메뉴 건너뛰기




Volumn 34, Issue 9, 2013, Pages 2235.e11-2235.e13

Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS

(14)  Ravenscroft, Thomas A a   Baker, Matt C a   Rutherford, Nicola J a   Neumann, Manuela b,c   Mackenzie, Ian R d   Josephs, Keith A e   Boeve, Bradley F e   Petersen, Ronald e   Halliday, Glenda M f,j   Kril, Jillian g   van Swieten, John C h,k   Seeley, William W i   Dickson, Dennis W a   Rademakers, Rosa a  


Author keywords

FET proteins; Frontotemporal lobar degeneration; FUS; PRMT1; PRMT3; PRMT8; Protein N arginine methyltransferase

Indexed keywords

FUSED IN SARCOMA PROTEIN; MESSENGER RNA; SYNAPTOPHYSIN;

EID: 84878943012     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2013.04.004     Document Type: Article
Times cited : (11)

References (19)
  • 1
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-beta s: recognition and inhibition
    • Chook Y.M., Suel K.E. Nuclear import by karyopherin-beta s: recognition and inhibition. Biochim. Biophys. Acta. Mol. Cell Res. 2011, 1813:1593-1606.
    • (2011) Biochim. Biophys. Acta. Mol. Cell Res. , vol.1813 , pp. 1593-1606
    • Chook, Y.M.1    Suel, K.E.2
  • 3
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
    • Jobert L., Argentini M., Tora L. PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function. Exp. Cell Res. 2009, 315:1273-1286.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1273-1286
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 5
    • 53049097189 scopus 로고    scopus 로고
    • EWS is a substrate of type I protein arginine methyltransferase, PRMT8
    • Kim J.D., Kako K., Kakiuchi M., Park G.G., Fukamizu A. EWS is a substrate of type I protein arginine methyltransferase, PRMT8. Int. J. Mol. Med. 2008, 22:309-315.
    • (2008) Int. J. Mol. Med. , vol.22 , pp. 309-315
    • Kim, J.D.1    Kako, K.2    Kakiuchi, M.3    Park, G.G.4    Fukamizu, A.5
  • 7
    • 84862149527 scopus 로고    scopus 로고
    • FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis
    • Mackenzie I.R.A., Neumann M. FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis. Brain Res. 2012, 1462:40-43.
    • (2012) Brain Res. , vol.1462 , pp. 40-43
    • Mackenzie, I.R.A.1    Neumann, M.2
  • 8
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie I.R.A., Rademakers R., Neumann M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurology 2010, 9:995-1007.
    • (2010) Lancet Neurology , vol.9 , pp. 995-1007
    • Mackenzie, I.R.A.1    Rademakers, R.2    Neumann, M.3
  • 12
    • 24344468254 scopus 로고    scopus 로고
    • Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing sarcoma protein and a peptide
    • Pahlich S., Bschir K., Chiavi C., Belyanskaya L., Gehring H. Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing sarcoma protein and a peptide. Proteins Struct. Function Bioinform. 2005, 61:164-175.
    • (2005) Proteins Struct. Function Bioinform. , vol.61 , pp. 164-175
    • Pahlich, S.1    Bschir, K.2    Chiavi, C.3    Belyanskaya, L.4    Gehring, H.5
  • 17
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • Tradewell M.L., Yu Z.B., Tibshirani M., Boulanger M.C., Durham H.D., Richard S. Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum Mol Genet. 2012, 21:136-149.
    • (2012) Hum Mol Genet. , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.B.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.