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Volumn 60, Issue 6, 2003, Pages 1118-1134

Isoprenoid biosynthesis in hereditary periodic fever syndromes and inflammation

Author keywords

Autoinflammatory syndromes; Fever; Hyper IgD and periodic fever syndrome; Inflammation; Isoprenoid biosynthesis; Mevalonate kinase; Mevalonic aciduria

Indexed keywords

CHOLESTEROL; FARNESOL; GERANYLGERANIOL; ISOPRENOID; MEVALONATE KINASE; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 0038724543     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-2296-4     Document Type: Review
Times cited : (83)

References (144)
  • 1
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey P. J. and Seabra M. C. (1996) Protein prenyltransferases. J. Biol. Chem. 271: 5289-5292
    • (1996) J. Biol. Chem. , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 2
    • 0034672717 scopus 로고    scopus 로고
    • Cholesterol and caveolae: Structural and functional relationships
    • Fielding C. J. and Fielding P. E. (2000) Cholesterol and caveolae: structural and functional relationships. Biochim. Biophys. Acta 1529: 210-222
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 210-222
    • Fielding, C.J.1    Fielding, P.E.2
  • 3
    • 0034672716 scopus 로고    scopus 로고
    • Cholesterol modification of proteins
    • Mann R. K. and Beachy P. A. (2000) Cholesterol modification of proteins. Biochim. Biophys. Acta 1529: 188-202
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 188-202
    • Mann, R.K.1    Beachy, P.A.2
  • 5
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein J. L. and 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
  • 6
    • 0034672705 scopus 로고    scopus 로고
    • Biochemical and genetic aspects of mevalonate kinase and its deficiency
    • Houten S. M., Wanders R. J. and Waterham H. R. (2000) Biochemical and genetic aspects of mevalonate kinase and its deficiency. Biochim. Biophys. Acta 1529: 19-32
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 19-32
    • Houten, S.M.1    Wanders, R.J.2    Waterham, H.R.3
  • 7
    • 0037088680 scopus 로고    scopus 로고
    • Structure of the Methanococcus jannaschii mevalonate kinase, a member of the GHMP kinase superfamily
    • Yang D., Shipman L. W., Roessner C. A., Scott A. I. and Sacchettini J. C. (2002) Structure of the Methanococcus jannaschii mevalonate kinase, a member of the GHMP kinase superfamily. J. Biol. Chem. 277: 9462-9467
    • (2002) J. Biol. Chem. , vol.277 , pp. 9462-9467
    • Yang, D.1    Shipman, L.W.2    Roessner, C.A.3    Scott, A.I.4    Sacchettini, J.C.5
  • 8
    • 0037124052 scopus 로고    scopus 로고
    • The structure of a binary complex between a mammalian mevalonate kinase and ATP
    • Fu Z., Wang M., Potter D., Miziorko H. M. and Kim J. J. (2002) The structure of a binary complex between a mammalian mevalonate kinase and ATP. J. Biol. Chem. 277: 18134-18142
    • (2002) J. Biol. Chem. , vol.277 , pp. 18134-18142
    • Fu, Z.1    Wang, M.2    Potter, D.3    Miziorko, H.M.4    Kim, J.J.5
  • 9
    • 0034672694 scopus 로고    scopus 로고
    • Isoprenyl diphosphate synthases
    • Wang K. C. and Ohnuma S. (2000) Isoprenyl diphosphate synthases. Biochim. Biophys. Acta 1529: 33-48
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 33-48
    • Wang, K.C.1    Ohnuma, S.2
  • 10
    • 0001415416 scopus 로고
    • Preputial gland tumor sterols: III. A metabolic pathway from lanosterol to cholesterol
    • Kandutsch A. A. and Russell A. E. (1960) Preputial gland tumor sterols: III. A metabolic pathway from lanosterol to cholesterol. J. Biol. Chem. 235: 2256-2261
    • (1960) J. Biol. Chem. , vol.235 , pp. 2256-2261
    • Kandutsch, A.A.1    Russell, A.E.2
  • 12
    • 0030858044 scopus 로고    scopus 로고
    • Cholesterol biosynthesis from lanosterol: Development of a novel assay method and characterization of rat liver microsomal lanosterol delta 24-reductase
    • Bae S. H. and Paik Y. K. (1997) Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol delta 24-reductase. Biochem. J. 326: 609-616
    • (1997) Biochem. J. , vol.326 , pp. 609-616
    • Bae, S.H.1    Paik, Y.K.2
  • 13
    • 0034672715 scopus 로고    scopus 로고
    • Biochemical and genetic aspects of 7-dehydrocholesterol reductase and Smith-Lemli-Opitz syndrome
    • Waterham H. R. and Wanders R. J. (2000) Biochemical and genetic aspects of 7-dehydrocholesterol reductase and Smith-Lemli-Opitz syndrome. Biochim. Biophys. Acta 1529: 340-356
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 340-356
    • Waterham, H.R.1    Wanders, R.J.2
  • 14
    • 0028027441 scopus 로고
    • Utilization of geranylgeraniol for protein isoprenylation in C6 glial cells
    • Crick D. C., Waechter C. J. and Andres D. A. (1994) Utilization of geranylgeraniol for protein isoprenylation in C6 glial cells. Biochem Biophys. Res. Commun. 205: 955-961
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 955-961
    • Crick, D.C.1    Waechter, C.J.2    Andres, D.A.3
  • 15
    • 0029020395 scopus 로고
    • Farnesol is utilized for protein isoprenylation and the biosynthesis of cholesterol in mammalian cells
    • Crick D. C., Andres D. A. and Waechter C. J. (1995) Farnesol is utilized for protein isoprenylation and the biosynthesis of cholesterol in mammalian cells. Biochem. Biophys. Res. Commun. 211: 590-599
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 590-599
    • Crick, D.C.1    Andres, D.A.2    Waechter, C.J.3
  • 16
    • 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
  • 17
    • 0033618378 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl-CoA reductase inhibitors attenuate vascular smooth muscle proliferation by preventing rho GTPase-induced down-regulation of p27(Kip1)
    • Laufs U., Marra D., Node K. and Liao J. K. (1999) 3-Hydroxy-3-methylglutaryl-CoA reductase inhibitors attenuate vascular smooth muscle proliferation by preventing rho GTPase-induced down-regulation of p27(Kip1). J. Biol. Chem. 274: 21926-21931
    • (1999) J. Biol. Chem. , vol.274 , pp. 21926-21931
    • Laufs, U.1    Marra, D.2    Node, K.3    Liao, J.K.4
  • 18
    • 0027288196 scopus 로고
    • Tocotrienols regulate cholesterol production in mammalian cells by post-transcriptional suppression of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Parker R. A., Pearce B. C., Clark R. W., Gordon D. A. and Wright J. J. (1993) Tocotrienols regulate cholesterol production in mammalian cells by post-transcriptional suppression of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 268: 11230-11238
    • (1993) J. Biol. Chem. , vol.268 , pp. 11230-11238
    • Parker, R.A.1    Pearce, B.C.2    Clark, R.W.3    Gordon, D.A.4    Wright, J.J.5
  • 19
    • 0028157541 scopus 로고
    • Mevalonic acid-dependent degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo and in vitro
    • Correll C. C. and Edwards P. A. (1994) Mevalonic acid-dependent degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo and in vitro. J. Biol. Chem. 269: 633-638
    • (1994) J. Biol. Chem. , vol.269 , pp. 633-638
    • Correll, C.C.1    Edwards, P.A.2
  • 20
    • 0028285272 scopus 로고
    • Non-sterol compounds that regulate cholesterogenesis. Analogues of farnesyl pyrophosphate reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels
    • Bradfute D. L. and Simoni R. D. (1994) Non-sterol compounds that regulate cholesterogenesis. Analogues of farnesyl pyrophosphate reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels. J. Biol. Chem. 269: 6645-6650
    • (1994) J. Biol. Chem. , vol.269 , pp. 6645-6650
    • Bradfute, D.L.1    Simoni, R.D.2
  • 21
    • 0028307290 scopus 로고
    • Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Correll C. C., Ng L. and Edwards P. A. (1994) Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 269: 17390-17393
    • (1994) J. Biol. Chem. , vol.269 , pp. 17390-17393
    • Correll, C.C.1    Ng, L.2    Edwards, P.A.3
  • 22
    • 0028035383 scopus 로고
    • Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes
    • Bansal V. S. and Vaidya S. (1994) Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes. Arch. Biochem. Biophys. 315: 393-399
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 393-399
    • Bansal, V.S.1    Vaidya, S.2
  • 23
    • 0029969302 scopus 로고    scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo
    • Meigs T. E., Roseman D. S. and Simoni R. D. (1996) Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo. J. Biol. Chem. 271: 7916-7922
    • (1996) J. Biol. Chem. , vol.271 , pp. 7916-7922
    • Meigs, T.E.1    Roseman, D.S.2    Simoni, R.D.3
  • 24
    • 0031239831 scopus 로고    scopus 로고
    • Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and role of farnesyl pyrophosphatase
    • Meigs T. E. and Simoni R. D. (1997) Farnesol as a regulator of HMG-CoA reductase degradation: characterization and role of farnesyl pyrophosphatase. Arch. Biochem. Biophys. 345: 1-9
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 1-9
    • Meigs, T.E.1    Simoni, R.D.2
  • 25
    • 0000812012 scopus 로고    scopus 로고
    • Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver
    • Keller R. K., Zhao Z., Chambers C. and Ness G. C. (1996) Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver. Arch. Biochem. Biophys. 328: 324-330
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 324-330
    • Keller, R.K.1    Zhao, Z.2    Chambers, C.3    Ness, G.C.4
  • 26
    • 0032476029 scopus 로고    scopus 로고
    • Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells
    • Miquel K., Pradines A., Terce F., Selmi S. and Favre G. (1998) Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells. J. Biol. Chem. 273: 26179-26186
    • (1998) J. Biol. Chem. , vol.273 , pp. 26179-26186
    • Miquel, K.1    Pradines, A.2    Terce, F.3    Selmi, S.4    Favre, G.5
  • 27
    • 0035816579 scopus 로고    scopus 로고
    • Uncoupling farnesol-induced apoptosis from its inhibition of phosphatidylcholine synthesis
    • Wright M. M., Henneberry A. L., Lagace T. A., Ridgway N. D. and McMaster C. R. (2001) Uncoupling farnesol-induced apoptosis from its inhibition of phosphatidylcholine synthesis. J. Biol. Chem. 276: 25254-25261
    • (2001) J. Biol. Chem. , vol.276 , pp. 25254-25261
    • Wright, M.M.1    Henneberry, A.L.2    Lagace, T.A.3    Ridgway, N.D.4    McMaster, C.R.5
  • 28
    • 0030598825 scopus 로고    scopus 로고
    • Farnesol and geranylgeraniol induce actin cytoskeleton disorganization and apoptosis in A549 lung adenocarcinoma cells
    • Miquel K., Pradines A. and Favre G. (1996) Farnesol and geranylgeraniol induce actin cytoskeleton disorganization and apoptosis in A549 lung adenocarcinoma cells. Biochem. Biophys. Res. Commun. 225: 869-876
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 869-876
    • Miquel, K.1    Pradines, A.2    Favre, G.3
  • 29
    • 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. E., Devarenne T., Rodgers D. L., Chappell J. et al. (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.E.3    Devarenne, T.4    Rodgers, D.L.5    Chappell, J.6
  • 30
    • 0031584090 scopus 로고    scopus 로고
    • Metabolism of farnesol: Phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions
    • Westfall D., Aboushadi N., Shackelford J. E. and Krisans S. K. (1997) Metabolism of farnesol: phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions. Biochem. Biophys. Res. Commun. 230: 562-568
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 562-568
    • Westfall, D.1    Aboushadi, N.2    Shackelford, J.E.3    Krisans, S.K.4
  • 31
    • 0032524373 scopus 로고    scopus 로고
    • Phosphorylation of farnesol in rat liver microsomes: Properties of farnesol kinase and farnesyl phosphate kinase
    • Bentinger M., Grunler J., Peterson E., Swiezewska E. and Dallner G. (1998) Phosphorylation of farnesol in rat liver microsomes: properties of farnesol kinase and farnesyl phosphate kinase. Arch. Biochem. Biophys. 353: 191-198
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 191-198
    • Bentinger, M.1    Grunler, J.2    Peterson, E.3    Swiezewska, E.4    Dallner, G.5
  • 32
    • 0027518332 scopus 로고
    • Zaragozic acids: A family of fungal metabolites that are picomolar competitive inhibitors of squalene synthase
    • Bergstrom J. D., Kurtz M. M., Rew D. J., Amend A. M., Karkas J. D., Bostedor R. G. et al. (1993) Zaragozic acids: a family of fungal metabolites that are picomolar competitive inhibitors of squalene synthase. Proc. Natl. Acad. Sci. USA 90: 80-84
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 80-84
    • Bergstrom, J.D.1    Kurtz, M.M.2    Rew, D.J.3    Amend, A.M.4    Karkas, J.D.5    Bostedor, R.G.6
  • 33
    • 0030903764 scopus 로고    scopus 로고
    • Farnesol-derived dicarboxylic acids in the urine of animals treated with zaragozic acid A or with farnesol
    • Bostedor R. G., Karkas J. D., Arison B. H., Bansal V. S., Vaidya S., Germershausen J. I. et al. (1997) Farnesol-derived dicarboxylic acids in the urine of animals treated with zaragozic acid A or with farnesol. J. Biol. Chem. 272: 9197-9203
    • (1997) J. Biol. Chem. , vol.272 , pp. 9197-9203
    • Bostedor, R.G.1    Karkas, J.D.2    Arison, B.H.3    Bansal, V.S.4    Vaidya, S.5    Germershausen, J.I.6
  • 34
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown M. S. and Goldstein J. L. (1997) The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89: 331-340
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 35
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells and blood
    • Brown M. S. and Goldstein J. L. (1999) A proteolytic pathway that controls the cholesterol content of membranes, cells and blood. Proc. Natl. Acad. Sci. USA 96: 11041-11048
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 37
    • 0034693259 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins (SREBPs): Key regulators of nutritional homeostasis and insulin action
    • Osborne T. F. (2000) Sterol regulatory element-binding proteins (SREBPs): key regulators of nutritional homeostasis and insulin action. J. Biol. Chem. 275: 32379-32382
    • (2000) J. Biol. Chem. , vol.275 , pp. 32379-32382
    • Osborne, T.F.1
  • 39
    • 0036251153 scopus 로고    scopus 로고
    • SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver
    • Horton J. D., Goldstein J. L. and Brown M. S. (2002) SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver. J. Clin. Invest. 109: 1125-1131
    • (2002) J. Clin. Invest. , vol.109 , pp. 1125-1131
    • Horton, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 42
    • 0030795333 scopus 로고    scopus 로고
    • Cloning and subcellular localization of hamster and rat isopentenyl diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets the enzyme to peroxisomes
    • Paton V. G., Shackelford J. E. and Krisans S. K. (1997) Cloning and subcellular localization of hamster and rat isopentenyl diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets the enzyme to peroxisomes. J. Biol. Chem. 272: 18945-18950
    • (1997) J. Biol. Chem. , vol.272 , pp. 18945-18950
    • Paton, V.G.1    Shackelford, J.E.2    Krisans, S.K.3
  • 43
    • 0032567674 scopus 로고    scopus 로고
    • Characterization of the mevalonate kinase 5′-untranslated region provides evidence for coordinate regulation of cholesterol biosynthesis
    • Bishop R. W., Chambliss K. L., Hoffmann G. F., Tanaka R. D. and Gibson K. M. (1998) Characterization of the mevalonate kinase 5′-untranslated region provides evidence for coordinate regulation of cholesterol biosynthesis. Biochem. Biophys. Res. Commun. 242: 518-524
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 518-524
    • Bishop, R.W.1    Chambliss, K.L.2    Hoffmann, G.F.3    Tanaka, R.D.4    Gibson, K.M.5
  • 44
    • 0032964743 scopus 로고    scopus 로고
    • Characterization of phosphomevalonate kinase: Chromosomal localization, regulation and subcellular targeting
    • Olivier L. M., Chambliss K. L., Gibson K. M. and Krisans S. K. (1999) Characterization of phosphomevalonate kinase: chromosomal localization, regulation and subcellular targeting. J. Lipid Res. 40: 672-679
    • (1999) J. Lipid Res. , vol.40 , pp. 672-679
    • Olivier, L.M.1    Chambliss, K.L.2    Gibson, K.M.3    Krisans, S.K.4
  • 45
    • 0023902411 scopus 로고
    • Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme
    • Nakanishi M., Goldstein J. L. and Brown M. S. (1988) Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme. J. Biol. Chem. 263: 8929-8937
    • (1988) J. Biol. Chem. , vol.263 , pp. 8929-8937
    • Nakanishi, M.1    Goldstein, J.L.2    Brown, M.S.3
  • 46
    • 0034680918 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Ravid T., Doolman R., Avner R., Harats D. and Roitelman J. (2000) The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 275: 35840-35847
    • (2000) J. Biol. Chem. , vol.275 , pp. 35840-35847
    • Ravid, T.1    Doolman, R.2    Avner, R.3    Harats, D.4    Roitelman, J.5
  • 47
    • 0027270349 scopus 로고
    • Defective cholesterol biosynthesis in Smith-Lemli-Opitz syndrome
    • Irons M., Elias E. R., Salen G., Tint G. S. and Batta A. K. (1993) Defective cholesterol biosynthesis in Smith-Lemli-Opitz syndrome. Lancet 341: 1414
    • (1993) Lancet , vol.341 , pp. 1414
    • Irons, M.1    Elias, E.R.2    Salen, G.3    Tint, G.S.4    Batta, A.K.5
  • 48
    • 0034097540 scopus 로고    scopus 로고
    • The Smith-Lemli-Opitz syndrome
    • Kelley R. I. and Hennekam R. C. (2000) The Smith-Lemli-Opitz syndrome. J. Med. Genet. 37: 321-335
    • (2000) J. Med. Genet. , vol.37 , pp. 321-335
    • Kelley, R.I.1    Hennekam, R.C.2
  • 50
    • 0033582939 scopus 로고    scopus 로고
    • Abnormal sterol metabolism in patients with Conradi-Hunermann-Happle syndrome and sporadic lethal chondrodysplasia punctata
    • Kelley R. I., Wilcox W. G., Smith M., Kratz L. E., Moser A. and Rimoin D. S. (1999) Abnormal sterol metabolism in patients with Conradi-Hunermann-Happle syndrome and sporadic lethal chondrodysplasia punctata. Am. J. Med. Genet. 83: 213-219
    • (1999) Am. J. Med. Genet. , vol.83 , pp. 213-219
    • Kelley, R.I.1    Wilcox, W.G.2    Smith, M.3    Kratz, L.E.4    Moser, A.5    Rimoin, D.S.6
  • 51
    • 0032987971 scopus 로고    scopus 로고
    • Mutations in the gene encoding 3 beta-hydroxysteroid-delta 8, delta 7-isomerase cause X-linked dominant Conradi-Hunermann syndrome
    • Braverman N, Lin P., Moebius F. F., Obie C., Moser A., Glossmann H. et al. (1999) Mutations in the gene encoding 3 beta-hydroxysteroid-delta 8, delta 7-isomerase cause X-linked dominant Conradi-Hunermann syndrome. Nat. Genet. 22: 291-294
    • (1999) Nat. Genet. , vol.22 , pp. 291-294
    • Braverman, N.1    Lin, P.2    Moebius, F.F.3    Obie, C.4    Moser, A.5    Glossmann, H.6
  • 52
    • 0033037717 scopus 로고    scopus 로고
    • Mutations in a delta 8-delta 7 sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata
    • Derry J. M., Gormally E., Means G. D., Zhao W., Meindl A., Kelley R. I. et al. (1999) Mutations in a delta 8-delta 7 sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata. Nat. Genet. 22: 286-290
    • (1999) Nat. Genet. , vol.22 , pp. 286-290
    • Derry, J.M.1    Gormally, E.2    Means, G.D.3    Zhao, W.4    Meindl, A.5    Kelley, R.I.6
  • 53
    • 0033950130 scopus 로고    scopus 로고
    • CHILD syndrome caused by deficiency of 3beta-hydroxysteroid-delta8, delta7-isomerase
    • Grange D. K., Kratz L. E., Braverman N. E. and Kelley R. I. (2000) CHILD syndrome caused by deficiency of 3beta-hydroxysteroid-delta8, delta7-isomerase. Am. J. Med. Genet. 90: 328-335
    • (2000) Am. J. Med. Genet. , vol.90 , pp. 328-335
    • Grange, D.K.1    Kratz, L.E.2    Braverman, N.E.3    Kelley, R.I.4
  • 54
    • 0033972847 scopus 로고    scopus 로고
    • Mutations in the NSDHL gene, encoding a 3beta-hydroxysteroid dehydrogenase, cause CHILD syndrome
    • Konig A., Happle R., Bornholdt D., Engel H. and Grzeschik K. H. (2000) Mutations in the NSDHL gene, encoding a 3beta-hydroxysteroid dehydrogenase, cause CHILD syndrome. Am. J. Med. Genet. 90: 339-346
    • (2000) Am. J. Med. Genet. , vol.90 , pp. 339-346
    • Konig, A.1    Happle, R.2    Bornholdt, D.3    Engel, H.4    Grzeschik, K.H.5
  • 55
    • 19044379648 scopus 로고    scopus 로고
    • Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase
    • Brunetti-Pierri N., Corso G., Rossi M., Ferrari P., Balli F., Rivasi F. et al. (2002) Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am. J. Hum. Genet. 71: 952-958
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 952-958
    • Brunetti-Pierri, N.1    Corso, G.2    Rossi, M.3    Ferrari, P.4    Balli, F.5    Rivasi, F.6
  • 57
    • 0037097340 scopus 로고    scopus 로고
    • Abnormal sterol metabolism in a patient with Antley-Bixler syndrome and ambiguous genitalia
    • Kelley R. I., Kratz L. E., Rivka L. G., Netzloff M. I., Wolf L. M. and Jabs E. W. (2002) Abnormal sterol metabolism in a patient with Antley-Bixler syndrome and ambiguous genitalia. Am. J. Med. Genet. 110: 95-102
    • (2002) Am. J. Med. Genet. , vol.110 , pp. 95-102
    • Kelley, R.I.1    Kratz, L.E.2    Rivka, L.G.3    Netzloff, M.I.4    Wolf, L.M.5    Jabs, E.W.6
  • 58
    • 0036626879 scopus 로고    scopus 로고
    • Inherited disorders of cholesterol biosynthesis
    • Waterham H. R. (2002) Inherited disorders of cholesterol biosynthesis. Clin. Genet. 61: 393-403
    • (2002) Clin. Genet. , vol.61 , pp. 393-403
    • Waterham, H.R.1
  • 60
    • 0034730011 scopus 로고    scopus 로고
    • Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency
    • Rotig A., Appelkvist E. L., Geromel V., Chretien D., Kadhom N., Edery P. et al. (2000) Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency. Lancet 356: 391-395
    • (2000) Lancet , vol.356 , pp. 391-395
    • Rotig, A.1    Appelkvist, E.L.2    Geromel, V.3    Chretien, D.4    Kadhom, N.5    Edery, P.6
  • 61
    • 0035827351 scopus 로고    scopus 로고
    • Prenylation of Rab GTPases: Molecular mechanisms and involvement in genetic disease
    • Pereira-Leal J. B., Hume A. N. and Seabra M. C. (2001) Prenylation of Rab GTPases: molecular mechanisms and involvement in genetic disease. FEBS Lett. 498: 197-200
    • (2001) FEBS Lett. , vol.498 , pp. 197-200
    • Pereira-Leal, J.B.1    Hume, A.N.2    Seabra, M.C.3
  • 64
    • 0032854744 scopus 로고    scopus 로고
    • Identification and characterization of three novel missense mutations in mevalonate kinase cDNA causing mevalonic aciduria, a disorder of isoprene biosynthesis
    • Houten S. M., Romeijn G. J., Koster J., Gray R. G., Darbyshire P., Smit G. P. et al. (1999) Identification and characterization of three novel missense mutations in mevalonate kinase cDNA causing mevalonic aciduria, a disorder of isoprene biosynthesis. Hum. Mol. Genet. 8: 1523-1528
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1523-1528
    • Houten, S.M.1    Romeijn, G.J.2    Koster, J.3    Gray, R.G.4    Darbyshire, P.5    Smit, G.P.6
  • 65
    • 0032987982 scopus 로고    scopus 로고
    • Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome
    • Houten S. M., Kuis W., Duran M., de Koning T. J., van Royen-Kerkhof A., Romeijn G. J. et al. (1999) Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome. Nat. Genet. 22: 175-177
    • (1999) Nat. Genet. , vol.22 , pp. 175-177
    • Houten, S.M.1    Kuis, W.2    Duran, M.3    De Koning, T.J.4    Van Royen-Kerkhof, A.5    Romeijn, G.J.6
  • 66
    • 0035063676 scopus 로고    scopus 로고
    • Organization of the mevalonate kinase (MVK) gene and identification of novel mutations causing mevalonic aciduria and hyperimmunoglobulinaemia D and periodic fever syndrome
    • Houten S. M., Koster J., Romeijn G. J., Frenkel J., Di Rocco M., Caruso U. et al. (2001) Organization of the mevalonate kinase (MVK) gene and identification of novel mutations causing mevalonic aciduria and hyperimmunoglobulinaemia D and periodic fever syndrome. Eur. J. Hum. Genet. 9: 253-259
    • (2001) Eur. J. Hum. Genet. , vol.9 , pp. 253-259
    • Houten, S.M.1    Koster, J.2    Romeijn, G.J.3    Frenkel, J.4    Di Rocco, M.5    Caruso, U.6
  • 68
    • 0034564537 scopus 로고    scopus 로고
    • Inborn errors of cholesterol biosynthesis
    • Kelley R. I. (2000) Inborn errors of cholesterol biosynthesis. Adv. Pediatr. 47: 1-53
    • (2000) Adv. Pediatr. , vol.47 , pp. 1-53
    • Kelley, R.I.1
  • 69
    • 0031830467 scopus 로고    scopus 로고
    • Hematological abnormalities and cholestatic liver disease in two patients with mevalonate kinase deficiency
    • Hinson D. D., Rogers Z. R., Hoffmann G. F., Schachtele M., Fingerhut R., Kohlschutter A. et al. (1998) Hematological abnormalities and cholestatic liver disease in two patients with mevalonate kinase deficiency. Am. J. Med. Genet. 78: 408-412
    • (1998) Am. J. Med. Genet. , vol.78 , pp. 408-412
    • Hinson, D.D.1    Rogers, Z.R.2    Hoffmann, G.F.3    Schachtele, M.4    Fingerhut, R.5    Kohlschutter, A.6
  • 70
    • 0036069089 scopus 로고    scopus 로고
    • An intestinal obstruction in an eight-month-old child suffering from mevalonic aciduria
    • Nimubona L., Laloum D., Rolland M. O., Read M. H., Guillois B. and Duhamel J. F. (2002) An intestinal obstruction in an eight-month-old child suffering from mevalonic aciduria. Acta Paediatr. 91: 714-716
    • (2002) Acta Paediatr. , vol.91 , pp. 714-716
    • Nimubona, L.1    Laloum, D.2    Rolland, M.O.3    Read, M.H.4    Guillois, B.5    Duhamel, J.F.6
  • 71
    • 0028026953 scopus 로고
    • Hyperimmunoglobulinemia D and periodic fever syndrome. The clinical spectrum in a series of 50 patients
    • International Hyper-IgD Study Group
    • Drenth J. P., Haagsma C. J. and van der Meer J. W. (1994) Hyperimmunoglobulinemia D and periodic fever syndrome. The clinical spectrum in a series of 50 patients. International Hyper-IgD Study Group. Medicine (Baltimore) 73: 133-144
    • (1994) Medicine (Baltimore) , vol.73 , pp. 133-144
    • Drenth, J.P.1    Haagsma, C.J.2    Van Der Meer, J.W.3
  • 74
    • 0014252802 scopus 로고
    • A description of two brothers with permanently raised non-esterified aetiocholanolone blood level
    • Driesen O., Voute P. A. Jr and Vermeulen A. (1968) A description of two brothers with permanently raised non-esterified aetiocholanolone blood level. Acta Endocrinol. 57: 177-186
    • (1968) Acta Endocrinol. , vol.57 , pp. 177-186
    • Driesen, O.1    Voute P.A., Jr.2    Vermeulen, A.3
  • 75
    • 0021771086 scopus 로고
    • Nosologic aspects of systemic forms of very-early-onset juvenile arthritis. Apropos of 17 cases
    • Prieur A. M. and Griscelli C. (1984) Nosologic aspects of systemic forms of very-early-onset juvenile arthritis. Apropos of 17 cases. Sem. Hop. 60: 163-167
    • (1984) Sem. Hop. , vol.60 , pp. 163-167
    • Prieur, A.M.1    Griscelli, C.2
  • 76
    • 0034987162 scopus 로고    scopus 로고
    • Clinical and molecular variability in childhood periodic fever with hyperimmunoglobulinaemia D
    • Frenkel J., Houten S. M., Waterham H. R., Wanders R. J., Rijkers G. T., Duran M. et al. (2001) Clinical and molecular variability in childhood periodic fever with hyperimmunoglobulinaemia D. Rheumatology 40: 579-584
    • (2001) Rheumatology , vol.40 , pp. 579-584
    • Frenkel, J.1    Houten, S.M.2    Waterham, H.R.3    Wanders, R.J.4    Rijkers, G.T.5    Duran, M.6
  • 77
    • 0035806948 scopus 로고    scopus 로고
    • Molecular analysis of the mevalonate kinase gene in a cohort of patients with the hyper-IgD and periodic fever syndrome: Its application as a diagnostic tool
    • Simon A., Cuisset L., Vincent M. F., van Der Velde-Visser S. D., Delpech M., van Der Meer J. W. et al. (2001) Molecular analysis of the mevalonate kinase gene in a cohort of patients with the hyper-IgD and periodic fever syndrome: its application as a diagnostic tool. Ann. Intern. Med. 135: 338-343
    • (2001) Ann. Intern. Med. , vol.135 , pp. 338-343
    • Simon, A.1    Cuisset, L.2    Vincent, M.F.3    Van Der Velde-Visser, S.D.4    Delpech, M.5    Van Der Meer, J.W.6
  • 78
    • 0034888835 scopus 로고    scopus 로고
    • Limited efficacy of thalidomide in the treatment of febrile attacks of the hyper-IgD and periodic fever syndrome: A randomized, double-blind, placebo-controlled trial
    • Drenth J. P., Vonk A. G., Simon A., Powell R. and van der Meer J. W. (2001) Limited efficacy of thalidomide in the treatment of febrile attacks of the hyper-IgD and periodic fever syndrome: a randomized, double-blind, placebo-controlled trial. J. Pharmacol. Exp. Ther. 298: 1221-1226
    • (2001) J. Pharmacol. Exp. Ther. , vol.298 , pp. 1221-1226
    • Drenth, J.P.1    Vonk, A.G.2    Simon, A.3    Powell, R.4    Van Der Meer, J.W.5
  • 79
    • 0034884697 scopus 로고    scopus 로고
    • Inherited disorders of cholesterol biosynthesis
    • Haas D., Kelley R. I. and Hoffmann G. F. (2001) Inherited disorders of cholesterol biosynthesis. Neuropediatrics 32: 113-122
    • (2001) Neuropediatrics , vol.32 , pp. 113-122
    • Haas, D.1    Kelley, R.I.2    Hoffmann, G.F.3
  • 80
    • 0027267216 scopus 로고
    • Enhanced urinary excretion of leukothene E4 in patients with mevalonate kinase deficiency
    • Mayatepek E., Hoffmann G. F. and Bremer H. J. (1993) Enhanced urinary excretion of leukothene E4 in patients with mevalonate kinase deficiency. J. Pediatr. 123: 96-98
    • (1993) J. Pediatr. , vol.123 , pp. 96-98
    • Mayatepek, E.1    Hoffmann, G.F.2    Bremer, H.J.3
  • 81
    • 0034926357 scopus 로고    scopus 로고
    • Increased urinary leukothene E(4) during febrile attacks in the hyperimmunoglobulinaemia D and periodic fever syndrome
    • Frenkel J., Willemsen M. A., Weemaes C. M., Dorland L. and Mayatepek E. (2001) Increased urinary leukothene E(4) during febrile attacks in the hyperimmunoglobulinaemia D and periodic fever syndrome. Arch. Dis. Child. 85: 158-159
    • (2001) Arch. Dis. Child. , vol.85 , pp. 158-159
    • Frenkel, J.1    Willemsen, M.A.2    Weemaes, C.M.3    Dorland, L.4    Mayatepek, E.5
  • 82
    • 0030800465 scopus 로고    scopus 로고
    • Enhanced excretion of urinary leukothene E4 in mevalonic aciduria is not caused by an impaired peroxisomal degradation of cysteinyl leukothenes
    • Mayatepek E., Tiepelmann B. and Hoffmann G. F. (1997) Enhanced excretion of urinary leukothene E4 in mevalonic aciduria is not caused by an impaired peroxisomal degradation of cysteinyl leukothenes. J. Inherit. Metab. Dis. 20: 721-722
    • (1997) J. Inherit. Metab. Dis. , vol.20 , pp. 721-722
    • Mayatepek, E.1    Tiepelmann, B.2    Hoffmann, G.F.3
  • 83
    • 0026748788 scopus 로고
    • Molecular cloning of human mevalonate kinase and identification of a missense mutation in the genetic disease mevalonic aciduria
    • Schafer B. L., Bishop R. W., Kratunis V. J., Kalinowski S. S., Mosley S. T., Gibson K. M. et al. (1992) Molecular cloning of human mevalonate kinase and identification of a missense mutation in the genetic disease mevalonic aciduria. J. Biol. Chem. 267: 13229-13238
    • (1992) J. Biol. Chem. , vol.267 , pp. 13229-13238
    • Schafer, B.L.1    Bishop, R.W.2    Kratunis, V.J.3    Kalinowski, S.S.4    Mosley, S.T.5    Gibson, K.M.6
  • 84
    • 0033039501 scopus 로고    scopus 로고
    • Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome
    • International Hyper-IgD Study Group
    • Drenth J. P., Cuisset L., Grateau G., Vasseur C., van de Velde-Visser S. D., de Jong J. G. et al. (1999) Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. International Hyper-IgD Study Group. Nat. Genet. 22: 178-181
    • (1999) Nat. Genet. , vol.22 , pp. 178-181
    • Drenth, J.P.1    Cuisset, L.2    Grateau, G.3    Vasseur, C.4    Van De Velde-Visser, S.D.5    De Jong, J.G.6
  • 85
    • 0030671277 scopus 로고    scopus 로고
    • Identification of an active site alanine in mevalonate kinase through characterization of a novel mutation in mevalonate kinase deficiency
    • Hinson D. D., Chambliss K. L., Hoffmann G. F., Krisans S., Keller R. K. and Gibson K. M. (1997) Identification of an active site alanine in mevalonate kinase through characterization of a novel mutation in mevalonate kinase deficiency. J. Biol. Chem. 272: 26756-26760
    • (1997) J. Biol. Chem. , vol.272 , pp. 26756-26760
    • Hinson, D.D.1    Chambliss, K.L.2    Hoffmann, G.F.3    Krisans, S.4    Keller, R.K.5    Gibson, K.M.6
  • 86
    • 0033358597 scopus 로고    scopus 로고
    • Identification of a mutation cluster in mevalonate kinase deficiency, including a new mutation in a patient of Mennonite ancestry
    • Hinson D. D., Ross R. M., Krisans S., Shaw J. L., Kozich V., Rolland M. O. et al. (1999) Identification of a mutation cluster in mevalonate kinase deficiency, including a new mutation in a patient of Mennonite ancestry. Am. J. Hum. Genet. 65: 327-335
    • (1999) Am. J. Hum. Genet. , vol.65 , pp. 327-335
    • Hinson, D.D.1    Ross, R.M.2    Krisans, S.3    Shaw, J.L.4    Kozich, V.5    Rolland, M.O.6
  • 87
    • 0037300287 scopus 로고    scopus 로고
    • Cartier frequency of the V377I (1129G>A) MVK mutation, associated with Hyper-IgD and periodic fever syndrome, in the Netherlands
    • Houten S. M., van Woerden C. S., Wijburg F. A., Wanders R. J. and Waterham H. R. (2003) Cartier frequency of the V377I (1129G>A) MVK mutation, associated with Hyper-IgD and periodic fever syndrome, in the Netherlands. Eur. J. Hum. Genet. 11: 196-200
    • (2003) Eur. J. Hum. Genet. , vol.11 , pp. 196-200
    • Houten, S.M.1    Van Woerden, C.S.2    Wijburg, F.A.3    Wanders, R.J.4    Waterham, H.R.5
  • 88
    • 0030881593 scopus 로고    scopus 로고
    • Identification of catalytic residues in human mevalonate kinase
    • Potter D. and Miziorko H. M. (1997) Identification of catalytic residues in human mevalonate kinase. J. Biol. Chem. 272: 25449-25454
    • (1997) J. Biol. Chem. , vol.272 , pp. 25449-25454
    • Potter, D.1    Miziorko, H.M.2
  • 89
    • 0031052035 scopus 로고    scopus 로고
    • Identification and functional characterization of an active-site lysine in mevalonate kinase
    • Potter D., Wojnar J. M., Narasimhan C. and Miziorko H. M. (1997) Identification and functional characterization of an active-site lysine in mevalonate kinase. J. Biol. Chem. 272: 5741-5746
    • (1997) J. Biol. Chem. , vol.272 , pp. 5741-5746
    • Potter, D.1    Wojnar, J.M.2    Narasimhan, C.3    Miziorko, H.M.4
  • 90
    • 0035918177 scopus 로고    scopus 로고
    • Investigation of invariant serine/threonine residues in mevalonate kinase. Tests of the functional significance of a proposed substrate binding motif and a site implicated in human inherited disease
    • Cho Y. K., Rios S. E., Kim J. J. and Miziorko H. M. (2001) Investigation of invariant serine/threonine residues in mevalonate kinase. Tests of the functional significance of a proposed substrate binding motif and a site implicated in human inherited disease. J. Biol. Chem. 276: 12573-12578
    • (2001) J. Biol. Chem. , vol.276 , pp. 12573-12578
    • Cho, Y.K.1    Rios, S.E.2    Kim, J.J.3    Miziorko, H.M.4
  • 92
    • 0035971542 scopus 로고    scopus 로고
    • Characterization of mevalonate kinase V377I, a mutant implicated in defective isoprenoid biosynthesis and HIDS/periodic fever syndrome
    • Rios S. E., Cho Y. K. and Miziorko H. M. (2001) Characterization of mevalonate kinase V377I, a mutant implicated in defective isoprenoid biosynthesis and HIDS/periodic fever syndrome. Biochim. Biophys. Acta 1531: 165-168
    • (2001) Biochim. Biophys. Acta , vol.1531 , pp. 165-168
    • Rios, S.E.1    Cho, Y.K.2    Miziorko, H.M.3
  • 93
    • 1842869873 scopus 로고    scopus 로고
    • Temperature dependence of mutant mevalonate kinase activity as a pathogenic factor in Hyper-IgD and periodic fever syndrome
    • Houten S. M., Frenkel J., Rijkers G. T., Wanders R. J., Kuis W. and Waterham H. R. (2002) Temperature dependence of mutant mevalonate kinase activity as a pathogenic factor in Hyper-IgD and periodic fever syndrome. Hum. Mol. Genet. 11: 3115-3124
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3115-3124
    • Houten, S.M.1    Frenkel, J.2    Rijkers, G.T.3    Wanders, R.J.4    Kuis, W.5    Waterham, H.R.6
  • 94
    • 0030888606 scopus 로고    scopus 로고
    • Regulatory adaptation of isoprenoid biosynthesis and the LDL receptor pathway in fibroblasts from patients with mevalonate kinase deficiency
    • Hoffmann G. F., Wiesmann U. N., Brendel S., Keller R. K. and Gibson K. M. (1997) Regulatory adaptation of isoprenoid biosynthesis and the LDL receptor pathway in fibroblasts from patients with mevalonate kinase deficiency. Pediatr. Res. 41: 541-546
    • (1997) Pediatr. Res. , vol.41 , pp. 541-546
    • Hoffmann, G.F.1    Wiesmann, U.N.2    Brendel, S.3    Keller, R.K.4    Gibson, K.M.5
  • 95
    • 0027293794 scopus 로고
    • Decreased plasma ubiquinone-10 concentration in patients with mevalonate kinase deficiency
    • Hubner C., Hoffmann G. F., Charpentier C., Gibson K. M., Finckh B., Puhl H. et al. (1993) Decreased plasma ubiquinone-10 concentration in patients with mevalonate kinase deficiency. Pediatr. Res. 34: 129-133
    • (1993) Pediatr. Res. , vol.34 , pp. 129-133
    • Hubner, C.1    Hoffmann, G.F.2    Charpentier, C.3    Gibson, K.M.4    Finckh, B.5    Puhl, H.6
  • 96
    • 0025220132 scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme A reductase activity in cultured fibroblasts from patients with mevalonate kinase deficiency: Differential response to lipid supplied by fetal bovine serum in tissue culture medium
    • Gibson K. M., Hoffmann G., Schwall A., Broock R. L., Aramaki S., Sweetman L. et al. (1990) 3-Hydroxy-3-methylglutaryl coenzyme A reductase activity in cultured fibroblasts from patients with mevalonate kinase deficiency: differential response to lipid supplied by fetal bovine serum in tissue culture medium. J. Lipid Res. 31: 515-521
    • (1990) J. Lipid Res. , vol.31 , pp. 515-521
    • Gibson, K.M.1    Hoffmann, G.2    Schwall, A.3    Broock, R.L.4    Aramaki, S.5    Sweetman, L.6
  • 97
    • 0019332402 scopus 로고
    • Properties of purified rat hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and regulation of enzyme activity
    • Edwards P. A., Lemongello D., Kane J., Shechter I. and Fogelman A. M. (1980) Properties of purified rat hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and regulation of enzyme activity. J. Biol. Chem. 255: 3715-3725
    • (1980) J. Biol. Chem. , vol.255 , pp. 3715-3725
    • Edwards, P.A.1    Lemongello, D.2    Kane, J.3    Shechter, I.4    Fogelman, A.M.5
  • 98
    • 0034050541 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: Antineoplastic mechanism and clinical prospects
    • Prendergast G. C. (2000) Farnesyltransferase inhibitors: antineoplastic mechanism and clinical prospects. Curr. Opin. Cell Biol. 12: 166-173
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 166-173
    • Prendergast, G.C.1
  • 99
    • 0029819523 scopus 로고    scopus 로고
    • Prenylation of an interferon-gamma-induced GTP-binding protein: The human guanylate binding protein, huGBP1
    • Nantais D. E., Schwemmle M., Stickney J. T., Vestal D. J. and Buss J. E. (1996) Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1. J. Leukoc. Biol. 60: 423-431
    • (1996) J. Leukoc. Biol. , vol.60 , pp. 423-431
    • Nantais, D.E.1    Schwemmle, M.2    Stickney, J.T.3    Vestal, D.J.4    Buss, J.E.5
  • 100
    • 0023882906 scopus 로고
    • Near normal levels of isoprenoid lipids in severe mevalonic aciduria
    • Keller R. K. and Simonet W. S. (1988) Near normal levels of isoprenoid lipids in severe mevalonic aciduria. Biochem. Biophys. Res. Commun. 152: 857-861
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 857-861
    • Keller, R.K.1    Simonet, W.S.2
  • 101
    • 0027177632 scopus 로고
    • Bile acid metabolism in three patients with mevalonic aciduria due to mevalonate kinase deficiency
    • Gibson K. M., Stellaard F., Hoffmann G. F., Rating D., Hrebicek M. and Jakobs C. (1993) Bile acid metabolism in three patients with mevalonic aciduria due to mevalonate kinase deficiency. Clin. Chim. Acta 217: 217-220
    • (1993) Clin. Chim. Acta , vol.217 , pp. 217-220
    • Gibson, K.M.1    Stellaard, F.2    Hoffmann, G.F.3    Rating, D.4    Hrebicek, M.5    Jakobs, C.6
  • 102
    • 0029047439 scopus 로고
    • Elevated serum level and altered glycosylation of alpha 1-acid glycoprotein in hyperimmunoglobulinemia D and periodic fever syndrome: Evidence for persistent inflammation
    • Havenaar E. C., Drenth J. P., van Ommen E. C., van der Meer J. W. and van Dijk W. (1995) Elevated serum level and altered glycosylation of alpha 1-acid glycoprotein in hyperimmunoglobulinemia D and periodic fever syndrome: evidence for persistent inflammation. Clin. Immunol. Immunopathol. 76: 279-284
    • (1995) Clin. Immunol. Immunopathol. , vol.76 , pp. 279-284
    • Havenaar, E.C.1    Drenth, J.P.2    Van Ommen, E.C.3    Van Der Meer, J.W.4    Van Dijk, W.5
  • 105
    • 0029978480 scopus 로고    scopus 로고
    • Immunoglobulin D enhances the release of tumor necrosis factor-alpha, and interleukin-1 beta as well as interleukin-1 receptor antagonist from human mononuclear cells
    • Drenth J. P., Goertz J., Daha M. R. and van der Meer J. W. (1996) Immunoglobulin D enhances the release of tumor necrosis factor-alpha, and interleukin-1 beta as well as interleukin-1 receptor antagonist from human mononuclear cells. Immunology 88: 355-362
    • (1996) Immunology , vol.88 , pp. 355-362
    • Drenth, J.P.1    Goertz, J.2    Daha, M.R.3    Van Der Meer, J.W.4
  • 107
    • 0034049299 scopus 로고    scopus 로고
    • Immunoglobulin D: Properties, measurement, and clinical relevance
    • Vladutiu A. O. (2000) Immunoglobulin D: properties, measurement, and clinical relevance. Clin. Diagn. Lab. Immunol. 7: 131-140
    • (2000) Clin. Diagn. Lab. Immunol. , vol.7 , pp. 131-140
    • Vladutiu, A.O.1
  • 108
    • 0028979302 scopus 로고
    • Interferon-gamma and urine neopterin in attacks of the hyperimmunoglobulinaemia D and periodic fever syndrome
    • Drenth J. P., Powell R. J., Brown N. S. and Van der Meer J. W. (1995) Interferon-gamma and urine neopterin in attacks of the hyperimmunoglobulinaemia D and periodic fever syndrome. Eur. J. Clin. Invest. 25: 683-686
    • (1995) Eur. J. Clin. Invest. , vol.25 , pp. 683-686
    • Drenth, J.P.1    Powell, R.J.2    Brown, N.S.3    Van Der Meer, J.W.4
  • 109
  • 110
    • 0029951663 scopus 로고    scopus 로고
    • Unstimulated peripheral blood mononuclear cells from patients with the hyper-IgD syndrome produce cytokines capable of potent induction of C-reactive protein and serum amyloid A in Hep3B cells
    • Drenth J. P., van der Meer J. W. and Kushner I. (1996) Unstimulated peripheral blood mononuclear cells from patients with the hyper-IgD syndrome produce cytokines capable of potent induction of C-reactive protein and serum amyloid A in Hep3B cells. J. Immunol. 157: 400-404
    • (1996) J. Immunol. , vol.157 , pp. 400-404
    • Drenth, J.P.1    Van Der Meer, J.W.2    Kushner, I.3
  • 112
    • 0030688041 scopus 로고    scopus 로고
    • Polyisoprenyl phosphates in intracellular signalling
    • Levy B. D., Petasis N. A. and Serhan C. N. (1997) Polyisoprenyl phosphates in intracellular signalling. Nature 389: 985-990
    • (1997) Nature , vol.389 , pp. 985-990
    • Levy, B.D.1    Petasis, N.A.2    Serhan, C.N.3
  • 113
    • 0034672674 scopus 로고    scopus 로고
    • Structure and regulation of mammalian squalene synthase
    • Tansey T. R. and Shechter I. (2000) Structure and regulation of mammalian squalene synthase. Biochim. Biophys. Acta 1529: 49-62
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 49-62
    • Tansey, T.R.1    Shechter, I.2
  • 114
    • 0027135157 scopus 로고
    • Effect of endotoxin on cholesterol biosynthesis and distribution in serum lipoproteins in Syrian hamsters
    • Feingold K. R., Hardardottir I., Memon R., Krul E. J., Moser A. H., Taylor J. M. et al. (1993) Effect of endotoxin on cholesterol biosynthesis and distribution in serum lipoproteins in Syrian hamsters. J. Lipid Res. 34: 2147-2158
    • (1993) J. Lipid Res. , vol.34 , pp. 2147-2158
    • Feingold, K.R.1    Hardardottir, I.2    Memon, R.3    Krul, E.J.4    Moser, A.H.5    Taylor, J.M.6
  • 115
    • 0029113729 scopus 로고
    • Discordant regulation of proteins of cholesterol metabolism during the acute phase response
    • Feingold K. R., Pollock A. S., Moser A. H., Shigenaga J. K. and Grunfeld C. (1995) Discordant regulation of proteins of cholesterol metabolism during the acute phase response. J. Lipid Res. 36: 1474-1482
    • (1995) J. Lipid Res. , vol.36 , pp. 1474-1482
    • Feingold, K.R.1    Pollock, A.S.2    Moser, A.H.3    Shigenaga, J.K.4    Grunfeld, C.5
  • 116
    • 0030823967 scopus 로고    scopus 로고
    • Endotoxin, tumor necrosis factor and interleukin-1 decrease hepatic squalene synthase activity, protein and mRNA levels in Syrian hamsters
    • Memon R. A., Shechter I., Moser A. H., Shigenaga J. K., Grunfeld C. and Feingold K. R. (1997) Endotoxin, tumor necrosis factor and interleukin-1 decrease hepatic squalene synthase activity, protein and mRNA levels in Syrian hamsters. J. Lipid Res. 38: 1620-1629
    • (1997) J. Lipid Res. , vol.38 , pp. 1620-1629
    • Memon, R.A.1    Shechter, I.2    Moser, A.H.3    Shigenaga, J.K.4    Grunfeld, C.5    Feingold, K.R.6
  • 118
    • 0036118915 scopus 로고    scopus 로고
    • Pleiotropic effects of HMG-CoA reductase inhibitors
    • Werner N., Nickenig G. and Laufs U. (2002) Pleiotropic effects of HMG-CoA reductase inhibitors. Basic Res. Cardiol. 97: 105-116
    • (2002) Basic Res. Cardiol. , vol.97 , pp. 105-116
    • Werner, N.1    Nickenig, G.2    Laufs, U.3
  • 119
    • 0036322869 scopus 로고    scopus 로고
    • Isoprenoids as mediators of the biological effects of statins
    • Liao J. K. (2002) Isoprenoids as mediators of the biological effects of statins. J. Clin. Invest. 110: 285-288
    • (2002) J. Clin. Invest. , vol.110 , pp. 285-288
    • Liao, J.K.1
  • 120
    • 0036805674 scopus 로고    scopus 로고
    • Statins as anti-inflammatory agents
    • Weitz-Schmidt G. (2002) Statins as anti-inflammatory agents. Trends Pharmacol. Sci. 23: 482-486
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 482-486
    • Weitz-Schmidt, G.1
  • 121
    • 0000306390 scopus 로고    scopus 로고
    • Statins do more than just lower cholesterol
    • Vaughan C. J., Murphy M. B. and Buckley B. M. (1996) Statins do more than just lower cholesterol. Lancet 348: 1079-1082
    • (1996) Lancet , vol.348 , pp. 1079-1082
    • Vaughan, C.J.1    Murphy, M.B.2    Buckley, B.M.3
  • 122
    • 0030058148 scopus 로고    scopus 로고
    • Inhibition of the mevalonate pathway: Benefits beyond cholesterol reduction?
    • Massy Z. A., Keane W. F. and Kasiske B. L. (1996) Inhibition of the mevalonate pathway: benefits beyond cholesterol reduction? Lancet 347: 102-103
    • (1996) Lancet , vol.347 , pp. 102-103
    • Massy, Z.A.1    Keane, W.F.2    Kasiske, B.L.3
  • 123
    • 0025202968 scopus 로고
    • Differential inhibitory effects of lovastatin on protein isoprenylation and sterol synthesis
    • Sinensky M., Beck L. A., Leonard S. and Evans R. (1990) Differential inhibitory effects of lovastatin on protein isoprenylation and sterol synthesis. J. Biol. Chem. 265: 19937-19941
    • (1990) J. Biol. Chem. , vol.265 , pp. 19937-19941
    • Sinensky, M.1    Beck, L.A.2    Leonard, S.3    Evans, R.4
  • 124
    • 0030723114 scopus 로고    scopus 로고
    • Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and non-sterol isoprene biosynthetic pathways
    • Hinson D. D., Chambliss K. L., Toth M. J., Tanaka R. D. and Gibson K. M. (1997) Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and non-sterol isoprene biosynthetic pathways. J. Lipid Res. 38: 2216-2223
    • (1997) J. Lipid Res. , vol.38 , pp. 2216-2223
    • Hinson, D.D.1    Chambliss, K.L.2    Toth, M.J.3    Tanaka, R.D.4    Gibson, K.M.5
  • 125
    • 0034283671 scopus 로고    scopus 로고
    • Simvastatin modulates cytokine-mediated endothelial cell adhesion molecule induction: Involvement of an inhibitory G protein
    • Sadeghi M. M., Collinge M., Pardi R. and Bender J. R. (2000) Simvastatin modulates cytokine-mediated endothelial cell adhesion molecule induction: involvement of an inhibitory G protein. J. Immunol. 165: 2712-2718
    • (2000) J. Immunol. , vol.165 , pp. 2712-2718
    • Sadeghi, M.M.1    Collinge, M.2    Pardi, R.3    Bender, J.R.4
  • 126
    • 0034515454 scopus 로고    scopus 로고
    • Hydroxymethylglutaryl-coenzyme A reductase inhibition stimulates caspase-1 activity and Th1-cytokine release in peripheral blood mononuclear cells
    • Montero M. T., Hernandez O., Suarez Y., Matilla J., Ferruelo A. J., Martinez-Botas J. et al. (2000) Hydroxymethylglutaryl-coenzyme A reductase inhibition stimulates caspase-1 activity and Th1-cytokine release in peripheral blood mononuclear cells. Atherosclerosis 153: 303-313
    • (2000) Atherosclerosis , vol.153 , pp. 303-313
    • Montero, M.T.1    Hernandez, O.2    Suarez, Y.3    Matilla, J.4    Ferruelo, A.J.5    Martinez-Botas, J.6
  • 127
    • 0035129882 scopus 로고    scopus 로고
    • Stimulation of inflammatory responses in vitro and in vivo by lipophilic HMG-CoA reductase inhibitors
    • Kiener P. A., Davis P. M., Murray J. L., Youssef S., Rankin B. M. and Kowala M. (2001) Stimulation of inflammatory responses in vitro and in vivo by lipophilic HMG-CoA reductase inhibitors. Int. Immunopharmacol. 1: 105-118
    • (2001) Int. Immunopharmacol. , vol.1 , pp. 105-118
    • Kiener, P.A.1    Davis, P.M.2    Murray, J.L.3    Youssef, S.4    Rankin, B.M.5    Kowala, M.6
  • 128
    • 0036822810 scopus 로고    scopus 로고
    • Lack of isoprenoid products raises ex vivo interleukin-1β secretion in Hypermmunoglobulinemia D periodic fever syndrome
    • Frenkel J., Rijkers G. T., Mandey S. H., Buurman S. W., Houten S. M., Wanders R. J. et al. (2002) Lack of isoprenoid products raises ex vivo interleukin-1β secretion in Hypermmunoglobulinemia D periodic fever syndrome. Arthritis Rheum. 46: 2794-2803
    • (2002) Arthritis Rheum. , vol.46 , pp. 2794-2803
    • Frenkel, J.1    Rijkers, G.T.2    Mandey, S.H.3    Buurman, S.W.4    Houten, S.M.5    Wanders, R.J.6
  • 131
    • 0035189451 scopus 로고    scopus 로고
    • A fever gene comes in from the cold
    • Kastner D. L. and O'Shea J. J. (2001) A fever gene comes in from the cold. Nat. Genet. 29: 241-242
    • (2001) Nat. Genet. , vol.29 , pp. 241-242
    • Kastner, D.L.1    O'Shea, J.J.2
  • 132
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • Hoffman H. M., Mueller J. L., Broide D. H., Wanderer A. A. and Kolodner R. D. (2001) Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 29: 301-305
    • (2001) Nat. Genet. , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 133
    • 0036302235 scopus 로고    scopus 로고
    • Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes
    • Feldmann J., Prieur A. M., Quartier P., Berquin P., Certain S., Cortis E. et al. (2002) Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. Am. J. Hum. Genet. 71: 198-203
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 198-203
    • Feldmann, J.1    Prieur, A.M.2    Quartier, P.3    Berquin, P.4    Certain, S.5    Cortis, E.6
  • 134
    • 0033515520 scopus 로고    scopus 로고
    • Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes
    • McDermott M. F., Aksentijevich I., Galon J., McDermott E. M., Ogunkolade B. W., Centola M. et al. (1999) Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes. Cell 97: 133-144
    • (1999) Cell , vol.97 , pp. 133-144
    • McDermott, M.F.1    Aksentijevich, I.2    Galon, J.3    McDermott, E.M.4    Ogunkolade, B.W.5    Centola, M.6
  • 135
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • The French FMF Consortium (1997) A candidate gene for familial Mediterranean fever. Nat. Genet. 17: 25-31
    • (1997) Nat. Genet. , vol.17 , pp. 25-31
  • 136
    • 0030745449 scopus 로고    scopus 로고
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever
    • The International FMF Consortium (1997) Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. Cell 90: 797-807
    • (1997) Cell , vol.90 , pp. 797-807
  • 137
    • 0034520137 scopus 로고    scopus 로고
    • The PYRIN domain: A novel motif found in apoptosis and inflammation proteins
    • Bertin J. and DiStefano P. S. (2000) The PYRIN domain: a novel motif found in apoptosis and inflammation proteins. Cell Death Differ. 7: 1273-1274
    • (2000) Cell Death Differ. , vol.7 , pp. 1273-1274
    • Bertin, J.1    DiStefano, P.S.2
  • 139
    • 0035916324 scopus 로고    scopus 로고
    • The pyrin domain: A possible member of the death domain-fold family implicated in apoptosis and inflammation
    • Martinon F., Hofmann K. and Tschopp J. (2001) The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation. Curr. Biol. 11: R118-120
    • (2001) Curr. Biol. , vol.11
    • Martinon, F.1    Hofmann, K.2    Tschopp, J.3
  • 140
    • 0035253123 scopus 로고    scopus 로고
    • PAAD - A new protein domain associated with apoptosis, cancer and autoimmune diseases
    • Pawlowski K., Pio F., Chu Z., Reed J. C. and Godzik A. (2001) PAAD - a new protein domain associated with apoptosis, cancer and autoimmune diseases. Trends Biochem. Sci. 26: 85-87
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 85-87
    • Pawlowski, K.1    Pio, F.2    Chu, Z.3    Reed, J.C.4    Godzik, A.5
  • 142
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F., Burns K. and Tschopp J. (2002) The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol. Cell 10: 417-426
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 144
    • 18344385660 scopus 로고    scopus 로고
    • New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold Urticaria: A novel mutation underlies both syndromes
    • Dode C., Le Du N., Cuisset L., Letourneur F., Berthelot J. M., Vaudour G. et al. (2002) New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold Urticaria: a novel mutation underlies both syndromes. Am. J. Hum. Genet. 70: 1498-1506
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 1498-1506
    • Dode, C.1    Le Du, N.2    Cuisset, L.3    Letourneur, F.4    Berthelot, J.M.5    Vaudour, G.6


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