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Volumn 12, Issue 9, 2002, Pages 555-562

Expression and characterization of a human cDNA that complements the temperature-sensitive defect in dolichol kinase activity in the yeast sec59-1 mutant: The enzymatic phosphorylation of dolichol and diacylglycerol are catalyzed by separate CTP-mediated kinase activities in Saccharomyces cerevisiae

Author keywords

Brain; Cytosine triphosphate; DNA cloning; Dolichol kinase; Endoplasmic reticulum

Indexed keywords

AMINO ACID; CARBOXYPEPTIDASE C; COMPLEMENTARY DNA; CYTIDINE TRIPHOSPHATE; DIACYLGLYCEROL; DNA; DOLICHOL; DOLICHOL PHOSPHATE; FUNGAL PROTEIN; PHOSPHOTRANSFERASE; POLYPEPTIDE; PROTEIN SEC59; UNCLASSIFIED DRUG;

EID: 0036744488     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwf068     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 0021109881 scopus 로고
    • Topography of dolichyl phosphate synthesis in rat liver microsomes. Transbilayer arrangement of dolichol kinase and long-chain prenyltransferase
    • Adair, W.L. Jr. and Cafmeyer, N. (1983) Topography of dolichyl phosphate synthesis in rat liver microsomes. Transbilayer arrangement of dolichol kinase and long-chain prenyltransferase. Biochim. Biophys. Acta, 751, 21-26.
    • (1983) Biochim. Biophys. Acta , vol.751 , pp. 21-26
    • Adair W.L., Jr.1    Cafmeyer, N.2
  • 2
    • 0024346917 scopus 로고
    • A 13-amino acid peptide in three yeast glycosyltransterases may be involved in dolichol recognition
    • Albright, C.F., Orlean, P., and Robbins, P.W. (1989) A 13-amino acid peptide in three yeast glycosyltransterases may be involved in dolichol recognition. Proc. Natl Acad. Sci. USA, 86, 7366-7369.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7366-7369
    • Albright, C.F.1    Orlean, P.2    Robbins, P.W.3
  • 3
    • 0018072479 scopus 로고
    • CTP-dependent dolichol phosphorylation by mammalian cell homogenates
    • Allen, C.M. Jr., Kalin, J.R., Sack, J., and Verizzo, D. (1978) CTP-dependent dolichol phosphorylation by mammalian cell homogenates. Biochemistry, 17, 5020-5026.
    • (1978) Biochemistry , vol.17 , pp. 5020-5026
    • Allen C.M., Jr.1    Kalin, J.R.2    Sack, J.3    Verizzo, D.4
  • 4
    • 0026067580 scopus 로고
    • Developmental changes in enzymes involved in dolichyl phosphate metabolism in cultured embryonic rat brain cells
    • Bhat, N.R., Frank, D.W., Wolf, M.J., and Waechter, C.J. (1991) Developmental changes in enzymes involved in dolichyl phosphate metabolism in cultured embryonic rat brain cells. J. Neurochem., 56, 339-344.
    • (1991) J. Neurochem , vol.56 , pp. 339-344
    • Bhat, N.R.1    Frank, D.W.2    Wolf, M.J.3    Waechter, C.J.4
  • 5
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • 1426
    • Burda, P. and Aebi, M. (1999) The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta, 1426, 239-257.
    • (1999) Biochim. Biophys. Acta , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 6
    • 0019485385 scopus 로고
    • Enhanced chick oviduct dolichol kinase activity during estrogen-induced differentiation
    • Burton, W.A., Lucas, J.J., and Waechter, C.J. (1981) Enhanced chick oviduct dolichol kinase activity during estrogen-induced differentiation. J. Biol. Chem., 256, 632-635.
    • (1981) J. Biol. Chem , vol.256 , pp. 632-635
    • Burton, W.A.1    Lucas, J.J.2    Waechter, C.J.3
  • 7
    • 0018290255 scopus 로고
    • Enzymatic phosphorylation of dolichol in central nervous tissue
    • Burton, W.A., Scher, M.G., and Waechter, C.J. (1979) Enzymatic phosphorylation of dolichol in central nervous tissue. J. Biol. Chem., 254, 7129-7136.
    • (1979) J. Biol. Chem , vol.254 , pp. 7129-7136
    • Burton, W.A.1    Scher, M.G.2    Waechter, C.J.3
  • 8
    • 0019888690 scopus 로고
    • Enhancement of protein glycosylation in tissue slices by dolichylphosphate
    • Carson, D.D., Earles, B.J., and Lennarz, W.J. (1981) Enhancement of protein glycosylation in tissue slices by dolichylphosphate. J Biol. Chem., 256, 11552-11557.
    • (1981) J Biol. Chem , vol.256 , pp. 11552-11557
    • Carson, D.D.1    Earles, B.J.2    Lennarz, W.J.3
  • 9
    • 0028045736 scopus 로고
    • Long-chain cis-isoprenyltransferase activity is induced early in the developmental program for protein N-glycosylation in embryonic rat brain cells
    • Crick, D.C. and Waechter, C.J. (1994) Long-chain cis-isoprenyltransferase activity is induced early in the developmental program for protein N-glycosylation in embryonic rat brain cells. J. Neurochem., 62, 247-256.
    • (1994) J. Neurochem , vol.62 , pp. 247-256
    • Crick, D.C.1    Waechter, C.J.2
  • 10
    • 0028243029 scopus 로고
    • Induction of dolichyl-saccharide intermediate biosynthesis corresponds to increased long chain cis-isoprenyltransferase activity during the mitogenic response in mouse B cells
    • Crick, D.C., Scocca, J.R., Rush, J.S., Frank, D.W., Krag, S.S., and Waechter, C.J. (1994) Induction of dolichyl-saccharide intermediate biosynthesis corresponds to increased long chain cis-isoprenyltransferase activity during the mitogenic response in mouse B cells. J. Biol.Chem.,269, 10559-10565.
    • (1994) J. Biol.Chem , vol.269 , pp. 10559-10565
    • Crick, D.C.1    Scocca, J.R.2    Rush, J.S.3    Frank, D.W.4    Krag, S.S.5    Waechter, C.J.6
  • 11
    • 0031589542 scopus 로고    scopus 로고
    • Novel salvage pathway utilizing farnesol and geranylgeraniol for protein isoprenylation
    • Crick, D.C., Andres, D.A., and Waechter, C.J. (1997) Novel salvage pathway utilizing farnesol and geranylgeraniol for protein isoprenylation. Biochem. Biophys. Res. Commun., 237, 483-487.
    • (1997) Biochem. Biophys. Res. Commun , vol.237 , pp. 483-487
    • Crick, D.C.1    Andres, D.A.2    Waechter, C.J.3
  • 12
    • 0031881719 scopus 로고    scopus 로고
    • Protein C- mannosylation is enzyme -catalysed and uses dolichol-phosphate-mannose as a precursor
    • Doucey, M.A., Hess, D., Cacan, R., and Hofsteenge, J. (1998) Protein C- mannosylation is enzyme -catalysed and uses dolichol-phosphate-mannose as a precursor. Mol. Biol. Cell, 9, 291-300.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 291-300
    • Doucey, M.A.1    Hess, D.2    Cacan, R.3    Hofsteenge, J.4
  • 13
    • 0035798688 scopus 로고    scopus 로고
    • The cwh8 gene encodes a dolichyl pyrophosphate phosphatase with a luminally oriented active site in the endoplasmic reticulum of Saccharomyces cerevisiae
    • Fernandez, F., Rush, J.S., Toke, D.A., Han, G-S., Quinn, J.E., Carman, G.M., Choi, J-Y., Voelker, D.R., Aebi, M., and Waechter, C.J. (2001) The cwh8 gene encodes a dolichyl pyrophosphate phosphatase with a luminally oriented active site in the endoplasmic reticulum of Saccharomyces cerevisiae. J. Biol. Chem., 276, 41455-41464.
    • (2001) J. Biol. Chem , vol.276 , pp. 41455-41464
    • Fernandez, F.1    Rush, J.S.2    Toke, D.A.3    Han, G.-S.4    Quinn, J.E.5    Carman, G.M.6    Choi, J.-Y.7    Voelker, D.R.8    Aebi, M.9    Waechter, C.J.10
  • 14
    • 0035716899 scopus 로고    scopus 로고
    • Update and perspectives on congenital disorders of glycosylation
    • Freeze, H. (2001) Update and perspectives on congenital disorders of glycosylation. Glycobiology, 11, 129R-143R.
    • (2001) Glycobiology , vol.11
    • Freeze, H.1
  • 15
    • 0025215974 scopus 로고
    • Separation of brain dolichol kinase from endogenous activating factors: Evidence that phospholipid enhances the interaction between enzyme and dolichol
    • Genain, C.P. and Waechter, C.J. (1990) Separation of brain dolichol kinase from endogenous activating factors: evidence that phospholipid enhances the interaction between enzyme and dolichol. J. Neurochem., 54, 855-862.
    • (1990) J. Neurochem , vol.54 , pp. 855-862
    • Genain, C.P.1    Waechter, C.J.2
  • 16
    • 0017403404 scopus 로고
    • Effect of exogenous dolichyl monophosphate on a developmental change in mannosylphosphoryl-dolichol biosynthesis
    • Harford, J.B., Waechter, C.J., and Earl, F.L. (1977) Effect of exogenous dolichyl monophosphate on a developmental change in mannosylphosphoryl-dolichol biosynthesis. Biochem. Biophys. Res. Commun., 76, 1036-1043.
    • (1977) Biochem. Biophys. Res. Commun , vol.76 , pp. 1036-1043
    • Harford, J.B.1    Waechter, C.J.2    Earl, F.L.3
  • 17
    • 0026648113 scopus 로고
    • Saccharomyces cerevisiae sec59-1 cells are deficient in dolichol kinase activity
    • Heller, L., Orlean, P., and Adair, W.L. Jr. (1992) Saccharomyces cerevisiae sec59-1 cells are deficient in dolichol kinase activity. Proc. Natl Acad. Sci. USA, 89, 7013-7016.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7013-7016
    • Heller, L.1    Orlean, P.2    Adair W.L., Jr.3
  • 18
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics, A. and Orlean, P. (1993) Glycoprotein biosynthesis in yeast. FASEB J., 7, 540-550.
    • (1993) FASEB J , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 19
    • 0014962514 scopus 로고
    • Biosynthesis of peptidoglycan of bacterial cell walls. XX. identification of phosphatidylglycerol and cardiolipin as cofactors for isoprenoid alcohol phosphokinase
    • Higashi, Y. and Strominger, J. L. (1970) Biosynthesis of peptidoglycan of bacterial cell walls. XX. identification of phosphatidylglycerol and cardiolipin as cofactors for isoprenoid alcohol phosphokinase. J Biol. Chem., 245, 3691-3696.
    • (1970) J Biol. Chem , vol.245 , pp. 3691-3696
    • Higashi, Y.1    Strominger, J.L.2
  • 20
    • 0019296388 scopus 로고
    • Synthesis of the N-linked oligosaccharides of glycoproteins. Assembly of the lipid-linked precursor oligosaccharide and its relation to protein synthesis in vivo
    • Hubbard, S.C. and Robbins, P.W. (1980) Synthesis of the N-linked oligosaccharides of glycoproteins. Assembly of the lipid-linked precursor oligosaccharide and its relation to protein synthesis in vivo. J. Biol. Chem., 255, 11782-11793.
    • (1980) J. Biol. Chem , vol.255 , pp. 11782-11793
    • Hubbard, S.C.1    Robbins, P.W.2
  • 21
    • 0033617742 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • Kikuno, R., Nagase, T., Ishikawa, K., Hirosawa, M., Miyajima, N., Tanaka, A., Kotani, H., Nomura, N., and Ohara, O. (1999) Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res., 6, 197-205.
    • (1999) DNA Res , vol.6 , pp. 197-205
    • Kikuno, R.1    Nagase, T.2    Ishikawa, K.3    Hirosawa, M.4    Miyajima, N.5    Tanaka, A.6    Kotani, H.7    Nomura, N.8    Ohara, O.9
  • 22
    • 0029939658 scopus 로고    scopus 로고
    • Long-term effect of cyclic AMP on N-glycosylation is caused by an increase in the activity of the cis-prenyltransferase
    • Konrad, M. and Metz, W.E. (1996) Long-term effect of cyclic AMP on N-glycosylation is caused by an increase in the activity of the cis-prenyltransferase. Biochem. J., 316, 575-581.
    • (1996) Biochem. J , vol.316 , pp. 575-581
    • Konrad, M.1    Metz, W.E.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0017407123 scopus 로고
    • Increase in the lipid intermediate pathway of protein glycosylation during hen oviduct differentiation
    • Lucas, J.J. and Levin, E. (1977) Increase in the lipid intermediate pathway of protein glycosylation during hen oviduct differentiation. J. Biol. Chem., 252, 4330-4336.
    • (1977) J. Biol. Chem , vol.252 , pp. 4330-4336
    • Lucas, J.J.1    Levin, E.2
  • 25
    • 0032711147 scopus 로고    scopus 로고
    • Physicochemical factors for helical segments and protein-length
    • Mitaku, S. and Hirokawa, T. (1999) Physicochemical factors for helical segments and protein-length. Protein Eng., 12, 953-957.
    • (1999) Protein Eng , vol.12 , pp. 953-957
    • Mitaku, S.1    Hirokawa, T.2
  • 26
    • 0039172560 scopus 로고    scopus 로고
    • Lipid phosphorylation in chloroplast envelopes: Evidence for galactolipid CTP-dependent kinase activities
    • Muller, M.-O., Meylan-Bettex, M., Eckstein, F., Martinoia, E., Siegenthaler, P.-A., and Bovet, L. (2000) Lipid phosphorylation in chloroplast envelopes: evidence for galactolipid CTP-dependent kinase activities. J. Biol. Chem., 275, 19475-19481.
    • (2000) J. Biol. Chem , vol.275 , pp. 19475-19481
    • Muller, M.-O.1    Meylan-Bettex, M.2    Eckstein, F.3    Martinoia, E.4    Siegenthaler, P.-A.5    Bovet, L.6
  • 27
    • 0032584739 scopus 로고    scopus 로고
    • The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases
    • Nagiec, M., Skrzypek, M., Nagiec, E., Lester, R., and Dickson R., (1998) The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases. J. Biol. Chem., 273, 19437-19442.
    • (1998) J. Biol. Chem , vol.273 , pp. 19437-19442
    • Nagiec, M.1    Skrzypek, M.2    Nagiec, E.3    Lester, R.4    Dickson, R.5
  • 28
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson, T., Jackson, M., and Peterson, P. (1989) Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell, 58, 707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.3
  • 29
    • 0001519162 scopus 로고    scopus 로고
    • Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase: Role of histidine in the conserved HGXH in catalysis
    • Park, Y.-S., Gee, P., Sanker, S., Schurter, E.J., Zuiderweg, E.R.P., and Kent, C. (1997) Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase: role of histidine in the conserved HGXH in catalysis. J. Biol. Chem., 272, 15161-15166.
    • (1997) J. Biol. Chem , vol.272 , pp. 15161-15166
    • Park, Y.-S.1    Gee, P.2    Sanker, S.3    Schurter, E.J.4    Zuiderweg, E.R.P.5    Kent, C.6
  • 30
    • 0025042575 scopus 로고
    • Regulation of glycosylation. Three enzymes compete for a common pool of dolichyl phosphate in vivo
    • Rosenwald, A.G., Stoll, J., and Krag, S.S. (1990) Regulation of glycosylation. Three enzymes compete for a common pool of dolichyl phosphate in vivo. J. Biol. Chem., 265, 14544-14553.
    • (1990) J. Biol. Chem , vol.265 , pp. 14544-14553
    • Rosenwald, A.G.1    Stoll, J.2    Krag, S.S.3
  • 31
    • 0019888488 scopus 로고
    • Induction of phosphorylation of dolichol during embryonic development of the sea urchin
    • Rossignol, D.P., Lennarz, W.J., and Waechter, C.J. (1981) Induction of phosphorylation of dolichol during embryonic development of the sea urchin. J. Biol. Chem., 256, 10538-10542.
    • (1981) J. Biol. Chem , vol.256 , pp. 10538-10542
    • Rossignol, D.P.1    Lennarz, W.J.2    Waechter, C.J.3
  • 32
    • 0020493415 scopus 로고
    • A differentiation-dependent polyisoprenol kinase in Dictyostelium discoideum
    • Rossler, H.H., Zimpfer, A., and Risse, H-J. (1982) A differentiation-dependent polyisoprenol kinase in Dictyostelium discoideum. Mol. Cell Biochem., 48, 183-189.
    • (1982) Mol. Cell Biochem , vol.48 , pp. 183-189
    • Rossler, H.H.1    Zimpfer, A.2    Risse, H.-J.3
  • 33
    • 0027215744 scopus 로고
    • Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver
    • Sagami, H., Kurisaki, A., and Ogura, K. (1993) Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver. J. Biol. Chem., 268, 10109-10113.
    • (1993) J. Biol. Chem , vol.268 , pp. 10109-10113
    • Sagami, H.1    Kurisaki, A.2    Ogura, K.3
  • 34
    • 0015130968 scopus 로고
    • C 55 -isoprenoid alcohol phosphokinase: An extremely hydrophobic protein from the bacterial membrane
    • Sandermann, H. Jr. and Strominger, J.L. (1971) C 55 -isoprenoid alcohol phosphokinase: an extremely hydrophobic protein from the bacterial membrane. Proc. Natl Acad. Sci. USA, 68, 2441-2443.
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 2441-2443
    • Sandermann H., Jr.1    Strominger, J.L.2
  • 35
    • 0034743158 scopus 로고    scopus 로고
    • The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum
    • Schenk, B., Fernandez, F., and Waechter, C.J. (2001a) The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum. Glycobiology, 11, 61R-70R.
    • (2001) Glycobiology , vol.11
    • Schenk, B.1    Fernandez, F.2    Waechter, C.J.3
  • 36
    • 0035094506 scopus 로고    scopus 로고
    • An alternative cis- isoprenyltransferase activity in yeast that produces polyisoprenols with chain length similar to mammalian dolichols
    • Schenk, B., Rush, J.S., Waechter, C.J., and Aebi, M. (2001b) An alternative cis- isoprenyltransferase activity in yeast that produces polyisoprenols with chain length similar to mammalian dolichols. Glycobiology, 11, 1-10.
    • (2001) Glycobiology , vol.11 , pp. 1-10
    • Schenk, B.1    Rush, J.S.2    Waechter, C.J.3    Aebi, M.4
  • 37
    • 0021287534 scopus 로고
    • Subcellular sites of enzymes catalyzing the phosphorylation-dephosphorylation of dolichol in the central nervous system
    • Scher, M.G., Devries, G.H., and Waechter, C.J. (1984) Subcellular sites of enzymes catalyzing the phosphorylation-dephosphorylation of dolichol in the central nervous system. Arch. Biochem. Biophys., 231, 293-302.
    • (1984) Arch. Biochem. Biophys , vol.231 , pp. 293-302
    • Scher, M.G.1    Devries, G.H.2    Waechter, C.J.3
  • 38
    • 0022393948 scopus 로고
    • Dolichyl phosphate metabolism in brain. Developmental increase in polyisoprenyl phosphate phosphatase activity
    • Scher, M.G., Sumbilla, C.M., and Waechter, C.J. (1985) Dolichyl phosphate metabolism in brain. Developmental increase in polyisoprenyl phosphate phosphatase activity. J. Biol. Chem., 260, 13742-13746.
    • (1985) J. Biol. Chem , vol.260 , pp. 13742-13746
    • Scher, M.G.1    Sumbilla, C.M.2    Waechter, C.J.3
  • 39
    • 0022853029 scopus 로고
    • Control of N-linked carbohydrate unit synthesis in thyroid endoplasmic reticulum by membrane organization and dolichyl phosphate availability
    • Spiro, M.J. and Spiro, R.G. (1986) Control of N-linked carbohydrate unit synthesis in thyroid endoplasmic reticulum by membrane organization and dolichyl phosphate availability. J. Biol. Chem., 261, 14725-14732.
    • (1986) J. Biol. Chem , vol.261 , pp. 14725-14732
    • Spiro, M.J.1    Spiro, R.G.2
  • 40
    • 0021891309 scopus 로고
    • Dolichol kinase, phosphatase, and esterase
    • Sumbilla, C. and Waechter, C.J. (1985) Dolichol kinase, phosphatase, and esterase. Methods Enzymol., 111, 471-482,
    • (1985) Methods Enzymol , vol.111 , pp. 471-482
    • Sumbilla, C.1    Waechter, C.J.2
  • 42
    • 0026607905 scopus 로고
    • The yeast WBP1 is essential for oligosaccharyl transferase activity in vivo and in vitro
    • Te Heesen, S., Janetzky, B., Lehle, L., and Aebi, M. (1992) The yeast WBP1 is essential for oligosaccharyl transferase activity in vivo and in vitro. EMBO J., 11, 2071-2075.
    • (1992) EMBO J , vol.11 , pp. 2071-2075
    • Te Heesen, S.1    Janetzky, B.2    Lehle, L.3    Aebi, M.4
  • 43
    • 0033539526 scopus 로고    scopus 로고
    • Farnesol is utilized for isoprenoid biosynthesis in plant cells via farnesyl pyrophosphate formed by successive monophosphorylation reactions
    • Thai, L., Rush, J.S., Maul, J. Rodgers, D.L., Chappell, J., and Waechter, C.J. (1999) Farnesol is utilized for isoprenoid biosynthesis in plant cells via farnesyl pyrophosphate formed by successive monophosphorylation reactions. Proc. Natl Acad. Sci. USA, 96, 13080-13085.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13080-13085
    • Thai, L.1    Rush, J.S.2    Maul, J.3    Rodgers, D.L.4    Chappell, J.5    Waechter, C.J.6
  • 44
    • 0033749209 scopus 로고    scopus 로고
    • Properties and functions of diacylglycerol kinases
    • van Blitterswijk, W.J. and Houssa, B. (2000) Properties and functions of diacylglycerol kinases. Cell. Signal., 12, 595-605.
    • (2000) Cell. Signal , vol.12 , pp. 595-605
    • van Blitterswijk, W.J.1    Houssa, B.2
  • 45
    • 0023286347 scopus 로고
    • Dolichol kinase and the regulation of dolichyl phosphate levels in developing brain
    • Volpe, J.J., Sakakihara, Y., and Rust, R.S. (1987) Dolichol kinase and the regulation of dolichyl phosphate levels in developing brain. Dev. Brain Res., 31, 193-200.
    • (1987) Dev. Brain Res , vol.31 , pp. 193-200
    • Volpe, J.J.1    Sakakihara, Y.2    Rust, R.S.3
  • 46
    • 0000235244 scopus 로고    scopus 로고
    • A protoypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis
    • Weber, C.H., Park, Y.-S., Sanker, S., Kent, C., and Ludwig, M.L. (1999) A protoypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis. Structure, 7, 1113-1124.
    • (1999) Structure , vol.7 , pp. 1113-1124
    • Weber, C.H.1    Park, Y.-S.2    Sanker, S.3    Kent, C.4    Ludwig, M.L.5


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