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Volumn 159, Issue PART 12, 2013, Pages 2444-2455

Conservation of the PTEN catalytic motif in the bacterial undecaprenyl pyrophosphate phosphatase, BacA/UppP

Author keywords

[No Author keywords available]

Indexed keywords

INORGANIC PYROPHOSPHATASE; ISOPRENOID PHOSPHATE; LIPID; PHOSPHATIDATE PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE;

EID: 84888878677     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.070474-0     Document Type: Review
Times cited : (20)

References (110)
  • 1
    • 0021263952 scopus 로고
    • Solubilization and characterization of the long chain prenyltransferase involved in dolichyl phosphate biosynthesis
    • Adair, W. L., Jr, Cafmeyer, N. & Keller, R. K. (1984). Solubilization and characterization of the long chain prenyltransferase involved in dolichyl phosphate biosynthesis. J Biol Chem 259, 4441-4446.
    • (1984) J Biol Chem , vol.259 , pp. 4441-4446
    • Adair Jr., W.L.1    Cafmeyer, N.2    Keller, R.K.3
  • 2
    • 0024346917 scopus 로고
    • A 13-amino acid peptide in three yeast glycosyltransferases may be involved in dolichol recognition
    • Albright, C. F., Orlean, P. & Robbins, P. W. (1989). A 13-amino acid peptide in three yeast glycosyltransferases may be involved in dolichol recognition. Proc Natl Acad Sci U S A 86, 7366-7369.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 7366-7369
    • Albright, C.F.1    Orlean, P.2    Robbins, P.W.3
  • 3
    • 84882373547 scopus 로고    scopus 로고
    • SHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound states
    • Alicea-Velazquez, N. L. & Boggon, T. J. (2013). SHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound states. Protein Pept Lett 20, 1039-1048.
    • (2013) Protein Pept Lett , vol.20 , pp. 1039-1048
    • Alicea-Velazquez, N.L.1    Boggon, T.J.2
  • 4
    • 0018072479 scopus 로고
    • CTPdependent dolichol phosphorylation by mammalian cell homogenates
    • Allen, C. M., Jr, Kalin, J. R., Sack, J. & Verizzo, D. (1978). CTPdependent dolichol phosphorylation by mammalian cell homogenates. Biochemistry 17, 5020-5026.
    • (1978) Biochemistry , vol.17 , pp. 5020-5026
    • Allen Jr., C.M.1    Kalin, J.R.2    Sack, J.3    Verizzo, D.4
  • 5
    • 0020487545 scopus 로고
    • Extraction and detergent/lipid activation of dolichol kinase
    • Allen, C. M., Muth, J. D. & Gildersleeve, N. (1982). Extraction and detergent/lipid activation of dolichol kinase. Biochim Biophys Acta 712, 33-41.
    • (1982) Biochim Biophys Acta , vol.712 , pp. 33-41
    • Allen, C.M.1    Muth, J.D.2    Gildersleeve, N.3
  • 7
    • 0242552645 scopus 로고    scopus 로고
    • YtsCD and YwoA, two independent systems that confer bacitracin resistance to Bacillus subtilis
    • Bernard, R., Joseph, P., Guiseppi, A., Chippaux, M. & Denizot, F. (2003). YtsCD and YwoA, two independent systems that confer bacitracin resistance to Bacillus subtilis. FEMS Microbiol Lett 228, 93-97.
    • (2003) FEMS Microbiol Lett , vol.228 , pp. 93-97
    • Bernard, R.1    Joseph, P.2    Guiseppi, A.3    Chippaux, M.4    Denizot, F.5
  • 8
    • 23844504519 scopus 로고    scopus 로고
    • BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate phosphatase in bacitracin resistance
    • Bernard, R., El Ghachi, M., Mengin-Lecreulx, D., Chippaux, M. & Denizot, F. (2005). BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate phosphatase in bacitracin resistance. J Biol Chem 280, 28852-28857.
    • (2005) J Biol Chem , vol.280 , pp. 28852-28857
    • Bernard, R.1    El Ghachi, M.2    Mengin-Lecreulx, D.3    Chippaux, M.4    Denizot, F.5
  • 10
    • 0001400097 scopus 로고
    • Dolichol: A naturally-occurring C100 isoprenoid alcohol
    • Burgos, J., Hemming, F. W., Pennock, J. F. & Morton, R. A. (1963). Dolichol: a naturally-occurring C100 isoprenoid alcohol. Biochem J 88, 470-482.
    • (1963) Biochem J , vol.88 , pp. 470-482
    • Burgos, J.1    Hemming, F.W.2    Pennock, J.F.3    Morton, R.A.4
  • 11
    • 0027204551 scopus 로고
    • Amplification of the bacA gene confers bacitracin resistance to Escherichia coli
    • Cain, B. D., Norton, P. J., Eubanks, W., Nick, H. S. & Allen, C. M. (1993). Amplification of the bacA gene confers bacitracin resistance to Escherichia coli. J Bacteriol 175, 3784-3789.
    • (1993) J Bacteriol , vol.175 , pp. 3784-3789
    • Cain, B.D.1    Norton, P.J.2    Eubanks, W.3    Nick, H.S.4    Allen, C.M.5
  • 12
    • 77955433290 scopus 로고    scopus 로고
    • Protein glycosylation in Archaea: Sweet and extreme
    • Calo, D., Kaminski, L. & Eichler, J. (2010). Protein glycosylation in Archaea: sweet and extreme. Glycobiology 20, 1065-1076.
    • (2010) Glycobiology , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 13
    • 79961169497 scopus 로고    scopus 로고
    • From glycosylation disorders to dolichol biosynthesis defects: A new class of metabolic diseases
    • Cantagrel, V. & Lefeber, D. J. (2011). From glycosylation disorders to dolichol biosynthesis defects: a new class of metabolic diseases. J Inherit Metab Dis 34, 859-867.
    • (2011) J Inherit Metab Dis , vol.34 , pp. 859-867
    • Cantagrel, V.1    Lefeber, D.J.2
  • 14
    • 77955057089 scopus 로고    scopus 로고
    • SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder
    • other authors
    • Cantagrel, V., Lefeber, D. J., Ng, B. G., Guan, Z., Silhavy, J. L., Bielas, S. L., Lehle, L., Hombauer, H., Adamowicz, M. & other authors (2010). SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder. Cell 142, 203-217.
    • (2010) Cell , vol.142 , pp. 203-217
    • Cantagrel, V.1    Lefeber, D.J.2    Ng, B.G.3    Guan, Z.4    Silhavy, J.L.5    Bielas, S.L.6    Lehle, L.7    Hombauer, H.8    Adamowicz, M.9
  • 15
    • 0026878946 scopus 로고
    • Dolichol: Function, metabolism, and accumulation in human tissues
    • Carroll, K. K., Guthrie, N. & Ravi, K. (1992). Dolichol: function, metabolism, and accumulation in human tissues. Biochem Cell Biol 70, 382-384.
    • (1992) Biochem Cell Biol , vol.70 , pp. 382-384
    • Carroll, K.K.1    Guthrie, N.2    Ravi, K.3
  • 16
    • 0033939587 scopus 로고    scopus 로고
    • The bacA gene, which determines bacitracin susceptibility in Streptococcus pneumoniae and Staphylococcus aureus, is also required for virulence
    • Chalker, A. F., Ingraham, K. A., Lunsford, R. D., Bryant, A. P., Bryant, J., Wallis, N. G., Broskey, J. P., Pearson, S. C. & Holmes, D. J. (2000). The bacA gene, which determines bacitracin susceptibility in Streptococcus pneumoniae and Staphylococcus aureus, is also required for virulence. Microbiology 146, 1547-1553.
    • (2000) Microbiology , vol.146 , pp. 1547-1553
    • Chalker, A.F.1    Ingraham, K.A.2    Lunsford, R.D.3    Bryant, A.P.4    Bryant, J.5    Wallis, N.G.6    Broskey, J.P.7    Pearson, S.C.8    Holmes, D.J.9
  • 17
    • 0023886858 scopus 로고
    • The biological role of dolichol
    • Chojnacki, T. & Dallner, G. (1988). The biological role of dolichol. Biochem J 251, 1-9.
    • (1988) Biochem J , vol.251 , pp. 1-9
    • Chojnacki, T.1    Dallner, G.2
  • 18
    • 0027180887 scopus 로고
    • Both potential dolichol recognition sequences of hamster GlcNAc-1-phosphate transferase are necessary for normal enzyme function
    • Datta, A. K. & Lehrman, M. A. (1993). Both potential dolichol recognition sequences of hamster GlcNAc-1-phosphate transferase are necessary for normal enzyme function. J Biol Chem 268, 12663-12668.
    • (1993) J Biol Chem , vol.268 , pp. 12663-12668
    • Datta, A.K.1    Lehrman, M.A.2
  • 19
    • 56449093547 scopus 로고    scopus 로고
    • Lipid II: A central component in bacterial cell wall synthesis and a target for antibiotics
    • de Kruijff, B., van Dam, V. & Breukink, E. (2008). Lipid II: a central component in bacterial cell wall synthesis and a target for antibiotics. Prostaglandins Leukot Essent Fatty Acids 79, 117-121.
    • (2008) Prostaglandins Leukot Essent Fatty Acids , vol.79 , pp. 117-121
    • de Kruijff, B.1    van Dam, V.2    Breukink, E.3
  • 20
    • 70249146888 scopus 로고    scopus 로고
    • Hypoglycosylation due to dolichol metabolism defects
    • Denecke, J. & Kranz, C. (2009). Hypoglycosylation due to dolichol metabolism defects. Biochim Biophys Acta 1792, 888-895.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 888-895
    • Denecke, J.1    Kranz, C.2
  • 21
    • 0029828862 scopus 로고    scopus 로고
    • The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity
    • Dillon, D. A., Wu, W.-I., Riedel, B., Wissing, J. B., Dowhan, W. & Carman, G. M. (1996). The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J Biol Chem 271, 30548-30553.
    • (1996) J Biol Chem , vol.271 , pp. 30548-30553
    • Dillon, D.A.1    Wu, W.-I.2    Riedel, B.3    Wissing, J.B.4    Dowhan, W.5    Carman, G.M.6
  • 22
    • 0029550728 scopus 로고
    • Structure and catalytic properties of protein tyrosine phosphatases
    • Dixon, J. E. (1995). Structure and catalytic properties of protein tyrosine phosphatases. Ann N Y Acad Sci 766, 18-22.
    • (1995) Ann N Y Acad Sci , vol.766 , pp. 18-22
    • Dixon, J.E.1
  • 23
    • 0021256116 scopus 로고
    • Metabolic labeling of dolichol and dolichyl phosphate in isolate hepatocytes
    • Ekström, T. J., Chojnacki, T. & Dallner, G. (1984). Metabolic labeling of dolichol and dolichyl phosphate in isolate hepatocytes. J Biol Chem 259, 10460-10468.
    • (1984) J Biol Chem , vol.259 , pp. 10460-10468
    • Ekström, T.J.1    Chojnacki, T.2    Dallner, G.3
  • 24
    • 0023664140 scopus 로고
    • The alphasaturation and terminal events in dolichol biosynthesis
    • Ekström, T. J., Chojnacki, T. & Dallner, G. (1987). The alphasaturation and terminal events in dolichol biosynthesis. J Biol Chem 262, 4090-4097.
    • (1987) J Biol Chem , vol.262 , pp. 4090-4097
    • Ekström, T.J.1    Chojnacki, T.2    Dallner, G.3
  • 25
    • 3142731370 scopus 로고    scopus 로고
    • The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity
    • El Ghachi, M., Bouhss, A., Blanot, D. & Mengin-Lecreulx, D. (2004). The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity. J Biol Chem 279, 30106-30113.
    • (2004) J Biol Chem , vol.279 , pp. 30106-30113
    • El Ghachi, M.1    Bouhss, A.2    Blanot, D.3    Mengin-Lecreulx, D.4
  • 26
    • 21444450859 scopus 로고    scopus 로고
    • Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli
    • El Ghachi, M., Derbise, A., Bouhss, A. & Mengin-Lecreulx, D. (2005). Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J Biol Chem 280, 18689-18695.
    • (2005) J Biol Chem , vol.280 , pp. 18689-18695
    • El Ghachi, M.1    Derbise, A.2    Bouhss, A.3    Mengin-Lecreulx, D.4
  • 27
    • 0037456053 scopus 로고    scopus 로고
    • Identification of human dehydrodolichyl diphosphate synthase gene
    • Endo, S., Zhang, Y. W., Takahashi, S. & Koyama, T. (2003). Identification of human dehydrodolichyl diphosphate synthase gene. Biochim Biophys Acta 1625, 291-295.
    • (2003) Biochim Biophys Acta , vol.1625 , pp. 291-295
    • Endo, S.1    Zhang, Y.W.2    Takahashi, S.3    Koyama, T.4
  • 28
    • 0027246192 scopus 로고
    • Biosynthesis of dolichol and cholesterol in rat liver peroxisomes
    • Ericsson, J., Appelkvist, E. L., Runquist, M. & Dallner, G. (1993). Biosynthesis of dolichol and cholesterol in rat liver peroxisomes. Biochimie 75, 167-173.
    • (1993) Biochimie , vol.75 , pp. 167-173
    • Ericsson, J.1    Appelkvist, E.L.2    Runquist, M.3    Dallner, G.4
  • 29
    • 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. & 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
  • 30
    • 0036744488 scopus 로고    scopus 로고
    • 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
    • Fernandez, F., Shridas, P., Jiang, S., Aebi, M. & Waechter, C. J. (2002). 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. Glycobiology 12, 555-562.
    • (2002) Glycobiology , vol.12 , pp. 555-562
    • Fernandez, F.1    Shridas, P.2    Jiang, S.3    Aebi, M.4    Waechter, C.J.5
  • 31
    • 0026597155 scopus 로고
    • The pgpA and pgpB genes of Escherichia coli are not essential: Evidence for a third phosphatidylglycerophosphate phosphatase
    • Funk, C. R., Zimniak, L. & Dowhan, W. (1992). The pgpA and pgpB genes of Escherichia coli are not essential: evidence for a third phosphatidylglycerophosphate phosphatase. J Bacteriol 174, 205-213.
    • (1992) J Bacteriol , vol.174 , pp. 205-213
    • Funk, C.R.1    Zimniak, L.2    Dowhan, W.3
  • 32
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L. & Brown, M. S. (1990). Regulation of the mevalonate pathway. Nature 343, 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 33
    • 0014804589 scopus 로고
    • The characterization and stereochemistry of biosynthesis of dolichols in rat liver
    • Gough, D. P. & Hemming, F. W. (1970). The characterization and stereochemistry of biosynthesis of dolichols in rat liver. Biochem J 118, 163-166.
    • (1970) Biochem J , vol.118 , pp. 163-166
    • Gough, D.P.1    Hemming, F.W.2
  • 35
    • 20144382151 scopus 로고    scopus 로고
    • Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: Roles of the metal ion and conserved residues in catalysis
    • Guo, R. T., Ko, T. P., Chen, A. P., Kuo, C. J., Wang, A. H. & Liang, P. H. (2005). Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J Biol Chem 280, 20762-20774.
    • (2005) J Biol Chem , vol.280 , pp. 20762-20774
    • Guo, R.T.1    Ko, T.P.2    Chen, A.P.3    Kuo, C.J.4    Wang, A.H.5    Liang, P.H.6
  • 36
    • 84855443549 scopus 로고    scopus 로고
    • At the membrane frontier: A prospectus on the remarkable evolutionary conservation of polyprenols and polyprenyl-phosphates
    • Hartley, M. D. & Imperiali, B. (2012). At the membrane frontier: a prospectus on the remarkable evolutionary conservation of polyprenols and polyprenyl-phosphates. Arch Biochem Biophys 517, 83-97.
    • (2012) Arch Biochem Biophys , vol.517 , pp. 83-97
    • Hartley, M.D.1    Imperiali, B.2
  • 37
    • 43049119634 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of polyprenyl phosphates
    • Hartley, M. D., Larkin, A. & Imperiali, B. (2008). Chemoenzymatic synthesis of polyprenyl phosphates. Bioorg Med Chem 16, 5149-5156.
    • (2008) Bioorg Med Chem , vol.16 , pp. 5149-5156
    • Hartley, M.D.1    Larkin, A.2    Imperiali, B.3
  • 38
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A. & Aebi, M. (2004). Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73, 1019-1049.
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 39
    • 0026648113 scopus 로고
    • Saccharomyces cerevisiae sec59 cells are deficient in dolichol kinase activity
    • Heller, L., Orlean, P. & Adair, W. L., Jr (1992). Saccharomyces cerevisiae sec59 cells are deficient in dolichol kinase activity. Proc Natl Acad Sci U S A 89, 7013-7016.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7013-7016
    • Heller, L.1    Orlean, P.2    Adair Jr., W.L.3
  • 40
    • 0030938579 scopus 로고    scopus 로고
    • From phosphatases to vanadium peroxidases: A similar architecture of the active site
    • Hemrika, W., Renirie, R., Dekker, H. L., Barnett, P. & Wever, R. (1997). From phosphatases to vanadium peroxidases: a similar architecture of the active site. Proc Natl Acad Sci U S A 94, 2145-2149.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2145-2149
    • Hemrika, W.1    Renirie, R.2    Dekker, H.L.3    Barnett, P.4    Wever, R.5
  • 42
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • Hirokawa, T., Boon-Chieng, S. & Mitaku, S. (1998). SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics 14, 378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 43
    • 33745243275 scopus 로고    scopus 로고
    • Bacterial glycoproteomics
    • Hitchen, P. G. & Dell, A. (2006). Bacterial glycoproteomics. Microbiology 152, 1575-1580.
    • (2006) Microbiology , vol.152 , pp. 1575-1580
    • Hitchen, P.G.1    Dell, A.2
  • 44
    • 0000207681 scopus 로고
    • TMbase-a database of membrane spanning proteins segments
    • Hofmann, K. & Stoffel, W. (1993). TMbase-a database of membrane spanning proteins segments. Biol Chem Hoppe Seyler 374, 166.
    • (1993) Biol Chem Hoppe Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 45
    • 34547609909 scopus 로고    scopus 로고
    • The non-mevalonate pathway of isoprenoid precursor biosynthesis
    • Hunter, W. N. (2007). The non-mevalonate pathway of isoprenoid precursor biosynthesis. J Biol Chem 282, 21573-21577.
    • (2007) J Biol Chem , vol.282 , pp. 21573-21577
    • Hunter, W.N.1
  • 46
    • 78049354410 scopus 로고    scopus 로고
    • Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins
    • Ivanov, S. S., Charron, G., Hang, H. C. & Roy, C. R. (2010). Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins. J Biol Chem 285, 34686-34698.
    • (2010) J Biol Chem , vol.285 , pp. 34686-34698
    • Ivanov, S.S.1    Charron, G.2    Hang, H.C.3    Roy, C.R.4
  • 47
    • 34547585389 scopus 로고    scopus 로고
    • Identification of a soluble diacylglycerol kinase required for lipoteichoic acid production in Bacillus subtilis
    • Jerga, A., Lu, Y. J., Schujman, G. E., deMendoza, D. & Rock, C. O. (2007). Identification of a soluble diacylglycerol kinase required for lipoteichoic acid production in Bacillus subtilis. J Biol Chem 282, 21738-21745.
    • (2007) J Biol Chem , vol.282 , pp. 21738-21745
    • Jerga, A.1    Lu, Y.J.2    Schujman, G.E.3    deMendoza, D.4    Rock, C.O.5
  • 48
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones, D. T., Taylor, W. R. & Thornton, J. M. (1994). A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry 33, 3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 49
    • 67349159116 scopus 로고    scopus 로고
    • Structure and synthesis of polyisoprenoids used in Nglycosylation across the three domains of life
    • Jones, M. B., Rosenberg, J. N., Betenbaugh, M. J. & Krag, S. S. (2009). Structure and synthesis of polyisoprenoids used in Nglycosylation across the three domains of life. Biochim Biophys Acta 1790, 485-494.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 485-494
    • Jones, M.B.1    Rosenberg, J.N.2    Betenbaugh, M.J.3    Krag, S.S.4
  • 50
    • 0036557845 scopus 로고    scopus 로고
    • Basic charge clusters and predictions of membrane protein topology
    • Juretić, D., Zoranić, L. & Zucić, D. (2002). Basic charge clusters and predictions of membrane protein topology. J Chem Inf Comput Sci 42, 620-632.
    • (2002) J Chem Inf Comput Sci , vol.42 , pp. 620-632
    • Juretić, D.1    Zoranić, L.2    Zucić, D.3
  • 51
    • 78650045637 scopus 로고    scopus 로고
    • Next generation sequencing in a family with autosomal recessive Kahrizi syndrome (OMIM 612713) reveals a homozygous frameshift mutation in SRD5A3
    • other authors
    • Kahrizi, K., Hu, C. H., Garshasbi, M., Abedini, S. S., Ghadami, S., Kariminejad, R., Ullmann, R., Chen, W., Ropers, H. H. & other authors (2011). Next generation sequencing in a family with autosomal recessive Kahrizi syndrome (OMIM 612713) reveals a homozygous frameshift mutation in SRD5A3. Eur J Hum Genet 19, 115-117.
    • (2011) Eur J Hum Genet , vol.19 , pp. 115-117
    • Kahrizi, K.1    Hu, C.H.2    Garshasbi, M.3    Abedini, S.S.4    Ghadami, S.5    Kariminejad, R.6    Ullmann, R.7    Chen, W.8    Ropers, H.H.9
  • 52
    • 84879464716 scopus 로고    scopus 로고
    • From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG)
    • other authors
    • Kapusta, L., Zucker, N., Frenckel, G., Medalion, B., Ben Gal, T., Birk, E., Mandel, H., Nasser, N., Morgenstern, S. & other authors (2013). From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG). Heart Fail Rev 18, 187-196.
    • (2013) Heart Fail Rev , vol.18 , pp. 187-196
    • Kapusta, L.1    Zucker, N.2    Frenckel, G.3    Medalion, B.4    Ben Gal, T.5    Birk, E.6    Mandel, H.7    Nasser, N.8    Morgenstern, S.9
  • 54
    • 33847228036 scopus 로고    scopus 로고
    • A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy
    • other authors
    • Kranz, C., Jungeblut, C., Denecke, J., Erlekotte, A., Sohlbach, C., Debus, V., Kehl, H. G., Harms, E., Reith, A. & other authors (2007). A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy. Am J Hum Genet 80, 433-440.
    • (2007) Am J Hum Genet , vol.80 , pp. 433-440
    • Kranz, C.1    Jungeblut, C.2    Denecke, J.3    Erlekotte, A.4    Sohlbach, C.5    Debus, V.6    Kehl, H.G.7    Harms, E.8    Reith, A.9
  • 55
    • 79954452580 scopus 로고    scopus 로고
    • Comparative genomics analysis of completely sequenced microbial genomes reveals the ubiquity of Nlinked glycosylation in prokaryotes
    • Kumar, M. & Balaji, P. V. (2011). Comparative genomics analysis of completely sequenced microbial genomes reveals the ubiquity of Nlinked glycosylation in prokaryotes. Mol Biosyst 7, 1629-1645.
    • (2011) Mol Biosyst , vol.7 , pp. 1629-1645
    • Kumar, M.1    Balaji, P.V.2
  • 56
    • 0036690439 scopus 로고    scopus 로고
    • Mevalonate and nonmevalonate pathways for the biosynthesis of isoprene units
    • Kuzuyama, T. (2002). Mevalonate and nonmevalonate pathways for the biosynthesis of isoprene units. Biosci Biotechnol Biochem 66, 1619-1627.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1619-1627
    • Kuzuyama, T.1
  • 57
    • 79958165964 scopus 로고    scopus 로고
    • The expanding horizons of asparagine-linked glycosylation
    • Larkin, A. & Imperiali, B. (2011). The expanding horizons of asparagine-linked glycosylation. Biochemistry 50, 4411-4426.
    • (2011) Biochemistry , vol.50 , pp. 4411-4426
    • Larkin, A.1    Imperiali, B.2
  • 58
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • Lee, J. O., Yang, H., Georgescu, M. M., Di Cristofano, A., Maehama, T., Shi, Y., Dixon, J. E., Pandolfi, P. & Pavletich, N. P. (1999). Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 99, 323-334.
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 60
    • 84861892432 scopus 로고    scopus 로고
    • Structural perspective of peptidoglycan biosynthesis and assembly
    • Lovering, A. L., Safadi, S. S. & Strynadka, N. C. (2012). Structural perspective of peptidoglycan biosynthesis and assembly. Annu Rev Biochem 81, 451-478.
    • (2012) Annu Rev Biochem , vol.81 , pp. 451-478
    • Lovering, A.L.1    Safadi, S.S.2    Strynadka, N.C.3
  • 61
    • 79953159519 scopus 로고    scopus 로고
    • Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli
    • Lu, Y. H., Guan, Z., Zhao, J. & Raetz, C. R. (2011). Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli. J Biol Chem 286, 5506-5518.
    • (2011) J Biol Chem , vol.286 , pp. 5506-5518
    • Lu, Y.H.1    Guan, Z.2    Zhao, J.3    Raetz, C.R.4
  • 62
    • 16844383874 scopus 로고    scopus 로고
    • Mycobacterial lipid II is composed of a complex mixture of modified muramyl and peptide moieties linked to decaprenyl phosphate
    • Mahapatra, S., Yagi, T., Belisle, J. T., Espinosa, B. J., Hill, P. J., McNeil, M. R., Brennan, P. J. & Crick, D. C. (2005). Mycobacterial lipid II is composed of a complex mixture of modified muramyl and peptide moieties linked to decaprenyl phosphate. J Bacteriol 187, 2747-2757.
    • (2005) J Bacteriol , vol.187 , pp. 2747-2757
    • Mahapatra, S.1    Yagi, T.2    Belisle, J.T.3    Espinosa, B.J.4    Hill, P.J.5    McNeil, M.R.6    Brennan, P.J.7    Crick, D.C.8
  • 63
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Möller, S., Croning, M. D. & Apweiler, R. (2001). Evaluation of methods for the prediction of membrane spanning regions. Bioinformatics 17, 646-653.
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Möller, S.1    Croning, M.D.2    Apweiler, R.3
  • 64
    • 0021076369 scopus 로고
    • Key role of dolichol phosphate in glycoprotein biosynthesis
    • Mookerjea, S., Coolbear, T. & Sarkar, M. L. (1983). Key role of dolichol phosphate in glycoprotein biosynthesis. Can J Biochem Cell Biol 61, 1032-1040.
    • (1983) Can J Biochem Cell Biol , vol.61 , pp. 1032-1040
    • Mookerjea, S.1    Coolbear, T.2    Sarkar, M.L.3
  • 66
    • 0030753213 scopus 로고    scopus 로고
    • An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
    • Neuwald, A. F. (1997). An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases. Protein Sci 6, 1764-1767.
    • (1997) Protein Sci , vol.6 , pp. 1764-1767
    • Neuwald, A.F.1
  • 67
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: Sweeter than ever
    • Nothaft, H. & Szymanski, C. M. (2010). Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol 8, 765-778.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 68
    • 0037214439 scopus 로고    scopus 로고
    • A bacitracin-resistant Bacillus subtilis gene encodes a homologue of the membrane-spanning subunit of the Bacillus licheniformis ABC transporter
    • Ohki, R., Tateno, K., Okada, Y., Okajima, H., Asai, K., Sadaie, Y., Murata, M. & Aiso, T. (2003). A bacitracin-resistant Bacillus subtilis gene encodes a homologue of the membrane-spanning subunit of the Bacillus licheniformis ABC transporter. J Bacteriol 185, 51-59.
    • (2003) J Bacteriol , vol.185 , pp. 51-59
    • Ohki, R.1    Tateno, K.2    Okada, Y.3    Okajima, H.4    Asai, K.5    Sadaie, Y.6    Murata, M.7    Aiso, T.8
  • 69
    • 0032834939 scopus 로고    scopus 로고
    • An hierarchical artificial neural network system for the classification of transmembrane proteins
    • Pasquier, C. & Hamodrakas, S. J. (1999). An hierarchical artificial neural network system for the classification of transmembrane proteins. Protein Eng 12, 631-634.
    • (1999) Protein Eng , vol.12 , pp. 631-634
    • Pasquier, C.1    Hamodrakas, S.J.2
  • 70
    • 0001601953 scopus 로고
    • Dolichol: A naturally occurring isoprenoid alcohol
    • Pennock, J. F., Hemming, F. W. & Morton, R. A. (1960). Dolichol: a naturally occurring isoprenoid alcohol. Nature 186, 470-472.
    • (1960) Nature , vol.186 , pp. 470-472
    • Pennock, J.F.1    Hemming, F.W.2    Morton, R.A.3
  • 71
    • 0029132858 scopus 로고
    • Bacillus licheniformis bacitracinresistance ABC transporter: Relationship to mammalian multidrug resistance
    • Podlesek, Z., Comino, A., Herzog-Velikonja, B., Zgur-Bertok, D., Komel, R. & Grabnar, M. (1995). Bacillus licheniformis bacitracinresistance ABC transporter: relationship to mammalian multidrug resistance. Mol Microbiol 16, 969-976.
    • (1995) Mol Microbiol , vol.16 , pp. 969-976
    • Podlesek, Z.1    Comino, A.2    Herzog-Velikonja, B.3    Zgur-Bertok, D.4    Komel, R.5    Grabnar, M.6
  • 72
    • 77955397296 scopus 로고    scopus 로고
    • Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila
    • Price, C. T., Al-Quadan, T., Santic, M., Jones, S. C. & Abu Kwaik, Y. (2010). Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila. J Exp Med 207, 1713-1726.
    • (2010) J Exp Med , vol.207 , pp. 1713-1726
    • Price, C.T.1    Al-Quadan, T.2    Santic, M.3    Jones, S.C.4    Abu Kwaik, Y.5
  • 73
    • 8644261622 scopus 로고    scopus 로고
    • 1-Deoxy-D-xylulose 5-phosphate reductoisomerase: An overview
    • Proteau, P. J. (2004). 1-Deoxy-D-xylulose 5-phosphate reductoisomerase: an overview. Bioorg Chem 32, 483-493.
    • (2004) Bioorg Chem , vol.32 , pp. 483-493
    • Proteau, P.J.1
  • 74
    • 59049105375 scopus 로고    scopus 로고
    • Characterization of dehydrodolichyl diphosphate synthase gene in rainbow trout (Oncorhynchus mykiss)
    • Rebl, A., Anders, E., Wimmers, K. & Goldammer, T. (2009). Characterization of dehydrodolichyl diphosphate synthase gene in rainbow trout (Oncorhynchus mykiss). Comp Biochem Physiol B Biochem Mol Biol 152, 260-265.
    • (2009) Comp Biochem Physiol B Biochem Mol Biol , vol.152 , pp. 260-265
    • Rebl, A.1    Anders, E.2    Wimmers, K.3    Goldammer, T.4
  • 75
    • 0021301852 scopus 로고
    • Lipopolymers, isoprenoids, and the assembly of the gram-positive cell wall
    • Reusch, V. M., Jr & Salton, M. R. J. (1984). Lipopolymers, isoprenoids, and the assembly of the gram-positive cell wall. Crit Rev Microbiol 11, 129-155.
    • (1984) Crit Rev Microbiol , vol.11 , pp. 129-155
    • Reusch Jr., V.M.1    Salton, M.R.J.2
  • 76
    • 0347928850 scopus 로고    scopus 로고
    • Identification and characterization of a cDNA encoding a dolichyl pyrophosphate phosphatase located in the endoplasmic reticulum of mammalian cells
    • Rush, J. S., Cho, S. K., Jiang, S., Hofmann, S. L. & Waechter, C. J. (2002). Identification and characterization of a cDNA encoding a dolichyl pyrophosphate phosphatase located in the endoplasmic reticulum of mammalian cells. J Biol Chem 277, 45226-45234.
    • (2002) J Biol Chem , vol.277 , pp. 45226-45234
    • Rush, J.S.1    Cho, S.K.2    Jiang, S.3    Hofmann, S.L.4    Waechter, C.J.5
  • 77
    • 0027215744 scopus 로고
    • Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver
    • Sagami, H., Kurisaki, A. & 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
  • 78
    • 0029996276 scopus 로고    scopus 로고
    • Enzymatic formation of dehydrodolichal and dolichal, new products related to yeast dolichol biosynthesis
    • Sagami, H., Igarashi, Y., Tateyama, S., Ogura, K., Roos, J. & Lennarz, W. J. (1996). Enzymatic formation of dehydrodolichal and dolichal, new products related to yeast dolichol biosynthesis. J Biol Chem 271, 9560-9566.
    • (1996) J Biol Chem , vol.271 , pp. 9560-9566
    • Sagami, H.1    Igarashi, Y.2    Tateyama, S.3    Ogura, K.4    Roos, J.5    Lennarz, W.J.6
  • 79
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of Nlinked protein glycosylation
    • Schwarz, F. & Aebi, M. (2011). Mechanisms and principles of Nlinked protein glycosylation. Curr Opin Struct Biol 21, 576-582.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 80
    • 17444408968 scopus 로고    scopus 로고
    • Protein farnesylation: Implications for normal physiology, malignant transformation, and cancer therapy
    • Sebti, S. M. (2005). Protein farnesylation: implications for normal physiology, malignant transformation, and cancer therapy. Cancer Cell 7, 297-300.
    • (2005) Cancer Cell , vol.7 , pp. 297-300
    • Sebti, S.M.1
  • 81
    • 33845991857 scopus 로고    scopus 로고
    • Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with a cytoplasmically oriented CTP-binding site
    • Shridas, P. & Waechter, C. J. (2006). Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with a cytoplasmically oriented CTP-binding site. J Biol Chem 281, 31696-31704.
    • (2006) J Biol Chem , vol.281 , pp. 31696-31704
    • Shridas, P.1    Waechter, C.J.2
  • 82
    • 0344063650 scopus 로고    scopus 로고
    • Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells
    • Shridas, P., Rush, J. S. & Waechter, C. J. (2003). Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells. Biochem Biophys Res Commun 312, 1349-1356.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 1349-1356
    • Shridas, P.1    Rush, J.S.2    Waechter, C.J.3
  • 83
    • 41349104685 scopus 로고    scopus 로고
    • Polyisoprenoid alcohols-recent results of structural studies
    • Skorupinska-Tudek, K., Wojcik, J. & Swiezewska, E. (2008). Polyisoprenoid alcohols-recent results of structural studies. Chem Rec 8, 33-45.
    • (2008) Chem Rec , vol.8 , pp. 33-45
    • Skorupinska-Tudek, K.1    Wojcik, J.2    Swiezewska, E.3
  • 84
    • 10244225308 scopus 로고    scopus 로고
    • TMRPres2D: High quality visual representation of transmembrane protein models
    • Spyropoulos, I. C., Liakopoulos, T. D., Bagos, P. G. & Hamodrakas, S. J. (2004). TMRPres2D: high quality visual representation of transmembrane protein models. Bioinformatics 20, 3258-3260.
    • (2004) Bioinformatics , vol.20 , pp. 3258-3260
    • Spyropoulos, I.C.1    Liakopoulos, T.D.2    Bagos, P.G.3    Hamodrakas, S.J.4
  • 85
    • 0031048876 scopus 로고    scopus 로고
    • Identification of a novel phosphatase sequence motif
    • Stukey, J. & Carman, G. M. (1997). Identification of a novel phosphatase sequence motif. Protein Sci 6, 469-472.
    • (1997) Protein Sci , vol.6 , pp. 469-472
    • Stukey, J.1    Carman, G.M.2
  • 86
    • 79955020381 scopus 로고    scopus 로고
    • Polyisoprenoids-secondary metabolites or physiologically important superlipids?
    • Surmacz, L. & Swiezewska, E. (2011). Polyisoprenoids-secondary metabolites or physiologically important superlipids? Biochem Biophys Res Commun 407, 627-632.
    • (2011) Biochem Biophys Res Commun , vol.407 , pp. 627-632
    • Surmacz, L.1    Swiezewska, E.2
  • 87
    • 22044458610 scopus 로고    scopus 로고
    • Polyisoprenoids: Structure, biosynthesis and function
    • Swiezewska, E. & Danikiewicz, W. (2005). Polyisoprenoids: structure, biosynthesis and function. Prog Lipid Res 44, 235-258.
    • (2005) Prog Lipid Res , vol.44 , pp. 235-258
    • Swiezewska, E.1    Danikiewicz, W.2
  • 88
    • 75649132267 scopus 로고    scopus 로고
    • Wall teichoic acid function, biosynthesis, and inhibition
    • Swoboda, J. G., Campbell, J., Meredith, T. C. & Walker, S. (2010). Wall teichoic acid function, biosynthesis, and inhibition. Chem-BioChem 11, 35-45.
    • (2010) Chem-BioChem , vol.11 , pp. 35-45
    • Swoboda, J.G.1    Campbell, J.2    Meredith, T.C.3    Walker, S.4
  • 89
    • 84888861930 scopus 로고    scopus 로고
    • Analysis of glycosylation motifs and glycosyltransferases in Bacteria and Archaea
    • Tabish, S., Raza, A., Nasir, A., Zafar, S. & Bokhari, H. (2011). Analysis of glycosylation motifs and glycosyltransferases in Bacteria and Archaea. Bioinformation 6, 191-195.
    • (2011) Bioinformation , vol.6 , pp. 191-195
    • Tabish, S.1    Raza, A.2    Nasir, A.3    Zafar, S.4    Bokhari, H.5
  • 90
    • 34547863963 scopus 로고    scopus 로고
    • An Escherichia coli undecaprenyl-pyrophosphate phosphatase implicated in undecaprenyl phosphate recycling
    • Tatar, L. D., Marolda, C. L., Polischuk, A. N., van Leeuwen, D. & Valvano, M. A. (2007). An Escherichia coli undecaprenyl-pyrophosphate phosphatase implicated in undecaprenyl phosphate recycling. Microbiology 153, 2518-2529.
    • (2007) Microbiology , vol.153 , pp. 2518-2529
    • Tatar, L.D.1    Marolda, C.L.2    Polischuk, A.N.3    van Leeuwen, D.4    Valvano, M.A.5
  • 91
    • 84862024512 scopus 로고    scopus 로고
    • Structures, mechanisms and inhibitors of undecaprenyl diphosphate synthase: A cis-prenyltransferase for bacterial peptidoglycan biosynthesis
    • Teng, K. H. & Liang, P. H. (2012a). Structures, mechanisms and inhibitors of undecaprenyl diphosphate synthase: a cis-prenyltransferase for bacterial peptidoglycan biosynthesis. Bioorg Chem 43, 51-57.
    • (2012) Bioorg Chem , vol.43 , pp. 51-57
    • Teng, K.H.1    Liang, P.H.2
  • 92
    • 84867972691 scopus 로고    scopus 로고
    • Undecaprenyl diphosphate synthase, a cis-prenyltransferase synthesizing lipid carrier for bacterial cell wall biosynthesis
    • Teng, K. H. & Liang, P. H. (2012b). Undecaprenyl diphosphate synthase, a cis-prenyltransferase synthesizing lipid carrier for bacterial cell wall biosynthesis. Mol Membr Biol 29, 267-273.
    • (2012) Mol Membr Biol , vol.29 , pp. 267-273
    • Teng, K.H.1    Liang, P.H.2
  • 93
    • 84872759784 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases-from housekeeping enzymes to master regulators of signal transduction
    • Tonks, N. K. (2013). Protein tyrosine phosphatases-from housekeeping enzymes to master regulators of signal transduction. FEBS J 280, 346-378.
    • (2013) FEBS J , vol.280 , pp. 346-378
    • Tonks, N.K.1
  • 94
    • 47749087497 scopus 로고    scopus 로고
    • Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase
    • Touzé, T., Blanot, D. & Mengin-Lecreulx, D. (2008a). Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase. J Biol Chem 283, 16573-16583.
    • (2008) J Biol Chem , vol.283 , pp. 16573-16583
    • Touzé, T.1    Blanot, D.2    Mengin-Lecreulx, D.3
  • 95
    • 37349106728 scopus 로고    scopus 로고
    • Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate
    • Touzé, T., Tran, A. X., Hankins, J. V., Mengin-Lecreulx, D. & Trent, M. S. (2008b). Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate. Mol Microbiol 67, 264-277.
    • (2008) Mol Microbiol , vol.67 , pp. 264-277
    • Touzé, T.1    Tran, A.X.2    Hankins, J.V.3    Mengin-Lecreulx, D.4    Trent, M.S.5
  • 96
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnády, G. E. & Simon, I. (1998). Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J Mol Biol 283, 489-506.
    • (1998) J Mol Biol , vol.283 , pp. 489-506
    • Tusnády, G.E.1    Simon, I.2
  • 97
    • 37349078291 scopus 로고    scopus 로고
    • Undecaprenyl phosphate recycling comes out of age
    • Valvano, M. A. (2008). Undecaprenyl phosphate recycling comes out of age. Mol Microbiol 67, 232-235.
    • (2008) Mol Microbiol , vol.67 , pp. 232-235
    • Valvano, M.A.1
  • 98
    • 0033055377 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae CWH8 gene is required for full levels of dolichol-linked oligosaccharides in the endoplasmic reticulum and for efficient N-glycosylation
    • van Berkel, M. A., Rieger, M., te Heesen, S., Ram, A. F., van den Ende, H., Aebi, M. & Klis, F. M. (1999). The Saccharomyces cerevisiae CWH8 gene is required for full levels of dolichol-linked oligosaccharides in the endoplasmic reticulum and for efficient N-glycosylation. Glycobiology 9, 243-253.
    • (1999) Glycobiology , vol.9 , pp. 243-253
    • van Berkel, M.A.1    Rieger, M.2    te Heesen, S.3    Ram, A.F.4    van den Ende, H.5    Aebi, M.6    Klis, F.M.7
  • 99
    • 84861396377 scopus 로고    scopus 로고
    • Prokaryotic diacylglycerol kinase and undecaprenol kinase
    • Van Horn, W. D. & Sanders, C. R. (2012). Prokaryotic diacylglycerol kinase and undecaprenol kinase. Annu Rev Biophys 41, 81-101.
    • (2012) Annu Rev Biophys , vol.41 , pp. 81-101
    • Van Horn, W.D.1    Sanders, C.R.2
  • 100
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: Improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund, H. & Elofsson, A. (2008). OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics 24, 1662-1668.
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 101
    • 0023286347 scopus 로고
    • Dolichol kinase and the regulation of dolichyl phosphate levels in developing brain
    • Volpe, J. J., Sakakihara, Y. & Rust, R. S. (1987). Dolichol kinase and the regulation of dolichyl phosphate levels in developing brain. Brain Res 428, 193-200.
    • (1987) Brain Res , vol.428 , pp. 193-200
    • Volpe, J.J.1    Sakakihara, Y.2    Rust, R.S.3
  • 102
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • Weerapana, E. & Imperiali, B. (2006). Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. Glycobiology 16, 91R-101R.
    • (2006) Glycobiology , vol.16
    • Weerapana, E.1    Imperiali, B.2
  • 103
    • 84872676605 scopus 로고    scopus 로고
    • Regulation of dolichol-linked glycosylation
    • Welti, M. (2013). Regulation of dolichol-linked glycosylation. Glycoconj J 30, 51-56.
    • (2013) Glycoconj J , vol.30 , pp. 51-56
    • Welti, M.1
  • 104
    • 79961063234 scopus 로고    scopus 로고
    • Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis
    • Xiao, J., Engel, J. L., Zhang, J., Chen, M. J., Manning, G. & Dixon, J. E. (2011). Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis. Proc Natl Acad Sci U S A 108, 11860-11865.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11860-11865
    • Xiao, J.1    Engel, J.L.2    Zhang, J.3    Chen, M.J.4    Manning, G.5    Dixon, J.E.6
  • 105
    • 79851508986 scopus 로고    scopus 로고
    • A missense mutation in DHDDS, encoding dehydrodolichyl diphosphate synthase, is associated with autosomal-recessive retinitis pigmentosa in Ashkenazi Jews
    • other authors
    • Zelinger, L., Banin, E., Obolensky, A., Mizrahi-Meissonnier, L., Beryozkin, A., Bandah-Rozenfeld, D., Frenkel, S., Ben-Yosef, T., Merin, S. & other authors (2011). A missense mutation in DHDDS, encoding dehydrodolichyl diphosphate synthase, is associated with autosomal-recessive retinitis pigmentosa in Ashkenazi Jews. Am J Hum Genet 88, 207-215.
    • (2011) Am J Hum Genet , vol.88 , pp. 207-215
    • Zelinger, L.1    Banin, E.2    Obolensky, A.3    Mizrahi-Meissonnier, L.4    Beryozkin, A.5    Bandah-Rozenfeld, D.6    Frenkel, S.7    Ben-Yosef, T.8    Merin, S.9
  • 106
    • 42049122998 scopus 로고    scopus 로고
    • Engineered inhibitor sensitivity in the WPD loop of a protein tyrosine phosphatase
    • Zhang, X. Y. & Bishop, A. C. (2008). Engineered inhibitor sensitivity in the WPD loop of a protein tyrosine phosphatase. Biochemistry 47, 4491-4500.
    • (2008) Biochemistry , vol.47 , pp. 4491-4500
    • Zhang, X.Y.1    Bishop, A.C.2
  • 107
    • 77956236877 scopus 로고    scopus 로고
    • PI(3)king apart PTEN's role in cancer
    • Zhang, S. & Yu, D. (2010). PI(3)king apart PTEN's role in cancer. Clin Cancer Res 16, 4325-4330.
    • (2010) Clin Cancer Res , vol.16 , pp. 4325-4330
    • Zhang, S.1    Yu, D.2


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