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Volumn 1782, Issue 7-8, 2008, Pages 433-446

Caenorhabditis elegans as a model for lysosomal storage disorders

Author keywords

Caenorhabditis elegans; Lysosomal storage disease; Lysosome

Indexed keywords

CATHEPSIN; CELL PROTEIN; CHLORIDE CHANNEL; GLYCOPROTEIN; CAENORHABDITIS ELEGANS PROTEIN; CHOLESTEROL; CUP 5 PROTEIN, C ELEGANS; CUP-5 PROTEIN, C ELEGANS; MCOLN1 PROTEIN, HUMAN; MEMBRANE PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL M;

EID: 49649113915     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2008.04.003     Document Type: Review
Times cited : (41)

References (93)
  • 1
    • 0002549377 scopus 로고
    • The lysosome
    • De Duve C. The lysosome. Sci. Am. 208 (1963) 64-72
    • (1963) Sci. Am. , vol.208 , pp. 64-72
    • De Duve, C.1
  • 2
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: emerging functions for lysosomal membrane proteins
    • Eskelinen E.L., Tanaka Y., and Saftig P. At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol. 3 (2003) 137-145
    • (2003) Trends Cell Biol. , vol.3 , pp. 137-145
    • Eskelinen, E.L.1    Tanaka, Y.2    Saftig, P.3
  • 3
    • 1342310842 scopus 로고    scopus 로고
    • Lysosome and lysosome-related organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase
    • Sun-Wada G.H., Wada Y., and Futai M. Lysosome and lysosome-related organelles responsible for specialized functions in higher organisms, with special emphasis on vacuolar-type proton ATPase. Cell Struct. Funct. 28 (2003) 455-463
    • (2003) Cell Struct. Funct. , vol.28 , pp. 455-463
    • Sun-Wada, G.H.1    Wada, Y.2    Futai, M.3
  • 4
    • 0035074341 scopus 로고    scopus 로고
    • The molecular machinery for lysosome biogenesis
    • Mullins C., and Bonifacino J.S. The molecular machinery for lysosome biogenesis. BioEssays 4 (2001) 333-343
    • (2001) BioEssays , vol.4 , pp. 333-343
    • Mullins, C.1    Bonifacino, J.S.2
  • 6
    • 38449103028 scopus 로고    scopus 로고
    • Intracellular trafficking
    • WormBook (Ed) 10.1895/wormbook.1.77.1 http://www.wormbook.org
    • Grant B.D., and Sato M. Intracellular trafficking. In: WormBook (Ed). The C. elegans Research Community (January 21, 2006). http://www.wormbook.org 10.1895/wormbook.1.77.1 http://www.wormbook.org
    • (2006) The C. elegans Research Community
    • Grant, B.D.1    Sato, M.2
  • 7
    • 0035396643 scopus 로고    scopus 로고
    • The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides
    • Guerardel Y., Balanzino L., Maes E., Leroy Y., Coddeville B., Oriol R., and Strecker G. The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides. Biochem. J. 357 (2001) 167-182
    • (2001) Biochem. J. , vol.357 , pp. 167-182
    • Guerardel, Y.1    Balanzino, L.2    Maes, E.3    Leroy, Y.4    Coddeville, B.5    Oriol, R.6    Strecker, G.7
  • 8
    • 49849089579 scopus 로고    scopus 로고
    • K. Paschinger, M. Gutternigg, D. Rendic, I.B.H. Wilson, The N-glycosylation pattern of Caenorhabditis elegans. Carbohydr. Res. (electronic publication ahead of print).
    • K. Paschinger, M. Gutternigg, D. Rendic, I.B.H. Wilson, The N-glycosylation pattern of Caenorhabditis elegans. Carbohydr. Res. (electronic publication ahead of print).
  • 9
    • 21344449339 scopus 로고    scopus 로고
    • Searching new targets for anthelminthic strategies: interference with glycosphingolipid biosynthesis and phosphorylcholine metabolism affects development of Caenorhabditis elegans
    • Lochnit G., Bongaards R., and Geyer R. Searching new targets for anthelminthic strategies: interference with glycosphingolipid biosynthesis and phosphorylcholine metabolism affects development of Caenorhabditis elegans. Int. J. Parasitol. 35 (2005) 911-923
    • (2005) Int. J. Parasitol. , vol.35 , pp. 911-923
    • Lochnit, G.1    Bongaards, R.2    Geyer, R.3
  • 11
    • 0000314638 scopus 로고
    • Over idiopathische hypertrophie van het hart Dutch
    • Pompe J.C. Over idiopathische hypertrophie van het hart Dutch. Ned. Tijdschr. Geneeskd. 76 (1932) 304-312
    • (1932) Ned. Tijdschr. Geneeskd. , vol.76 , pp. 304-312
    • Pompe, J.C.1
  • 12
    • 0000995321 scopus 로고    scopus 로고
    • Glycogen storage disease type II: acid α-glucosidase (acid maltase) deficiency
    • Scriver C.R., and Sly W.S. (Eds), McGraw-Hill Inc., New York
    • Hirschhorn R., and Reuser A.J.J. Glycogen storage disease type II: acid α-glucosidase (acid maltase) deficiency. In: Scriver C.R., and Sly W.S. (Eds). The Metabolic and Molecular Bases of Inherited Disease. 8th edition (2001), McGraw-Hill Inc., New York 3389-3420
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. 8th edition , pp. 3389-3420
    • Hirschhorn, R.1    Reuser, A.J.J.2
  • 13
    • 0001261457 scopus 로고    scopus 로고
    • I-cell disease and pseudo-Hurler polydystrophy: disorders of lysosomal enzyme phosphorylation and localization
    • Scriver C.R., and Sly W.S. (Eds), McGraw-Hill Inc., New York
    • Kornfeld S., and Sly W.S. I-cell disease and pseudo-Hurler polydystrophy: disorders of lysosomal enzyme phosphorylation and localization. In: Scriver C.R., and Sly W.S. (Eds). The Metabolic and Molecular Bases of Inherited Disease. 8th edition (2001), McGraw-Hill Inc., New York 3421-3452
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. 8th edition , pp. 3421-3452
    • Kornfeld, S.1    Sly, W.S.2
  • 14
    • 14144255733 scopus 로고    scopus 로고
    • Lysosomal storage disorders
    • Vellodi A. Lysosomal storage disorders. Br. J. Haematol. 128 (2005) 413-431
    • (2005) Br. J. Haematol. , vol.128 , pp. 413-431
    • Vellodi, A.1
  • 15
    • 0027517038 scopus 로고
    • Neuronal ceroid-lipofuscinoses in childhood
    • Rapola J. Neuronal ceroid-lipofuscinoses in childhood. Perspect. Pediatr. Pathol. 17 (1993) 7-44
    • (1993) Perspect. Pediatr. Pathol. , vol.17 , pp. 7-44
    • Rapola, J.1
  • 16
    • 0036247196 scopus 로고    scopus 로고
    • New prospects for the treatment of lysosomal storage diseases
    • Schiffmann R., and Brady R.O. New prospects for the treatment of lysosomal storage diseases. Drugs 62 (2002) 733-742
    • (2002) Drugs , vol.62 , pp. 733-742
    • Schiffmann, R.1    Brady, R.O.2
  • 17
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman A.H., and van Meer G. The cell biology of lysosomal storage disorders. Nat. Rev., Mol. Cell Biol. 7 (2004) 554-565
    • (2004) Nat. Rev., Mol. Cell Biol. , vol.7 , pp. 554-565
    • Futerman, A.H.1    van Meer, G.2
  • 18
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S. The genetics of Caenorhabditis elegans. Genetics 77 (1974) 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 19
    • 0034999073 scopus 로고    scopus 로고
    • The use of functional genomics in C. elegans for studying human development and disease
    • Kuwabara P.E., and O'Neil N. The use of functional genomics in C. elegans for studying human development and disease. J. Inherit. Metab. Dis. 24 (2001) 127-138
    • (2001) J. Inherit. Metab. Dis. , vol.24 , pp. 127-138
    • Kuwabara, P.E.1    O'Neil, N.2
  • 20
    • 0022585682 scopus 로고
    • The autofluorescent "lipofuscin granules" in the intestinal cells of Caenorhabditis elegans are secondary lysosomes
    • Clokey G.V., and Jacobson L.A. The autofluorescent "lipofuscin granules" in the intestinal cells of Caenorhabditis elegans are secondary lysosomes. Mech. Ageing Dev. 35 (1986) 79-94
    • (1986) Mech. Ageing Dev. , vol.35 , pp. 79-94
    • Clokey, G.V.1    Jacobson, L.A.2
  • 21
    • 1842428593 scopus 로고    scopus 로고
    • Caenorhabditis elegans functional orthologue of human protein h-mucolipin-1 is required for lysosome biogenesis
    • Treusch S., Knuth S., Slaugenhaupt S.A., Goldin E., Grant B.D., and Fares H. Caenorhabditis elegans functional orthologue of human protein h-mucolipin-1 is required for lysosome biogenesis. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 4483-4488
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4483-4488
    • Treusch, S.1    Knuth, S.2    Slaugenhaupt, S.A.3    Goldin, E.4    Grant, B.D.5    Fares, H.6
  • 22
    • 0033874081 scopus 로고    scopus 로고
    • Identification and molecular-genetic characterization of a LAMP/CD68-like protein from Caenorhabditis elegans
    • Kostich M., Fire A., and Fambrough D.M. Identification and molecular-genetic characterization of a LAMP/CD68-like protein from Caenorhabditis elegans. J. Cell Sci. 113 (2000) 2595-2606
    • (2000) J. Cell Sci. , vol.113 , pp. 2595-2606
    • Kostich, M.1    Fire, A.2    Fambrough, D.M.3
  • 23
    • 0034811429 scopus 로고    scopus 로고
    • Genetic analysis of endocytosis in Caenorhabditis elegans: coelomocyte uptake defective mutants
    • Fares H., and Greenwald I. Genetic analysis of endocytosis in Caenorhabditis elegans: coelomocyte uptake defective mutants. Genetics 159 (2001) 133-145
    • (2001) Genetics , vol.159 , pp. 133-145
    • Fares, H.1    Greenwald, I.2
  • 25
    • 49849106194 scopus 로고    scopus 로고
    • WormBase web site, http://www.wormbase.org, release WS173, date March 23, 2007.
    • WormBase web site, http://www.wormbase.org, release WS173, date March 23, 2007.
  • 29
    • 0033760264 scopus 로고    scopus 로고
    • Cloning of the gene encoding a novel integral membrane protein, mucolipidin- and identification of the two major founder mutations causing Mucolipidosis type IV
    • Bassi M.T., Manzoni M., Monti E., Pizzo M.T., Ballabio A., and Borsani G. Cloning of the gene encoding a novel integral membrane protein, mucolipidin- and identification of the two major founder mutations causing Mucolipidosis type IV. Am. J. Hum. Genet. 67 (2000) 1110-1120
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 1110-1120
    • Bassi, M.T.1    Manzoni, M.2    Monti, E.3    Pizzo, M.T.4    Ballabio, A.5    Borsani, G.6
  • 32
    • 0037007142 scopus 로고    scopus 로고
    • The Caenorhabditis elegans mucolipin-like gene cup-5 is essential for viability and regulates lysosomes in multiple cell types
    • Hersh B.M., Hartwieg E., and Horvitz H.R. The Caenorhabditis elegans mucolipin-like gene cup-5 is essential for viability and regulates lysosomes in multiple cell types. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 4355-4360
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4355-4360
    • Hersh, B.M.1    Hartwieg, E.2    Horvitz, H.R.3
  • 33
    • 0035031192 scopus 로고    scopus 로고
    • Regulation of endocytosis by CUP-5, the Caenorhabditis elegans mucolipin-1 homolog
    • Fares H., and Greenwald I. Regulation of endocytosis by CUP-5, the Caenorhabditis elegans mucolipin-1 homolog. Nat. Genet. 28 (2001) 64-68
    • (2001) Nat. Genet. , vol.28 , pp. 64-68
    • Fares, H.1    Greenwald, I.2
  • 34
    • 33745685199 scopus 로고    scopus 로고
    • Basis of lethality in C. elegans lacking CUP-5, the Mucolipidosis type IV orthologue
    • Schaheen L., Dang H., and Fares H. Basis of lethality in C. elegans lacking CUP-5, the Mucolipidosis type IV orthologue. Dev. Biol. 293 (2006) 382-391
    • (2006) Dev. Biol. , vol.293 , pp. 382-391
    • Schaheen, L.1    Dang, H.2    Fares, H.3
  • 35
    • 18744363612 scopus 로고    scopus 로고
    • Identification and characterization of the single channel function of human mucolipin-1 implicated in Mucolipidosis type IV, a disorder affecting the lysosomal pathway
    • LaPlante J.M., Falardeau J., Sun M., Kanazirska M., Brown E.M., Slaugenhaupt S.A., and Vassilev P.M. Identification and characterization of the single channel function of human mucolipin-1 implicated in Mucolipidosis type IV, a disorder affecting the lysosomal pathway. FEBS Lett. 532 (2002) 183-187
    • (2002) FEBS Lett. , vol.532 , pp. 183-187
    • LaPlante, J.M.1    Falardeau, J.2    Sun, M.3    Kanazirska, M.4    Brown, E.M.5    Slaugenhaupt, S.A.6    Vassilev, P.M.7
  • 36
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • Pryor P.R., Mullock B.M., Bright N.A., Gray S.R., and Luzio J.P. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. (2000) 1053-1062
    • (2000) J. Cell Biol. , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 37
    • 33750429328 scopus 로고    scopus 로고
    • Suppression of the cup-5 Mucolipidosis type IV-related lysosomal dysfunction by the inactivation of an ABC transporter in C. elegans
    • Schaheen L., Patton G., and Fares H. Suppression of the cup-5 Mucolipidosis type IV-related lysosomal dysfunction by the inactivation of an ABC transporter in C. elegans. Development 133 (2006) 3939-3948
    • (2006) Development , vol.133 , pp. 3939-3948
    • Schaheen, L.1    Patton, G.2    Fares, H.3
  • 38
    • 0000842144 scopus 로고    scopus 로고
    • Niemann-Pick disease
    • Neurodystrophies and Neurolipidioses. Moser H.W. (Ed), Elsevier B.V., Amsterdam
    • Vanier M.T., and Suzuki K. Niemann-Pick disease. In: Moser H.W. (Ed). Neurodystrophies and Neurolipidioses. Handbook of Clinical Neurology vol. 66 (1996), Elsevier B.V., Amsterdam 133-162
    • (1996) Handbook of Clinical Neurology , vol.66 , pp. 133-162
    • Vanier, M.T.1    Suzuki, K.2
  • 39
    • 0001745899 scopus 로고    scopus 로고
    • Type A and B Niemann-Pick disease: deficiencies of acid sphingomyelinase activity
    • Scriver C.R., and Sly W.S. (Eds), McGraw-Hill Inc., New York
    • Schuchman E.H., and Desnick R.J. Type A and B Niemann-Pick disease: deficiencies of acid sphingomyelinase activity. In: Scriver C.R., and Sly W.S. (Eds). The Metabolic and Molecular Bases of Inherited Disease. 8th edition (2001), McGraw-Hill Inc., New York 3589-3610
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. 8th edition , pp. 3589-3610
    • Schuchman, E.H.1    Desnick, R.J.2
  • 41
    • 0032486480 scopus 로고    scopus 로고
    • Caenorhabditis elegans contains two distinct acid sphingomyelinases
    • Lin X., Hengartner M.O., and Kolesnick R. Caenorhabditis elegans contains two distinct acid sphingomyelinases. J. Biol. Chem. 273 (1998) 14374-14379
    • (1998) J. Biol. Chem. , vol.273 , pp. 14374-14379
    • Lin, X.1    Hengartner, M.O.2    Kolesnick, R.3
  • 44
    • 0034192462 scopus 로고    scopus 로고
    • A model for Niemann-Pick type C disease in the nematode Caenorhabditis elegans
    • Sym M., Basson M., and Johnson C. A model for Niemann-Pick type C disease in the nematode Caenorhabditis elegans. Curr. Biol. 10 (2000) 527-530
    • (2000) Curr. Biol. , vol.10 , pp. 527-530
    • Sym, M.1    Basson, M.2    Johnson, C.3
  • 45
    • 10344229417 scopus 로고    scopus 로고
    • NCR-1 and NCR-2, the C. elegans homologs of the human Niemann-Pick type C1 disease protein, function upstream of DAF-9 in the dauer formation pathways
    • Li J., Brown G., Ailion M., Lee S., and Thomas J.H. NCR-1 and NCR-2, the C. elegans homologs of the human Niemann-Pick type C1 disease protein, function upstream of DAF-9 in the dauer formation pathways. Development 131 (2004) 5741-5752
    • (2004) Development , vol.131 , pp. 5741-5752
    • Li, J.1    Brown, G.2    Ailion, M.3    Lee, S.4    Thomas, J.H.5
  • 46
    • 2342420089 scopus 로고    scopus 로고
    • Hormonal signals produced by DAF-9/cytochrome P450 regulate C. elegans dauer diapause in response to environmental cues
    • Gerisch B., and Antebi A. Hormonal signals produced by DAF-9/cytochrome P450 regulate C. elegans dauer diapause in response to environmental cues. Development 131 (2004) 1765-1776
    • (2004) Development , vol.131 , pp. 1765-1776
    • Gerisch, B.1    Antebi, A.2
  • 47
    • 2342428206 scopus 로고    scopus 로고
    • Intercellular signaling of reproductive development by the C. elegans DAF-9 cytochrome P450
    • Mak H.Y., and Ruvkun G. Intercellular signaling of reproductive development by the C. elegans DAF-9 cytochrome P450. Development 131 (2004) 1777-1786
    • (2004) Development , vol.131 , pp. 1777-1786
    • Mak, H.Y.1    Ruvkun, G.2
  • 54
    • 0036254584 scopus 로고    scopus 로고
    • The art and design of genetic screens: Caenorhabditis elegans
    • Jorgensen E.M., and Mango S.E. The art and design of genetic screens: Caenorhabditis elegans. Nat. Rev., Genet. 3 (2002) 356-369
    • (2002) Nat. Rev., Genet. , vol.3 , pp. 356-369
    • Jorgensen, E.M.1    Mango, S.E.2
  • 57
    • 21044448584 scopus 로고    scopus 로고
    • The cell biology of Hermansky-Pudlak syndrome: recent advances
    • Di Pietro S.M., and Dell'Angelica E.C. The cell biology of Hermansky-Pudlak syndrome: recent advances. Traffic 6 (2005) 525-533
    • (2005) Traffic , vol.6 , pp. 525-533
    • Di Pietro, S.M.1    Dell'Angelica, E.C.2
  • 58
    • 0042307384 scopus 로고    scopus 로고
    • Biogenesis of lysosome-related organelles complex 3 (BLOC-3): a complex containing the Hermansky-Pudlak syndrome (HPS) proteins HPS1 and HPS4
    • Nazarian R., Falcon-Perez J.M., and Dell'Angelica E.C. Biogenesis of lysosome-related organelles complex 3 (BLOC-3): a complex containing the Hermansky-Pudlak syndrome (HPS) proteins HPS1 and HPS4. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 8770-8775
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8770-8775
    • Nazarian, R.1    Falcon-Perez, J.M.2    Dell'Angelica, E.C.3
  • 59
    • 0043208690 scopus 로고    scopus 로고
    • BLOC-3, a protein complex containing the Hermansky-Pudlak syndrome gene products HPS1 and HPS4
    • Martina J.A., Moriyama K., and Bonifacino J.S. BLOC-3, a protein complex containing the Hermansky-Pudlak syndrome gene products HPS1 and HPS4. J. Biol. Chem. 278 (2003) 29376-29384
    • (2003) J. Biol. Chem. , vol.278 , pp. 29376-29384
    • Martina, J.A.1    Moriyama, K.2    Bonifacino, J.S.3
  • 60
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor
    • Dell'Angelica E.C., Shotelersuk V., Aguilar R.C., Gahl W.A., and Bonifacino J.S. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor. Mol. Cell 3 (1999) 11-21
    • (1999) Mol. Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 61
    • 1842509099 scopus 로고    scopus 로고
    • Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins
    • Peden A.A., Oorschot V., Hesser B.A., Austin C.D., Scheller R.H., and Klumperman J. Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins. J. Cell Biol. 164 (2004) 1065-1076
    • (2004) J. Cell Biol. , vol.164 , pp. 1065-1076
    • Peden, A.A.1    Oorschot, V.2    Hesser, B.A.3    Austin, C.D.4    Scheller, R.H.5    Klumperman, J.6
  • 63
    • 27244457650 scopus 로고    scopus 로고
    • The AP-3 clathrin-associated complex is essential for embryonic and larval development in Caenorhabditis elegans
    • Shim J., and Lee J. The AP-3 clathrin-associated complex is essential for embryonic and larval development in Caenorhabditis elegans. Mol. Cell 19 (2005) 452-457
    • (2005) Mol. Cell , vol.19 , pp. 452-457
    • Shim, J.1    Lee, J.2
  • 66
    • 0029147298 scopus 로고
    • Isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium
    • IBDC. Isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium. Cell 82 (1995) 949-957
    • (1995) Cell , vol.82 , pp. 949-957
    • IBDC1
  • 67
    • 25844517550 scopus 로고    scopus 로고
    • Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses
    • Mole S.E., Williams R.E., and Goebel H.H. Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses. Neurogenetics 6 (2005) 107-126
    • (2005) Neurogenetics , vol.6 , pp. 107-126
    • Mole, S.E.1    Williams, R.E.2    Goebel, H.H.3
  • 68
    • 0034659833 scopus 로고    scopus 로고
    • A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration
    • Tyynela J., Sohar I., Sleat D.E., Gin R.M., Donnelly R.J., Baumann M., Haltia M., and Lobel P. A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration. EMBO J. 19 (2000) 2786-2792
    • (2000) EMBO J. , vol.19 , pp. 2786-2792
    • Tyynela, 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
  • 69
    • 33847303003 scopus 로고    scopus 로고
    • Cathepsin E deficiency induces a novel form of lysosomal storage disorder showing the accumulation of lysosomal membrane sialoglycoproteins and the elevation of lysosomal pH in macrophages
    • Yanagawa M., Tsukuba T., Nishioku T., Okamoto Y., Okamoto K., Takii R., Terada Y., Nakayama K.I., Kadowaki T., and Yamamoto K. Cathepsin E deficiency induces a novel form of lysosomal storage disorder showing the accumulation of lysosomal membrane sialoglycoproteins and the elevation of lysosomal pH in macrophages. J. Biol. Chem. 282 (2007) 1851-1862
    • (2007) J. Biol. Chem. , vol.282 , pp. 1851-1862
    • Yanagawa, M.1    Tsukuba, T.2    Nishioku, T.3    Okamoto, Y.4    Okamoto, K.5    Takii, R.6    Terada, Y.7    Nakayama, K.I.8    Kadowaki, T.9    Yamamoto, K.10
  • 70
    • 0037206901 scopus 로고    scopus 로고
    • Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans
    • Syntichaki P., Xu K., Driscoll M., and Tavernarakis N. Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans. Nature 419 (2002) 939-944
    • (2002) Nature , vol.419 , pp. 939-944
    • Syntichaki, P.1    Xu, K.2    Driscoll, M.3    Tavernarakis, N.4
  • 71
    • 33744741034 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced caspase-4 activation mediates apoptosis and neurodegeneration in INCL
    • Kim S.J., Zhang Z., Hitomi E., Lee Y.C., and Mukherjee A.B. Endoplasmic reticulum stress-induced caspase-4 activation mediates apoptosis and neurodegeneration in INCL. Hum. Mol. Genet. 15 (2006) 1826-1834
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1826-1834
    • Kim, S.J.1    Zhang, Z.2    Hitomi, E.3    Lee, Y.C.4    Mukherjee, A.B.5
  • 72
    • 0035167162 scopus 로고    scopus 로고
    • Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles: implications for infantile neuronal ceroid lipofuscinosis (INCL)
    • Lehtovirta M., Kyttälä A., Eskelinen E.L., Hess M., Heinonen O., and Jalanko A. Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles: implications for infantile neuronal ceroid lipofuscinosis (INCL). Hum. Mol. Genet. 10 (2001) 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
  • 73
    • 16444380927 scopus 로고    scopus 로고
    • Identification and characterization of Caenorhabditis elegans palmitoyl protein thioesterase1
    • Porter M.Y., Turmaine M., and Mole S.E. Identification and characterization of Caenorhabditis elegans palmitoyl protein thioesterase1. J. Neurosci. Res. 79 (2005) 836-848
    • (2005) J. Neurosci. Res. , vol.79 , pp. 836-848
    • Porter, M.Y.1    Turmaine, M.2    Mole, S.E.3
  • 74
    • 31644449018 scopus 로고    scopus 로고
    • Deletion of the Caenorhabditis elegans homologues of the CLN3 gene, involved in human juvenile neuronal ceroid lipofuscinosis, causes a mild progeric phenotype
    • De Voer G., van der Bent P., Rodrigues A.J., van Ommen G.J., Peters D.J., and Taschner P.E. Deletion of the Caenorhabditis elegans homologues of the CLN3 gene, involved in human juvenile neuronal ceroid lipofuscinosis, causes a mild progeric phenotype. J. Inherit. Metab. Dis. 28 (2005) 1065-1080
    • (2005) J. Inherit. Metab. Dis. , vol.28 , pp. 1065-1080
    • De Voer, G.1    van der Bent, P.2    Rodrigues, A.J.3    van Ommen, G.J.4    Peters, D.J.5    Taschner, P.E.6
  • 76
    • 0036174123 scopus 로고    scopus 로고
    • Abnormal osteoclast morphology and bone remodeling in a murine model of a lysosomal storage disease
    • Monroy M.A., Ross F.P., Teitelbaum S.L., and Sands M.S. Abnormal osteoclast morphology and bone remodeling in a murine model of a lysosomal storage disease. Bone 30 (2002) 352-359
    • (2002) Bone , vol.30 , pp. 352-359
    • Monroy, M.A.1    Ross, F.P.2    Teitelbaum, S.L.3    Sands, M.S.4
  • 77
    • 33745584383 scopus 로고    scopus 로고
    • The phosphoinositide kinase PIKfyve/Fab1p regulates terminal lysosome maturation in Caenorhabditis elegans
    • Nicot A.S., Fares H., Payrastre B., Chisholm A.D., Labouesse M., and Laporte J. The phosphoinositide kinase PIKfyve/Fab1p regulates terminal lysosome maturation in Caenorhabditis elegans. Mol. Biol. Cell 17 (2006) 3062-3074
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3062-3074
    • Nicot, A.S.1    Fares, H.2    Payrastre, B.3    Chisholm, A.D.4    Labouesse, M.5    Laporte, J.6
  • 79
    • 33644861728 scopus 로고    scopus 로고
    • ClC-7 requires Ostm1 as a beta-subunit to support bone resorption and lysosomal function
    • Lange P.F., Wartosch L., Jentsch T.J., and Fuhrmann J.C. ClC-7 requires Ostm1 as a beta-subunit to support bone resorption and lysosomal function. Nature 440 (2006) 220-223
    • (2006) Nature , vol.440 , pp. 220-223
    • Lange, P.F.1    Wartosch, L.2    Jentsch, T.J.3    Fuhrmann, J.C.4
  • 80
    • 33747052036 scopus 로고    scopus 로고
    • The role of megalin (LRP-2/Gp330) during development
    • Fisher C.E., and Howie S.E. The role of megalin (LRP-2/Gp330) during development. Dev. Biol. 296 (2006) 279-297
    • (2006) Dev. Biol. , vol.296 , pp. 279-297
    • Fisher, C.E.1    Howie, S.E.2
  • 81
    • 0033000965 scopus 로고    scopus 로고
    • A gp330/megalin-related protein is required in the major epidermis of Caenorhabditis elegans for completion of molting
    • Yochem J., Tuck S., Greenwald I., and Han M. A gp330/megalin-related protein is required in the major epidermis of Caenorhabditis elegans for completion of molting. Development 126 (1999) 597-606
    • (1999) Development , vol.126 , pp. 597-606
    • Yochem, J.1    Tuck, S.2    Greenwald, I.3    Han, M.4
  • 82
    • 0001531616 scopus 로고    scopus 로고
    • Extracellular matrix
    • Riddle D.L., Blumenthal T., Meyer B.J., and Priess J.R. (Eds), Cold Spring Harbor Laboratory Press, New York
    • Kramer J.M. Extracellular matrix. In: Riddle D.L., Blumenthal T., Meyer B.J., and Priess J.R. (Eds). C. elegans II (1997), Cold Spring Harbor Laboratory Press, New York 471-500
    • (1997) C. elegans II , pp. 471-500
    • Kramer, J.M.1
  • 83
    • 21844450464 scopus 로고    scopus 로고
    • CeVPS-27 is an endosomal protein required for the molting and the endocytic trafficking of the low-density lipoprotein receptor-related protein 1 in Caenorhabditis elegans
    • Roudier N., Lefebvre C., and Legouis R. CeVPS-27 is an endosomal protein required for the molting and the endocytic trafficking of the low-density lipoprotein receptor-related protein 1 in Caenorhabditis elegans. Traffic 6 (2005) 695-705
    • (2005) Traffic , vol.6 , pp. 695-705
    • Roudier, N.1    Lefebvre, C.2    Legouis, R.3
  • 84
  • 86
    • 1242316967 scopus 로고    scopus 로고
    • The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1, has a multifunctional role during the worms' development
    • Hashmi S., Zhang J., Oksov Y., and Lustigman S. The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1, has a multifunctional role during the worms' development. J. Biol. Chem. 279 (2004) 6035-6045
    • (2004) J. Biol. Chem. , vol.279 , pp. 6035-6045
    • Hashmi, S.1    Zhang, J.2    Oksov, Y.3    Lustigman, S.4
  • 89
    • 3142580943 scopus 로고    scopus 로고
    • Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)
    • Starcevic M., and Dell'Angelica E.C. Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1). J. Biol. Chem. 279 (2004) 28393-28401
    • (2004) J. Biol. Chem. , vol.279 , pp. 28393-28401
    • Starcevic, M.1    Dell'Angelica, E.C.2
  • 91
    • 33947158693 scopus 로고    scopus 로고
    • Function of the Caenorhabditis elegans ABC transporter PGP-2 in the biogenesis of a lysosome-related fat storage organelle
    • Schroeder L.D., Kremer S., Kramer M.J., Currie E., Kwan E., Watts J.L., Lawrenson A.L., and Hermann G.J. Function of the Caenorhabditis elegans ABC transporter PGP-2 in the biogenesis of a lysosome-related fat storage organelle. Mol. Biol. Cell 18 (2007) 995-1008
    • (2007) Mol. Biol. Cell , vol.18 , pp. 995-1008
    • Schroeder, L.D.1    Kremer, S.2    Kramer, M.J.3    Currie, E.4    Kwan, E.5    Watts, J.L.6    Lawrenson, A.L.7    Hermann, G.J.8
  • 92
    • 25444525460 scopus 로고    scopus 로고
    • Characterization of gana-1, a Caenorhabditis elegans gene encoding a single ortholog of vertebrate α-galactosidase and α-N-acetylgalactosaminidase
    • Hujova J., Sikora J., Dobrovolny R., Poupetova H., Ledvinova J., Kostrouchova M., and Hrebicek M. Characterization of gana-1, a Caenorhabditis elegans gene encoding a single ortholog of vertebrate α-galactosidase and α-N-acetylgalactosaminidase. BMC Cell Biol. 6 (2005) 5
    • (2005) BMC Cell Biol. , vol.6 , pp. 5
    • Hujova, J.1    Sikora, J.2    Dobrovolny, R.3    Poupetova, H.4    Ledvinova, J.5    Kostrouchova, M.6    Hrebicek, M.7
  • 93
    • 0035113642 scopus 로고    scopus 로고
    • High-throughput reverse genetics: RNAi screens in Caenorhabditis elegans
    • REVIEWS1005
    • Bargmann C.I. High-throughput reverse genetics: RNAi screens in Caenorhabditis elegans. Genome Biol. 2 (2001) REVIEWS1005
    • (2001) Genome Biol. , vol.2
    • Bargmann, C.I.1


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