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Volumn 9, Issue 2, 1998, Pages 137-140

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

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL SURFACE RECEPTOR; CHOLESTEROL; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MEMBRANE PROTEIN; REGULATOR PROTEIN; STEROL;

EID: 0031899024     PISSN: 09579672     EISSN: None     Source Type: Journal    
DOI: 10.1097/00041433-199804000-00010     Document Type: Short Survey
Times cited : (40)

References (15)
  • 1
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS, Goldstein JL. A receptor-mediated pathway for cholesterol homeostasis. Science 1986; 232:34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 2
    • 0021141736 scopus 로고
    • Nucleotide sequence of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum
    • Chin DJ, Gil G, Russell DW, Liscum L, Luskey KL, Basu SK, et al. Nucleotide sequence of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. Nature 1984; 308:613-617.
    • (1984) Nature , vol.308 , pp. 613-617
    • Chin, D.J.1    Gil, G.2    Russell, D.W.3    Liscum, L.4    Luskey, K.L.5    Basu, S.K.6
  • 3
    • 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. Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell 1985; 41:249-258.
    • (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
  • 4
    • 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, Dun WAJ, Simoni RD. 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 Biol Chem 1992; 117:959-973.
    • (1992) J Biol Chem , vol.117 , pp. 959-973
    • Roitelman, J.1    Olender, E.H.2    Bar-Nun, S.3    Dun, W.A.J.4    Simoni, R.D.5
  • 5
    • 0029045589 scopus 로고
    • Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Kumagi H, Chun KT, Simoni RD. Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem 1995; 270:19107-19113.
    • (1995) J Biol Chem , vol.270 , pp. 19107-19113
    • Kumagi, H.1    Chun, K.T.2    Simoni, R.D.3
  • 6
    • 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. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell 1996; 87:415-426.
    • (1996) Cell , vol.87 , pp. 415-426
    • Hua, X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 8
    • 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. 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 1996; 93:13709-13714.
    • (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
  • 9
    • 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, Nohturtf A, Cheng D, Ho YK, B MS, Goldstein JL. Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein. J Biol Chem 1997; 272:20213-20221.
    • (1997) J Biol Chem , vol.272 , pp. 20213-20221
    • Sakai, J.1    Nohturtf, A.2    Cheng, D.3    Ho, Y.K.4    B., M.S.5    Goldstein, J.L.6
  • 10
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown MS, Goldstein JL. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 1997; 89:331-340.
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 11
    • 0031106071 scopus 로고    scopus 로고
    • Cholesterol homeostasis: Clipping out a slippery regulator
    • Osborne TF. Cholesterol homeostasis: Clipping out a slippery regulator. Curr Biol 1997: 7 (Suppl):R172-R174.
    • (1997) Curr Biol , vol.7 , Issue.SUPPL.
    • Osborne, T.F.1
  • 12
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signaling proteins in animal development
    • Porter JA, Young KE, Beachy PA. Cholesterol modification of hedgehog signaling proteins in animal development. Science 1996; 274:255-259.
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 13
  • 14
    • 0011102935 scopus 로고    scopus 로고
    • The tumour-suppressor gene patched encodes a candidate receptor for sonic hedgehog
    • Stone DM, Hynes M, Armanini M, Swanson TA, Gu Q, Johnson RL. et al. The tumour-suppressor gene patched encodes a candidate receptor for sonic hedgehog. Nature 1996; 384:129-134.
    • (1996) Nature , vol.384 , pp. 129-134
    • Stone, D.M.1    Hynes, M.2    Armanini, M.3    Swanson, T.A.4    Gu, Q.5    Johnson, R.L.6
  • 15
    • 15844386540 scopus 로고    scopus 로고
    • Hedgehog patterning activity: Role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain
    • Porter JA, Ekker SC, Park W-J, von Kessler DP, Young KE, Chen CH, et al. Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain. Cell 1996; 86:21-34.
    • (1996) Cell , vol.86 , pp. 21-34
    • Porter, J.A.1    Ekker, S.C.2    Park, W.-J.3    Von Kessler, D.P.4    Young, K.E.5    Chen, C.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.