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Volumn 4, Issue 11, 2005, Pages 1851-1862

Saccharomyces cerevisiae Npc2p is a functionally conserved homologue of the human Niemann-Pick Disease Type C 2 protein, hNPC2

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHOLESTEROL; GLYCOPROTEIN; HYBRID PROTEIN; NPC2 PROTEIN, HUMAN; NPC2 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 27744528392     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.4.11.1851-1862.2005     Document Type: Article
Times cited : (39)

References (51)
  • 2
    • 24944583281 scopus 로고    scopus 로고
    • A yeast model system for functional analysis of the Niemann-Pick type C protein 1 (NPC1) homologue, Ncr1p
    • Berger, A. C., P. K. Hanson, J. W. Nichols, and A. H. Corbett. 2005. A yeast model system for functional analysis of the Niemann-Pick type C protein 1 (NPC1) homologue, Ncr1p. Traffic 6:907-917.
    • (2005) Traffic , vol.6 , pp. 907-917
    • Berger, A.C.1    Hanson, P.K.2    Nichols, J.W.3    Corbett, A.H.4
  • 4
    • 0342424187 scopus 로고    scopus 로고
    • Fast prediction and visualization of protein binding pockets with PASS
    • Brady, G. P., Jr., and P. F. Stouten. 2000. Fast prediction and visualization of protein binding pockets with PASS. J. Comput. Aided Mol. Des. 14:383-401.
    • (2000) J. Comput. Aided Mol. Des. , vol.14 , pp. 383-401
    • Brady Jr., G.P.1    Stouten, P.F.2
  • 7
    • 4744347394 scopus 로고    scopus 로고
    • Niemann-Pick type C disease: Importance of N glycosylation sites for function and cellular location of the NPC2 protein
    • Chikh, K., S. Vey, C. Simonot, M. T. Vanier, and G. Millat. 2004. Niemann-Pick type C disease: importance of N glycosylation sites for function and cellular location of the NPC2 protein. Mol. Genet. Metab. 83:220-230.
    • (2004) Mol. Genet. Metab. , vol.83 , pp. 220-230
    • Chikh, K.1    Vey, S.2    Simonot, C.3    Vanier, M.T.4    Millat, G.5
  • 9
    • 0015980909 scopus 로고
    • Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes. 3. Molecular structure of the polyene antibiotic-cholesterol complexes
    • de Kruijff, B., and R. A. Demel. 1974. Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes. 3. Molecular structure of the polyene antibiotic-cholesterol complexes. Biochim. Biophys. Acta 339:57-70.
    • (1974) Biochim. Biophys. Acta , vol.339 , pp. 57-70
    • De Kruijff, B.1    Demel, R.A.2
  • 11
    • 0039311662 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 is required for synaptic vesicle budding in PC12 cells
    • Faundez, V., J. T. Horng, and R. B. Kelly. 1997. ADP-ribosylation factor 1 is required for synaptic vesicle budding in PC12 cells. J. Cell Biol. 138:505-515.
    • (1997) J. Cell Biol. , vol.138 , pp. 505-515
    • Faundez, V.1    Horng, J.T.2    Kelly, R.B.3
  • 12
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser, A., R. K. Do, and A. Sali. 2000. Modeling of loops in protein structures. Protein Sci. 9:1753-1773.
    • (2000) Protein Sci. , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 13
    • 0037418188 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease
    • USA
    • Friedland, N., H. L. Liou, P. Lobel, and A. M. Stock. 2003. Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease. Proc. Natl. Acad. Sci. USA 100:2512-2517.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 2512-2517
    • Friedland, N.1    Liou, H.L.2    Lobel, P.3    Stock, A.M.4
  • 14
    • 0037815282 scopus 로고    scopus 로고
    • NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols
    • Frolov, A., S. E. Zielinski, J. R. Crowley, N. Dudley-Rucker, J. E. Schaffer, and D. S. Ory. 2003. NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols. J. Biol. Chem. 278:25517-25525.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25517-25525
    • Frolov, A.1    Zielinski, S.E.2    Crowley, J.R.3    Dudley-Rucker, N.4    Schaffer, J.E.5    Ory, D.S.6
  • 15
    • 0035102329 scopus 로고    scopus 로고
    • NBD-labeled phosphatidylcholine and phosphatidylethanolamine are internalized by transbilayer transport across the yeast plasma membrane
    • Grant, A. M., P. K. Hanson, L. Malone, and J. W. Nichols. 2001. NBD-labeled phosphatidylcholine and phosphatidylethanolamine are internalized by transbilayer transport across the yeast plasma membrane. Traffic 2:37-50.
    • (2001) Traffic , vol.2 , pp. 37-50
    • Grant, A.M.1    Hanson, P.K.2    Malone, L.3    Nichols, J.W.4
  • 16
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 17
    • 0036629344 scopus 로고    scopus 로고
    • NBD-labeled phosphatidylcholine enters the yeast vacuole via the pre-vacuolar compartment
    • Hanson, P. K., A. M. Grant, and J. W. Nichols. 2002. NBD-labeled phosphatidylcholine enters the yeast vacuole via the pre-vacuolar compartment. J. Cell Sci. 115:2725-2733.
    • (2002) J. Cell Sci. , vol.115 , pp. 2725-2733
    • Hanson, P.K.1    Grant, A.M.2    Nichols, J.W.3
  • 18
    • 0141704333 scopus 로고    scopus 로고
    • Lem3p is essential for the uptake and potency of alkylphosphocholine drugs, edelfosine and miltefosine
    • Hanson, P. K., L. Malone, J. L. Birchmore, and J. W. Nichols. 2003. Lem3p is essential for the uptake and potency of alkylphosphocholine drugs, edelfosine and miltefosine. J. Biol. Chem. 278:36041-36050.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36041-36050
    • Hanson, P.K.1    Malone, L.2    Birchmore, J.L.3    Nichols, J.W.4
  • 19
    • 0035971152 scopus 로고    scopus 로고
    • Energy-dependent flip of fluorescence-labeled phospholipids is regulated by nutrient starvation and transcription factors, PDR1 and PDR3
    • Hanson, P. K., and J. W. Nichols. 2001. Energy-dependent flip of fluorescence-labeled phospholipids is regulated by nutrient starvation and transcription factors, PDR1 and PDR3. J. Biol. Chem. 276:9861-9867.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9861-9867
    • Hanson, P.K.1    Nichols, J.W.2
  • 21
    • 0036558018 scopus 로고    scopus 로고
    • ML: A conserved domain involved in innate immunity and lipid metabolism
    • Inohara, N., and G. Nunez. 2002. ML: a conserved domain involved in innate immunity and lipid metabolism. Trends Biochem. Sci. 27:219-221.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 219-221
    • Inohara, N.1    Nunez, G.2
  • 23
    • 0028788038 scopus 로고
    • Kinetics of spindle pole body separation in budding yeast
    • USA
    • Kahana, J. A., B. J. Schnapp, and P. A. Silver. 1995. Kinetics of spindle pole body separation in budding yeast. Proc. Natl. Acad. Sci. USA 92:9707-9711.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9707-9711
    • Kahana, J.A.1    Schnapp, B.J.2    Silver, P.A.3
  • 24
    • 0029866407 scopus 로고    scopus 로고
    • Molecular cloning and characterization of HE1, a major secretory protein of the human epididymis
    • Kirchhoff, C., C. Osterhoff, and L. Young. 1996. Molecular cloning and characterization of HE1, a major secretory protein of the human epididymis. Biol. Reprod. 54:847-856.
    • (1996) Biol. Reprod. , vol.54 , pp. 847-856
    • Kirchhoff, C.1    Osterhoff, C.2    Young, L.3
  • 26
    • 0344838432 scopus 로고    scopus 로고
    • The integrity of a cholesterol-binding pocket in Niemann-Pick C2 protein is necessary to control lysosome cholesterol levels
    • USA
    • Ko, D. C., J. Binkley, A. Sidow, and M. P. Scott. 2003. The integrity of a cholesterol-binding pocket in Niemann-Pick C2 protein is necessary to control lysosome cholesterol levels. Proc. Natl. Acad. Sci. USA 100:2518-2525.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 2518-2525
    • Ko, D.C.1    Binkley, J.2    Sidow, A.3    Scott, M.P.4
  • 27
    • 0029897642 scopus 로고    scopus 로고
    • Dynamic localization of the nuclear import receptor and its interactions with transport factors
    • Koepp, D. M., D. H. Wong, A. H. Corbett, and P. A. Silver. 1996. Dynamic localization of the nuclear import receptor and its interactions with transport factors. J. Cell Biol. 133:1163-1176.
    • (1996) J. Cell Biol. , vol.133 , pp. 1163-1176
    • Koepp, D.M.1    Wong, D.H.2    Corbett, A.H.3    Silver, P.A.4
  • 28
    • 0031035738 scopus 로고    scopus 로고
    • Primary structure of EPV20, a secretory glycoprotein containing a previously uncharacterized type of domain
    • Larsen, L. B., P. Ravn, A. Boisen, L. Berglund, and T. E. Petersen. 1997. Primary structure of EPV20, a secretory glycoprotein containing a previously uncharacterized type of domain. Eur. J. Biochem. 243:437-441.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 437-441
    • Larsen, L.B.1    Ravn, P.2    Boisen, A.3    Berglund, L.4    Petersen, T.E.5
  • 29
    • 0034158443 scopus 로고    scopus 로고
    • Niemann-Pick type C mutations cause lipid traffic jam
    • Liscum, L. 2000. Niemann-Pick type C mutations cause lipid traffic jam. Traffic. 1:218-225.
    • (2000) Traffic , vol.1 , pp. 218-225
    • Liscum, L.1
  • 36
    • 0141753992 scopus 로고    scopus 로고
    • Identification of 58 novel mutations in Niemann-Pick disease type C: Correlation with biochemical phenotype and importance of PTC1-like domains in NPC1
    • Park, W. D., J. F. O'Brien, P. A. Lundquist, D. L. Kraft, C. W. Vockley, P. S. Karnes, M. C. Patterson, and K. Snow. 2003. Identification of 58 novel mutations in Niemann-Pick disease type C: correlation with biochemical phenotype and importance of PTC1-like domains in NPC1. Hum. Mutat. 22:313-325.
    • (2003) Hum. Mutat. , vol.22 , pp. 313-325
    • Park, W.D.1    O'Brien, J.F.2    Lundquist, P.A.3    Kraft, D.L.4    Vockley, C.W.5    Karnes, P.S.6    Patterson, M.C.7    Snow, K.8
  • 38
    • 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., V. Oorschot, B. A. Hesser, C. D. Austin, R. H. Scheller, and J. Klumperman. 2004. Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins. J. Cell Biol. 164:1065-1076.
    • (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
  • 39
    • 0033574029 scopus 로고    scopus 로고
    • Characterization and expression of the cDNA encoding a new kind of phospholipid transfer protein, the phosphatidylglycerol/phosphatidylinositol transfer protein from Aspergillus oryzae: Evidence of a putative membrane targeted phospholipid transfer protein in fungi
    • Record, E., S. Moukha, and M. Asther. 1999. Characterization and expression of the cDNA encoding a new kind of phospholipid transfer protein, the phosphatidylglycerol/phosphatidylinositol transfer protein from Aspergillus oryzae: evidence of a putative membrane targeted phospholipid transfer protein in fungi. Biochim. Biophys. Acta 1444:276-282.
    • (1999) Biochim. Biophys. Acta , vol.1444 , pp. 276-282
    • Record, E.1    Moukha, S.2    Asther, M.3
  • 41
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali, A., and T. L. Blundell. 1993. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 43
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • Schmidt, H. A., K. Strimmer, M. Vingron, and A. von Haeseler. 2002. TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. Bioinformatics 18:502-504.
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    Von Haeseler, A.4
  • 44
    • 0032962940 scopus 로고    scopus 로고
    • Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase
    • Seedorf, M., M. Damelin, J. Kahana, T. Taura, and P. A. Silver. 1999. Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Mol. Cell. Biol. 19:1547-1557.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1547-1557
    • Seedorf, M.1    Damelin, M.2    Kahana, J.3    Taura, T.4    Silver, P.A.5
  • 45
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 46
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 47
    • 0034731399 scopus 로고    scopus 로고
    • Mutations in yeast ARV1 alter intracellular sterol distribution and are complemented by human ARV1
    • Tinkelenberg, A. H., Y. Liu, F. Alcantara, S. Khan, Z. Guo, M. Bard, and S. L. Sturley. 2000. Mutations in yeast ARV1 alter intracellular sterol distribution and are complemented by human ARV1. J. Biol. Chem. 275:40667-40670.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40667-40670
    • Tinkelenberg, A.H.1    Liu, Y.2    Alcantara, F.3    Khan, S.4    Guo, Z.5    Bard, M.6    Sturley, S.L.7
  • 48
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some application
    • USA
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some application. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 50
    • 0028794516 scopus 로고
    • Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S288C
    • Winston, F., C. Dollard, and S. L. Ricupero-Hovasse. 1995. Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S288C. Yeast 11:53-55.
    • (1995) Yeast , vol.11 , pp. 53-55
    • Winston, F.1    Dollard, C.2    Ricupero-Hovasse, S.L.3


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