메뉴 건너뛰기




Volumn 382, Issue 2, 2009, Pages 247-251

Spectral properties and mechanisms that underlie autofluorescent accumulations in Batten disease

Author keywords

Autofluorescent storage material; Microtubule assembly; Neuronal Ceroid Lipofuscinosis; Non muscle myosin II

Indexed keywords

MYOSIN II;

EID: 63349086264     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.02.099     Document Type: Article
Times cited : (20)

References (23)
  • 1
    • 0028879016 scopus 로고
    • The neuronal ceroid-lipofuscinoses
    • Goebel H.H. The neuronal ceroid-lipofuscinoses. J. Child Neurol. 10 (1995) 424-437
    • (1995) J. Child Neurol. , vol.10 , pp. 424-437
    • Goebel, H.H.1
  • 3
    • 0027225696 scopus 로고
    • Human forms of neuronal ceroid-lipofuscinosis (Batten disease): consensus on diagnostic criteria, Hamburg 1992
    • Kohlschutter A., Gardiner R.M., and Goebel H.H. Human forms of neuronal ceroid-lipofuscinosis (Batten disease): consensus on diagnostic criteria, Hamburg 1992. J. Inherit. Metab. Dis. 16 (1993) 241-244
    • (1993) J. Inherit. Metab. Dis. , vol.16 , pp. 241-244
    • Kohlschutter, A.1    Gardiner, R.M.2    Goebel, H.H.3
  • 4
    • 16444366586 scopus 로고    scopus 로고
    • CLN3, the protein associated with batten disease: structure, function and localization
    • Phillips S.N., Benedict J.W., Weimer J.M., and Pearce D.A. CLN3, the protein associated with batten disease: structure, function and localization. J. Neurosci. Res. 79 (2005) 573-583
    • (2005) J. Neurosci. Res. , vol.79 , pp. 573-583
    • Phillips, S.N.1    Benedict, J.W.2    Weimer, J.M.3    Pearce, D.A.4
  • 5
    • 0023038776 scopus 로고
    • Ceroid lipofuscinosis in sheep. II. The major component of the lipopigment in liver, kidney, pancreas, and brain is low molecular weight protein
    • Palmer D.N., Barns G., Husbands D.R., and Jolly R.D. Ceroid lipofuscinosis in sheep. II. The major component of the lipopigment in liver, kidney, pancreas, and brain is low molecular weight protein. J. Biol. Chem. 261 (1986) 1773-1777
    • (1986) J. Biol. Chem. , vol.261 , pp. 1773-1777
    • Palmer, D.N.1    Barns, G.2    Husbands, D.R.3    Jolly, R.D.4
  • 6
    • 33344469599 scopus 로고    scopus 로고
    • You say lipofuscin, we say ceroid: defining autofluorescent storage material
    • Seehafer S.S., and Pearce D.A. You say lipofuscin, we say ceroid: defining autofluorescent storage material. Neurobiol. Aging 27 (2006) 576-588
    • (2006) Neurobiol. Aging , vol.27 , pp. 576-588
    • Seehafer, S.S.1    Pearce, D.A.2
  • 9
    • 0028959309 scopus 로고
    • An efficient method for routine Epstein-Barr virus immortalization of human B lymphocytes
    • Wall F.E., Stern M.P., Jenson H.B., and Moyer M.P. An efficient method for routine Epstein-Barr virus immortalization of human B lymphocytes. In Vitro Cell. Dev. Biol. Anim. 31 (1995) 156-159
    • (1995) In Vitro Cell. Dev. Biol. Anim. , vol.31 , pp. 156-159
    • Wall, F.E.1    Stern, M.P.2    Jenson, H.B.3    Moyer, M.P.4
  • 10
    • 0020515704 scopus 로고
    • Retardation of fading and enhancement of intensity of immunofluorescence by p-phenylenediamine
    • Platt J.L., and Michael A.F. Retardation of fading and enhancement of intensity of immunofluorescence by p-phenylenediamine. J. Histochem. Cytochem. 31 (1983) 840-842
    • (1983) J. Histochem. Cytochem. , vol.31 , pp. 840-842
    • Platt, J.L.1    Michael, A.F.2
  • 11
    • 0030845481 scopus 로고    scopus 로고
    • Different patterns of hydrophobic protein storage in different forms of neuronal ceroid lipofuscinosis (NCL, Batten disease)
    • Palmer D.N., Jolly R.D., van Mil H.C., Tyynela J., and Westlake V.J. Different patterns of hydrophobic protein storage in different forms of neuronal ceroid lipofuscinosis (NCL, Batten disease). Neuropediatrics 28 (1997) 45-48
    • (1997) Neuropediatrics , vol.28 , pp. 45-48
    • Palmer, D.N.1    Jolly, R.D.2    van Mil, H.C.3    Tyynela, J.4    Westlake, V.J.5
  • 12
    • 0003404143 scopus 로고    scopus 로고
    • Definitions of Ultrastructure Patterns found in NCL, IOS Press, Netherlands
    • Definitions of Ultrastructure Patterns found in NCL, The Neuronal Ceroid Lipofuscinoses (Batten Disease), IOS Press, Netherlands, 1999, pp. 5-15.
    • (1999) The Neuronal Ceroid Lipofuscinoses (Batten Disease) , pp. 5-15
  • 13
    • 0023946368 scopus 로고
    • Light and electron microscopic appearance of the inner ear in juvenile ceroid lipofuscinosis (CL)
    • Elleder M., Voldrich L., Ulehlova L., Dimitt S., and Armstrong D. Light and electron microscopic appearance of the inner ear in juvenile ceroid lipofuscinosis (CL). Pathol. Res. Pract. 183 (1988) 301-307
    • (1988) Pathol. Res. Pract. , vol.183 , pp. 301-307
    • Elleder, M.1    Voldrich, L.2    Ulehlova, L.3    Dimitt, S.4    Armstrong, D.5
  • 14
    • 0021867665 scopus 로고
    • Inhibition of aspartic proteases by pepstatin and 3-methylstatine derivatives of pepstatin. Evidence for collected-substrate enzyme inhibition
    • Rich D.H., Bernatowicz M.S., Agarwal N.S., Kawai M., Salituro F.G., and Schmidt P.G. Inhibition of aspartic proteases by pepstatin and 3-methylstatine derivatives of pepstatin. Evidence for collected-substrate enzyme inhibition. Biochemistry 24 (1985) 3165-3173
    • (1985) Biochemistry , vol.24 , pp. 3165-3173
    • Rich, D.H.1    Bernatowicz, M.S.2    Agarwal, N.S.3    Kawai, M.4    Salituro, F.G.5    Schmidt, P.G.6
  • 15
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases
    • Drose S., and Altendorf K. Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J. Exp. Biol. 200 (1997) 1-8
    • (1997) J. Exp. Biol. , vol.200 , pp. 1-8
    • Drose, S.1    Altendorf, K.2
  • 16
    • 0021058602 scopus 로고
    • Alkalinizing the intralysosomal pH inhibits degranulation of human neutrophils
    • Klempner M.S., and Styrt B. Alkalinizing the intralysosomal pH inhibits degranulation of human neutrophils. J. Clin. Invest. 72 (1983) 1793-1800
    • (1983) J. Clin. Invest. , vol.72 , pp. 1793-1800
    • Klempner, M.S.1    Styrt, B.2
  • 17
    • 0036364455 scopus 로고    scopus 로고
    • The neuronal ceroid lipofuscinoses: mutations in different proteins result in similar disease
    • Weimer J.M., Kriscenski-Perry E., Elshatory Y., and Pearce D.A. The neuronal ceroid lipofuscinoses: mutations in different proteins result in similar disease. Neuromolecular Med. 1 (2002) 111-124
    • (2002) Neuromolecular Med. , vol.1 , pp. 111-124
    • Weimer, J.M.1    Kriscenski-Perry, E.2    Elshatory, Y.3    Pearce, D.A.4
  • 18
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella V.J., Rando O.J., Goldberg A.L., and Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78 (1994) 773-785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 19
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M., Kijima M., Akita M., and Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 265 (1990) 17174-17179
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 20
    • 0023729899 scopus 로고
    • 3-Methyladenine, an inhibitor of autophagy, has multiple effects on metabolism
    • Caro L.H., Plomp P.J., Wolvetang E.J., Kerkhof C., and Meijer A.J. 3-Methyladenine, an inhibitor of autophagy, has multiple effects on metabolism. Eur. J. Biochem. 175 (1988) 325-329
    • (1988) Eur. J. Biochem. , vol.175 , pp. 325-329
    • Caro, L.H.1    Plomp, P.J.2    Wolvetang, E.J.3    Kerkhof, C.4    Meijer, A.J.5
  • 21
    • 0019276123 scopus 로고
    • Effects of nocodazole on structures of calf brain tubulin
    • Lee J.C., Field D.J., and Lee L.L. Effects of nocodazole on structures of calf brain tubulin. Biochemistry 19 (1980) 6209-6215
    • (1980) Biochemistry , vol.19 , pp. 6209-6215
    • Lee, J.C.1    Field, D.J.2    Lee, L.L.3
  • 22
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue M., Brenner S.L., Spector I., and Korn E.D. Inhibition of actin polymerization by latrunculin A. FEBS Lett. 213 (1987) 316-318
    • (1987) FEBS Lett. , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.