메뉴 건너뛰기




Volumn 18, Issue , 2002, Pages 345-378

Proteolysis and sterol regulation

Author keywords

ER; HMG CoA reductase; HRD pathway; SREBP; Sterols; Ubiquitin

Indexed keywords

HELIX LOOP HELIX PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; LOW DENSITY LIPOPROTEIN RECEPTOR; MEMBRANE PROTEIN; STEROL; STEROL REGULATORY ELEMENT BINDING PROTEIN; ZARAGOZIC ACID A; CCAAT ENHANCER BINDING PROTEIN; DNA BINDING PROTEIN; PEPTIDE HYDROLASE; SREBF1 PROTEIN, HUMAN; STEROL REGULATORY ELEMENT BINDING PROTEIN 1; TRANSCRIPTION FACTOR; UBIQUITIN;

EID: 0036437316     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.18.032002.131219     Document Type: Review
Times cited : (93)

References (212)
  • 1
    • 0023779728 scopus 로고
    • Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzymes of sterol biosynthesis
    • Basson ME, Thorsness M, Finer MJ, Stroud RM, Rine J. 1988. Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzymes of sterol biosynthesis. Mol. Cell. Biol. 8:3797-808
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3797-3808
    • Basson, M.E.1    Thorsness, M.2    Finer, M.J.3    Stroud, R.M.4    Rine, J.5
  • 2
    • 1442283623 scopus 로고
    • Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase
    • Basson ME, Thorsness M, Rine J. 1986. Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase. Proc. Natl. Acad. Sci. USA 83:5563-67
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5563-5567
    • Basson, M.E.1    Thorsness, M.2    Rine, J.3
  • 3
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY. 2001a. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat. Cell Biol. 3:24-29
    • (2001) Nat. Cell Biol. , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 4
    • 0037076507 scopus 로고    scopus 로고
    • Cdc48p/Np14p/ Ufd1p: Stuck in the middle with Ub
    • Bays NW, Hampton RY. 2002. Cdc48p/Np14p/ Ufd1p: Stuck in the middle with Ub. Curr. Biol. 12:R366-71
    • (2002) Curr. Biol. , vol.12
    • Bays, N.W.1    Hampton, R.Y.2
  • 6
    • 0027505073 scopus 로고
    • Human cytomegalovirus down-regulates HLA class I expression by reducing the stability of class I H chains
    • Beersma MF, Bijlmakers MJ, Ploegh HL. 1993. Human cytomegalovirus down-regulates HLA class I expression by reducing the stability of class I H chains. J. Immunol. 151:4455-64
    • (1993) J. Immunol. , vol.151 , pp. 4455-4464
    • Beersma, M.F.1    Bijlmakers, M.J.2    Ploegh, H.L.3
  • 7
    • 0017284223 scopus 로고
    • Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in hepatoma tissue culture cells by pure cholesterol and several cholesterol derivatives. Evidence supporting two distinct mechanisms
    • Bell JJ, Sargeant TE, Watson JA. 1976. Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in hepatoma tissue culture cells by pure cholesterol and several cholesterol derivatives. Evidence supporting two distinct mechanisms. J. Biol. Chem. 251:1745-58
    • (1976) J. Biol. Chem. , vol.251 , pp. 1745-1758
    • Bell, J.J.1    Sargeant, T.E.2    Watson, J.A.3
  • 8
    • 0034061761 scopus 로고    scopus 로고
    • SEL1L, the human homolog of C. elegans sel-l: Refined physical mapping, gene structure and identification of polymorphic markers
    • Biunno I, Bernard L, Dear P, Cattaneo M, Volorio S, et al. 2000. SEL1L, the human homolog of C. elegans sel-l: Refined physical mapping, gene structure and identification of polymorphic markers. Hum. Genet. 106:227-35
    • (2000) Hum. Genet. , vol.106 , pp. 227-235
    • Biunno, I.1    Bernard, L.2    Dear, P.3    Cattaneo, M.4    Volorio, S.5
  • 10
    • 0032417711 scopus 로고    scopus 로고
    • Procollagen traverses the Golgi stack without leaving the lumen of cisternae: Evidence for cisternal maturation
    • Bonfanti L, Mironov AA Jr, Martinez-Menarguez JA, Martella O, Fusella A, et al. 1998. Procollagen traverses the Golgi stack without leaving the lumen of cisternae: Evidence for cisternal maturation. Cell 95:993-1003
    • (1998) Cell , vol.95 , pp. 993-1003
    • Bonfanti, L.1    Mironov A.A., Jr.2    Martinez-Menarguez, J.A.3    Martella, O.4    Fusella, A.5
  • 11
    • 0026200684 scopus 로고
    • Degradation of proteins within the endoplasmic reticulum
    • Bonifacino JS, Lippincott SJ. 1991. Degradation of proteins within the endoplasmic reticulum. Curr. Opin. Cell Biol. 3:592-600
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 592-600
    • Bonifacino, J.S.1    Lippincott, S.J.2
  • 12
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino JS, Weissman AM. 1998. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell Dev. Biol. 14:19-57
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 13
    • 0031885043 scopus 로고    scopus 로고
    • Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
    • Bordallo J, Plemper RK, Finger A, Wolf DH. 1998. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol. Biol. Cell 9:209-22
    • (1998) Mol. Biol. Cell , vol.9 , pp. 209-222
    • Bordallo, J.1    Plemper, R.K.2    Finger, A.3    Wolf, D.H.4
  • 14
    • 0032960581 scopus 로고    scopus 로고
    • A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae
    • Bordallo J, Wolf DH. 1999. A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae. FEBS Lett. 448:244-48
    • (1999) FEBS Lett. , vol.448 , pp. 244-248
    • Bordallo, J.1    Wolf, D.H.2
  • 15
    • 0034939491 scopus 로고    scopus 로고
    • Bacterial origin for the isoprenoid biosynthesis enzyme HMG-CoA reductase of the archaeal orders Thermoplasmatales and Archaeoglobales
    • Boucher Y, Huber H, L'Haridon S, Stetter KO, Doolittle WF. 2001. Bacterial origin for the isoprenoid biosynthesis enzyme HMG-CoA reductase of the archaeal orders Thermoplasmatales and Archaeoglobales. Mol. Biol. Evol. 18:1378-88
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1378-1388
    • Boucher, Y.1    Huber, H.2    L'Haridon, S.3    Stetter, K.O.4    Doolittle, W.F.5
  • 16
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun S, Matuschewski K, Rape M, Thoms S, Jentsch S. 2002. Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21:615-21
    • (2002) EMBO J. , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 17
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • Brodsky JL, McCracken AA. 1999. ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. 10:507-13
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 507-513
    • Brodsky, J.L.1    McCracken, A.A.2
  • 18
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein
    • Brown CR, Hong-Brown LQ, Biwersi J, Verkman AS, Welch WJ. 1996. Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones 1:117-25
    • (1996) Cell Stress Chaperones , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 19
    • 0242613116 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts by lipoproteins
    • Brown MS, Dana SE, Goldstein JL. 1973. Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts by lipoproteins. Proc. Natl. Acad. Sci. USA 70:2162-66
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 2162-2166
    • Brown, M.S.1    Dana, S.E.2    Goldstein, J.L.3
  • 20
    • 0030077017 scopus 로고    scopus 로고
    • Michael S. Brown, MD and Joseph L. Goldstein, MD. 1985 Nobel laureates in medicine
    • Brown MS, Goldstein JL. 1996. Michael S. Brown, MD and Joseph L. Goldstein, MD. 1985 Nobel laureates in medicine. J. Invest. Med. 44:14-23
    • (1996) J. Invest. Med. , vol.44 , pp. 14-23
    • Brown, M.S.1    Goldstein, J.L.2
  • 21
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown MS, Goldstein JL. 1997. The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89:331-40
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 22
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown MS, Ye J, Rawson RB, Goldstein JL. 2000. Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans. Cell 100:391-98
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 24
    • 0033598964 scopus 로고    scopus 로고
    • Dispatched, a novel sterolsensing domain protein dedicated to the release of cholesterol-modified hedgehog from signaling cells
    • Burke R, Nellen D, Bellotto M, Hafen E, Senti KA, et al. 1999. Dispatched, a novel sterolsensing domain protein dedicated to the release of cholesterol-modified hedgehog from signaling cells. Cell 99:803-15
    • (1999) Cell , vol.99 , pp. 803-815
    • Burke, R.1    Nellen, D.2    Bellotto, M.3    Hafen, E.4    Senti, K.A.5
  • 25
    • 0030863352 scopus 로고    scopus 로고
    • Niemann-Pick C1 disease gene: Homology to mediators of cholesterol homeostasis
    • Carstea ED, Morris JA, Coleman KG, Loftus SK, Zhang D, et al. 1997. Niemann-Pick C1 disease gene: Homology to mediators of cholesterol homeostasis. Science 277:228-31
    • (1997) Science , vol.277 , pp. 228-231
    • Carstea, E.D.1    Morris, J.A.2    Coleman, K.G.3    Loftus, S.K.4    Zhang, D.5
  • 26
    • 0019215066 scopus 로고
    • Regulation of cytosolic acetoacetyl coenzyme A thiolase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and mevalonate kinase by low density lipoprotein and by 25-hy-droxycholesterol in Chinese hamster ovary cells
    • Chang TY, Limanek JS. 1980. Regulation of cytosolic acetoacetyl coenzyme A thiolase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and mevalonate kinase by low density lipoprotein and by 25-hy-droxycholesterol in Chinese hamster ovary cells. J. Biol. Chem. 255:7787-95
    • (1980) J. Biol. Chem. , vol.255 , pp. 7787-7795
    • Chang, T.Y.1    Limanek, J.S.2
  • 27
    • 0030004897 scopus 로고    scopus 로고
    • Sitespecific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity
    • Chen ZJ, Parent L, Maniatis T. 1996. Sitespecific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. Cell 84:853-62
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 28
    • 0033529545 scopus 로고    scopus 로고
    • Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins
    • Cheng D, Espenshade PJ, Slaughter CA, Jaen JC, Brown MS, Goldstein JL. 1999a. Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins. J. Biol. Chem. 274:22805-12
    • (1999) J. Biol. Chem. , vol.274 , pp. 22805-22812
    • Cheng, D.1    Espenshade, P.J.2    Slaughter, C.A.3    Jaen, J.C.4    Brown, M.S.5    Goldstein, J.L.6
  • 29
    • 0033546303 scopus 로고    scopus 로고
    • Oligomerization state influences the degradation rate of 3-hydroxy-3-methyl-glutaryl-CoA reductase
    • Cheng HH, Xu L, Kumagai H, Simoni RD. 1999b. Oligomerization state influences the degradation rate of 3-hydroxy-3-methyl-glutaryl-CoA reductase. J. Biol. Chem. 274:17171-78
    • (1999) J. Biol. Chem. , vol.274 , pp. 17171-17178
    • Cheng, H.H.1    Xu, L.2    Kumagai, H.3    Simoni, R.D.4
  • 30
    • 0021917375 scopus 로고
    • Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA
    • Chin DJ, Gil G, Faust JR, Goldstein JL, Brown MS, Luskey KL. 1985. Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA. Mol. Cell. Biol. 5:634-41
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 634-641
    • Chin, D.J.1    Gil, G.2    Faust, J.R.3    Goldstein, J.L.4    Brown, M.S.5    Luskey, K.L.6
  • 32
    • 0028025326 scopus 로고
    • Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome
    • Chu PM, Vu JH, Proske RJ, Slaughter CA, DeMartino GN. 1994. Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome. J. Biol. Chem. 269:3539-47
    • (1994) J. Biol. Chem. , vol.269 , pp. 3539-3547
    • Chu, P.M.1    Vu, J.H.2    Proske, R.J.3    Slaughter, C.A.4    DeMartino, G.N.5
  • 33
    • 0025649280 scopus 로고
    • The regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase requires a short-lived protein and occurs in the endoplasmic reficulum
    • Chun KT, Bar NS, Simoni RD. 1990. The regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase requires a short-lived protein and occurs in the endoplasmic reficulum. J. Biol. Chem. 265:22004-10
    • (1990) J. Biol. Chem. , vol.265 , pp. 22004-22010
    • Chun, K.T.1    Bar, N.S.2    Simoni, R.D.3
  • 34
    • 0026742974 scopus 로고
    • The role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Chun KT, Simoni RD. 1992. The role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 267:4236-46
    • (1992) J. Biol. Chem. , vol.267 , pp. 4236-4246
    • Chun, K.T.1    Simoni, R.D.2
  • 35
    • 0036139950 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of cellular proteins in health and disease
    • Ciechanover A, Schwartz AL. 2002. Ubiquitin-mediated degradation of cellular proteins in health and disease. Hepatology 35:3-6
    • (2002) Hepatology , vol.35 , pp. 3-6
    • Ciechanover, A.1    Schwartz, A.L.2
  • 36
    • 0029681753 scopus 로고    scopus 로고
    • Genetic factors that contribute to interindividual variations in plasma low density lipoprotein-cholesterol levels
    • Cohen J, Gaw A, Barnes RI, Landschulz KT, Hobbs HH. 1996. Genetic factors that contribute to interindividual variations in plasma low density lipoprotein-cholesterol levels. Ciba Found. Syrup. 197:194-206, 10
    • (1996) Ciba Found. Syrup. , vol.197 , pp. 194-206
    • Cohen, J.1    Gaw, A.2    Barnes, R.I.3    Landschulz, K.T.4    Hobbs, H.H.5
  • 37
    • 0028307290 scopus 로고
    • Identification of famesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Correll CC, Ng L, Edwards PA. 1994. Identification of famesol 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; 17390-93
    • (1994) J. Biol. Chem. , vol.269 , pp. 17390-17393
    • Correll, C.C.1    Ng, L.2    Edwards, P.A.3
  • 38
  • 39
    • 0032907667 scopus 로고    scopus 로고
    • Measuring protein degradation with GFP
    • Cronin S, Hampton RY. 1999. Measuring protein degradation with GFP. Meth. Enzymol. 302:58-73
    • (1999) Meth. Enzymol. , vol.302 , pp. 58-73
    • Cronin, S.1    Hampton, R.Y.2
  • 40
    • 0037054541 scopus 로고    scopus 로고
    • Cod1p/ Spf1 is an ER P-type ATPase required for ER function and calcium homeostasis
    • In press
    • Cronin S, Rao R, Hampton RY. 2002. Cod1p/ Spf1 is an ER P-type ATPase required for ER function and calcium homeostasis. J. Cell Biol. 157:In press
    • (2002) J. Cell Biol. , vol.157
    • Cronin, S.1    Rao, R.2    Hampton, R.Y.3
  • 41
    • 0034611014 scopus 로고    scopus 로고
    • Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p
    • Cronin SR, Khoury A, Ferry DK, Hampton RY. 2000. Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p. J. Cell Biol. 148:915-24
    • (2000) J. Cell Biol. , vol.148 , pp. 915-924
    • Cronin, S.R.1    Khoury, A.2    Ferry, D.K.3    Hampton, R.Y.4
  • 42
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai RM, Li CC. 2001. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 3:740-44
    • (2001) Nat. Cell Biol. , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 43
    • 0025816877 scopus 로고
    • Genetic distinction between sterol-mediated transcriptional nd posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Dawson PA, Metherall JE, Ridgway ND, Brown MS, Goldstein JL. 1991. Genetic distinction between sterol-mediated transcriptional nd posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 266:9128-34
    • (1991) J. Biol. Chem. , vol.266 , pp. 9128-9134
    • Dawson, P.A.1    Metherall, J.E.2    Ridgway, N.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 44
    • 0033599028 scopus 로고    scopus 로고
    • Transport-dependent proteolysis of SREBP: Relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
    • DeBose-Boyd RA, Brown MS, Li WP, Nohturfft A, Goldstein JL, Espenshade PJ. 1999. Transport-dependent proteolysis of SREBP: Relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi. Cell 99:703-12
    • (1999) Cell , vol.99 , pp. 703-712
    • DeBose-Boyd, R.A.1    Brown, M.S.2    Li, W.P.3    Nohturfft, A.4    Goldstein, J.L.5    Espenshade, P.J.6
  • 45
    • 0028087582 scopus 로고
    • PA700, an ATP-dependent activator of the 20 S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family
    • DeMartino GN, Moomaw CR, Zagnitko OP, Proske RJ, Chu PM, et al. 1994. PA700, an ATP-dependent activator of the 20 S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family. J. Biol. Chem. 269:20878-84
    • (1994) J. Biol. Chem. , vol.269 , pp. 20878-20884
    • DeMartino, G.N.1    Moomaw, C.R.2    Zagnitko, O.P.3    Proske, R.J.4    Chu, P.M.5
  • 46
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • DeMartino GN, Slaughter CA. 1999. The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 274:22123-26
    • (1999) J. Biol. Chem. , vol.274 , pp. 22123-22126
    • DeMartino, G.N.1    Slaughter, C.A.2
  • 47
    • 0033279836 scopus 로고    scopus 로고
    • SCF and cullin/RING H2-based ubiquitin ligases
    • Deshaies RJ. 1999. SCF and cullin/RING H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15:435-67
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 48
    • 0037012907 scopus 로고    scopus 로고
    • Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila
    • Dobrosotskaya IY, Seegmiller AC, Brown MS, Goldstein JL, Rawson RB. 2002. Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila. Science 296:879-83
    • (2002) Science , vol.296 , pp. 879-883
    • Dobrosotskaya, I.Y.1    Seegmiller, A.C.2    Brown, M.S.3    Goldstein, J.L.4    Rawson, R.B.5
  • 49
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson G, Wlodawer A. 1998. Catalytic triads and their relatives. Trends Biochem. Sci. 23:347-52
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 50
    • 0034988110 scopus 로고    scopus 로고
    • Secretases as therapeutic targets for the treatment of Alzheimer's disease
    • Dominguez DI, De Strooper B, Annaert W. 2001. Secretases as therapeutic targets for the treatment of Alzheimer's disease. Amyloid 8:124-42
    • (2001) Amyloid , vol.8 , pp. 124-142
    • Dominguez, D.I.1    De Strooper, B.2    Annaert, W.3
  • 51
    • 0030772492 scopus 로고    scopus 로고
    • Effects of overproduction of the catalytic domain of 3-hyctroxy-3-methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae
    • Donald KA, Hampton RY, Fritz IB. 1997. Effects of overproduction of the catalytic domain of 3-hyctroxy-3-methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 63:3341-44
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3341-3344
    • Donald, K.A.1    Hampton, R.Y.2    Fritz, I.B.3
  • 52
    • 0031678880 scopus 로고    scopus 로고
    • Cloning and characterization of Sel-11, a murine homolog of the C. elegans sel-1 gene
    • Donoviel DB, Donoviel MS, Fan E, Hadjantonakis A, Bernstein A. 1998. Cloning and characterization of Sel-11, a murine homolog of the C. elegans sel-1 gene. Mech. Dev. 78:203-7
    • (1998) Mech. Dev. , vol.78 , pp. 203-207
    • Donoviel, D.B.1    Donoviel, M.S.2    Fan, E.3    Hadjantonakis, A.4    Bernstein, A.5
  • 53
    • 0030911517 scopus 로고    scopus 로고
    • Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2
    • Duncan EA, Brown MS, Goldstein JL, Sakai J. 1997. Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2. J. Biol. Chem. 272:12778-85
    • (1997) J. Biol. Chem. , vol.272 , pp. 12778-12785
    • Duncan, E.A.1    Brown, M.S.2    Goldstein, J.L.3    Sakai, J.4
  • 54
    • 0032504202 scopus 로고    scopus 로고
    • Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning
    • Duncan EA, Dave UP, Sakai J, Goldstein JL, Brown MS. 1998. Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning. J. Biol. Chem. 273:17801-9
    • (1998) J. Biol. Chem. , vol.273 , pp. 17801-17809
    • Duncan, E.A.1    Dave, U.P.2    Sakai, J.3    Goldstein, J.L.4    Brown, M.S.5
  • 55
    • 0036164154 scopus 로고    scopus 로고
    • BAREing it all. The adoption of lxr and fxr and their roles in lipid homeostasis
    • Edwards PA, Kast HR, Anisfeld AM. 2002. BAREing it all. The adoption of lxr and fxr and their roles in lipid homeostasis. J. Lipid. Res. 43:2-12
    • (2002) J. Lipid. Res. , vol.43 , pp. 2-12
    • Edwards, P.A.1    Kast, H.R.2    Anisfeld, A.M.3
  • 56
    • 0021042806 scopus 로고
    • Alterations in the rates of synthesis and degradation of rat liver 3-hydroxy-3-methyl-glutaryl coenzyme A reductase produced by cholestyramine and mevinolin
    • Edwards PA, Lan SF, Fogelman AM. 1983a. Alterations in the rates of synthesis and degradation of rat liver 3-hydroxy-3-methyl-glutaryl coenzyme A reductase produced by cholestyramine and mevinolin. J. Biol. Chem. 258:10219-22
    • (1983) J. Biol. Chem. , vol.258 , pp. 10219-10222
    • Edwards, P.A.1    Lan, S.F.2    Fogelman, A.M.3
  • 57
    • 0020619724 scopus 로고
    • Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes
    • Edwards PA, Lan SF, Tanaka RD, Fogelman AM. 1983b. Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes. J. Biol. Chem. 258:7272-75
    • (1983) J. Biol. Chem. , vol.258 , pp. 7272-7275
    • Edwards, P.A.1    Lan, S.F.2    Tanaka, R.D.3    Fogelman, A.M.4
  • 58
    • 0033529560 scopus 로고    scopus 로고
    • Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins
    • Espenshade PJ, Cheng D, Goldstein JL, Brown MS. 1999. Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins. J. Biol. Chem. 274:22795-804
    • (1999) J. Biol. Chem. , vol.274 , pp. 22795-22804
    • Espenshade, P.J.1    Cheng, D.2    Goldstein, J.L.3    Brown, M.S.4
  • 59
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM. 2001. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 98:14422-27
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 61
    • 0020183575 scopus 로고
    • Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-1 cells
    • Faust JR, Luskey KL, Chin DJ, Goldstein JL, Brown MS. 1982. Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-1 cells. Proc. Natl. Acad. Sci. USA 79:5205-9
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 5205-5209
    • Faust, J.R.1    Luskey, K.L.2    Chin, D.J.3    Goldstein, J.L.4    Brown, M.S.5
  • 62
    • 0017395458 scopus 로고
    • Isolation of 2,3;22,23-dioxidosqualene and 24,25-oxidolanosterol from yeast
    • Field RB, Holmlund CE. 1977. Isolation of 2,3;22,23-dioxidosqualene and 24,25-oxidolanosterol from yeast. Arch. Biochem. Biophys. 180:465-71
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 465-471
    • Field, R.B.1    Holmlund, C.E.2
  • 63
    • 0032126426 scopus 로고    scopus 로고
    • Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle
    • Finley D, Tanaka K, Mann C, Feldmann H, Hochstrasser M, et al. 1998. Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends Biochem. Sci. 23:244-45
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 244-245
    • Finley, D.1    Tanaka, K.2    Mann, C.3    Feldmann, H.4    Hochstrasser, M.5
  • 64
    • 0030860899 scopus 로고    scopus 로고
    • The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70
    • Fisher EA, Zhou M, Mitchell DM, Wu X, Omura S, et al. 1997. The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70. J. Biol. Chem. 272:20427-34
    • (1997) J. Biol. Chem. , vol.272 , pp. 20427-20434
    • Fisher, E.A.1    Zhou, M.2    Mitchell, D.M.3    Wu, X.4    Omura, S.5
  • 65
    • 0034829757 scopus 로고    scopus 로고
    • 7-Dehydrocholesterol-dependent proteolysis of HMG-CoA reductase suppresses sterol biosynthesis in a mouse model of Smith-Lemli-Opitz/RSH syndrome
    • Fitzky BU, Moebius FF, Asaoka H, Waage-Baudet H, Xu L, et al. 2001. 7-Dehydrocholesterol-dependent proteolysis of HMG-CoA reductase suppresses sterol biosynthesis in a mouse model of Smith-Lemli-Opitz/RSH syndrome. J. Clin. Invest. 108:905-15
    • (2001) J. Clin. Invest. , vol.108 , pp. 905-915
    • Fitzky, B.U.1    Moebius, F.F.2    Asaoka, H.3    Waage-Baudet, H.4    Xu, L.5
  • 67
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R, Jarosch E, Urban J, Volkwein C, Sommer T. 2000. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat. Cell Biol. 2:379-84
    • (2000) Nat. Cell Biol. , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 68
    • 0017098270 scopus 로고
    • Effect of triparanol and 3beta-(beta-dimethyl-aminoethoxy)-and rost-5-en-17-one on growth and non-saponifiable lipids of Saccharomyces cerevisiae
    • Fung B, Holmlund CE. 1976. Effect of triparanol and 3beta-(beta-dimethyl-aminoethoxy)-and rost-5-en-17-one on growth and non-saponifiable lipids of Saccharomyces cerevisiae. Biochem. Pharmacol. 25:1249-54
    • (1976) Biochem. Pharmacol. , vol.25 , pp. 1249-1254
    • Fung, B.1    Holmlund, C.E.2
  • 69
    • 0031713885 scopus 로고    scopus 로고
    • Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Gardner R, Cronin S, Leader B, Rine J, Hampton R, Leder B. 1998. Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 9:2611-26
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2611-2626
    • Gardner, R.1    Cronin, S.2    Leader, B.3    Rine, J.4    Hampton, R.5    Leder, B.6
  • 70
    • 0033231014 scopus 로고    scopus 로고
    • A 'distributed degron' allows regulated entry into the ER degradation pathway
    • Gardner RG, Hampton RY. 1999a. A 'distributed degron' allows regulated entry into the ER degradation pathway. EMBO J. 18:5994-6004
    • (1999) EMBO J. , vol.18 , pp. 5994-6004
    • Gardner, R.G.1    Hampton, R.Y.2
  • 71
    • 0033615648 scopus 로고    scopus 로고
    • A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes
    • Gardner RG, Hampton RY. 1999b. A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes. J. Biol. Chem. 274:31671-78
    • (1999) J. Biol. Chem. , vol.274 , pp. 31671-31678
    • Gardner, R.G.1    Hampton, R.Y.2
  • 72
    • 0035937843 scopus 로고    scopus 로고
    • An oxysterol-derived positive signal for 3-hydroxy-3-methylglutaryl- CoA reductase degradation in yeast
    • Gardner RG, Shan H, Matsuda SP, Hampton RY. 2001a. An oxysterol-derived positive signal for 3-hydroxy-3-methylglutaryl- CoA reductase degradation in yeast. J. Biol. Chem. 276:8681-94
    • (2001) J. Biol. Chem. , vol.276 , pp. 8681-8694
    • Gardner, R.G.1    Shan, H.2    Matsuda, S.P.3    Hampton, R.Y.4
  • 73
    • 0034971386 scopus 로고    scopus 로고
    • In vivo action of the hrd ubiquitin ligase complex: Mechanisms of endoplasmic reticulum quality control and sterol regulation
    • Gardner RG, Shearer AG, Hampton RY. 2001b. In vivo action of the hrd ubiquitin ligase complex: Mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol. Cell. Biol. 21:4276-91
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4276-4291
    • Gardner, R.G.1    Shearer, A.G.2    Hampton, R.Y.3
  • 74
    • 0034597161 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p
    • Gardner RG, Swarbrick GM, Bays NW, Cronin SR, Wilhovsky S, et al. 2000. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p. J. Cell Biol. 151:69-82
    • (2000) J. Cell Biol. , vol.151 , pp. 69-82
    • Gardner, R.G.1    Swarbrick, G.M.2    Bays, N.W.3    Cronin, S.R.4    Wilhovsky, S.5
  • 76
    • 0021856440 scopus 로고
    • Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
    • Gil G, Faust JR, Chin DJ, Goldstein JL, Brown MS. 1985. Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell 41:249-58
    • (1985) Cell , vol.41 , pp. 249-258
    • Gil, G.1    Faust, J.R.2    Chin, D.J.3    Goldstein, J.L.4    Brown, M.S.5
  • 77
    • 0030906716 scopus 로고    scopus 로고
    • Role of lipid synthesis, chaperone proteins and proteasomes in the assembly and secretion of apoprotein B-containing lipoproteins from cultured liver cells
    • Ginsberg HN. 1997. Role of lipid synthesis, chaperone proteins and proteasomes in the assembly and secretion of apoprotein B-containing lipoproteins from cultured liver cells. Clin. Exp. Pharmacol. Physiol. 24:A29-32
    • (1997) Clin. Exp. Pharmacol. Physiol. , vol.24
    • Ginsberg, H.N.1
  • 78
    • 0031559885 scopus 로고    scopus 로고
    • A cisternal maturation mechanism can explain the asymmetry of the Golgi stack
    • Glick BS, Elston T, Oster G. 1997. A cisternal maturation mechanism can explain the asymmetry of the Golgi stack. FEBS Lett. 414:177-81
    • (1997) FEBS Lett. , vol.414 , pp. 177-181
    • Glick, B.S.1    Elston, T.2    Oster, G.3
  • 80
    • 0016241915 scopus 로고
    • Binding and degradation of low density lipoproteins by cultured human fibroblasts. Comparison of cells from a normal subject and from a patient with homozygous familial hypercholes-terolemia
    • Goldstein JL, Brown MS. 1974. Binding and degradation of low density lipoproteins by cultured human fibroblasts. Comparison of cells from a normal subject and from a patient with homozygous familial hypercholes-terolemia. J. Biol. Chem. 249:5153-62
    • (1974) J. Biol. Chem. , vol.249 , pp. 5153-5162
    • Goldstein, J.L.1    Brown, M.S.2
  • 81
    • 0022334353 scopus 로고
    • The LDL receptor and the regulation of cellular cholesterol metabolism
    • Goldstein JL, Brown MS. 1985. The LDL receptor and the regulation of cellular cholesterol metabolism. J. Cell Sci. Suppl. 3:131-37
    • (1985) J. Cell Sci. Suppl. , vol.3 , pp. 131-137
    • Goldstein, J.L.1    Brown, M.S.2
  • 82
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL, Brown MS. 1990. Regulation of the mevalonate pathway. Nature 343:425-30
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 83
    • 0037082099 scopus 로고    scopus 로고
    • Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis
    • Goldstein JL, Rawson RB, Brown MS. 2002. Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis. Arch. Biochem. Biophys. 397:139-48
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 139-148
    • Goldstein, J.L.1    Rawson, R.B.2    Brown, M.S.3
  • 85
    • 0034884697 scopus 로고    scopus 로고
    • Inherited disorders of cholesterol biosynthesis
    • Haas D, Kelley RI, Hoffmann GF. 2001. Inherited disorders of cholesterol biosynthesis. Neuropediatrics 32:113-22
    • (2001) Neuropediatrics , vol.32 , pp. 113-122
    • Haas, D.1    Kelley, R.I.2    Hoffmann, G.F.3
  • 86
  • 87
    • 0029917248 scopus 로고    scopus 로고
    • The biology of HMG-CoA reductase: The pros of contra-regulation
    • Hampton R, Dimster-Denk D, Rine J. 1996a. The biology of HMG-CoA reductase: The pros of contra-regulation. Trends Biochem. Sci. 21:140-45
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 140-145
    • Hampton, R.1    Dimster-Denk, D.2    Rine, J.3
  • 88
    • 0034175819 scopus 로고    scopus 로고
    • Cholesterol homeostasis: ESCAPe from the ER
    • Hampton RY. 2000a. Cholesterol homeostasis: ESCAPe from the ER. Curr. Biol. 10:R298-301
    • (2000) Curr. Biol. , vol.10
    • Hampton, R.Y.1
  • 89
    • 0034644111 scopus 로고    scopus 로고
    • ER stress response: Getting the UPR hand on misfolded proteins
    • Hampton RY. 2000b. ER stress response: Getting the UPR hand on misfolded proteins. Curr. Biol. 10:R518-21
    • (2000) Curr. Biol. , vol.10
    • Hampton, R.Y.1
  • 90
    • 0030660267 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Hampton RY, Bhakta H. 1997. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc. Natl. Acad. Sci. USA 94:12944-48
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 91
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton RY, Gardner RG, Rine J. 1996b. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7:2029-44
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 92
    • 0030069686 scopus 로고    scopus 로고
    • In vivo examination of membrane protein localization and degradation with green fluorescent protein
    • Hampton RY, Koning A, Wright R, Rine J. 1996c. In vivo examination of membrane protein localization and degradation with green fluorescent protein. Proc. Natl. Acad. Sci. USA 93:828-33
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 828-833
    • Hampton, R.Y.1    Koning, A.2    Wright, R.3    Rine, J.4
  • 93
    • 0028213166 scopus 로고
    • Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
    • Hampton RY, Rine J. 1994. Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast. J. Cell Biol. 125:299-312
    • (1994) J. Cell Biol. , vol.125 , pp. 299-312
    • Hampton, R.Y.1    Rine, J.2
  • 95
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller MM, Finger A, Schweiger M, Wolf DH. 1996. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273:1725-28
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 96
    • 0034746779 scopus 로고    scopus 로고
    • The conserved np14 protein complex mediates proteasome-dependent membrane-bound transcription factor activation
    • Hitchcock AL, Krebber H, Frietze S, Lin A, Latterich M, Silver PA. 2001. The conserved np14 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol. Biol. Cell 12:3226-41
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3226-3241
    • Hitchcock, A.L.1    Krebber, H.2    Frietze, S.3    Lin, A.4    Latterich, M.5    Silver, P.A.6
  • 97
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405-39
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 98
    • 0024468746 scopus 로고
    • The Drosophila patched gene encodes a putative membrane protein required for segmental patterning
    • Hooper JE, Scott MP. 1989. The Drosophila patched gene encodes a putative membrane protein required for segmental patterning. Cell 59:751-65
    • (1989) Cell , vol.59 , pp. 751-765
    • Hooper, J.E.1    Scott, M.P.2
  • 99
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper NM. 1994. Families of zinc metalloproteases. FEBS Lett. 354:1-6
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 100
    • 0030298339 scopus 로고    scopus 로고
    • Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein
    • Hua X, Nohturfft A, Goldstein JL, Brown MS. 1996. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell 87:415-26
    • (1996) Cell , vol.87 , pp. 415-426
    • Hua, X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 101
    • 0028960739 scopus 로고
    • Structure of the human gene encoding sterol regulatory element binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes 17p11.2 and 22q13
    • Hua X, Wu J, Goldstein JL, Brown MS, Hobbs HH. 1995. Structure of the human gene encoding sterol regulatory element binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes 17p11.2 and 22q13. Genomics 25:667-73
    • (1995) Genomics , vol.25 , pp. 667-673
    • Hua, X.1    Wu, J.2    Goldstein, J.L.3    Brown, M.S.4    Hobbs, H.H.5
  • 102
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Erratum. 1995. Proc. Natl. Acad. Sci. USA 92(11):5249
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM. 1995. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA 92:2563-67. Erratum. 1995. Proc. Natl. Acad. Sci. USA 92(11):5249
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 103
    • 0025915504 scopus 로고
    • Inhibition of degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo by cysteine protease inhibitors
    • Inoue S, Bar NS, Roitelman J, Simoni RD. 1991. Inhibition of degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo by cysteine protease inhibitors. J. Biol. Chem. 266:13311-17
    • (1991) J. Biol. Chem. , vol.266 , pp. 13311-13317
    • Inoue, S.1    Bar, N.S.2    Roitelman, J.3    Simoni, R.D.4
  • 104
    • 0026795608 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A reductase and T cell receptor alpha subunit are differentially degraded in the endoplasmic reticulum
    • Inoue S, Simoni RD. 1992. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase and T cell receptor alpha subunit are differentially degraded in the endoplasmic reticulum. J. Biol. Chem. 267:9080-86
    • (1992) J. Biol. Chem. , vol.267 , pp. 9080-9086
    • Inoue, S.1    Simoni, R.D.2
  • 105
    • 0035976936 scopus 로고    scopus 로고
    • The hypocholesterolemic agent LY295427 reverses suppression of sterol regulatory element-binding protein processing mediated by oxysterols
    • Janowski BA, Shan B, Russell DW. 2001. The hypocholesterolemic agent LY295427 reverses suppression of sterol regulatory element-binding protein processing mediated by oxysterols. J. Biol. Chem. 276:45408-16
    • (2001) J. Biol. Chem. , vol.276 , pp. 45408-45416
    • Janowski, B.A.1    Shan, B.2    Russell, D.W.3
  • 106
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, et al. 2002. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat. Cell Biol. 4:134-39
    • (2002) Nat. Cell Biol. , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5
  • 107
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM. 2000. RING finger proteins: Mediators of ubiquitin ligase activity. Cell 102:549-52
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 108
    • 0000812012 scopus 로고    scopus 로고
    • Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver
    • Keller RK, Zhao Z, Chambers C, Ness GC. 1996. Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver. Arch. Biochem. Biophys. 328:324-30
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 324-330
    • Keller, R.K.1    Zhao, Z.2    Chambers, C.3    Ness, G.C.4
  • 110
    • 0028963743 scopus 로고
    • Dual DNA binding specificity of ADD1/SREBP1 controlled by a single amino acid in the basic helixloop-helix domain
    • Kim JB, Spotts GD, Halvorsen YD, Shih HM, Ellenberger T, et al. 1995. Dual DNA binding specificity of ADD1/SREBP1 controlled by a single amino acid in the basic helixloop-helix domain. Mol. Cell. Biol. 15:2582-88
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2582-2588
    • Kim, J.B.1    Spotts, G.D.2    Halvorsen, Y.D.3    Shih, H.M.4    Ellenberger, T.5
  • 112
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner RD, Sitia R. 1990. Protein degradation in the endoplasmic reticulum. Cell 62:611-14
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 113
    • 0028607143 scopus 로고
    • Regulated degradation of the transcription factor Gcn4
    • Kornitzer D, Raboy B, Kulka RG, Fink GR. 1994. Regulated degradation of the transcription factor Gcn4. EMBO J. 13:6021-30
    • (1994) EMBO J. , vol.13 , pp. 6021-6030
    • Kornitzer, D.1    Raboy, B.2    Kulka, R.G.3    Fink, G.R.4
  • 114
    • 0033981032 scopus 로고    scopus 로고
    • Molecular and conformational features of a transportrelevant domain in the C-terminal tail of the vasopressin V(2) receptor
    • Krause G, Hermosilla R, Oksche A, Rutz C, Rosenthal W, Schulein R. 2000. Molecular and conformational features of a transportrelevant domain in the C-terminal tail of the vasopressin V(2) receptor. Mol. Pharmacol. 57:232-42
    • (2000) Mol. Pharmacol. , vol.57 , pp. 232-242
    • Krause, G.1    Hermosilla, R.2    Oksche, A.3    Rutz, C.4    Rosenthal, W.5    Schulein, R.6
  • 115
    • 0029045589 scopus 로고
    • Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Kumagai H, Chun KT, Simoni RD. 1995. Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 270:19107-13
    • (1995) J. Biol. Chem. , vol.270 , pp. 19107-19113
    • Kumagai, H.1    Chun, K.T.2    Simoni, R.D.3
  • 116
    • 0026713882 scopus 로고
    • Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii
    • Lam WL, Doolittle WF. 1992. Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii. J. Biol. Chem. 267:5829-34
    • (1992) J. Biol. Chem. , vol.267 , pp. 5829-5834
    • Lam, W.L.1    Doolittle, W.F.2
  • 117
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney JD, Hochstrasser M. 1999. Substrate targeting in the ubiquitin system. Cell 97:427-30
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 118
    • 0034700150 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes
    • Lange BM, Rujan T, Martin W, Croteau R. 2000. Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes. Proc. Natl. Acad. Sci. USA 97:13172-77
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13172-13177
    • Lange, B.M.1    Rujan, T.2    Martin, W.3    Croteau, R.4
  • 119
    • 0025042675 scopus 로고
    • Intracellular degradation of the transport-impaired human PiZ alpha 1-antitrypsin variant. Biochemical mapping of the degradative event among compartments of the secretory pathway
    • Le A, Graham KS, Sifers RN. 1990. Intracellular degradation of the transport-impaired human PiZ alpha 1-antitrypsin variant. Biochemical mapping of the degradative event among compartments of the secretory pathway. J. Biol. Chem. 265:14001-7
    • (1990) J. Biol. Chem. , vol.265 , pp. 14001-14007
    • Le, A.1    Graham, K.S.2    Sifers, R.N.3
  • 120
    • 0028015928 scopus 로고
    • The regulated degradation of a 3-hydroxy-3-methylglutaryl-coenzyme A reductase reporter construct occurs in the endoplasmic reticulum
    • Lecureux LW, Wattenberg BW. 1994. The regulated degradation of a 3-hydroxy-3-methylglutaryl-coenzyme A reductase reporter construct occurs in the endoplasmic reticulum. J. Cell Sci. 107:2635-42
    • (1994) J. Cell Sci. , vol.107 , pp. 2635-2642
    • Lecureux, L.W.1    Wattenberg, B.W.2
  • 121
    • 0021913335 scopus 로고
    • Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum
    • Liscum L, Finer-Moore J, Stroud RM, Luskey KL, Brown MS, Goldstein JL. 1985. Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. J. Biol. Chem. 260:522-30
    • (1985) J. Biol. Chem. , vol.260 , pp. 522-530
    • Liscum, L.1    Finer-Moore, J.2    Stroud, R.M.3    Luskey, K.L.4    Brown, M.S.5    Goldstein, J.L.6
  • 122
    • 0031690373 scopus 로고    scopus 로고
    • Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae
    • Loayza D, Tam A, Schmidt WK, Michaelis S. 1998. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Mol. Biol. Cell 9:2767-84
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2767-2784
    • Loayza, D.1    Tam, A.2    Schmidt, W.K.3    Michaelis, S.4
  • 124
    • 0030064188 scopus 로고    scopus 로고
    • Effects of a novel 2,3-oxidosqualene cyclase inhibitor on the regulation of cholesterol biosynthesis in HepG2 cells
    • Mark M, Muller P, Maier R, Eisele B. 1996. Effects of a novel 2,3-oxidosqualene cyclase inhibitor on the regulation of cholesterol biosynthesis in HepG2 cells. J. Lipid Res. 37:148-58
    • (1996) J. Lipid Res. , vol.37 , pp. 148-158
    • Mark, M.1    Muller, P.2    Maier, R.3    Eisele, B.4
  • 125
    • 0035873619 scopus 로고    scopus 로고
    • SREBP cleavage-activating protein (SCAP) is required for increased lipid synthesis in liver induced by cholesterol deprivation and insulin elevation
    • Matsuda M, Korn BS, Hammer RE, Moon YA, Komuro R, et al. 2001. SREBP cleavage-activating protein (SCAP) is required for increased lipid synthesis in liver induced by cholesterol deprivation and insulin elevation. Genes Dev. 15:1206-16
    • (2001) Genes Dev. , vol.15 , pp. 1206-1216
    • Matsuda, M.1    Korn, B.S.2    Hammer, R.E.3    Moon, Y.A.4    Komuro, R.5
  • 126
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin and ATP
    • McCracken AA, Brodsky JL. 1996. Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin and ATP. J. Cell Biol. 132:291-98
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 127
    • 0029837381 scopus 로고    scopus 로고
    • Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis
    • McGee TP, Cheng HH, Kumagai H, Omura S, Simoni RD. 1996. Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J. Biol. Chem. 271:25630-38
    • (1996) J. Biol. Chem. , vol.271 , pp. 25630-25638
    • McGee, T.P.1    Cheng, H.H.2    Kumagai, H.3    Omura, S.4    Simoni, R.D.5
  • 128
    • 0029969302 scopus 로고    scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo
    • Meigs TE, Roseman DS, Simoni RD. 1996. Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo. J. Biol. Chem. 271:7916-22
    • (1996) J. Biol. Chem. , vol.271 , pp. 7916-7922
    • Meigs, T.E.1    Roseman, D.S.2    Simoni, R.D.3
  • 129
    • 0026681612 scopus 로고
    • Regulated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in permeabilized cells
    • Meigs TE, Simoni RD. 1992. Regulated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in permeabilized cells. J. Biol. Chem. 267:13547-52
    • (1992) J. Biol. Chem. , vol.267 , pp. 13547-13552
    • Meigs, T.E.1    Simoni, R.D.2
  • 130
    • 0031239831 scopus 로고    scopus 로고
    • Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and role of famesyl pyrophosphatase
    • Meigs TE, Simoni RD. 1997. Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and role of famesyl pyrophosphatase. Arch. Biochem. Biophys. 345:1-9
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 1-9
    • Meigs, T.E.1    Simoni, R.D.2
  • 131
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G. 2000. A complex of mammalian ufd1 and np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19:2181-92
    • (2000) EMBO J. , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 132
    • 0030615072 scopus 로고    scopus 로고
    • Ro 48-8.071, a new 2,3-oxidosqualene: Lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: Comparison to simvastatin
    • Morand OH, Aebi JD, Dehmlow H, Ji YH, Gains N, et al. 1997. Ro 48-8.071, a new 2,3-oxidosqualene: Lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: Comparison to simvastatin. J. Lipid. Res. 38:373-90
    • (1997) J. Lipid. Res. , vol.38 , pp. 373-390
    • Morand, O.H.1    Aebi, J.D.2    Dehmlow, H.3    Ji, Y.H.4    Gains, N.5
  • 133
    • 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 JL, Brown MS. 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. 263:8929-37
    • (1988) J. Biol. Chem. , vol.263 , pp. 8929-8937
    • Nakanishi, M.1    Goldstein, J.L.2    Brown, M.S.3
  • 134
    • 0024440611 scopus 로고
    • A protein with several possible membrane-spanning domains encoded by the Drosophila segment polarity gene patched
    • Nakano Y, Guerrero I, Hidalgo A, Taylor A, Whittle JR, Ingham PW. 1989. A protein with several possible membrane-spanning domains encoded by the Drosophila segment polarity gene patched. Nature 341:508-13
    • (1989) Nature , vol.341 , pp. 508-513
    • Nakano, Y.1    Guerrero, I.2    Hidalgo, A.3    Taylor, A.4    Whittle, J.R.5    Ingham, P.W.6
  • 135
    • 0033200131 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum: Lessons from hereditary myeloperoxidase deficiency
    • Nauseef WM. 1999. Quality control in the endoplasmic reticulum: Lessons from hereditary myeloperoxidase deficiency. J. Lab. Clin. Med. 134:215-21
    • (1999) J. Lab. Clin. Med. , vol.134 , pp. 215-221
    • Nauseef, W.M.1
  • 136
    • 0032573056 scopus 로고    scopus 로고
    • Sterols regulate processing of carbohydrate chains of wild-type SREBP cleavage-activating protein (SCAP), but not sterol-resistant mutants Y298C or D443N
    • Nohturfft A, Brown MS, Goldstein JL. 1998a. Sterols regulate processing of carbohydrate chains of wild-type SREBP cleavage-activating protein (SCAP), but not sterol-resistant mutants Y298C or D443N. Proc. Natl. Acad. Sci. USA 95:12848-53
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12848-12853
    • Nohturfft, A.1    Brown, M.S.2    Goldstein, J.L.3
  • 137
    • 0032479439 scopus 로고    scopus 로고
    • Topology of SREBP cleavage-activating protein, a polytopic membrane protein with a sterol-sensing domain
    • Nohturfft A, Brown MS, Goldstein JL. 1998b. Topology of SREBP cleavage-activating protein, a polytopic membrane protein with a sterol-sensing domain. J. Biol. Chem. 273:17243-50
    • (1998) J. Biol. Chem. , vol.273 , pp. 17243-17250
    • Nohturfft, A.1    Brown, M.S.2    Goldstein, J.L.3
  • 138
    • 0033613126 scopus 로고    scopus 로고
    • Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi
    • Nohturfft A, DeBose-Boyd RA, Scheek S, Goldstein JL, Brown MS. 1999. Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi. Proc. Natl. Acad. Sci. USA 96:11235-40
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11235-11240
    • Nohturfft, A.1    DeBose-Boyd, R.A.2    Scheek, S.3    Goldstein, J.L.4    Brown, M.S.5
  • 139
    • 0030472004 scopus 로고    scopus 로고
    • Recurrent G-to-A substitution in a single codon of SREBP cleavage-activating protein causes sterol resistance in three mutant Chinese hamster ovary cell lines
    • Nohturfft A, Hua X, Brown MS, Goldstein JL. 1996. Recurrent G-to-A substitution in a single codon of SREBP cleavage-activating protein causes sterol resistance in three mutant Chinese hamster ovary cell lines. Proc. Natl. Acad. Sci. USA 93:13709-14
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13709-13714
    • Nohturfft, A.1    Hua, X.2    Brown, M.S.3    Goldstein, J.L.4
  • 140
    • 0034604350 scopus 로고    scopus 로고
    • Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes
    • Nohturfft A, Yabe D, Goldstein JL, Brown MS, Espenshade PJ. 2000. Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes. Cell 102:315-23
    • (2000) Cell , vol.102 , pp. 315-323
    • Nohturfft, A.1    Yabe, D.2    Goldstein, J.L.3    Brown, M.S.4    Espenshade, P.J.5
  • 141
    • 0026673416 scopus 로고
    • The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Olender EH, Simon RD. 1992. The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267:4223-35
    • (1992) J. Biol. Chem. , vol.267 , pp. 4223-4235
    • Olender, E.H.1    Simon, R.D.2
  • 142
    • 0025739267 scopus 로고
    • Single nucleotide resolution of sterol regulatory region in promoter for 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Osborne TF. 1991. Single nucleotide resolution of sterol regulatory region in promoter for 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 266:13947-51
    • (1991) J. Biol. Chem. , vol.266 , pp. 13947-13951
    • Osborne, T.F.1
  • 143
    • 0034693259 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins (SREBPs): Key regulators of nutritional homeostasis and insulin action
    • Osborne TF. 2000. Sterol regulatory element-binding proteins (SREBPs): Key regulators of nutritional homeostasis and insulin action. J. Biol. Chem. 275:32379-82
    • (2000) J. Biol. Chem. , vol.275 , pp. 32379-32382
    • Osborne, T.F.1
  • 144
    • 0031899024 scopus 로고    scopus 로고
    • Related membrane domains in proteins of sterol sensing and cell signaling provide a glimpse of treasures still buried within the dynamic realm of intracellular metabolic regulation
    • Osborne TF, Rosenfeld JM. 1998. Related membrane domains in proteins of sterol sensing and cell signaling provide a glimpse of treasures still buried within the dynamic realm of intracellular metabolic regulation. Curr. Opin. Lipidol. 9:137-40
    • (1998) Curr. Opin. Lipidol. , vol.9 , pp. 137-140
    • Osborne, T.F.1    Rosenfeld, J.M.2
  • 145
    • 0032852311 scopus 로고    scopus 로고
    • The anaphase-promoting complex: New subunits and regulators
    • Page AM, Hieter P. 1999. The anaphase-promoting complex: New subunits and regulators. Annu. Rev. Biochem. 68:583-609
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 583-609
    • Page, A.M.1    Hieter, P.2
  • 146
    • 0026627805 scopus 로고
    • Post-transcriptional regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 24(S),25-oxidolanosterol
    • Panini SR, Delate TA, Sinensky M. 1992. Post-transcriptional regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 24(S),25-oxidolanosterol. J. Biol. Chem. 267:12647-54
    • (1992) J. Biol. Chem. , vol.267 , pp. 12647-12654
    • Panini, S.R.1    Delate, T.A.2    Sinensky, M.3
  • 147
    • 0024328138 scopus 로고
    • Sterol-independent regulation of 3-hydroxy-3-methylglutaryl-CoA reductase by mevalonate in Chinese hamster ovary cells. Magnitude and specificity
    • Panini SR, Schnitzer PR, Spencer TA, Sinensky M. 1989. Sterol-independent regulation of 3-hydroxy-3-methylglutaryl-CoA reductase by mevalonate in Chinese hamster ovary cells. Magnitude and specificity. J. Biol. Chem. 264:11044-52
    • (1989) J. Biol. Chem. , vol.264 , pp. 11044-11052
    • Panini, S.R.1    Schnitzer, P.R.2    Spencer, T.A.3    Sinensky, M.4
  • 148
    • 0031750617 scopus 로고    scopus 로고
    • Down-regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase mRNA levels and synthesis in Syrian hamster C100 cells by the oxidosqualene cyclase inhibitor [4′-(6-allyl-ethyl-amino-hexyloxy)-2′-fluorophenyl]-(4- bromophenyl)-methanone (Ro 48-8071): Comparison to simvastatin
    • Peffley DM, Gayen AK, Morand OH. 1998. Down-regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase mRNA levels and synthesis in Syrian hamster C100 cells by the oxidosqualene cyclase inhibitor [4′-(6-allyl-ethyl-amino-hexyloxy)-2′-fluorophenyl]-(4- bromophenyl)-methanone (Ro 48-8071): Comparison to simvastatin. Biochem. Pharmacol. 56:439-49
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 439-449
    • Peffley, D.M.1    Gayen, A.K.2    Morand, O.H.3
  • 149
    • 0031772952 scopus 로고    scopus 로고
    • SCF and APC: The Yin and Yang of cell cycle regulated proteolysis
    • Peters JM. 1998. SCF and APC: The Yin and Yang of cell cycle regulated proteolysis. Curt. Opin. Cell Biol. 10:759-68
    • (1998) Curt. Opin. Cell Biol. , vol.10 , pp. 759-768
    • Peters, J.M.1
  • 150
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon M, Schekman R, Romisch K. 1997. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16:4540-48
    • (1997) EMBO J. , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Romisch, K.3
  • 151
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper RK, Bohmler S, Bordallo J, Sommer T, Wolf DH. 1997. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388:891-95
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 152
    • 0033492290 scopus 로고    scopus 로고
    • Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation
    • Plemper RK, Bordallo J, Deak PM, Taxis C, Hitt R, Wolf DH. 1999a. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. J. Cell Sci. 112:4123-34
    • (1999) J. Cell Sci. , vol.112 , pp. 4123-4134
    • Plemper, R.K.1    Bordallo, J.2    Deak, P.M.3    Taxis, C.4    Hitt, R.5    Wolf, D.H.6
  • 153
    • 0033031194 scopus 로고    scopus 로고
    • Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species
    • Plemper RK, Deak PM, Otto RT, Wolf DH. 1999b. Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. FEBS Lett. 443:241-45
    • (1999) FEBS Lett. , vol.443 , pp. 241-245
    • Plemper, R.K.1    Deak, P.M.2    Otto, R.T.3    Wolf, D.H.4
  • 154
    • 0032484024 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome
    • Plemper RK, Egner R, Kuchler K, Wolf DH. 1998. Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome. J. Biol. Chem. 273:32848-56
    • (1998) J. Biol. Chem. , vol.273 , pp. 32848-32856
    • Plemper, R.K.1    Egner, R.2    Kuchler, K.3    Wolf, D.H.4
  • 155
    • 0033118448 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome
    • Plemper RK, Wolf DH. 1999. Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome. Mol. Biol. Rep. 26:125-30
    • (1999) Mol. Biol. Rep. , vol.26 , pp. 125-130
    • Plemper, R.K.1    Wolf, D.H.2
  • 156
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signaling proteins in animal development
    • Erratum. Science 274:1597
    • Porter JA, Young KE, Beachy PA. 1996. Cholesterol modification of hedgehog signaling proteins in animal development. Science 274:255-59. Erratum. Science 274:1597
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 157
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S. 2002. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22:626-34
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 158
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPLA), a ubiquitin-selective chaperone
    • Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S. 2001. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPLA), a ubiquitin-selective chaperone. Cell 107:667-77
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 159
    • 0032832568 scopus 로고    scopus 로고
    • Impaired regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation in lovastatin-resistant cells
    • Ravid T, Avner R, Polak-Charcon S, Faust JR, Roitelman J. 1999. Impaired regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation in lovastatin-resistant cells. J. Biol. Chem. 274:29341-51
    • (1999) J. Biol. Chem. , vol.274 , pp. 29341-29351
    • Ravid, T.1    Avner, R.2    Polak-Charcon, S.3    Faust, J.R.4    Roitelman, J.5
  • 160
    • 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, Roitelman J. 2000. The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 275:35840-47
    • (2000) J. Biol. Chem. , vol.275 , pp. 35840-35847
    • Ravid, T.1    Doolman, R.2    Avner, R.3    Harats, D.4    Roitelman, J.5
  • 161
    • 0032561323 scopus 로고    scopus 로고
    • Isolation of cholesterol-requiring mutant Chinese hamster ovary cells with defects in cleavage of sterol regulatory element-binding proteins at site 1
    • Rawson RB, Cheng D, Brown MS, Goldstein JL. 1998. Isolation of cholesterol-requiring mutant Chinese hamster ovary cells with defects in cleavage of sterol regulatory element-binding proteins at site 1. J. Biol. Chem. 273:28261-69
    • (1998) J. Biol. Chem. , vol.273 , pp. 28261-28269
    • Rawson, R.B.1    Cheng, D.2    Brown, M.S.3    Goldstein, J.L.4
  • 162
    • 0033215204 scopus 로고    scopus 로고
    • Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating protein
    • Rawson RB, DeBose-Boyd R, Goldstein JL, Brown MS. 1999. Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating protein. J. Biol. Chem. 274:28549-56
    • (1999) J. Biol. Chem. , vol.274 , pp. 28549-28556
    • Rawson, R.B.1    DeBose-Boyd, R.2    Goldstein, J.L.3    Brown, M.S.4
  • 163
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • Rawson RB, Zelenski NG, Nijhawan D, Ye J, Sakai J, et al. 1997. Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs. Mol. Cell 1:47-57
    • (1997) Mol. Cell , vol.1 , pp. 47-57
    • Rawson, R.B.1    Zelenski, N.G.2    Nijhawan, D.3    Ye, J.4    Sakai, J.5
  • 164
    • 0034284918 scopus 로고    scopus 로고
    • Regulation of absorption and ABC1-mediated efflux of cholesterol by RXR heterodimers
    • Repa JJ, Turley SD, Lobaccaro JA, Medina J, Li L, et al. 2000. Regulation of absorption and ABC1-mediated efflux of cholesterol by RXR heterodimers. Science 289:1524-29
    • (2000) Science , vol.289 , pp. 1524-1529
    • Repa, J.J.1    Turley, S.D.2    Lobaccaro, J.A.3    Medina, J.4    Li, L.5
  • 165
    • 0028902989 scopus 로고
    • Brefeldin A renders Chinese hamster ovary cells insensitive to transcriptional suppression by 25-hydroxycholesterol
    • Ridgway ND, Lagace TA. 1995. Brefeldin A renders Chinese hamster ovary cells insensitive to transcriptional suppression by 25-hydroxycholesterol. J. Biol. Chem. 270:8023-31
    • (1995) J. Biol. Chem. , vol.270 , pp. 8023-8031
    • Ridgway, N.D.1    Lagace, T.A.2
  • 166
    • 0033599080 scopus 로고    scopus 로고
    • Getting a handle on "good" cholesterol with the high-density lipoprotein receptor
    • Rigotti A, Krieger M. 1999. Getting a handle on "good" cholesterol with the high-density lipoprotein receptor. N. Engl. J. Med. 341:2011-13
    • (1999) N. Engl. J. Med. , vol.341 , pp. 2011-2013
    • Rigotti, A.1    Krieger, M.2
  • 167
    • 0026072178 scopus 로고
    • Involvement of calcium in the mevalonate-accelerated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Roitelman J, Bar-Nun S, Inoue S, Simoni RD. 1991. Involvement of calcium in the mevalonate-accelerated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 266:16085-91
    • (1991) J. Biol. Chem. , vol.266 , pp. 16085-16091
    • Roitelman, J.1    Bar-Nun, S.2    Inoue, S.3    Simoni, R.D.4
  • 168
    • 0026720521 scopus 로고
    • Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Implications for enzyme degradation in the endoplasmic reticulum
    • Roitelman J, Olender EH, Bar-Nun S, Dunn WA Jr, Simoni RD. 1992. Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Implications for enzyme degradation in the endoplasmic reticulum. J. Cell Biol. 117:959-73
    • (1992) J. Cell Biol. , vol.117 , pp. 959-973
    • Roitelman, J.1    Olender, E.H.2    Bar-Nun, S.3    Dunn W.A., Jr.4    Simoni, R.D.5
  • 169
    • 0026461126 scopus 로고
    • Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Roitelman J, Simoni RD. 1992. Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267:25264-73
    • (1992) J. Biol. Chem. , vol.267 , pp. 25264-25273
    • Roitelman, J.1    Simoni, R.D.2
  • 170
    • 0033593022 scopus 로고    scopus 로고
    • A family of membrane-embedded metallopro-teases involved in regulated proteolysis of membrane-associated transcription factors
    • Rudner DZ, Fawcett P, Losick R. 1999. A family of membrane-embedded metallopro-teases involved in regulated proteolysis of membrane-associated transcription factors. Proc. Natl. Acad. Sci. USA 96:14765-70
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14765-14770
    • Rudner, D.Z.1    Fawcett, P.2    Losick, R.3
  • 171
    • 0034672672 scopus 로고    scopus 로고
    • Oxysterol biosynthetic enzymes
    • Russell DW. 2000. Oxysterol biosynthetic enzymes. Biochim. Biophys. Acta 1529:126-35
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 126-135
    • Russell, D.W.1
  • 172
    • 0030604717 scopus 로고    scopus 로고
    • Sterolregulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment
    • Sakai J, Duncan EA, Rawson RB, Hua X, Brown MS, Goldstein JL. 1996. Sterolregulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell 85:1037-46
    • (1996) Cell , vol.85 , pp. 1037-1046
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3    Hua, X.4    Brown, M.S.5    Goldstein, J.L.6
  • 173
    • 0030854859 scopus 로고    scopus 로고
    • Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein
    • Sakai J, Nohturfft A, Cheng D, Ho YK, Brown MS, Goldstein JL. 1997. Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein. J. Biol. Chem. 272:20213-21
    • (1997) J. Biol. Chem. , vol.272 , pp. 20213-20221
    • Sakai, J.1    Nohturfft, A.2    Cheng, D.3    Ho, Y.K.4    Brown, M.S.5    Goldstein, J.L.6
  • 174
    • 0032489460 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies
    • Sakai J, Nohturfft A, Goldstein JL, Brown MS. 1998a. Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies. J. Biol. Chem. 273:5785-93
    • (1998) J. Biol. Chem. , vol.273 , pp. 5785-5793
    • Sakai, J.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 175
    • 0032185770 scopus 로고    scopus 로고
    • Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells
    • Sakai J, Rawson RB, Espenshade PJ, Cheng D, Seegmiller AC, et al. 1998b. Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol. Cell 2:505-14
    • (1998) Mol. Cell , vol.2 , pp. 505-514
    • Sakai, J.1    Rawson, R.B.2    Espenshade, P.J.3    Cheng, D.4    Seegmiller, A.C.5
  • 176
    • 0028360111 scopus 로고
    • Assignment of the membrane attachment, DNA binding, and transcriptional activation domains of sterol regulatory element-binding protein-1 (SREBP-1)
    • Sato R, Yang J, Wang X, Evans MJ, Ho YK, et al. 1994. Assignment of the membrane attachment, DNA binding, and transcriptional activation domains of sterol regulatory element-binding protein-1 (SREBP-1). J. Biol. Chem. 269:17267-73
    • (1994) J. Biol. Chem. , vol.269 , pp. 17267-17273
    • Sato, R.1    Yang, J.2    Wang, X.3    Evans, M.J.4    Ho, Y.K.5
  • 177
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • Sato S, Ward CL, Krouse ME, Wine JJ, Kopito RR. 1996, Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271:635-38
    • (1996) J. Biol. Chem. , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 179
    • 13044279492 scopus 로고    scopus 로고
    • Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization
    • Seidah NG, Mowla SJ, Hamelin J, Mamarbachi AM, Benjannet S, et al. 1999. Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization. Proc. Natl. Acad. Sci. USA 96:1321-26
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1321-1326
    • Seidah, N.G.1    Mowla, S.J.2    Hamelin, J.3    Mamarbachi, A.M.4    Benjannet, S.5
  • 180
    • 0030512257 scopus 로고    scopus 로고
    • Isoprene synthesis by plants and animals
    • Sharkey TD. 1996. Isoprene synthesis by plants and animals. Endeavour 20:74-78
    • (1996) Endeavour , vol.20 , pp. 74-78
    • Sharkey, T.D.1
  • 181
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: The superfamily of subtilisin-like serine proteases
    • Siezen RJ, Leunissen JA. 1997. Subtilases: The superfamily of subtilisin-like serine proteases. Protein Sci. 6:501-23
    • (1997) Protein Sci. , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.2
  • 182
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons K, Ikonen E. 2000. How cells handle cholesterol. Science 290:1721-26
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 183
    • 0019888626 scopus 로고
    • Radioimmune precipitation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from Chinese hamster fibroblasts. Effect of 25-hydroxycholesterol
    • Sinensky M, Torget R, Edwards PA. 1981. Radioimmune precipitation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from Chinese hamster fibroblasts. Effect of 25-hydroxycholesterol. J. Biol. Chem. 256:11774-79
    • (1981) J. Biol. Chem. , vol.256 , pp. 11774-11779
    • Sinensky, M.1    Torget, R.2    Edwards, P.A.3
  • 184
    • 0019920504 scopus 로고
    • Analysis of regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in a somatic cell mutant auxotrophic for mevalonate
    • Sinensky M, Torget R, Schnitzer-Polokoff R, Edwards PA. 1982. Analysis of regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in a somatic cell mutant auxotrophic for mevalonate. J. Biol. Chem. 257:7284-86
    • (1982) J. Biol. Chem. , vol.257 , pp. 7284-7286
    • Sinensky, M.1    Torget, R.2    Schnitzer-Polokoff, R.3    Edwards, P.A.4
  • 185
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • Sommer T, Wolf DH. 1997. Endoplasmic reticulum degradation: Reverse protein flow of no return. FASEB J. 11:1227-33
    • (1997) FASEB J. , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 186
    • 0025720479 scopus 로고
    • A permeabilized cell system identifies the endoplasmic reticulnm as a site of protein degradation
    • Stafford FJ, Bonifacino JS. 1991. A permeabilized cell system identifies the endoplasmic reticulnm as a site of protein degradation. J. Cell Biol. 115:1225-36
    • (1991) J. Cell Biol. , vol.115 , pp. 1225-1236
    • Stafford, F.J.1    Bonifacino, J.S.2
  • 187
    • 0023666142 scopus 로고
    • 42 bp element from LDL receptor gene confers end-product repression by sterols when inserted into viral TK promoter
    • Südhof TC, Russell DW, Brown MS, Goldstein JL. 1987. 42 bp element from LDL receptor gene confers end-product repression by sterols when inserted into viral TK promoter. Cell 48:1061-69
    • (1987) Cell , vol.48 , pp. 1061-1069
    • Südhof, T.C.1    Russell, D.W.2    Brown, M.S.3    Goldstein, J.L.4
  • 188
    • 0033011212 scopus 로고    scopus 로고
    • P-type ATPase spf1 mutants show a novel resistance mechanism for the killer toxin SMKT Mol
    • Suzuki C, Shimma YI, 1999. P-type ATPase spf1 mutants show a novel resistance mechanism for the killer toxin SMKT Mol. Microbiol. 32:813-23
    • (1999) Microbiol. , vol.32 , pp. 813-823
    • Suzuki, C.1    Shimma, Y.I.2
  • 189
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson R, Locher M, Hochstrasser M. 2001. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev. 15:2660-74
    • (2001) Genes Dev. , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 190
    • 0031105921 scopus 로고    scopus 로고
    • The 26S proteasome: Subunits and functions
    • Tanaka K, Tsurumi C, 1997, The 26S proteasome: Subunits and functions. Mol. Biol. Rep. 24:3-11
    • (1997) Mol. Biol. Rep. , vol.24 , pp. 3-11
    • Tanaka, K.1    Tsurumi, C.2
  • 191
    • 0035661566 scopus 로고    scopus 로고
    • APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex
    • Tang Z, Li B, Bharadwaj R, Zhu H, Ozkan E, et al. 2001. APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Mol. Biol. Cell 12:3839-51
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3839-3851
    • Tang, Z.1    Li, B.2    Bharadwaj, R.3    Zhu, H.4    Ozkan, E.5
  • 193
    • 0027648820 scopus 로고
    • ADD1: A novel helix-loophelix transcription factor associated with adipocyte determination and differentiation
    • Tontonoz P, Kim JB, Graves RA, Spiegelman BM. 1993. ADD1: A novel helix-loophelix transcription factor associated with adipocyte determination and differentiation. Mol. Cell. Biol. 13:4753-59
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4753-4759
    • Tontonoz, P.1    Kim, J.B.2    Graves, R.A.3    Spiegelman, B.M.4
  • 194
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-58
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 195
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier M, Staszewski LM, Bohmann D. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78:787-98
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 197
    • 0034810736 scopus 로고    scopus 로고
    • Upc2p and Ecm22p, dual regulators of sterol biosynthesis in Saccharomyces cerevisiae
    • Vik A, Rine J. 2001. Upc2p and Ecm22p, dual regulators of sterol biosynthesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 21:6395-405
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6395-6405
    • Vik, A.1    Rine, J.2
  • 198
    • 0027167918 scopus 로고
    • Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization
    • Wang X, Briggs MR, Hua X, Yokoyama C, Goldstein JL, Brown MS. 1993. Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization. J. Biol. Chem. 268:14497-504
    • (1993) J. Biol. Chem. , vol.268 , pp. 14497-14504
    • Wang, X.1    Briggs, M.R.2    Hua, X.3    Yokoyama, C.4    Goldstein, J.L.5    Brown, M.S.6
  • 199
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • Wang X, Sato R, Brown MS, Hua X, Goldstein JL. 1994. SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis. Cell 77:53-62
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 200
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward CL, Kopito RR. 1994. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem. 269:25710-18
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 201
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward CL, Omura S, Kopito RR. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121-27
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 202
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • Welch WJ, Brown CR. 1996. Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperones 1:109-15
    • (1996) Cell Stress Chaperones , vol.1 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 203
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
    • Werner ED, Brodsky JL, McCracken AA. 1996. Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 93:13797-801
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 204
    • 0035489304 scopus 로고    scopus 로고
    • The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic
    • Whyte JR, Munro S. 2001. The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev. Cell 1:527-37
    • (2001) Dev. Cell , vol.1 , pp. 527-537
    • Whyte, J.R.1    Munro, S.2
  • 205
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz EJHJ, Jones TR, Sun L, Bogyo M, Geuze HJ, Ploegh HL. 1996. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84:769-79
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 206
    • 0034108089 scopus 로고    scopus 로고
    • HRD gene dependence of endoplasmic reticulum-associated degradation
    • Wilhovsky S, Gardner R, Hampton R. 2000. HRD gene dependence of endoplasmic reticulum-associated degradation. Mol. Biol. Cell 11:1697-708
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1697-1708
    • Wilhovsky, S.1    Gardner, R.2    Hampton, R.3
  • 207
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye J, Rawson RB, Komuro R, Chen X, Dave UP, et al. 2000. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6:1355-64
    • (2000) Mol. Cell , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5
  • 208
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414:652-56
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 209
    • 0027490174 scopus 로고
    • SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene
    • Yokoyama C, Wang X, Briggs MR, Admon A, Wu J, et al. 1993. SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene. Cell 75:187-97
    • (1993) Cell , vol.75 , pp. 187-197
    • Yokoyama, C.1    Wang, X.2    Briggs, M.R.3    Admon, A.4    Wu, J.5
  • 210
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu H, Kaung G, Kobayashi S, Kopito RR. 1997. Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J. Biol. Chem. 272:20800-4
    • (1997) J. Biol. Chem. , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 211
    • 0033618342 scopus 로고    scopus 로고
    • Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins
    • Zelenski NG, Rawson RB, Brown MS, Goldstein JL. 1999. Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins. J. Biol. Chem. 274:21973-80
    • (1999) J. Biol. Chem. , vol.274 , pp. 21973-21980
    • Zelenski, N.G.1    Rawson, R.B.2    Brown, M.S.3    Goldstein, J.L.4
  • 212
    • 0033382189 scopus 로고    scopus 로고
    • The engagement of Sec61p in the ER dislocation process
    • Zhou M, Schekman R. 1999. The engagement of Sec61p in the ER dislocation process. Mol. Cell 4:925-34
    • (1999) Mol. Cell , vol.4 , pp. 925-934
    • Zhou, M.1    Schekman, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.