메뉴 건너뛰기




Volumn 14, Issue 1, 2004, Pages 77-85

The Intracellular Location and Function of Proteins of Neuronal Ceroid Lipofuscinoses

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN D; CELL PROTEIN; CHLORIDE CHANNEL; MANNOSE 6 PHOSPHATE; MEMBRANE PROTEIN; PALMITOYL PROTEIN THIOESTERASE; PROTEIN CLC 3; PROTEIN CLN1P; SPHINGOLIPID ACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 1042288280     PISSN: 10156305     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3639.2004.tb00501.x     Document Type: Conference Paper
Times cited : (38)

References (103)
  • 1
    • 0037434057 scopus 로고    scopus 로고
    • Palmitoyl protein thioesterase 1 is targeted to the axons in neurons
    • Ahtiainen L, van Diggelen OP, Jalanko A, Kopra O (2003) Palmitoyl protein thioesterase 1 is targeted to the axons in neurons. J Comp Neurol 455:368-377.
    • (2003) J Comp Neurol , vol.455 , pp. 368-377
    • Ahtiainen, L.1    Van Diggelen, O.P.2    Jalanko, A.3    Kopra, O.4
  • 2
    • 0032799431 scopus 로고    scopus 로고
    • Progress toward the cloning of CLN6, the gene underlying a variant LINCL
    • Auger KJ, Ajene A, Lerner T (1999) Progress toward the cloning of CLN6, the gene underlying a variant LINCL. Mol Genet Metab 66:332-336.
    • (1999) Mol Genet Metab , vol.66 , pp. 332-336
    • Auger, K.J.1    Ajene, A.2    Lerner, T.3
  • 3
    • 0036713679 scopus 로고    scopus 로고
    • Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: Implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis
    • Bernardini F, Warburton MJ (2002) Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis. Biochem J 366:521-529.
    • (2002) Biochem J , vol.366 , pp. 521-529
    • Bernardini, F.1    Warburton, M.J.2
  • 5
    • 0031846129 scopus 로고    scopus 로고
    • Ovine neuronal ceroid lipofuscinosis: A large animal model syntenic with the human neuronal ceroid lipofuscinosis variant CLN6
    • Broom MF, Zhou C, Broom JE, Barwell KJ, Jolly RD, Hill D (1998) Ovine neuronal ceroid lipofuscinosis: a large animal model syntenic with the human neuronal ceroid lipofuscinosis variant CLN6. J Med Genet 35:717-721.
    • (1998) J Med Genet , vol.35 , pp. 717-721
    • Broom, M.F.1    Zhou, C.2    Broom, J.E.3    Barwell, K.J.4    Jolly, R.D.5    Hill, D.6
  • 6
    • 0027518208 scopus 로고
    • Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate form H-ras
    • Camp LA, Hofmann SL (1993) Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate form H-ras. J Biol Chem 268:22566-22574.
    • (1993) J Biol Chem , vol.268 , pp. 22566-22574
    • Camp, L.A.1    Hofmann, S.L.2
  • 9
  • 10
    • 0028857502 scopus 로고
    • Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten disease)
    • Ezaki J, Wolfe LS, Higuti T, Ishidoh K, Kominami E (1995) Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten disease). J Neurochem 64:733-741.
    • (1995) J Neurochem , vol.64 , pp. 733-741
    • Ezaki, J.1    Wolfe, L.S.2    Higuti, T.3    Ishidoh, K.4    Kominami, E.5
  • 11
    • 0029817316 scopus 로고    scopus 로고
    • Specific delay in the degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis is derived from cellular proteolytic dysfunction rather than structural alteration of subunit c
    • Ezaki J, Wolfe LS, Kominami E (1996) Specific delay in the degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis is derived from cellular proteolytic dysfunction rather than structural alteration of subunit c. J Neurochem 67:1677-1687.
    • (1996) J Neurochem , vol.67 , pp. 1677-1687
    • Ezaki, J.1    Wolfe, L.S.2    Kominami, E.3
  • 12
    • 0030741684 scopus 로고    scopus 로고
    • Decreased lysosomal subunit c-degrading activity in fibroblasts from patients with late infantile neuronal ceroid lipofuscinosis
    • Ezaki J, Wolfe LS, Kominami E (1997) Decreased lysosomal subunit c-degrading activity in fibroblasts from patients with late infantile neuronal ceroid lipofuscinosis. Neuropediatrics 28:53-55.
    • (1997) Neuropediatrics , vol.28 , pp. 53-55
    • Ezaki, J.1    Wolfe, L.S.2    Kominami, E.3
  • 13
    • 0032973867 scopus 로고    scopus 로고
    • A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase
    • Ezaki J, Tanida I, Kanehagi N, Kominami E (1999) A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase. J Neurochem 72:2573-2582.
    • (1999) J Neurochem , vol.72 , pp. 2573-2582
    • Ezaki, J.1    Tanida, I.2    Kanehagi, N.3    Kominami, E.4
  • 14
    • 0034708173 scopus 로고    scopus 로고
    • Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis
    • Ezaki J, Takeda-Ezaki M, Oda K, Kominami E (2000) Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. Biochem Biophys Res Commun 268:904-908.
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 904-908
    • Ezaki, J.1    Takeda-Ezaki, M.2    Oda, K.3    Kominami, E.4
  • 15
    • 0033809338 scopus 로고    scopus 로고
    • Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase
    • Ezaki J, Takeda-Ezaki M, Kominami E (2000) Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase. J Biochem 128:509-516.
    • (2000) J Biochem , vol.128 , pp. 509-516
    • Ezaki, J.1    Takeda-Ezaki, M.2    Kominami, E.3
  • 16
    • 0344011621 scopus 로고    scopus 로고
    • Characterization of Cln3p, the gene product responsible for juvenile neuronal ceroid lipofuscinosis, as a lysosomal integral membrane glycoprotein
    • Ezaki J, Takeda-Ezaki M, Koike M, Ohsawa Y, Kaka H, Mineki R, Murayama K, Uchida Y, Ueno T, Kominami E (2003) Characterization of Cln3p, the gene product responsible for juvenile neuronal ceroid lipofuscinosis, as a lysosomal integral membrane glycoprotein. J Neurochem 87:1296-1308.
    • (2003) J Neurochem , vol.87 , pp. 1296-1308
    • Ezaki, J.1    Takeda-Ezaki, M.2    Koike, M.3    Ohsawa, Y.4    Kaka, H.5    Mineki, R.6    Murayama, K.7    Uchida, Y.8    Ueno, T.9    Kominami, E.10
  • 17
    • 0028341126 scopus 로고
    • Two related proteolipids and dolichol-linked oligosaccharides accumulate in motor neuron degeneration mice (mnd/mnd), a model for neuronal ceroid lipofuscinosis
    • Faust JR, Rodman JS, Daniel PF, Dice JF Bronson RT (1994) Two related proteolipids and dolichol-linked oligosaccharides accumulate in motor neuron degeneration mice (mnd/mnd), a model for neuronal ceroid lipofuscinosis. J Biol Chem 269:10150-10155.
    • (1994) J Biol Chem , vol.269 , pp. 10150-10155
    • Faust, J.R.1    Rodman, J.S.2    Daniel, P.F.3    Dice, J.F.4    Bronson, R.T.5
  • 18
    • 0025290956 scopus 로고
    • The sequence of major protein stored in ovine ceroid lipofuscinosis is identical with that of dicyclohexylcarbodiimide-reactive proteolipid of mitochondrial ATP synthase
    • Fearnley IM, Walker JE, Martinus RD, Jolly RD, Kirkland KB, Shaw GJ, Palmer DN (1990) The sequence of major protein stored in ovine ceroid lipofuscinosis is identical with that of dicyclohexylcarbodiimide-reactive proteolipid of mitochondrial ATP synthase. Biochem J 268:751-758.
    • (1990) Biochem J , vol.268 , pp. 751-758
    • Fearnley, I.M.1    Walker, J.E.2    Martinus, R.D.3    Jolly, R.D.4    Kirkland, K.B.5    Shaw, G.J.6    Palmer, D.N.7
  • 20
    • 0032811446 scopus 로고    scopus 로고
    • Expression studies of CLN3 protein (Battenin) in fusion with the green fluorescent protein in mammalian cells in vitro
    • Golabek AA, Kaczmarski W, Kida E, Kaczmarski A, Michalewski MP, Wisniewski KE (1999) Expression studies of CLN3 protein (Battenin) in fusion with the green fluorescent protein in mammalian cells in vitro. Mol Genet Metab 66:277-282.
    • (1999) Mol Genet Metab , vol.66 , pp. 277-282
    • Golabek, A.A.1    Kaczmarski, W.2    Kida, E.3    Kaczmarski, A.4    Michalewski, M.P.5    Wisniewski, K.E.6
  • 21
    • 0033864041 scopus 로고    scopus 로고
    • CLN3 protein regulates lysosomal pH and alters intracellular processing of Alzheimer's disease amyloid-(protein precursor and cathepsin D in human cells
    • Golabek AA, Kida E, Walus M, Kaczmarski W, Michalewski M, Wisniewski KE (2000) CLN3 protein regulates lysosomal pH and alters intracellular processing of Alzheimer's disease amyloid-(protein precursor and cathepsin D in human cells. Mol Genet Metab 70:203-213.
    • (2000) Mol Genet Metab , vol.70 , pp. 203-213
    • Golabek, A.A.1    Kida, E.2    Walus, M.3    Kaczmarski, W.4    Michalewski, M.5    Wisniewski, K.E.6
  • 22
    • 0037470135 scopus 로고    scopus 로고
    • Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I
    • Golabek AA, Kida E, Walus M, Wujek P, Mehta P, Wisniewski KE (2003) Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I. J Biol Chem 278:7135-7145.
    • (2003) J Biol Chem , vol.278 , pp. 7135-7145
    • Golabek, A.A.1    Kida, E.2    Walus, M.3    Wujek, P.4    Mehta, P.5    Wisniewski, K.E.6
  • 26
    • 0025854327 scopus 로고
    • Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease (ceroid-lipofuscinosis)
    • Hall NA, Lake BD, Dewji NN, Patrick AD (1991) Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease (ceroid-lipofuscinosis). Biochem J 275:269-272.
    • (1991) Biochem J , vol.275 , pp. 269-272
    • Hall, N.A.1    Lake, B.D.2    Dewji, N.N.3    Patrick, A.D.4
  • 29
    • 0029843717 scopus 로고    scopus 로고
    • Human palmitoyl protein thioesterase: Evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis
    • Hellsten E, Vesa J, Olkkonen VM, Jalanko A, Peltonen L (1996) Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis. EMBO J 15:5240-5245.
    • (1996) EMBO J , vol.15 , pp. 5240-5245
    • Hellsten, E.1    Vesa, J.2    Olkkonen, V.M.3    Jalanko, A.4    Peltonen, L.5
  • 30
    • 19244385377 scopus 로고    scopus 로고
    • Lysosomal proteolysis of prosaponin, the precursor of saponins (sphingolipid activator proteins): Its mechanism and inhibition by ganglioside
    • Hiraiwa M, Martin BM, Kishimoto Y, Conner GE, Tsuji S, O'Brien JS (1997) Lysosomal proteolysis of prosaponin, the precursor of saponins (sphingolipid activator proteins): its mechanism and inhibition by ganglioside. Arch Biochem Biophys 341:17-24.
    • (1997) Arch Biochem Biophys , vol.341 , pp. 17-24
    • Hiraiwa, M.1    Martin, B.M.2    Kishimoto, Y.3    Conner, G.E.4    Tsuji, S.5    O'Brien, J.S.6
  • 33
    • 0037091074 scopus 로고    scopus 로고
    • Lysosomal localization of the neuronal ceroid lipofuscinosis CLN5 protein
    • Isosomppi J, Vesa J, Jalanko A, Peltonen (2002) Lysosomal localization of the neuronal ceroid lipofuscinosis CLN5 protein. Hum Mol Genet 11:885-891.
    • (2002) Hum Mol Genet , vol.11 , pp. 885-891
    • Isosomppi, J.1    Vesa, J.2    Jalanko, A.3    Peltonen4
  • 36
    • 0344867852 scopus 로고    scopus 로고
    • Defective intracellular transport of CLN3 is the molecular basis of Batten disease (JNCL)
    • Järvelä I, Lehtovirta M, Tikkanen R, Kyttälä A, Jalanko A (1999) Defective intracellular transport of CLN3 is the molecular basis of Batten disease (JNCL). Hum Mol Genet 8:1091-1098.
    • (1999) Hum Mol Genet , vol.8 , pp. 1091-1098
    • Järvelä, I.1    Lehtovirta, M.2    Tikkanen, R.3    Kyttälä, A.4    Jalanko, A.5
  • 37
    • 0033515854 scopus 로고    scopus 로고
    • Increased brain lysosomal pepstatin-insensitive proteinase activity in patients with neurodegenerative disease
    • Junaid MA, Pullarkat RK (1999) Increased brain lysosomal pepstatin-insensitive proteinase activity in patients with neurodegenerative disease. Neurosci Lett 264:157-160.
    • (1999) Neurosci Lett , vol.264 , pp. 157-160
    • Junaid, M.A.1    Pullarkat, R.K.2
  • 38
    • 0033961791 scopus 로고    scopus 로고
    • Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis
    • Junaid MA, Wu G, Pullarkat RK (2000) Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis. J Neurochem 74:287-294.
    • (2000) J Neurochem , vol.74 , pp. 287-294
    • Junaid, M.A.1    Wu, G.2    Pullarkat, R.K.3
  • 40
    • 0035234733 scopus 로고    scopus 로고
    • Cellular pathology and pathogenic aspects of neuronal ceroid lipofuscinoses
    • Kida E, Golabek AA, Wisniewski KE (2001) Cellular pathology and pathogenic aspects of neuronal ceroid lipofuscinoses. Adv Genet 45:35-68.
    • (2001) Adv Genet , vol.45 , pp. 35-68
    • Kida, E.1    Golabek, A.A.2    Wisniewski, K.E.3
  • 44
    • 0026526712 scopus 로고
    • Specific storage of subunit c of mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease)
    • Kominami E, Ezaki J, Muno D, Ishido K, Ueno T, Wolfe LS (1992) Specific storage of subunit c of mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease) J Biochem 111:278-282.
    • (1992) J Biochem , vol.111 , pp. 278-282
    • Kominami, E.1    Ezaki, J.2    Muno, D.3    Ishido, K.4    Ueno, T.5    Wolfe, L.S.6
  • 45
    • 0036796221 scopus 로고    scopus 로고
    • Altered flurothyl seizure induction latency,phenotype, and subsequent mortality in a mouse model of juvenile neuronal ceroid lipofuscinosis/Batten disease
    • Kriscenski-Perry E, Applegate CD, Serour A, Mhyre TR, Leonardo CC, Pearce DA (2002) Altered flurothyl seizure induction latency,phenotype, and subsequent mortality in a mouse model of juvenile neuronal ceroid lipofuscinosis/Batten disease. Epilepsia 43:1137-1140.
    • (2002) Epilepsia , vol.43 , pp. 1137-1140
    • Kriscenski-Perry, E.1    Applegate, C.D.2    Serour, A.3    Mhyre, T.R.4    Leonardo, C.C.5    Pearce, D.A.6
  • 46
    • 0034907976 scopus 로고    scopus 로고
    • Distribution and development of CLN2 protein, the late-infantile neuronal ceroid lipofuscinosis gene product
    • Kurachi Y, Oka A, Itoh M, Mizuguchi M, Hayashi M, Takashima S (2001) Distribution and development of CLN2 protein, the late-infantile neuronal ceroid lipofuscinosis gene product. Acta Neuropathol (Berl) 102:20-26.
    • (2001) Acta Neuropathol (Berl) , vol.102 , pp. 20-26
    • Kurachi, Y.1    Oka, A.2    Itoh, M.3    Mizuguchi, M.4    Hayashi, M.5    Takashima, S.6
  • 47
    • 0035167162 scopus 로고    scopus 로고
    • Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: Implications for infantile neuronal ceroid lipofuscinosis (INCL)
    • Lehtovirta M, Kyttälä A, Eskelinen E-L, Hess M, Heinonen O, Jalanko A (2001) Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: implications for infantile neuronal ceroid lipofuscinosis (INCL). Hum Mol Genet 10:69-75.
    • (2001) Hum Mol Genet , vol.10 , pp. 69-75
    • Lehtovirta, M.1    Kyttälä, A.2    Eskelinen, E.-L.3    Hess, M.4    Heinonen, O.5    Jalanko, A.6
  • 48
    • 0035910463 scopus 로고    scopus 로고
    • The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH
    • Lin L, Sohar I, Lackland H, Lobel P (2001) The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. J Biol Chem 276:2249-2255.
    • (2001) J Biol Chem , vol.276 , pp. 2249-2255
    • Lin, L.1    Sohar, I.2    Lackland, H.3    Lobel, P.4
  • 49
    • 18844471093 scopus 로고    scopus 로고
    • The neuronal ceroid lipofuscinosis CLN8 membrane protein is a resident of the endoplasmic reticulum
    • Lonka L, Kyttälä A, Ranta S, Jalanko A, Lehesjoki A-E (2000) The neuronal ceroid lipofuscinosis CLN8 membrane protein is a resident of the endoplasmic reticulum. Hum Mol Genet 9:1691-1697.
    • (2000) Hum Mol Genet , vol.9 , pp. 1691-1697
    • Lonka, L.1    Kyttälä, A.2    Ranta, S.3    Jalanko, A.4    Lehesjoki, A.-E.5
  • 51
    • 0037464472 scopus 로고    scopus 로고
    • Membrane topology of CLN3, the protein underlying Batten disease
    • Mao Q, Foster BL, Xia H, Davidson BL (2003) Membrane topology of CLN3, the protein underlying Batten disease. FEBS Lett 541:40-46.
    • (2003) FEBS Lett , vol.541 , pp. 40-46
    • Mao, Q.1    Foster, B.L.2    Xia, H.3    Davidson, B.L.4
  • 55
    • 0033533048 scopus 로고    scopus 로고
    • Batten's disease: Eight genes and still counting
    • Mole SE (1999) Batten's disease: eight genes and still counting. Lancet 354:443-445.
    • (1999) Lancet , vol.354 , pp. 443-445
    • Mole, S.E.1
  • 58
    • 0028046586 scopus 로고
    • Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101
    • Oda K, Takahashi T, Tokuda Y, Shibano Y, Takahashi S (1994) Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101. J Biol Chem 42:26518-26524.
    • (1994) J Biol Chem , vol.42 , pp. 26518-26524
    • Oda, K.1    Takahashi, T.2    Tokuda, Y.3    Shibano, Y.4    Takahashi, S.5
  • 59
    • 0029761009 scopus 로고    scopus 로고
    • Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Xanthomonas sp. T-22
    • Oda K, Ito M, Uchida K, Shibano Y, Fukuhara K, Takahashi S (1996) Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Xanthomonas sp. T-22. J Biochem 120:564-572.
    • (1996) J Biochem , vol.120 , pp. 564-572
    • Oda, K.1    Ito, M.2    Uchida, K.3    Shibano, Y.4    Fukuhara, K.5    Takahashi, S.6
  • 60
    • 0036090236 scopus 로고    scopus 로고
    • A CLN2-related and thermostable serine-carboxyl protease, kumamolysine: Cloning, expression, and identification of catalytic serine residue
    • Oyama H, Hamada T, Ogasawara S, Uchida K, Murao S, Beyer BB, Dunn BM, Oda K (2002) A CLN2-related and thermostable serine-carboxyl protease, kumamolysine: cloning, expression, and identification of catalytic serine residue. J Biochem 131:757-765.
    • (2002) J Biochem , vol.131 , pp. 757-765
    • Oyama, H.1    Hamada, T.2    Ogasawara, S.3    Uchida, K.4    Murao, S.5    Beyer, B.B.6    Dunn, B.M.7    Oda, K.8
  • 64
    • 0030855171 scopus 로고    scopus 로고
    • BTN1, a yeast gene corresponding to the human gene responsible for Batten's disease, is not essential for viability, mitochondrial function, or degradation of mitochondrial ATP synthase
    • Pearce DA, Sherman F (1997) BTN1, a yeast gene corresponding to the human gene responsible for Batten's disease, is not essential for viability, mitochondrial function, or degradation of mitochondrial ATP synthase. Yeast 13:691-697.
    • (1997) Yeast , vol.13 , pp. 691-697
    • Pearce, D.A.1    Sherman, F.2
  • 65
    • 0032905252 scopus 로고    scopus 로고
    • Action of BTN1, the yeast orthologue of the gene mutated in Batten disease
    • Pearce DA, Ferea T, Nosel SA, Das B, Sherman F (1999) Action of BTN1, the yeast orthologue of the gene mutated in Batten disease. Nat Genet 22:55-58.
    • (1999) Nat Genet , vol.22 , pp. 55-58
    • Pearce, D.A.1    Ferea, T.2    Nosel, S.A.3    Das, B.4    Sherman, F.5
  • 67
    • 0033778919 scopus 로고    scopus 로고
    • Northern epilepsy, a new member of the NCL family
    • Ranta S, Lehesjoki AE (2000) Northern epilepsy, a new member of the NCL family. Neurol Sci 21:S43-47.
    • (2000) Neurol Sci , vol.21
    • Ranta, S.1    Lehesjoki, A.E.2
  • 68
    • 0032897884 scopus 로고    scopus 로고
    • Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis
    • Rawling ND, Barrett AJ (1999) Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis. Biochim Biophys Acta 1429:496-500.
    • (1999) Biochim Biophys Acta , vol.1429 , pp. 496-500
    • Rawling, N.D.1    Barrett, A.J.2
  • 70
    • 0028041361 scopus 로고
    • Defined chromosomal assignment of CLN5 demonstrates that at least four genetic loci are involved in the pathogenesis of human ceroid lipofuscinoses
    • Savukoski M, Kestilä M, Williams R, Järvelä I, Sharp J, Harris J, Santavuori P, Gardiner M, Peltonen L (1994) Defined chromosomal assignment of CLN5 demonstrates that at least four genetic loci are involved in the pathogenesis of human ceroid lipofuscinoses. Am J Hum Genet 55:695-701.
    • (1994) Am J Hum Genet , vol.55 , pp. 695-701
    • Savukoski, M.1    Kestilä, M.2    Williams, R.3    Järvelä, I.4    Sharp, J.5    Harris, J.6    Santavuori, P.7    Gardiner, M.8    Peltonen, L.9
  • 71
    • 0031803649 scopus 로고    scopus 로고
    • CLN5, a novel gene encoding a putative transmembrane protein mutated in Finnish variant late infantile neuronal ceroid lipofuscinosis
    • Savukoski M, Klockars T, Holmberg V, Santavuori P, Lander ES, Peltonen L (1998) CLN5, a novel gene encoding a putative transmembrane protein mutated in Finnish variant late infantile neuronal ceroid lipofuscinosis. Nat Genet 19:286-288.
    • (1998) Nat Genet , vol.19 , pp. 286-288
    • Savukoski, M.1    Klockars, T.2    Holmberg, V.3    Santavuori, P.4    Lander, E.S.5    Peltonen, L.6
  • 76
    • 0029782734 scopus 로고    scopus 로고
    • Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis
    • Sleat DE, Sohar I, Lackland H, Majercak J, Lobel P (1996) Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis. J Biol Chem 271:19191-19198.
    • (1996) J Biol Chem , vol.271 , pp. 19191-19198
    • Sleat, D.E.1    Sohar, I.2    Lackland, H.3    Majercak, J.4    Lobel, P.5
  • 77
    • 0030866233 scopus 로고    scopus 로고
    • Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis
    • Sleat DE, Donnely RJ, Lackland H, Liu C-G, Sohar I, Pullarkat RK, Lobel P (1997) Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis. Science 277:1802-1806.
    • (1997) Science , vol.277 , pp. 1802-1806
    • Sleat, D.E.1    Donnely, R.J.2    Lackland, H.3    Liu, C.-G.4    Sohar, I.5    Pullarkat, R.K.6    Lobel, P.7
  • 78
    • 0030871064 scopus 로고    scopus 로고
    • Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity
    • Soyombo AA, Hofmann SL (1997) Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity. J Biol Chem 272:27456-27463.
    • (1997) J Biol Chem , vol.272 , pp. 27456-27463
    • Soyombo, A.A.1    Hofmann, S.L.2
  • 79
    • 0032778867 scopus 로고    scopus 로고
    • Biochemical characterization of a lysosomal protease deficient in classical late infantile neuronal ceroid lipofuscinosis (LINCL) and development of an enzyme-based assay for diagnosis and exclusion of LINCL in human specimens and animal models
    • Sohar I, Sleat DE, Jadot M, Lobel P (1999) Biochemical characterization of a lysosomal protease deficient in classical late infantile neuronal ceroid lipofuscinosis (LINCL) and development of an enzyme-based assay for diagnosis and exclusion of LINCL in human specimens and animal models. J Neurochem 73:700-711.
    • (1999) J Neurochem , vol.73 , pp. 700-711
    • Sohar, I.1    Sleat, D.E.2    Jadot, M.3    Lobel, P.4
  • 81
    • 0033538010 scopus 로고    scopus 로고
    • Palmitoyl-protein thioesterase, an enzyme implicated in neurodegeneration, is localized in neurons and is developmentally regulated in rat brain
    • Suopanki J, Tyynelä J, Baumann M, Haltia M (1999) Palmitoyl-protein thioesterase, an enzyme implicated in neurodegeneration, is localized in neurons and is developmentally regulated in rat brain. Neurosci Lett 265:53-56.
    • (1999) Neurosci Lett , vol.265 , pp. 53-56
    • Suopanki, J.1    Tyynelä, J.2    Baumann, M.3    Haltia, M.4
  • 85
    • 0035910423 scopus 로고    scopus 로고
    • The human homolog of Saccharomyces cerevisiae Apg7p is a protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3
    • Tanida I, Tanida-Miyake E, Ueno T, Kominami E (2001) The human homolog of Saccharomyces cerevisiae Apg7p is a protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3. J Biol Chem 276:1701-1706.
    • (2001) J Biol Chem , vol.276 , pp. 1701-1706
    • Tanida, I.1    Tanida-Miyake, E.2    Ueno, T.3    Kominami, E.4
  • 86
    • 0037134443 scopus 로고    scopus 로고
    • Human Apg3p/Aut1p homologues is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p
    • Tanida I, Tanida-Miyake E, Komatsu M, Ueno T, Kominami E (2002) Human Apg3p/Aut1p homologues is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p. J Biol Chem 277:13739-13744.
    • (2002) J Biol Chem , vol.277 , pp. 13739-13744
    • Tanida, I.1    Tanida-Miyake, E.2    Komatsu, M.3    Ueno, T.4    Kominami, E.5
  • 88
    • 0035910577 scopus 로고    scopus 로고
    • Degradation of lipid vesicles in the yeast vacuole requires a function of Cvt17, putative lipase
    • Teter SA, Eggerton KP, Scott SV, Kim J, Fischer AM, Klionsky DJ (2001) Degradation of lipid vesicles in the yeast vacuole requires a function of Cvt17, putative lipase. J Biol Chem 276:2083-2087.
    • (2001) J Biol Chem , vol.276 , pp. 2083-2087
    • Teter, S.A.1    Eggerton, K.P.2    Scott, S.V.3    Kim, J.4    Fischer, A.M.5    Klionsky, D.J.6
  • 89
    • 0029147298 scopus 로고
    • Isolation of a novel gene underlying Batten disease, CLN3
    • The International Batten Disease Consortium (1995) Isolation of a novel gene underlying Batten disease, CLN3. Cell 82:949-957.
    • (1995) Cell , vol.82 , pp. 949-957
  • 90
    • 0027224115 scopus 로고
    • Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis
    • Tyynelä J, Palmer DN, Baumann M, Haltia M (1993) Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis. FEBS Lett 330:8-12.
    • (1993) FEBS Lett , vol.330 , pp. 8-12
    • Tyynelä, J.1    Palmer, D.N.2    Baumann, M.3    Haltia, M.4
  • 91
    • 0034659833 scopus 로고    scopus 로고
    • A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration
    • Tyynelä J, Sohar I, Sleat DE, Gin RM, Donnelly RJ, Baumann M, Haltia M, Lobel P (2000) A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration. EMBO J 19:2786-2792.
    • (2000) EMBO J , vol.19 , pp. 2786-2792
    • Tyynelä, J.1    Sohar, I.2    Sleat, D.E.3    Gin, R.M.4    Donnelly, R.J.5    Baumann, M.6    Haltia, M.7    Lobel, P.8
  • 92
    • 0030009044 scopus 로고    scopus 로고
    • Lysosomal targeting of palmitoyl-protein thioesterase
    • Verkruyse LA, Hofmann SL (1996) Lysosomal targeting of palmitoyl-protein thioesterase. J Biol Chem 271:15831-15836.
    • (1996) J Biol Chem , vol.271 , pp. 15831-15836
    • Verkruyse, L.A.1    Hofmann, S.L.2
  • 95
    • 0032546626 scopus 로고    scopus 로고
    • Purification and characterization of a tripeptidyl aminopeptidase I from rat spleen
    • Vines D, Warburton MJ (1998) Purification and characterization of a tripeptidyl aminopeptidase I from rat spleen. Biochim Biophys Acta 1384:233-242.
    • (1998) Biochim Biophys Acta , vol.1384 , pp. 233-242
    • Vines, D.1    Warburton, M.J.2
  • 96
    • 0033052570 scopus 로고    scopus 로고
    • Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I
    • Vines DJ, Warburton MJ (1999) Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I. FEBS Lett 443:131-135.
    • (1999) FEBS Lett , vol.443 , pp. 131-135
    • Vines, D.J.1    Warburton, M.J.2
  • 97
    • 0035816437 scopus 로고    scopus 로고
    • The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues
    • Warburton MJ, Bernardini F (2001) The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues. FEBS Lett 500:145-148.
    • (2001) FEBS Lett , vol.500 , pp. 145-148
    • Warburton, M.J.1    Bernardini, F.2
  • 99
    • 0036155408 scopus 로고    scopus 로고
    • The gene mutated in variant late-infantile neuronal ceroid lipofuscinosis (CLN6) and in nclf mutant mice encodes a novel predicted transmembrane protein
    • Wheeler RB, Sharp JD, Schultz RA, Joslin JM, Williams RE, Mole SE (2002) The gene mutated in variant late-infantile neuronal ceroid lipofuscinosis (CLN6) and in nclf mutant mice encodes a novel predicted transmembrane protein. Am J Hum Genet 70:537-542.
    • (2002) Am J Hum Genet , vol.70 , pp. 537-542
    • Wheeler, R.B.1    Sharp, J.D.2    Schultz, R.A.3    Joslin, J.M.4    Williams, R.E.5    Mole, S.E.6
  • 100
    • 0036682881 scopus 로고    scopus 로고
    • TRAM, LAG1 and CLN8: Members of a novel family of lipid-sensing domains?
    • Winter E, Ponting CP (2002) TRAM, LAG1 and CLN8: members of a novel family of lipid-sensing domains? Trends Biochem Sci 27:381-383.
    • (2002) Trends Biochem Sci , vol.27 , pp. 381-383
    • Winter, E.1    Ponting, C.P.2
  • 102
    • 0037779903 scopus 로고    scopus 로고
    • Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidase
    • Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K (2003) Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidase. Acta Biochim Pol 50:81-102.
    • (2003) Acta Biochim Pol , vol.50 , pp. 81-102
    • Wlodawer, A.1    Li, M.2    Gustchina, A.3    Oyama, H.4    Dunn, B.M.5    Oda, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.