메뉴 건너뛰기




Volumn 25, Issue 5, 2005, Pages 1655-1668

The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ACID LIPASE; ESTER; GENE PRODUCT; LYSOZYME; STEROL; TRIACYLGLYCEROL LIPASE;

EID: 14044272811     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.5.1655-1668.2005     Document Type: Article
Times cited : (118)

References (54)
  • 1
    • 0026556144 scopus 로고
    • Molecular cloning and physical analysis of an 8.2 kb segment of chromosome XI of Saccharomyces cerevisiae reveals five tightly linked genes
    • Abraham, P. R., A. Mulder, J. Van't Riet, R. J. Planta, and H. A. Raue. 1992. Molecular cloning and physical analysis of an 8.2 kb segment of chromosome XI of Saccharomyces cerevisiae reveals five tightly linked genes. Yeast 8:227-238.
    • (1992) Yeast , vol.8 , pp. 227-238
    • Abraham, P.R.1    Mulder, A.2    Van't Riet, J.3    Planta, R.J.4    Raue, H.A.5
  • 2
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • Alani, E., L. Cao, and N. Kleckner. 1987. A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics 116:541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 3
    • 0027954965 scopus 로고
    • Purification, characterization and molecular cloning of human hepatic lysosomal acid lipase
    • Ameis, D., M. Merkel, C. Eckerskorn, and H. Greten. 1994. Purification, characterization and molecular cloning of human hepatic lysosomal acid lipase. Eur. J. Biochem. 219:905-914.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 905-914
    • Ameis, D.1    Merkel, M.2    Eckerskorn, C.3    Greten, H.4
  • 4
    • 23444460383 scopus 로고
    • Mutations at the lysosomal acid cholesteryl ester hydrolase gene locus in Wolman disease
    • Anderson, R. A., R. S. Byrum, P. M. Coates, and G. N. Sando. 1994. Mutations at the lysosomal acid cholesteryl ester hydrolase gene locus in Wolman disease. Proc. Natl. Acad. Sci. USA 91:2718-2722.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2718-2722
    • Anderson, R.A.1    Byrum, R.S.2    Coates, P.M.3    Sando, G.N.4
  • 5
    • 0025791980 scopus 로고
    • Cloning and expression of cDNA encoding human lysosomal acid lipase/cholesteryl ester hydrolase. Similarities to gastric and lingual lipases
    • Anderson, R. A., and G. N. Sando. 1991. Cloning and expression of cDNA encoding human lysosomal acid lipase/cholesteryl ester hydrolase. Similarities to gastric and lingual lipases. J. Biol. Chem. 266:22479-22484.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22479-22484
    • Anderson, R.A.1    Sando, G.N.2
  • 6
    • 0002416162 scopus 로고
    • Acid lipase deficiency: Wolman disease and cholesteryl ester storage disease
    • C. R. Scriver, A. L. Beaduet, W. S. Sly, and D. Valle (ed.), McGraw-Hill, New York, N.Y.
    • Assmann, G., and U. Seedorf. 1995. Acid lipase deficiency: Wolman disease and cholesteryl ester storage disease, p. 2563-2587. In C. R. Scriver, A. L. Beaduet, W. S. Sly, and D. Valle (ed.), The metabolic and molecular bases of inherited disease. McGraw-Hill, New York, N.Y.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 2563-2587
    • Assmann, G.1    Seedorf, U.2
  • 7
    • 0037931415 scopus 로고    scopus 로고
    • YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae
    • Athenstaedt, K., and G. Daum. 2003. YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae. J. Biol. Chem. 278:23317-23323.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23317-23323
    • Athenstaedt, K.1    Daum, G.2
  • 8
    • 0032693609 scopus 로고    scopus 로고
    • Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae
    • Athenstaedt, K., D. Zweytick, A. Jandrositz, S. D. Kohlwein, and G. Daum. 1999. Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J. Bacteriol. 181:6441-6448.
    • (1999) J. Bacteriol. , vol.181 , pp. 6441-6448
    • Athenstaedt, K.1    Zweytick, D.2    Jandrositz, A.3    Kohlwein, S.D.4    Daum, G.5
  • 9
    • 0016818790 scopus 로고
    • Yeast sterol esters and their relationship to the growth of yeast
    • Bailey, R. B., and L. W. Parks. 1975. Yeast sterol esters and their relationship to the growth of yeast. J. Bacteriol. 124:606-612.
    • (1975) J. Bacteriol. , vol.124 , pp. 606-612
    • Bailey, R.B.1    Parks, L.W.2
  • 11
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M. S., and J. L. Goldstein. 1986. A receptor-mediated pathway for cholesterol homeostasis. Science 232:34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 12
    • 0019162068 scopus 로고
    • The cholesteryl ester cycle in macrophage foam cells. Continual hydrolysis and re-esterification of cytoplasmic cholesteryl esters
    • Brown, M. S., Y. K. Ho, and J. L. Goldstein. 1980. The cholesteryl ester cycle in macrophage foam cells. Continual hydrolysis and re-esterification of cytoplasmic cholesteryl esters. J. Biol. Chem. 255:9344-9352.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9344-9352
    • Brown, M.S.1    Ho, Y.K.2    Goldstein, J.L.3
  • 13
    • 0015518311 scopus 로고
    • Deficient activity of hepatic acid lipase in cholesterol ester storage disease
    • Burke, J. A., and W. K. Schubert. 1972. Deficient activity of hepatic acid lipase in cholesterol ester storage disease. Science 176:309-310.
    • (1972) Science , vol.176 , pp. 309-310
    • Burke, J.A.1    Schubert, W.K.2
  • 14
    • 0030943621 scopus 로고    scopus 로고
    • Acyl-coenzyme A:cholesterol acyltransferase
    • Chang, T. Y., C. C. Chang, and D. Cheng. 1997. Acyl-coenzyme A:cholesterol acyltransferase. Annu. Rev. Biochem. 66:613-638.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 613-638
    • Chang, T.Y.1    Chang, C.C.2    Cheng, D.3
  • 15
    • 0030930513 scopus 로고    scopus 로고
    • The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae
    • Corsi, A. K., and R. Schekman. 1997. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J. Cell Biol. 137:1483-1493.
    • (1997) J. Cell Biol. , vol.137 , pp. 1483-1493
    • Corsi, A.K.1    Schekman, R.2
  • 16
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • Cowles, C. R., G. Odorizzi, G. S. Payne, and S. D. Emr. 1997. The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell 91:109-118.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 17
    • 0026305078 scopus 로고
    • Relationships among serine hydrolases: Evidence for a common structural motif in triacylglyceride lipases and esterases
    • Derewenda, Z. S., and U. Derewenda. 1991. Relationships among serine hydrolases: evidence for a common structural motif in triacylglyceride lipases and esterases. Biochem. Cell. Biol. 69:842-851.
    • (1991) Biochem. Cell. Biol. , vol.69 , pp. 842-851
    • Derewenda, Z.S.1    Derewenda, U.2
  • 18
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • Dupree, P., R. G. Parton, G. Raposo, T. V. Kurzchalia, and K. Simons. 1993. Caveolae and sorting in the trans-Golgi network of epithelial cells. EMBO J. 12:1597-1605.
    • (1993) EMBO J. , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 19
    • 0016836751 scopus 로고
    • Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease
    • Goldstein, J. L., S. E. Dana, J. R. Faust, A. L. Beaudet, and M. S. Brown. 1975. Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease. J. Biol. Chem. 250:8487-8495.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8487-8495
    • Goldstein, J.L.1    Dana, S.E.2    Faust, J.R.3    Beaudet, A.L.4    Brown, M.S.5
  • 20
    • 0028980860 scopus 로고
    • Sorting of yeast α1,3-mannosyltransferase is mediated by a lumenal domain interaction, and a transmembrane domain signal that can confer clathrin-dependent Golgi localization to a secreted protein
    • Graham, T. R., and V. A. Krasnov. 1995. Sorting of yeast α1,3-mannosyltransferase is mediated by a lumenal domain interaction, and a transmembrane domain signal that can confer clathrin-dependent Golgi localization to a secreted protein. Mol. Biol. Cell 6:809-824.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 809-824
    • Graham, T.R.1    Krasnov, V.A.2
  • 21
    • 0026756118 scopus 로고
    • SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex
    • Hardwick, K. G., and H. R. Pelham. 1992. SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J. Cell Biol. 119:513-521.
    • (1992) J. Cell Biol. , vol.119 , pp. 513-521
    • Hardwick, K.G.1    Pelham, H.R.2
  • 22
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • Heim, R., D. C. Prasher, and R. Y. Tsien. 1994. Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc. Natl. Acad. Sci. USA 91:12501-12504.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 23
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologues in the TGN/endosomal system of yeast
    • Holthuis, J. C., B. J. Nichols, S. Dhruvakumar, and H. R. Pelham. 1998. Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 17:113-126.
    • (1998) EMBO J. , vol.17 , pp. 113-126
    • Holthuis, J.C.1    Nichols, B.J.2    Dhruvakumar, S.3    Pelham, H.R.4
  • 25
    • 0020529962 scopus 로고
    • Transformation of intact cells with alkali cations
    • Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact cells with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 26
    • 0026041521 scopus 로고
    • The gene encoding squalene epoxidase from Saccharomyces cerevisiae: Cloning and characterization
    • Jandrositz, A., F. Turnowsky, and G. Hogenauer. 1991. The gene encoding squalene epoxidase from Saccharomyces cerevisiae: cloning and characterization. Gene 107:155-160.
    • (1991) Gene , vol.107 , pp. 155-160
    • Jandrositz, A.1    Turnowsky, F.2    Hogenauer, G.3
  • 27
    • 0024509922 scopus 로고
    • Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts
    • Lange, Y., M. H. Swaisgood, B. V. Ramos, and T. L. Steck. 1989. Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts. J. Biol. Chem. 264:3786-3793.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3786-3793
    • Lange, Y.1    Swaisgood, M.H.2    Ramos, B.V.3    Steck, T.L.4
  • 28
    • 0028942598 scopus 로고
    • Export of steryl esters from lipid particles and release of free sterols in the yeast, Saccharomyces cerevisiae
    • Leber, R., E. Zinser, C. Hrastnik, F. Paltauf, and G. Daum. 1995. Export of steryl esters from lipid particles and release of free sterols in the yeast, Saccharomyces cerevisiae. Biochim. Biophys. Acta 1234:119-126.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 119-126
    • Leber, R.1    Zinser, E.2    Hrastnik, C.3    Paltauf, F.4    Daum, G.5
  • 29
    • 0028081336 scopus 로고
    • Characterization of lipid particles of the yeast, Saccharomyces cerevisiae
    • Leber, R., E. Zinser, G. Zellnig, F. Paltauf, and G. Daum. 1994. Characterization of lipid particles of the yeast, Saccharomyces cerevisiae. Yeast 10:1421-1428.
    • (1994) Yeast , vol.10 , pp. 1421-1428
    • Leber, R.1    Zinser, E.2    Zellnig, G.3    Paltauf, F.4    Daum, G.5
  • 30
    • 0030983202 scopus 로고    scopus 로고
    • Human lysosomal acid lipase/cholesteryl ester hydrolase and human gastric lipase: Identification of the catalytically active serine, aspartic acid, and histidine residues
    • Lohse, P., S. Chahrokh-Zadeh, and D. Seidel. 1997. Human lysosomal acid lipase/cholesteryl ester hydrolase and human gastric lipase: identification of the catalytically active serine, aspartic acid, and histidine residues. J. Lipid Res. 38:892-903.
    • (1997) J. Lipid Res. , vol.38 , pp. 892-903
    • Lohse, P.1    Chahrokh-Zadeh, S.2    Seidel, D.3
  • 31
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., A. McKenzie III, D. J. Demarini, N. G. Shah, A. Wach, A. Brachat, P. Philippsen, and J. R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 32
    • 0022449910 scopus 로고
    • Characteristics of sterol uptake in Saccharomyces cerevisiae
    • Lorenz, R. T., R. J. Rodriguez, T. A. Lewis, and L. W. Parks. 1986. Characteristics of sterol uptake in Saccharomyces cerevisiae. J. Bacteriol. 167:981-985.
    • (1986) J. Bacteriol. , vol.167 , pp. 981-985
    • Lorenz, R.T.1    Rodriguez, R.J.2    Lewis, T.A.3    Parks, L.W.4
  • 36
    • 0034194152 scopus 로고    scopus 로고
    • Phosphoinositide signaling and the regulation of membrane trafficking in yeast
    • Odrorizzi, G., M. Babst, and S. D. Emr. 2000. Phosphoinositide signaling and the regulation of membrane trafficking in yeast. Trends Biochem. Sci. 25:229-235.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 229-235
    • Odrorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 38
    • 0019763102 scopus 로고
    • Cerulenin
    • Omura, S. 1981. Cerulenin. Methods Enzymol. 72:520-532.
    • (1981) Methods Enzymol. , vol.72 , pp. 520-532
    • Omura, S.1
  • 39
    • 0031852450 scopus 로고    scopus 로고
    • New lysosomal acid lipase gene mutants explain the phenotype of Wolman disease and cholesteryl ester storage disease
    • Pagani, F., R. Pariyarath, R. Garcia, C. Stuani, A. B. Burlina, G. Ruotolo, M. Rabusin, and F. E. Baralle. 1998. New lysosomal acid lipase gene mutants explain the phenotype of Wolman disease and cholesteryl ester storage disease. J. Lipid Res. 39:1382-1388.
    • (1998) J. Lipid Res. , vol.39 , pp. 1382-1388
    • Pagani, F.1    Pariyarath, R.2    Garcia, R.3    Stuani, C.4    Burlina, A.B.5    Ruotolo, G.6    Rabusin, M.7    Baralle, F.E.8
  • 40
    • 0030924426 scopus 로고    scopus 로고
    • Cysteine residues in human lysosomal acid lipase are involved in selective cholesteryl esterase activity
    • Pagani, F., R. Pariyarath, C. Stuani, R. Garcia, and F. E. Baralle. 1997. Cysteine residues in human lysosomal acid lipase are involved in selective cholesteryl esterase activity. Biochem. J. 326:265-269.
    • (1997) Biochem. J. , vol.326 , pp. 265-269
    • Pagani, F.1    Pariyarath, R.2    Stuani, C.3    Garcia, R.4    Baralle, F.E.5
  • 41
    • 0014674556 scopus 로고
    • Deficiency of an acid lipase in Wolman's disease
    • Patrick, A. D., and B. D. Lake. 1969. Deficiency of an acid lipase in Wolman's disease. Nature 222:1067-1068.
    • (1969) Nature , vol.222 , pp. 1067-1068
    • Patrick, A.D.1    Lake, B.D.2
  • 42
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and alpha/beta hydrolase fold
    • Schrag, J. D., and M. Cygler. 1997. Lipases and alpha/beta hydrolase fold. Methods Enzymol. 284:85-107.
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 43
    • 0024227621 scopus 로고
    • +-ATPase from plasma membranes of Saccharomyces cerevisiae and Avena sativa roots: Purification and reconstitution
    • +-ATPase from plasma membranes of Saccharomyces cerevisiae and Avena sativa roots: purification and reconstitution. Methods Enzymol. 157:533-544.
    • (1988) Methods Enzymol. , vol.157 , pp. 533-544
    • Serrano, R.1
  • 44
    • 0037477829 scopus 로고    scopus 로고
    • Perilipin a is essential for the translocation of hormone-sensitive lipase during lipolytic activation
    • Sztalryd, C., G. Xu, H. Dorward, J. T. Tansey, J. A. Contreras, A. R. Kimmel, and C. Londos. 2003. Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation. J. Cell Biol. 161:1093-1103.
    • (2003) J. Cell Biol. , vol.161 , pp. 1093-1103
    • Sztalryd, C.1    Xu, G.2    Dorward, H.3    Tansey, J.T.4    Contreras, J.A.5    Kimmel, A.R.6    Londos, C.7
  • 45
    • 0019404190 scopus 로고
    • Purification and properties of sterol-ester hydrolase from Saccharomyces cerevisiae
    • Tokyo
    • Taketani, S., T. Nishino, and H. Katsuki. 1981. Purification and properties of sterol-ester hydrolase from Saccharomyces cerevisiae. J. Biochem. (Tokyo) 89:1667-1673.
    • (1981) J. Biochem. , vol.89 , pp. 1667-1673
    • Taketani, S.1    Nishino, T.2    Katsuki, H.3
  • 46
    • 0017822390 scopus 로고
    • Characterization of sterol-ester hydrolase in Saccharomyces cerevisiae
    • Taketani, S., T. Osumi, and H. Katsuki. 1978. Characterization of sterol-ester hydrolase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 525:87-92.
    • (1978) Biochim. Biophys. Acta , vol.525 , pp. 87-92
    • Taketani, S.1    Osumi, T.2    Katsuki, H.3
  • 47
    • 1842865488 scopus 로고    scopus 로고
    • Lipid-dependent subcellular relocalization of the acyl chain desaturase in yeast
    • Tatzer, V., G. Zellnig, S. D. Kohlwein, and R. Schneiter. 2002. Lipid-dependent subcellular relocalization of the acyl chain desaturase in yeast. Mol. Biol. Cell 13:4429-4442.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4429-4442
    • Tatzer, V.1    Zellnig, G.2    Kohlwein, S.D.3    Schneiter, R.4
  • 48
    • 0018123233 scopus 로고
    • Metabolic interconversion of free sterols and steryl esters in Saccharomyces cerevisiae
    • Taylor, F. R., and L. W. Parks. 1978. Metabolic interconversion of free sterols and steryl esters in Saccharomyces cerevisiae. J. Bacteriol. 136:531-537.
    • (1978) J. Bacteriol. , vol.136 , pp. 531-537
    • Taylor, F.R.1    Parks, L.W.2
  • 49
    • 2642589009 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae TGL2 gene encodes a protein with lipolytic activity and can complement an Escherichia coli diacylglycerol kinase disruptant
    • Van Heusden, G. P., M. Nebohacova, T. L. Overbeeke, and H. Y. Steensma. 1998. The Saccharomyces cerevisiae TGL2 gene encodes a protein with lipolytic activity and can complement an Escherichia coli diacylglycerol kinase disruptant. Yeast 14:225-232.
    • (1998) Yeast , vol.14 , pp. 225-232
    • Van Heusden, G.P.1    Nebohacova, M.2    Overbeeke, T.L.3    Steensma, H.Y.4
  • 51
    • 0036317550 scopus 로고    scopus 로고
    • The lipase gene family
    • Wong, H., and M. C. Schotz. 2002. The lipase gene family. J. Lipid Res. 43:993-999.
    • (2002) J. Lipid Res. , vol.43 , pp. 993-999
    • Wong, H.1    Schotz, M.C.2
  • 53
    • 0029835340 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two isoforms of Saccharomyces cerevisiae acyl-CoA:sterol acyltransferase
    • Yu, C., N. J. Kennedy, C. C. Chang, and J. A. Rothblatt. 1996. Molecular cloning and characterization of two isoforms of Saccharomyces cerevisiae acyl-CoA:sterol acyltransferase. J. Biol. Chem. 271:24157-24163.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24157-24163
    • Yu, C.1    Kennedy, N.J.2    Chang, C.C.3    Rothblatt, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.