered at intranuclear inclusions caused by polyalanine expansions in PABPN1
    • Tavanez JP, Bengoechea R, Berciano MT, Lafarga M, Carmo-Fonseca M, &, Enguita FJ, (2009) Hsp70 chaperones and type I PRMTs are sequestered at intranuclear inclusions caused by polyalanine expansions in PABPN1. PLoS ONE 4, e6418.
    • (2009) PLoS ONE , vol.4
    • Tavanez, J.P.1    Bengoechea, R.2    Berciano, M.T.3    Lafarga, M.4    Carmo-Fonseca, M.5    Enguita, F.J.6
  • 66
    • 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, Tome FM, Brais B, Rouleau GA, Kuhn U, Wahle E, &, Carmo-Fonseca M, (2000) Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Human Mol Genet 9, 2321-2328.
    • (2000) Human Mol Genet , vol.9 , pp. 2321-2328
    • Calado, A.1    Tome, F.M.2    Brais, B.3    Rouleau, G.A.4    Kuhn, U.5    Wahle, E.6    Carmo-Fonseca, M.7
  • 69
    • 0037023781 scopus 로고    scopus 로고
    • Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy
    • Bao YP, Cook LJ, O'Donovan D, Uyama E, &, Rubinsztein DC, (2002) Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy. J Biol Chem 277, 12263-12269.
    • (2002) J Biol Chem , vol.277 , pp. 12263-12269
    • Bao, Y.P.1    Cook, L.J.2    O'Donovan, D.3    Uyama, E.4    Rubinsztein, D.C.5
  • 71
    • 23844440597 scopus 로고    scopus 로고
    • Cytoplasmic targeting of mutant poly(A)-binding protein nuclear 1 suppresses protein aggregation and toxicity in oculopharyngeal muscular dystrophy
    • Abu-Baker A, Laganiere S, Fan X, Laganiere J, Brais B, &, Rouleau GA, (2005) Cytoplasmic targeting of mutant poly(A)-binding protein nuclear 1 suppresses protein aggregation and toxicity in oculopharyngeal muscular dystrophy. Traffic 6, 766-779.
    • (2005) Traffic , vol.6 , pp. 766-779
    • Abu-Baker, A.1    Laganiere, S.2    Fan, X.3    Laganiere, J.4    Brais, B.5    Rouleau, G.A.6
  • 72
    • 84865082575 scopus 로고    scopus 로고
    • Expression of the poly alanine expansion mutatant of nuclear poly (A) binding protein induces apoptosis via the p53 pathway
    • Bhattacharjee RB, Zannat T, &, Bag J, (2012) Expression of the poly alanine expansion mutatant of nuclear poly (A) binding protein induces apoptosis via the p53 pathway. Cell Biol Int 36, 697-704.
    • (2012) Cell Biol Int , vol.36 , pp. 697-704
    • Bhattacharjee, R.B.1    Zannat, T.2    Bag, J.3
  • 73
    • 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, &, Rubinsztein DC, (2004) Congo red, doxycycline, and HSP70 overexpression reduce aggregate formation and cell death in cell models of oculopharyngeal muscular dystrophy. J Med Genet 41, 47-51.
    • (2004) J Med Genet , vol.41 , pp. 47-51
    • Bao, Y.P.1    Sarkar, S.2    Uyama, E.3    Rubinsztein, D.C.4
  • 74
    • 78651254160 scopus 로고    scopus 로고
    • P53 activation mediates polyglutamine-expanded ataxin-3 upregulation of Bax expression in cerebellar and pontine nuclei neurons
    • Chou AH, Lin AC, Hong KY, Hu SH, Chen YL, Chen JY, &, Wang HL, (2011) p53 activation mediates polyglutamine-expanded ataxin-3 upregulation of Bax expression in cerebellar and pontine nuclei neurons. Neurochem Int 58, 145-152.
    • (2011) Neurochem Int , vol.58 , pp. 145-152
    • Chou, A.H.1    Lin, A.C.2    Hong, K.Y.3    Hu, S.H.4    Chen, Y.L.5    Chen, J.Y.6    Wang, H.L.7
  • 76
    • 29644437591 scopus 로고    scopus 로고
    • Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy
    • Davies JE, Sarkar S, &, Rubinsztein DC, (2006) Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy. Human Mol Genet 15, 23-31.
    • (2006) Human Mol Genet , vol.15 , pp. 23-31
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 77
    • 0029364173 scopus 로고
    • Determination versus differentiation and the MyoD family of transcription factors
    • Megeney LA, &, Rudnicki MA, (1995) Determination versus differentiation and the MyoD family of transcription factors. Biochem Cell Biol 73, 723-732.
    • (1995) Biochem Cell Biol , vol.73 , pp. 723-732
    • Megeney, L.A.1    Rudnicki, M.A.2
  • 81
    • 77953586729 scopus 로고    scopus 로고
    • Molecular and phenotypic characterization of a mouse model of oculopharyngeal muscular dystrophy reveals severe muscular atrophy restricted to fast glycolytic fibres
    • Trollet C, Anvar SY, Venema A, Hargreaves IP, Foster K, Vignaud A, Ferry A, Negroni E, Hourde C, Baraibar MA, et al,. (2010) Molecular and phenotypic characterization of a mouse model of oculopharyngeal muscular dystrophy reveals severe muscular atrophy restricted to fast glycolytic fibres. Human Mol Genet 19, 2191-2207.
    • (2010) Human Mol Genet , vol.19 , pp. 2191-2207
    • Trollet, C.1    Anvar, S.Y.2    Venema, A.3    Hargreaves, I.P.4    Foster, K.5    Vignaud, A.6    Ferry, A.7    Negroni, E.8    Hourde, C.9    Baraibar, M.A.10
  • 83
    • 77952552967 scopus 로고    scopus 로고
    • Cross-talk between canonical Wnt signaling and the sirtuin-FoxO longevity pathway to protect against muscular pathology induced by mutant PABPN1 expression in C. Elegans
    • Pasco MY, Catoire H, Parker JA, Brais B, Rouleau GA, &, Neri C, (2010) Cross-talk between canonical Wnt signaling and the sirtuin-FoxO longevity pathway to protect against muscular pathology induced by mutant PABPN1 expression in C. elegans. Neurobiol Dis 38, 425-433.
    • (2010) Neurobiol Dis , vol.38 , pp. 425-433
    • Pasco, M.Y.1    Catoire, H.2    Parker, J.A.3    Brais, B.4    Rouleau, G.A.5    Neri, C.6
  • 84
    • 33646768641 scopus 로고    scopus 로고
    • A Drosophila model of oculopharyngeal muscular dystrophy reveals intrinsic toxicity of PABPN1
    • Chartier A, Benoit B, &, Simonelig M, (2006) A Drosophila model of oculopharyngeal muscular dystrophy reveals intrinsic toxicity of PABPN1. EMBO J 25, 2253-2262.
    • (2006) EMBO J , vol.25 , pp. 2253-2262
    • Chartier, A.1    Benoit, B.2    Simonelig, M.3
  • 85
    • 65449169579 scopus 로고    scopus 로고
    • Prevention of oculopharyngeal muscular dystrophy by muscular expression of Llama single-chain intrabodies in vivo
    • Chartier A, Raz V, Sterrenburg E, Verrips CT, van der Maarel SM, &, Simonelig M, (2009) Prevention of oculopharyngeal muscular dystrophy by muscular expression of Llama single-chain intrabodies in vivo. Human Mol Genet 18, 1849-1859.
    • (2009) Human Mol Genet , vol.18 , pp. 1849-1859
    • Chartier, A.1    Raz, V.2    Sterrenburg, E.3    Verrips, C.T.4    Van Der Maarel, S.M.5    Simonelig, M.6
  • 87
    • 20944432778 scopus 로고    scopus 로고
    • Doxycycline attenuates and delays toxicity of the oculopharyngeal muscular dystrophy mutation in transgenic mice
    • Davies JE, Wang L, Garcia-Oroz L, Cook LJ, Vacher C, O'Donovan DG, &, Rubinsztein DC, (2005) Doxycycline attenuates and delays toxicity of the oculopharyngeal muscular dystrophy mutation in transgenic mice. Nat Med 11, 672-677.
    • (2005) Nat Med , vol.11 , pp. 672-677
    • Davies, J.E.1    Wang, L.2    Garcia-Oroz, L.3    Cook, L.J.4    Vacher, C.5    O'Donovan, D.G.6    Rubinsztein, D.C.7
  • 88
    • 77955617537 scopus 로고    scopus 로고
    • Cystamine suppresses polyalanine toxicity in a mouse model of oculopharyngeal muscular dystrophy
    • Davies JE, Rose C, Sarkar S, &, Rubinsztein DC, (2010) Cystamine suppresses polyalanine toxicity in a mouse model of oculopharyngeal muscular dystrophy. Sci Translational Med 2, 34ra40.
    • (2010) Sci Translational Med , vol.2
    • Davies, J.E.1    Rose, C.2    Sarkar, S.3    Rubinsztein, D.C.4
  • 89
    • 84856141914 scopus 로고    scopus 로고
    • Myoblast fusion: Lessons from flies and mice
    • Abmayr SM, &, Pavlath GK, (2012) Myoblast fusion: lessons from flies and mice. Development 139, 641-656.
    • (2012) Development , vol.139 , pp. 641-656
    • Abmayr, S.M.1    Pavlath, G.K.2
  • 90
    • 0001940779 scopus 로고    scopus 로고
    • In C. elegans II 2nd edition (Riddle D.L. Blumenthal T. Meyer B.J. et al., eds), Chapter 1. Cold Spring Harbor Laboratory. CSHL Press, New York
    • Riddle DL, Blumenthal T, Meyer BJ, &, Priess JR, (1997) Introduction to C. elegans. In C. elegans II 2nd edition (, Riddle DL, Blumenthal T, Meyer BJ, et al., eds), Chapter 1. Cold Spring Harbor Laboratory. CSHL Press, New York.
    • (1997) Introduction to C. Elegans
    • Riddle, D.L.1    Blumenthal, T.2    Meyer, B.J.3    Priess, J.R.4
  • 93
    • 0036135243 scopus 로고    scopus 로고
    • Neurogenic involvement in a case of oculopharyngeal muscular dystrophy
    • Boukriche Y, Maisonobe T, &, Masson C, (2002) Neurogenic involvement in a case of oculopharyngeal muscular dystrophy. Muscle Nerve 25, 98-101.
    • (2002) Muscle Nerve , vol.25 , pp. 98-101
    • Boukriche, Y.1    Maisonobe, T.2    Masson, C.3
  • 94
    • 0035068493 scopus 로고    scopus 로고
    • Unusual triplet expansion associated with neurogenic changes in a family with oculopharyngeal muscular dystrophy
    • Schober R, Kress W, Grahmann F, Kellermann S, Baum P, Gunzel S, &, Wagner A, (2001) Unusual triplet expansion associated with neurogenic changes in a family with oculopharyngeal muscular dystrophy. Neuropathology 21, 45-52.
    • (2001) Neuropathology , vol.21 , pp. 45-52
    • Schober, R.1    Kress, W.2    Grahmann, F.3    Kellermann, S.4    Baum, P.5    Gunzel, S.6    Wagner, A.7
  • 96
    • 84862583612 scopus 로고    scopus 로고
    • Executive functions are impaired in heterozygote patients with oculopharyngeal muscular dystrophy
    • Dubbioso R, Moretta P, Manganelli F, Fiorillo C, Iodice R, Trojano L, &, Santoro L, (2012) Executive functions are impaired in heterozygote patients with oculopharyngeal muscular dystrophy. J Neurol 259, 833-837.
    • (2012) J Neurol , vol.259 , pp. 833-837
    • Dubbioso, R.1    Moretta, P.2    Manganelli, F.3    Fiorillo, C.4    Iodice, R.5    Trojano, L.6    Santoro, L.7
  • 98
    • 41949116233 scopus 로고    scopus 로고
    • Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation
    • Davies JE, Sarkar S, &, Rubinsztein DC, (2008) Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation. Human Mol Genet 17, 1097-1108.
    • (2008) Human Mol Genet , vol.17 , pp. 1097-1108
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 99
    • 79960120588 scopus 로고    scopus 로고
    • Oculopharyngeal muscle dystrophy: Fine structure and mRNA expression levels of PABPN1
    • Schroder JM, Klossok T, &, Weis J, (2011) Oculopharyngeal muscle dystrophy: fine structure and mRNA expression levels of PABPN1. Clin Neuropathol 30, 94-103.
    • (2011) Clin Neuropathol , vol.30 , pp. 94-103
    • Schroder, J.M.1    Klossok, T.2    Weis, J.3
  • 100
    • 33750440221 scopus 로고    scopus 로고
    • Premature proliferative arrest of cricopharyngeal myoblasts in oculo-pharyngeal muscular dystrophy: Therapeutic perspectives of autologous myoblast transplantation
    • Perie S, Mamchaoui K, Mouly V, Blot S, Bouazza B, Thornell LE, St Guily JL, &, Butler-Browne G, (2006) Premature proliferative arrest of cricopharyngeal myoblasts in oculo-pharyngeal muscular dystrophy: therapeutic perspectives of autologous myoblast transplantation. Neuromuscul Disord 16, 770-781.
    • (2006) Neuromuscul Disord , vol.16 , pp. 770-781
    • Perie, S.1    Mamchaoui, K.2    Mouly, V.3    Blot, S.4    Bouazza, B.5    Thornell, L.E.6    St Guily, J.L.7    Butler-Browne, G.8
  • 102
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, &, Poirier MA, (2004) Protein aggregation and neurodegenerative disease. Nat Med 10 (Suppl), S10-S17.
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 105
    • 1942485876 scopus 로고    scopus 로고
    • Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus
    • Berciano MT, Villagra NT, Ojeda JL, Navascues J, Gomes A, Lafarga M, &, Carmo-Fonseca M, (2004) Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus. Human Mol Genet 13, 829-838.
    • (2004) Human Mol Genet , vol.13 , 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
  • 107
    • 0033614768 scopus 로고    scopus 로고
    • Evidence for a recruitment and sequestration mechanism in Huntington's disease
    • Preisinger E, Jordan BM, Kazantsev A, &, Housman D, (1999) Evidence for a recruitment and sequestration mechanism in Huntington's disease. Phil Trans R Soc Lond 354, 1029-1034.
    • (1999) Phil Trans R Soc Lond , vol.354 , pp. 1029-1034
    • Preisinger, E.1    Jordan, B.M.2    Kazantsev, A.3    Housman, D.4
  • 109
    • 0035884587 scopus 로고    scopus 로고
    • The mouse Hoxd13(spdh) mutation, a polyalanine expansion similar to human type II synpolydactyly (SPD), disrupts the function but not the expression of other Hoxd genes
    • Bruneau S, Johnson KR, Yamamoto M, Kuroiwa A, &, Duboule D, (2001) The mouse Hoxd13(spdh) mutation, a polyalanine expansion similar to human type II synpolydactyly (SPD), disrupts the function but not the expression of other Hoxd genes. Develop Biol 237, 345-353.
    • (2001) Develop Biol , vol.237 , pp. 345-353
    • Bruneau, S.1    Johnson, K.R.2    Yamamoto, M.3    Kuroiwa, A.4    Duboule, D.5
  • 110
    • 84858155192 scopus 로고    scopus 로고
    • Nuclear speckles are involved in nuclear aggregation of PABPN1 and in the pathophysiology of oculopharyngeal muscular dystrophy
    • Bengoechea R, Tapia O, Casafont I, Berciano J, Lafarga M, &, Berciano MT, (2012) Nuclear speckles are involved in nuclear aggregation of PABPN1 and in the pathophysiology of oculopharyngeal muscular dystrophy. Neurobiol Dis 46, 118-129.
    • (2012) Neurobiol Dis , vol.46 , pp. 118-129
    • Bengoechea, R.1    Tapia, O.2    Casafont, I.3    Berciano, J.4    Lafarga, M.5    Berciano, M.T.6
  • 111
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, &, Greenberg ME, (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 115
    • 25444478907 scopus 로고    scopus 로고
    • Aging, stem cells and tissue regeneration: Lessons from muscle
    • Conboy IM, &, Rando TA, (2005) Aging, stem cells and tissue regeneration: lessons from muscle. Cell Cycle 4, 407-410.
    • (2005) Cell Cycle , vol.4 , pp. 407-410
    • Conboy, I.M.1    Rando, T.A.2
  • 118
    • 33645814876 scopus 로고    scopus 로고
    • Distinctive morphological and gene/protein expression signatures during myogenesis in novel cell lines from extraocular and hindlimb muscle
    • Porter JD, Israel S, Gong B, Merriam AP, Feuerman J, Khanna S, &, Kaminski HJ, (2006) Distinctive morphological and gene/protein expression signatures during myogenesis in novel cell lines from extraocular and hindlimb muscle. Physiol Genomics 24, 264-275.
    • (2006) Physiol Genomics , vol.24 , pp. 264-275
    • Porter, J.D.1    Israel, S.2    Gong, B.3    Merriam, A.P.4    Feuerman, J.5    Khanna, S.6    Kaminski, H.J.7
  • 119
    • 0031881052 scopus 로고    scopus 로고
    • Heterogeneity among muscle precursor cells in adult skeletal muscles with differing regenerative capacities
    • Pavlath GK, Thaloor D, Rando TA, Cheong M, English AW, &, Zheng B, (1998) Heterogeneity among muscle precursor cells in adult skeletal muscles with differing regenerative capacities. Develop Dynamics 212, 495-508.
    • (1998) Develop Dynamics , vol.212 , pp. 495-508
    • Pavlath, G.K.1    Thaloor, D.2    Rando, T.A.3    Cheong, M.4    English, A.W.5    Zheng, B.6
  • 120
    • 79957628666 scopus 로고    scopus 로고
    • An eye on the head: The development and evolution of craniofacial muscles
    • Sambasivan R, Kuratani S, &, Tajbakhsh S, (2011) An eye on the head: the development and evolution of craniofacial muscles. Development 138, 2401-2415.
    • (2011) Development , vol.138 , pp. 2401-2415
    • Sambasivan, R.1    Kuratani, S.2    Tajbakhsh, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.