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Volumn 19, Issue 2, 2013, Pages 129-140

Neurodegenerative diseases: Quantitative predictions of protein-RNA interactions

Author keywords

Autogenous regulation; Neurodegeneration; Noncoding RNA; Protein RNA interactions; RNA aptamers

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; FRAGILE X MENTAL RETARDATION PROTEIN; TAR DNA BINDING PROTEIN;

EID: 84872525680     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.034777.112     Document Type: Article
Times cited : (59)

References (55)
  • 1
    • 84871806618 scopus 로고    scopus 로고
    • X-inactivation: Quantitative predictions of protein interactions in the Xist network
    • doi: 10.1093/nar/gks968
    • Agostini F, Cirillo D, Bolognesi B, Tartaglia GG. 2012. X-inactivation: Quantitative predictions of protein interactions in the Xist network. Nucleic Acids Res doi: 10.1093/nar/gks968.
    • (2012) Nucleic Acids Res
    • Agostini, F.1    Cirillo, D.2    Bolognesi, B.3    Tartaglia, G.G.4
  • 2
    • 77952581425 scopus 로고    scopus 로고
    • Aberrant RNA processing events in neurological disorders
    • Anthony K, Gallo J-M. 2010. Aberrant RNA processing events in neurological disorders. Brain Res 1338: 67-77.
    • (2010) Brain Res , vol.1338 , pp. 67-77
    • Anthony, K.1    Gallo, J.-M.2
  • 6
  • 7
    • 33646063185 scopus 로고    scopus 로고
    • Dopamine transporter immunoreactivity in peripheral blood mononuclear cells in amyotrophic lateral sclerosis
    • Buttarelli FR, Circella A, Pellicano C, Pontieri FE. 2006. Dopamine transporter immunoreactivity in peripheral blood mononuclear cells in amyotrophic lateral sclerosis. Eur J Neurol 13: 416-418.
    • (2006) Eur J Neurol , vol.13 , pp. 416-418
    • Buttarelli, F.R.1    Circella, A.2    Pellicano, C.3    Pontieri, F.E.4
  • 8
    • 77950867149 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 in neurodegenerative disease
    • Chen-Plotkin AS, Lee VM-Y, Trojanowski JQ. 2010. TAR DNA-binding protein 43 in neurodegenerative disease. Nat Rev Neurol 6: 211-220.
    • (2010) Nat Rev Neurol , vol.6 , pp. 211-220
    • Chen-Plotkin, A.S.1    Vm-Y, L.2    Trojanowski, J.Q.3
  • 9
    • 77957771842 scopus 로고    scopus 로고
    • Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1
    • Cho H-H, Cahill CM, Vanderburg CR, Scherzer CR, Wang B, Huang X, Rogers JT. 2010. Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1. J Biol Chem 285: 31217-31232.
    • (2010) J Biol Chem , vol.285 , pp. 31217-31232
    • Cho, H.-H.1    Cahill, C.M.2    Vanderburg, C.R.3    Scherzer, C.R.4    Wang, B.5    Huang, X.6    Rogers, J.T.7
  • 10
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • Darnell JC, Jensen KB, Jin P, Brown V, Warren ST, Darnell RB. 2001. Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell 107: 489-499.
    • (2001) Cell , vol.107 , pp. 489-499
    • Darnell, J.C.1    Jensen, K.B.2    Jin, P.3    Brown, V.4    Warren, S.T.5    Darnell, R.B.6
  • 11
    • 17444384228 scopus 로고    scopus 로고
    • Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes
    • Darnell JC, Fraser CE, Mostovetsky O, Stefani G, Jones TA, Eddy SR, Darnell RB. 2005. Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes. Genes Dev 19: 903-918.
    • (2005) Genes Dev , vol.19 , pp. 903-918
    • Darnell, J.C.1    Fraser, C.E.2    Mostovetsky, O.3    Stefani, G.4    Jones, T.A.5    Eddy, S.R.6    Darnell, R.B.7
  • 12
    • 83055168319 scopus 로고    scopus 로고
    • A metabolomic and systems biology perspective on the brain of the fragile X syndrome mouse model
    • Davidovic L, Navratil V, Bonaccorso CM, Catania MV, Bardoni B, Dumas M-E. 2011. A metabolomic and systems biology perspective on the brain of the fragile X syndrome mouse model. Genome Res 21: 2190-2202.
    • (2011) Genome Res , vol.21 , pp. 2190-2202
    • Davidovic, L.1    Navratil, V.2    Bonaccorso, C.M.3    Catania, M.V.4    Bardoni, B.5    Dumas, M.-E.6
  • 13
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault NR, Lucassen RW, Supattapone S. 2003. RNA molecules stimulate prion protein conversion. Nature 425: 717-720.
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 14
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM. 1999. Protein misfolding, evolution and disease. Trends Biochem Sci 24: 329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 15
    • 80052968310 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Cellular functions and implications for neurodegeneration
    • Fiesel FC, Kahle PJ. 2011. TDP-43 and FUS/TLS: Cellular functions and implications for neurodegeneration. FEBS J 278: 3550-3568.
    • (2011) FEBS J , vol.278 , pp. 3550-3568
    • Fiesel, F.C.1    Kahle, P.J.2
  • 16
    • 80052136588 scopus 로고    scopus 로고
    • TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase 6
    • Fiesel FC, Schurr C, Weber SS, Kahle PJ. 2011. TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase 6. Mol Neurodegener 6: 64.
    • (2011) Mol Neurodegener , vol.6 , pp. 64
    • Fiesel, F.C.1    Schurr, C.2    Weber, S.S.3    Kahle, P.J.4
  • 17
    • 68349125007 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases
    • Geser F, Martinez-Lage M, Kwong LK, Lee VM-Y, Trojanowski JQ. 2009. Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases. J Neurol 256: 1205-1214.
    • (2009) J Neurol , vol.256 , pp. 1205-1214
    • Geser, F.1    Martinez-Lage, M.2    Kwong, L.K.3    Vm-Y, L.4    Trojanowski, J.Q.5
  • 18
    • 2342635196 scopus 로고    scopus 로고
    • The fragile-X premutation: A maturing perspective
    • Hagerman PJ, Hagerman RJ. 2004. The fragile-X premutation: A maturing perspective. Am J Hum Genet 74: 805-816.
    • (2004) Am J Hum Genet , vol.74 , pp. 805-816
    • Hagerman, P.J.1    Hagerman, R.J.2
  • 19
    • 0037115819 scopus 로고    scopus 로고
    • Identification of cellular mRNA targets for RNA-binding protein Sam68
    • Itoh M, Haga I, Li Q-H, Fujisawa J. 2002. Identification of cellular mRNA targets for RNA-binding protein Sam68. Nucleic Acids Res 30: 5452-5464.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5452-5464
    • Itoh, M.1    Haga, I.2    Li, Q.-H.3    Fujisawa, J.4
  • 20
    • 77957282325 scopus 로고    scopus 로고
    • Major vault protein forms complexes with hypoxia-inducible factor (HIF)-1α and reduces HIF-1α level in ACHN human renal adenocarcinoma cells
    • Iwashita K, Ikeda R, Takeda Y, Sumizawa T, Furukawa T, Yamaguchi T, Akiyama S, Yamada K. 2010. Major vault protein forms complexes with hypoxia-inducible factor (HIF)-1α and reduces HIF-1α level in ACHN human renal adenocarcinoma cells. Cancer Sci 101: 920-926.
    • (2010) Cancer Sci , vol.101 , pp. 920-926
    • Iwashita, K.1    Ikeda, R.2    Takeda, Y.3    Sumizawa, T.4    Furukawa, T.5    Yamaguchi, T.6    Akiyama, S.7    Yamada, K.8
  • 21
    • 34547681603 scopus 로고    scopus 로고
    • Pur α binds to rCGG repeats and modulates repeat- mediated neurodegeneration in a Drosophila model of Fragile X Tremor/Ataxia Syndrome
    • Jin P, Duan R, Qurashi A, Qin Y, Tian D, Rosser TC, Liu H, Feng Y, Warren ST. 2007. Pur α binds to rCGG repeats and modulates repeat- mediated neurodegeneration in a Drosophila model of Fragile X Tremor/Ataxia Syndrome. Neuron 55: 556-564.
    • (2007) Neuron , vol.55 , pp. 556-564
    • Jin, P.1    Duan, R.2    Qurashi, A.3    Qin, Y.4    Tian, D.5    Rosser, T.C.6    Liu, H.7    Feng, Y.8    Warren, S.T.9
  • 22
    • 0020340153 scopus 로고
    • Autogenous control: Ribosomal protein L10-L12 complex binds to the leader sequence of its mRNA
    • Johnsen M, Christensen T, Dennis PP, Fiil NP. 1982. Autogenous control: Ribosomal protein L10-L12 complex binds to the leader sequence of its mRNA. EMBO J 1: 999-1004.
    • (1982) EMBO J , vol.1 , pp. 999-1004
    • Johnsen, M.1    Christensen, T.2    Dennis, P.P.3    Fiil, N.P.4
  • 23
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, Gitler AD. 2009. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 284: 20329-20339.
    • (2009) J Biol Chem , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5    Gitler, A.D.6
  • 24
    • 0023003549 scopus 로고
    • Isolation and characterization of a novel ribonucleoprotein particle: Large structures contain a single species of small RNA
    • Kedersha NL, Rome LH. 1986. Isolation and characterization of a novel ribonucleoprotein particle: Large structures contain a single species of small RNA. J Cell Biol 103: 699-709.
    • (1986) J Cell Biol , vol.103 , pp. 699-709
    • Kedersha, N.L.1    Rome, L.H.2
  • 25
    • 0035394437 scopus 로고    scopus 로고
    • Reduced FMRP and increased FMR1 transcription is proportionally associated with CGG repeat number in intermediate-length and premutation carriers
    • Kenneson A, Zhang F, Hagedorn CH, Warren ST. 2001. Reduced FMRP and increased FMR1 transcription is proportionally associated with CGG repeat number in intermediate-length and premutation carriers. Hum Mol Genet 10: 1449-1454.
    • (2001) Hum Mol Genet , vol.10 , pp. 1449-1454
    • Kenneson, A.1    Zhang, F.2    Hagedorn, C.H.3    Warren, S.T.4
  • 27
    • 30344475200 scopus 로고    scopus 로고
    • Progress over the first decade of CASP experiments
    • Kryshtafovych A, Venclovas C, Fidelis K, Moult J. 2005. Progress over the first decade of CASP experiments. Proteins 61 (Suppl 7): 225-236.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 225-236
    • Kryshtafovych, A.1    Venclovas, C.2    Fidelis, K.3    Moult, J.4
  • 28
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • Lagier-Tourenne C, Cleveland DW. 2009. Rethinking ALS: The FUS about TDP-43. Cell 136: 1001-1004.
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 30
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee EB, Lee VM-Y, Trojanowski JQ. 2012. Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci 13: 38-50.
    • (2012) Nat Rev Neurosci , vol.13 , pp. 38-50
    • Lee, E.B.1    Vm-Y, L.2    Trojanowski, J.Q.3
  • 31
    • 33750322434 scopus 로고    scopus 로고
    • Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns
    • Mercey R, Lantier I, Maurel M-C, Grosclaude J, Lantier F, Marc D. 2006. Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Arch Virol 151: 2197-2214.
    • (2006) Arch Virol , vol.151 , pp. 2197-2214
    • Mercey, R.1    Lantier, I.2    Maurel, M.-C.3    Grosclaude, J.4    Lantier, F.5    Marc, D.6
  • 32
    • 63449129338 scopus 로고    scopus 로고
    • Physiological and pathological role of α-synuclein in Parkinson's disease through iron mediated oxidative stress; The role of a putative iron-responsive element
    • Olivares D, Huang X, Branden L, Greig NH, Rogers JT. 2009. Physiological and pathological role of α-synuclein in Parkinson's disease through iron mediated oxidative stress; The role of a putative iron-responsive element. Int J Mol Sci 10: 1226-1260.
    • (2009) Int J Mol Sci , vol.10 , pp. 1226-1260
    • Olivares, D.1    Huang, X.2    Branden, L.3    Greig, N.H.4    Rogers, J.T.5
  • 35
    • 0028276577 scopus 로고
    • The bifunctional iron-responsive element binding protein/cytosolic aconitase: The role of active- site residues in ligand binding and regulation
    • Philpott CC, Klausner RD, Rouault TA. 1994. The bifunctional iron-responsive element binding protein/cytosolic aconitase: The role of active- site residues in ligand binding and regulation. Proc Natl Acad Sci 91: 7321-7325.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 7321-7325
    • Philpott, C.C.1    Klausner, R.D.2    Rouault, T.A.3
  • 38
    • 0036918690 scopus 로고    scopus 로고
    • Reduced FMR1 mRNA translation efficiency in fragile X patients with premutations
    • Primerano B, Tassone F, Hagerman RJ, Hagerman P, Amaldi F, Bagni C. 2002. Reduced FMR1 mRNA translation efficiency in fragile X patients with premutations. RNA 8: 1482-1488.
    • (2002) RNA , vol.8 , pp. 1482-1488
    • Primerano, B.1    Tassone, F.2    Hagerman, R.J.3    Hagerman, P.4    Amaldi, F.5    Bagni, C.6
  • 42
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC. 2006. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443: 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 43
    • 84855991876 scopus 로고    scopus 로고
    • Non-coding RNAs with essential roles in neurodegenerative disorders
    • Salta E, De Strooper B. 2012. Non-coding RNAs with essential roles in neurodegenerative disorders. Lancet Neurol 11: 189-200.
    • (2012) Lancet Neurol , vol.11 , pp. 189-200
    • Salta, E.1    De Strooper, B.2
  • 44
    • 0035801393 scopus 로고    scopus 로고
    • The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif
    • Schaeffer C, Bardoni B, Mandel J-L, Ehresmann B, Ehresmann C, Moine H. 2001. The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif. EMBO J 20: 4803-4813.
    • (2001) EMBO J , vol.20 , pp. 4803-4813
    • Schaeffer, C.1    Bardoni, B.2    Mandel, J.-L.3    Ehresmann, B.4    Ehresmann, C.5    Moine, H.6
  • 46
    • 79952186027 scopus 로고    scopus 로고
    • Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion
    • Silva JL, Vieira TCRG, Gomes MPB, Rangel LP, Scapin SMN, Cordeiro Y. 2011. Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion. Methods 53: 306-317.
    • (2011) Methods , vol.53 , pp. 306-317
    • Silva, J.L.1    Vieira, T.C.R.G.2    Gomes, M.P.B.3    Rangel, L.P.4    Scapin, S.M.N.5    Cordeiro, Y.6
  • 49
    • 25844466604 scopus 로고    scopus 로고
    • Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
    • Tartaglia GG, Cavalli A, Pellarin R, Caflisch A. 2005. Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci 14: 2723-2734.
    • (2005) Protein Sci , vol.14 , pp. 2723-2734
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 51
    • 0034684031 scopus 로고    scopus 로고
    • Fragile X males with unmethylated, full mutation trinucleotide repeat expansions have elevated levels of FMR1 messenger RNA
    • Tassone F, Hagerman RJ, Loesch DZ, Lachiewicz A, Taylor AK, Hagerman PJ. 2000. Fragile X males with unmethylated, full mutation trinucleotide repeat expansions have elevated levels of FMR1 messenger RNA. Am J Med Genet 94: 232-236.
    • (2000) Am J Med Genet , vol.94 , pp. 232-236
    • Tassone, F.1    Hagerman, R.J.2    Loesch, D.Z.3    Lachiewicz, A.4    Taylor, A.K.5    Hagerman, P.J.6
  • 52
    • 80052185880 scopus 로고    scopus 로고
    • Accumulation of transactive response DNA binding protein 43 in mild cognitive impairment and Alzheimer disease
    • Tremblay C, St-Amour I, Schneider J, Bennett DA, Calon F. 2011. Accumulation of transactive response DNA binding protein 43 in mild cognitive impairment and Alzheimer disease. J Neuropathol Exp Neurol 70: 788-798.
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 788-798
    • Tremblay, C.1    St-Amour, I.2    Schneider, J.3    Bennett, D.A.4    Calon, F.5
  • 54
    • 33947195786 scopus 로고    scopus 로고
    • FMRP mediates mGluR5-dependent translation of amyloid precursor protein
    • Westmark CJ, Malter JS. 2007. FMRP mediates mGluR5-dependent translation of amyloid precursor protein. PLoS Biol 5: e52.
    • (2007) PLoS Biol , vol.5
    • Westmark, C.J.1    Malter, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.