메뉴 건너뛰기




Volumn 1802, Issue 11, 2010, Pages 1112-1117

Elevated CSF N-acetylaspartylglutamate suggests specific molecular diagnostic abnormalities in patients with white matter diseases

Author keywords

Biomarker; Leukodystrophy; N acetylaspartylglutamate; NMR spectroscopy; Pelizaeus Merzbacher disease

Indexed keywords

N ACETYLASPARTYLGLUTAMIC ACID;

EID: 77956652849     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2010.07.005     Document Type: Article
Times cited : (21)

References (22)
  • 1
    • 33748037039 scopus 로고    scopus 로고
    • Regulation of N-acetylaspartate and N-acetylaspartylglutamate biosynthesis by protein kinase activators
    • Arun P., Madhavarao C.N., Moffett J.R., Namboodiri M.A. Regulation of N-acetylaspartate and N-acetylaspartylglutamate biosynthesis by protein kinase activators. J. Neurochem. 2006, 98:2034-2042.
    • (2006) J. Neurochem. , vol.98 , pp. 2034-2042
    • Arun, P.1    Madhavarao, C.N.2    Moffett, J.R.3    Namboodiri, M.A.4
  • 4
    • 43549084841 scopus 로고    scopus 로고
    • Increased level of N-acetylaspartylglutamate (NAAG) in the CSF of a patient with Pelizaeus-Merzbacher-like disease due to mutation in the GJA12 gene
    • Sartori S., Burlina A.B., Salviati L., Trevisson E., Toldo I., Laverda A.M., Burlina A.P. Increased level of N-acetylaspartylglutamate (NAAG) in the CSF of a patient with Pelizaeus-Merzbacher-like disease due to mutation in the GJA12 gene. Eur. J. Paediatr. Neurol. 2008, 12:348-350.
    • (2008) Eur. J. Paediatr. Neurol. , vol.12 , pp. 348-350
    • Sartori, S.1    Burlina, A.B.2    Salviati, L.3    Trevisson, E.4    Toldo, I.5    Laverda, A.M.6    Burlina, A.P.7
  • 7
    • 62349126641 scopus 로고    scopus 로고
    • Invited article: an MRI-based approach to the diagnosis of white matter disorders
    • Schiffmann R., van der Knaap M.S. Invited article: an MRI-based approach to the diagnosis of white matter disorders. Neurology 2009, 72:750-759.
    • (2009) Neurology , vol.72 , pp. 750-759
    • Schiffmann, R.1    van der Knaap, M.S.2
  • 8
    • 0028239867 scopus 로고
    • X-linked spastic paraplegia and Pelizaeus-Merzbacher disease are allelic disorders at the proteolipid protein locus
    • Saugier-Veber P., Munnich A., Bonneau D., Rozet J.M., Le Merrer M., Gil R., Boespflug-Tanguy O. X-linked spastic paraplegia and Pelizaeus-Merzbacher disease are allelic disorders at the proteolipid protein locus. Nat. Genet. 1994, 6:257-262.
    • (1994) Nat. Genet. , vol.6 , pp. 257-262
    • Saugier-Veber, P.1    Munnich, A.2    Bonneau, D.3    Rozet, J.M.4    Le Merrer, M.5    Gil, R.6    Boespflug-Tanguy, O.7
  • 14
    • 0033914812 scopus 로고    scopus 로고
    • Functions of N-acetyl-l-aspartate and N-acetyl-l-aspartylglutamate in the vertebrate brain: role in glial cell-specific signaling
    • Baslow M.H. Functions of N-acetyl-l-aspartate and N-acetyl-l-aspartylglutamate in the vertebrate brain: role in glial cell-specific signaling. J. Neurochem. 2000, 75:453-459.
    • (2000) J. Neurochem. , vol.75 , pp. 453-459
    • Baslow, M.H.1
  • 15
    • 0034890751 scopus 로고    scopus 로고
    • Intraneuronal N-acetylaspartate supplies acetyl groups for myelin lipid synthesis: evidence for myelin-associated aspartoacylase
    • Chakraborty G., Mekala P., Yahya D., Wu G., Ledeen R.W. Intraneuronal N-acetylaspartate supplies acetyl groups for myelin lipid synthesis: evidence for myelin-associated aspartoacylase. J. Neurochem. 2001, 78:736-745.
    • (2001) J. Neurochem. , vol.78 , pp. 736-745
    • Chakraborty, G.1    Mekala, P.2    Yahya, D.3    Wu, G.4    Ledeen, R.W.5
  • 16
    • 67349110501 scopus 로고    scopus 로고
    • PLP1 gene duplication causes overexpression and alteration of the PLP/DM20 splicing balance in fibroblasts from Pelizaeus-Merzbacher disease patients
    • Regis S., Grossi S., Corsolini F., Biancheri R., Filocamo M. PLP1 gene duplication causes overexpression and alteration of the PLP/DM20 splicing balance in fibroblasts from Pelizaeus-Merzbacher disease patients. Biochim. Biophys. Acta 2009, 1792:548-554.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 548-554
    • Regis, S.1    Grossi, S.2    Corsolini, F.3    Biancheri, R.4    Filocamo, M.5
  • 17
    • 36749104299 scopus 로고    scopus 로고
    • A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease
    • Dhaunchak A.S., Nave K.A. A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. Proc. Natl Acad. Sci. USA 2007, 104:17813-17818.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 17813-17818
    • Dhaunchak, A.S.1    Nave, K.A.2
  • 18
    • 0036523094 scopus 로고    scopus 로고
    • Proteolipid protein gene modulates viability and phenotype of neurons
    • Boucher S.E., Cypher M.A., Carlock L.R., Skoff R.P. Proteolipid protein gene modulates viability and phenotype of neurons. J. Neurosci. 2002, 22:1772-1783.
    • (2002) J. Neurosci. , vol.22 , pp. 1772-1783
    • Boucher, S.E.1    Cypher, M.A.2    Carlock, L.R.3    Skoff, R.P.4
  • 19
    • 0027424792 scopus 로고
    • A proteolipid protein gene family: expression in sharks and rays and possible evolution from an ancestral gene encoding a pore-forming polypeptide
    • Kitagawa K., Sinoway M.P., Yang C., Gould R.M., Colman D.R. A proteolipid protein gene family: expression in sharks and rays and possible evolution from an ancestral gene encoding a pore-forming polypeptide. Neuron 1993, 11:433-448.
    • (1993) Neuron , vol.11 , pp. 433-448
    • Kitagawa, K.1    Sinoway, M.P.2    Yang, C.3    Gould, R.M.4    Colman, D.R.5
  • 20
    • 26944484034 scopus 로고    scopus 로고
    • Connexin-47 and connexin-32 in gap junctions of oligodendrocyte somata, myelin sheaths, paranodal loops and Schmidt-Lanterman incisures: implications for ionic homeostasis and potassium siphoning
    • Kamasawa N., Sik A., Morita M., Yasumura T., Davidson K.G., Nagy J.I., Rash J.E. Connexin-47 and connexin-32 in gap junctions of oligodendrocyte somata, myelin sheaths, paranodal loops and Schmidt-Lanterman incisures: implications for ionic homeostasis and potassium siphoning. Neuroscience 2005, 136:65-86.
    • (2005) Neuroscience , vol.136 , pp. 65-86
    • Kamasawa, N.1    Sik, A.2    Morita, M.3    Yasumura, T.4    Davidson, K.G.5    Nagy, J.I.6    Rash, J.E.7
  • 22
    • 1542330707 scopus 로고    scopus 로고
    • Sialin expression in the CNS implicates extralysosomal function in neurons
    • Aula N., Kopra O., Jalanko A., Peltonen L. Sialin expression in the CNS implicates extralysosomal function in neurons. Neurobiol. Dis. 2004, 15:251-261.
    • (2004) Neurobiol. Dis. , vol.15 , pp. 251-261
    • Aula, N.1    Kopra, O.2    Jalanko, A.3    Peltonen, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.