메뉴 건너뛰기




Volumn 23, Issue 8, 2009, Pages 2349-2359

Identification and characterization of a complete carnitine biosynthesis pathway in Candida albicans

Author keywords

Acetyl unit transport; Carnitine acetyltransferase; Hydroxytrimethyllysine aldolase; Nonfermentable carbon source; Threonine aldolase

Indexed keywords

ACETIC ACID; ALCOHOL; BUTYROBETAINE DIOXYGENASE; CARNITINE; FATTY ACID; FUNGAL ENZYME; HYDROXYTRIMETHYLLYSINE ALDOLASE; OXIDOREDUCTASE; TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; TRIMETHYLLYSINE DIOXYGENASE; UNCLASSIFIED DRUG; 4 N TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 4-N-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 6 N TRIMETHYLLYSINE HYDROXYLASE; ALDEHYDE DEHYDROGENASE; BETA HYDROXY TRIMETHYLLYSINE ALDOLASE; BETA-HYDROXY-TRIMETHYLLYSINE ALDOLASE; EPSILON-N-TRIMETHYLLYSINE HYDROXYLASE; GAMMA BUTYROBETAINE DIOXYGENASE; LYASE; MIXED FUNCTION OXIDASE;

EID: 68849090311     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.08-127985     Document Type: Article
Times cited : (33)

References (41)
  • 1
    • 0021024932 scopus 로고
    • Carnitine-metabolism and functions
    • Bremer, J. (1983) Carnitine-metabolism and functions. Physiol. Rev. 63, 1420-1480
    • (1983) Physiol. Rev. , vol.63 , pp. 1420-1480
    • Bremer, J.1
  • 2
    • 0021362187 scopus 로고
    • Kinetic compartmental analysis of carnitine metabolism in the human carnitine deficiency syndromes. Evidence for alterations in tissue carnitine transport
    • Rebouche, C. J., and Engel, A. G. (1984) Kinetic compartmental analysis of carnitine metabolism in the human carnitine deficiency syndromes. Evidence for alterations in tissue carnitine transport. J. Clin. Invest. 73, 857-867
    • (1984) J. Clin. Invest. , vol.73 , pp. 857-867
    • Rebouche, C.J.1    Engel, A.G.2
  • 3
    • 0017707410 scopus 로고
    • Biosynthesis of carnitine in Neurospora crassa
    • Kaufman, R. A., and Broquist, H. P. (1977) Biosynthesis of carnitine in Neurospora crassa. J. Biol. Chem. 252, 7437-7439
    • (1977) J. Biol. Chem. , vol.252 , pp. 7437-7439
    • Kaufman, R.A.1    Broquist, H.P.2
  • 4
    • 0005818582 scopus 로고
    • Carnitine precursors in the rat
    • Bremer, J. (1962) Carnitine precursors in the rat. Biochim. Biophys. Acta 57, 327-335
    • (1962) Biochim. Biophys. Acta , vol.57 , pp. 327-335
    • Bremer, J.1
  • 5
    • 0015935341 scopus 로고
    • Role of lysine and -N-trimethyllysine in carnitine biosynthesis. II. Studies in the rat
    • Tanphaichitr, V., and Broquist, H. P. (1973) Role of lysine and -N-trimethyllysine in carnitine biosynthesis. II. Studies in the rat. J. Biol. Chem. 248, 2176-2181
    • (1973) J. Biol. Chem. , vol.248 , pp. 2176-2181
    • Tanphaichitr, V.1    Broquist, H.P.2
  • 6
    • 0017164060 scopus 로고
    • Carnitine biosynthesis: The formation of glycine from carbons 1 and 2 of 6-N-trimethyl-L-lysine
    • Hochalter, J. B., and Henderson, L. M. (1976) Carnitine biosynthesis: the formation of glycine from carbons 1 and 2 of 6-N-trimethyl-L-lysine. Biochem. Biophys. Res. Commun. 70, 364-368
    • (1976) Biochem. Biophys. Res. Commun. , vol.70 , pp. 364-368
    • Hochalter, J.B.1    Henderson, L.M.2
  • 7
    • 0017891065 scopus 로고
    • Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase
    • Hulse, J. D., Ellis, S. R., and Henderson, L. M. (1978) Carnitine biosynthesis. beta-Hydroxylation of trimethyllysine by an alpha-ketoglutarate- dependent mitochondrial dioxygenase. J. Biol. Chem. 253, 1654-1659
    • (1978) J. Biol. Chem. , vol.253 , pp. 1654-1659
    • Hulse, J.D.1    Ellis, S.R.2    Henderson, L.M.3
  • 8
    • 0015215623 scopus 로고
    • Protein methylation
    • Paik, W. K., and Kim, S. (1971) Protein methylation. Science 174, 114-119
    • (1971) Science , vol.174 , pp. 114-119
    • Paik, W.K.1    Kim, S.2
  • 9
    • 0036471216 scopus 로고    scopus 로고
    • Carnitine biosynthesis in mammals
    • Vaz, F. M., and Wanders, R. J. (2002) Carnitine biosynthesis in mammals. Biochem. J. 361, 417-429
    • (2002) Biochem. J. , vol.361 , pp. 417-429
    • Vaz, F.M.1    Wanders, R.J.2
  • 10
    • 0035823607 scopus 로고    scopus 로고
    • Molecular and Biochemical Characterization of Rat epsilon-N- Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis
    • DOI 10.1074/jbc.M105929200
    • Vaz, F. M., Ofman, R., Westinga, K., Back, J. W., and Wanders, R. J. (2001) Molecular and biochemical characterization of rat epsilon-N- trimethyllysine hydroxylase, the first enzyme of carnitine biosynthesis. J. Biol. Chem. 276, 33512-33517 (Pubitemid 37384562)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.36 , pp. 33512-33517
    • Vaz, F.M.1    Ofman, R.2    Westinga, K.3    Back, J.W.4    Wanders, R.J.A.5
  • 11
  • 12
    • 0034629439 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of rat gamma- Trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis
    • DOI 10.1074/jbc.275.10.7390
    • Vaz, F. M., Fouchier, S. W., Ofman, R., Sommer, M., and Wanders, R. J. (2000) Molecular and biochemical characterization of rat gamma- trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J. Biol. Chem. 275, 7390-7394 (Pubitemid 30146293)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.10 , pp. 7390-7394
    • Vaz, F.M.1    Fouchier, S.W.2    Ofman, R.3    Sommer, M.4    Wanders, R.J.A.5
  • 13
    • 2042503352 scopus 로고
    • Purification of the enzymes involved in the conversion of trimethyl-lysine to trimethylaminobutyrate
    • (Frenkel, R. A., and McGarry, J. D., eds) Academic Press, New York
    • Henderson, L. M., Hulse, J. D., and Henderson, L. L. (1980) Purification of the enzymes involved in the conversion of trimethyl-lysine to trimethylaminobutyrate. In Carnitine Biosynthesis, Metabolism and Functions (Frenkel, R. A., and McGarry, J. D., eds) pp. 35-43, Academic Press, New York
    • (1980) Carnitine Biosynthesis, Metabolism and Functions , pp. 35-43
    • Henderson, L.M.1    Hulse, J.D.2    Henderson, L.L.3
  • 14
    • 0020413515 scopus 로고
    • Mammalian enzymes of trimethyllysine conversion to trimethylaminobutyrate
    • Henderson, L. M., Nelson, P. J., and Henderson, L. (1982) Mammalian enzymes of trimethyllysine conversion to trimethylaminobutyrate. Fed. Proc. 41, 2843-2847
    • (1982) Fed. Proc. , vol.41 , pp. 2843-2847
    • Henderson, L.M.1    Nelson, P.J.2    Henderson, L.3
  • 15
    • 0019826749 scopus 로고
    • Purification and characterization of cytosolic and mitochondrial serine hydroxymethyltransferases from rat liver
    • Ogawa, H., and Fujioka, M. (1981) Purification and characterization of cytosolic and mitochondrial serine hydroxymethyltransferases from rat liver. J. Biochem. 90, 381-390 (Pubitemid 11012618)
    • (1981) Journal of Biochemistry , vol.90 , Issue.2 , pp. 381-390
    • Ogawa, H.1    Fujioka, M.2
  • 16
    • 0020404409 scopus 로고
    • The effects of 1-amino-D-proline on the production of carnitine from exogenous protein-bound trimethyllysine by the perfused rat liver
    • Dunn, W. A., Aronson, N. N. Jr., and Englard, S. (1982) The effects of 1-amino-D-proline on the production of carnitine from exogenous protein-bound trimethyllysine by the perfused rat liver. J. Biol. Chem. 257, 7948-7951
    • (1982) J. Biol. Chem. , vol.257 , pp. 7948-7951
    • Dunn, W.A.1    Aronson Jr., N.N.2    Englard, S.3
  • 17
    • 0034200611 scopus 로고    scopus 로고
    • A new high-alkaline and high-molecular-weight pectate lyase from a Bacillus isolate: Enzymatic properties and cloning of the gene for the enzyme
    • Ogawa, A., Sawada, K., Saito, K., Hakamada, Y., Sumitomo, N., Hatada, Y., Kobayashi, T., and Ito, S. (2000) A new high-alkaline and high-molecular-weight pectate lyase from a Bacillus isolate: enzymatic properties and cloning of the gene for the enzyme. Biosci. Biotechnol. Biochem. 64, 1133-1141
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1133-1141
    • Ogawa, A.1    Sawada, K.2    Saito, K.3    Hakamada, Y.4    Sumitomo, N.5    Hatada, Y.6    Kobayashi, T.7    Ito, S.8
  • 18
    • 0033963660 scopus 로고    scopus 로고
    • Serine hydroxymethyltransferase and threonine aldolase: Are they identical?
    • DOI 10.1016/S1357-2725(99)00113-2, PII S1357272599001132
    • Ogawa, H., Gomi, T., and Fujioka, M. (2000) Serine hydroxymethyltransferase and threonine aldolase: are they identical? Int. J. Biochem. Cell Biol. 32, 289-301 (Pubitemid 30069971)
    • (2000) International Journal of Biochemistry and Cell Biology , vol.32 , Issue.3 , pp. 289-301
    • Ogawa, H.1    Gomi, T.2    Fujioka, M.3
  • 19
    • 0030945741 scopus 로고    scopus 로고
    • Identification of Saccharomyces cerevisiae GLY1 as a threonine aldolase: A key enzyme in glycine biosynthesis
    • DOI 10.1016/S0378-1097(97)00096-7, PII S0378109797000967
    • Monschau, N., Stahmann, K. P., Sahm, H., McNeil, J. B., and Bognar, A. L. (1997) Identification of Saccharomyces cerevisiae GLY1 as a threonine aldolase: a key enzyme in glycine biosynthesis. FEMS Microbiol. Lett. 150, 55-60 (Pubitemid 27234412)
    • (1997) FEMS Microbiology Letters , vol.150 , Issue.1 , pp. 55-60
    • Monschau, N.1    Stahmann, K.-P.2    Sahm, H.3    McNeil, J.B.4    Bognar, A.L.5
  • 20
    • 0034985293 scopus 로고    scopus 로고
    • Carnitine-dependent metabolic activities in Saccharomyces cerevisiae: Three carnitine acetyltransferases are essential in a carnitine-dependent strain
    • DOI 10.1002/yea.712
    • Swiegers, J. H., Dippenaar, N., Pretorius, I. S., and Bauer, F. F. (2001) Carnitine-dependent metabolic activities in Saccharomyces cerevisiae: three carnitine acetyltransferases are essential in a carnitine-dependent strain. Yeast 18, 585-595 (Pubitemid 32496335)
    • (2001) Yeast , vol.18 , Issue.7 , pp. 585-595
    • Swiegers, J.H.1    Dippenaar, N.2    Pretorius, I.S.3    Bauer, F.F.4
  • 21
    • 0033231013 scopus 로고    scopus 로고
    • Molecular characterization of carnitine-dependent transport of acetyl-CoA from peroxisomes to mitochondria in Saccharomyces cerevisiae and identification of a plasma membrane carnitine transporter, Agp2p
    • van Roermund, C. W., Hettema, E. H., van den Berg, M., Tabak, H. F., and Wanders, R. J. (1999) Molecular characterization of carnitine-dependent transport of acetyl-CoA from peroxisomes to mitochondria in Saccharomyces cerevisiae and identification of a plasma membrane carnitine transporter, Agp2p. EMBO J. 18, 5843-5852
    • (1999) EMBO J. , vol.18 , pp. 5843-5852
    • Van Roermund, C.W.1    Hettema, E.H.2    Van Den Berg, M.3    Tabak, H.F.4    Wanders, R.J.5
  • 23
    • 42249115250 scopus 로고    scopus 로고
    • Carnitine-dependent transport of acetyl coenzyme a in Candida albicans is essential for growth on nonfermentable carbon sources and contributes to biofilm formation
    • DOI 10.1128/EC.00017-08
    • Strijbis, K., van Roermund, C. W., Visser, W. F., Mol, E. C., van den Burg, J., MacCallum, D. M., Odds, F. C., Paramonova, E., Krom, B. P., and Distel, B. (2008) Carnitine-dependent transport of acetyl coenzyme A in Candida albicans is essential for growth on nonfermentable carbon sources and contributes to biofilm formation. Eukaryot. Cell 7, 610-618 (Pubitemid 351959895)
    • (2008) Eukaryotic Cell , vol.7 , Issue.4 , pp. 610-618
    • Strijbis, K.1    Van Roermund, C.W.T.2    Visser, W.F.3    Mol, E.C.4    Van Den Burg, J.5    MacCallum, D.M.6    Odds, F.C.7    Paramonova, E.8    Krom, B.P.9    Distel, B.10
  • 24
    • 39749093831 scopus 로고    scopus 로고
    • Carnitine acetyltransferases are required for growth on non-fermentable carbon sources but not for pathogenesis in Candida albicans
    • DOI 10.1099/mic.0.2007/014555-0
    • Zhou, H., and Lorenz, M. C. (2008) Carnitine acetyltransferases are required for growth on non-fermentable carbon sources but not for pathogenesis in Candida albicans. Microbiology 154, 500-509 (Pubitemid 351292304)
    • (2008) Microbiology , vol.154 , Issue.2 , pp. 500-509
    • Zhou, H.1    Lorenz, M.C.2
  • 25
    • 13844316993 scopus 로고    scopus 로고
    • Strains and strategies for large-scale gene deletion studies of the diploid human fungal pathogen Candida albicans
    • DOI 10.1128/EC.4.2.298-309.2005
    • Noble, S. M., and Johnson, A. D. (2005) Strains and strategies for large-scale gene deletion studies of the diploid human fungal pathogen Candida albicans. Eukaryot. Cell 4, 298-309 (Pubitemid 40257130)
    • (2005) Eukaryotic Cell , vol.4 , Issue.2 , pp. 298-309
    • Noble, S.M.1    Johnson, A.D.2
  • 26
    • 0346252368 scopus 로고    scopus 로고
    • New modules for PCR-based gene targeting in Candida albicans: Rapid and efficient gene targeting using 100 bp of flanking homology region
    • DOI 10.1002/yea.1044
    • Gola, S., Martin, R., Walther, A., Dunkler, A., and Wendland, J. (2003) New modules for PCR-based gene targeting in Candida albicans: rapid and efficient gene targeting using 100 bp of flanking homology region. Yeast 20, 1339-1347 (Pubitemid 38016628)
    • (2003) Yeast , vol.20 , Issue.16 , pp. 1339-1347
    • Gola, S.1    Martin, R.2    Walther, A.3    Dunkler, A.4    Wendland, J.5
  • 27
    • 33750070351 scopus 로고    scopus 로고
    • New pFA-cassettes for PCR-based gene manipulation in Candida albicans
    • DOI 10.1002/jobm.200510133
    • Schaub, Y., Dunkler, A., Walther, A., and Wendland, J. (2006) New pFA-cassettes for PCR-based gene manipulation in Candida albicans. J. Basic Microbiol. 46, 416-429 (Pubitemid 44582323)
    • (2006) Journal of Basic Microbiology , vol.46 , Issue.5 , pp. 416-429
    • Schaub, Y.1    Dunkler, A.2    Walther, A.3    Wendland, J.4
  • 28
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J. D., Trueheart, J., Natsoulis, G., and Fink, G. R. (1987) 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154, 164-175
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 29
    • 0043023517 scopus 로고    scopus 로고
    • Diverged binding specificity of Rim101p, the Candida albicans ortholog of PacC
    • Ramon, A. M., and Fonzi, W. A. (2003) Diverged binding specificity of Rim101p, the Candida albicans ortholog of PacC. Eukaryot. Cell 2, 718-728
    • (2003) Eukaryot. Cell , vol.2 , pp. 718-728
    • Ramon, A.M.1    Fonzi, W.A.2
  • 30
    • 0037354365 scopus 로고    scopus 로고
    • An improved transformation protocol for the human fungal pathogen Candida albicans
    • DOI 10.1007/s00294-002-0349-0
    • Walther, A., and Wendland, J. (2003) An improved transformation protocol for the human fungal pathogen Candida albicans. Curr. Genet. 42, 339-343 (Pubitemid 36432355)
    • (2003) Current Genetics , vol.42 , Issue.6 , pp. 339-343
    • Walther, A.1    Wendland, J.2
  • 31
    • 0037629168 scopus 로고
    • Preparation and assay of phosphorylating submitochondrial systems: Mechanically ruptured mitochondria
    • (Colowick, S. P., and Kaplan, N. O., eds) 6 Academic Press, New York
    • Pullman, M., and Penefsky, H. S. (1963) Preparation and assay of phosphorylating submitochondrial systems: mechanically ruptured mitochondria. In Methods in Enzymology, Vol.6 (Colowick, S. P., and Kaplan, N. O., eds) 6 pp. 277-284, Academic Press, New York
    • (1963) Methods in Enzymology , vol.6 , pp. 277-284
    • Pullman, M.1    Penefsky, H.S.2
  • 32
    • 0037930740 scopus 로고    scopus 로고
    • ESI-MS/MS analysis of underivatised amino acids: A new tool for the diagnosis of inherited disorders of amino acid metabolism. Fragmentation study of 79 molecules of biological interest in positive and negative ionisation mode
    • DOI 10.1002/rcm.1054
    • Piraud, M., Vianey-Saban, C., Petritis, K., Elfakir, C., Steghens, J. P., Morla, A., and Bouchu, D. (2003) ESI-MS/MS analysis of underivatised amino acids: a new tool for the diagnosis of inherited disorders of amino acid metabolism. Fragmentation study of 79 molecules of biological interest in positive and negative ionisation mode. Rapid Commun. Mass Spectrom. 17, 1297-1311 (Pubitemid 36750014)
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , Issue.12 , pp. 1297-1311
    • Piraud, M.1    Vianey-Saban, C.2    Petritis, K.3    Elfakir, C.4    Steghens, J.-P.5    Morla, A.6    Bouchu, D.7
  • 33
    • 33744524787 scopus 로고    scopus 로고
    • Measurement of carnitine biosynthesis enzyme activities by tandem mass spectrometry: Differences between the mouse and the rat
    • Van Vlies, N., Wanders, R. J., and Vaz, F. M. (2006) Measurement of carnitine biosynthesis enzyme activities by tandem mass spectrometry: differences between the mouse and the rat. Anal. Biochem. 354, 132-139
    • (2006) Anal. Biochem. , vol.354 , pp. 132-139
    • Van Vlies, N.1    Wanders, R.J.2    Vaz, F.M.3
  • 34
    • 0034731826 scopus 로고    scopus 로고
    • Glycine metabolism in Candida albicans: Characterization of the serine hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1) genes
    • DOI 10.1002/(SICI)1097-0061(20000130)16:2<167::AID-YEA519>3.0.CO;2- 1
    • McNeil, J. B., Flynn, J., Tsao, N., Monschau, N., Stahmann, K., Haynes, R. H., McIntosh, E. M., and Pearlman, R. E. (2000) Glycine metabolism in Candida albicans: characterization of the serine hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1) genes. Yeast 16, 167-175 (Pubitemid 30088206)
    • (2000) Yeast , vol.16 , Issue.2 , pp. 167-175
    • McNeil, J.B.1    Flynn, J.2    Tsao, N.3    Monschau, N.4    Stahmann, K.-P.5    Haynes, R.H.6    McIntosh, E.M.7    Pearlman, R.E.8
  • 36
    • 0028071511 scopus 로고
    • Dietary threonine imbalance alters threonine dehydrogenase activity in isolated hepatic mitochondria of chicks and rats
    • Davis, A. J., and Austic, R. E. (1994) Dietary threonine imbalance alters threonine dehydrogenase activity in isolated hepatic mitochondria of chicks and rats. J. Nutr. 124, 1667-1677
    • (1994) J. Nutr. , vol.124 , pp. 1667-1677
    • Davis, A.J.1    Austic, R.E.2
  • 37
    • 25444506890 scopus 로고    scopus 로고
    • Mice have a transcribed L-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene
    • Edgar, A. J. (2005) Mice have a transcribed L-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene. BMC Genomics 6, 32
    • (2005) BMC Genomics , vol.6 , pp. 32
    • Edgar, A.J.1
  • 38
    • 0035666383 scopus 로고    scopus 로고
    • L-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase: A subgroup of strictly related enzymes specialized for different functions
    • DOI 10.1046/j.0014-2956.2001.02606.x
    • Contestabile, R., Paiardini, A., Pascarella, S., di Salvo, M. L., D'Aguanno, S., and Bossa, F. (2001) l-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions. Eur. J. Biochem. 268, 6508-6525 (Pubitemid 34014759)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.24 , pp. 6508-6525
    • Contestabile, R.1    Paiardini, A.2    Pascarella, S.3    Di Salvo, M.L.4    D'Aguanno, S.5    Bossa, F.6
  • 39
    • 0019310364 scopus 로고
    • Tissue distribution of carnitine biosynthetic enzymes in man
    • Rebouche, C. J., and Engel, A. G. (1980) Tissue distribution of carnitine biosynthetic enzymes in man. Biochim. Biophys. Acta 630, 22-29
    • (1980) Biochim. Biophys. Acta , vol.630 , pp. 22-29
    • Rebouche, C.J.1    Engel, A.G.2
  • 40
    • 0022560507 scopus 로고
    • Epsilon- N-trimethyllysine availability regulates the rate of carnitine biosynthesis in the growing rat
    • Rebouche, C. J., Lehman, L. J., and Olson, L. (1986) epsilon- N-trimethyllysine availability regulates the rate of carnitine biosynthesis in the growing rat. J. Nutr. 116, 751-759
    • (1986) J. Nutr. , vol.116 , pp. 751-759
    • Rebouche, C.J.1    Lehman, L.J.2    Olson, L.3
  • 41
    • 4444315751 scopus 로고    scopus 로고
    • Carnitine: A nutritional, biosynthetic, and functional perspective
    • DOI 10.1016/j.mam.2004.06.006, PII S0098299704000512
    • Steiber, A., Kerner, J., and Hoppel, C. L. (2004) Carnitine: a nutritional, biosynthetic, and functional perspective. Mol. Aspects Med. 25, 455-473 (Pubitemid 39195071)
    • (2004) Molecular Aspects of Medicine , vol.25 , Issue.5-6 , pp. 455-473
    • Steiber, A.1    Kerner, J.2    Hoppel, C.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.