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Volumn 8, Issue 13, 1998, Pages 729-739

The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; MAMMALIA;

EID: 0032543562     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(98)70296-9     Document Type: Article
Times cited : (210)

References (57)
  • 1
    • 0030602819 scopus 로고    scopus 로고
    • αLβ2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
    • Kolanus W, Nagel W, Schiller B, Zeitlmann L, Godar S, Stockinger H, et al.: αLβ2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell 1996, 86:233-242.
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1    Nagel, W.2    Schiller, B.3    Zeitlmann, L.4    Godar, S.5    Stockinger, H.6
  • 2
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund JK, Guilherme A, Holik JJ, Virbasius JV, Chawla A, Czech MP: Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 1997, 275:1927-1930.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 3
    • 0031976015 scopus 로고    scopus 로고
    • Localization of proteins to the Golgi apparatus
    • Munro S: Localization of proteins to the Golgi apparatus. Trends Cell Biol 1998, 8:11-15.
    • (1998) Trends Cell Biol , vol.8 , pp. 11-15
    • Munro, S.1
  • 4
    • 0021747172 scopus 로고
    • Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
    • Taylor FR, Saucier SE, Shown EP, Parish EJ, Kandutsch AA: Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase. J Biol Chem 1984, 259:2382-2387.
    • (1984) J Biol Chem , vol.259 , pp. 2382-2387
    • Taylor, F.R.1    Saucier, S.E.2    Shown, E.P.3    Parish, E.J.4    Kandutsch, A.A.5
  • 5
    • 0024422669 scopus 로고
    • cDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper
    • Dawson PA, Ridgway ND, Slaughter CA, Brown MS, Goldstein JL: cDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper. J Biol Chem 1989, 264:16798-16803.
    • (1989) J Biol Chem , vol.264 , pp. 16798-16803
    • Dawson, P.A.1    Ridgway, N.D.2    Slaughter, C.A.3    Brown, M.S.4    Goldstein, J.L.5
  • 6
    • 0029945036 scopus 로고    scopus 로고
    • Review of progress in sterol oxidations - 1987-1995
    • Smith LL: Review of progress in sterol oxidations - 1987-1995. Lipids 1996, 31:453-487.
    • (1996) Lipids , vol.31 , pp. 453-487
    • Smith, L.L.1
  • 7
    • 0028566165 scopus 로고
    • In vivo formation of 25-hydroxycholesterol from endogenous cholesterol after a single meal, dietary-cholesterol challenge
    • Johnson KA, Morrow CJ, Knight GD, Scallen TJ: In vivo formation of 25-hydroxycholesterol from endogenous cholesterol after a single meal, dietary-cholesterol challenge. J Lipid Res 1994, 35:2241-2253.
    • (1994) J Lipid Res , vol.35 , pp. 2241-2253
    • Johnson, K.A.1    Morrow, C.J.2    Knight, G.D.3    Scallen, T.J.4
  • 8
    • 0029055367 scopus 로고
    • Low-density-lipoprotein (LDL) cholesterol is converted to 27-hydroxycholesterol in human fibroblasts: Evidence that 27-hydroxycholesterol can be an important intracellular mediator between LDL and the suppression of cholesterol production
    • Axelson M, Larsson O: Low-density-lipoprotein (LDL) cholesterol is converted to 27-hydroxycholesterol in human fibroblasts: evidence that 27-hydroxycholesterol can be an important intracellular mediator between LDL and the suppression of cholesterol production. J Biol Chem 1995, 270:15102-15110.
    • (1995) J Biol Chem , vol.270 , pp. 15102-15110
    • Axelson, M.1    Larsson, O.2
  • 9
    • 0026564767 scopus 로고
    • Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding
    • Ridgway N, Dawson P, Ho Y, Brown M, Goldstein J: Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding. J Cell Biol 1992, 116:307-319.
    • (1992) J Cell Biol , vol.116 , pp. 307-319
    • Ridgway, N.1    Dawson, P.2    Ho, Y.3    Brown, M.4    Goldstein, J.5
  • 10
    • 0030882949 scopus 로고    scopus 로고
    • Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain
    • Lagace TA, Byers DM, Cook HW, Ridgway ND: Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain. Biochem J 1997, 326:205-213.
    • (1997) Biochem J , vol.326 , pp. 205-213
    • Lagace, T.A.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 11
    • 0028902989 scopus 로고
    • Brefeldin-A renders Chinese-hamster ovary cells insensitive to transcriptional suppression by 25-hydroxycholesterol
    • Ridgway ND, Lagace TA: Brefeldin-A renders Chinese-hamster ovary cells insensitive to transcriptional suppression by 25-hydroxycholesterol. J Biol Chem 1995, 270:8023-8031.
    • (1995) J Biol Chem , vol.270 , pp. 8023-8031
    • Ridgway, N.D.1    Lagace, T.A.2
  • 12
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T, Simons K: Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr Opin Cell Biol 1997, 9:534-542.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 13
    • 0028979940 scopus 로고
    • 25-Hydroxycholesterol stimulates sphingomyelin synthesis in Chinese hamster ovary cells
    • Ridgway ND: 25-Hydroxycholesterol stimulates sphingomyelin synthesis in Chinese hamster ovary cells. J Lipid Res 1995, 36:1345-1358.
    • (1995) J Lipid Res , vol.36 , pp. 1345-1358
    • Ridgway, N.D.1
  • 14
    • 0030298339 scopus 로고    scopus 로고
    • Sterol resistance in CHO cells traced to point mutation in SREBP cleavage activating protein
    • Hua XX, 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.X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 15
    • 0027183541 scopus 로고
    • The PH domain: A common piece in the structural patchwork of signaling proteins
    • Musacchio A, Gibson T, Rice P, Thompson J, Saraste M: The PH domain: a common piece in the structural patchwork of signaling proteins. Trends Biochem Sci 1993, 18:343-348.
    • (1993) Trends Biochem Sci , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Rice, P.3    Thompson, J.4    Saraste, M.5
  • 16
    • 0029157058 scopus 로고
    • Pleckstrin homology domains - A fact file
    • Saraste M, Hyvonen M: Pleckstrin homology domains - a fact file. Curr Opin Struct Biol 1995, 5:403-408.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 403-408
    • Saraste, M.1    Hyvonen, M.2
  • 17
    • 0030040967 scopus 로고    scopus 로고
    • The pleckstrin homology domain - An intriguing multifunctional protein module
    • Shaw G: The pleckstrin homology domain - an intriguing multifunctional protein module. Bioessays 1996, 18:35-46.
    • (1996) Bioessays , vol.18 , pp. 35-46
    • Shaw, G.1
  • 18
    • 0029844904 scopus 로고    scopus 로고
    • A human exchange factor for ARF contains Sec7-homology and pleckstrin-homology domains
    • Chardin P, Paris S, Antonny B, Robineau S, Berauddufour S, Jackson CL, et al.: A human exchange factor for ARF contains Sec7-homology and pleckstrin-homology domains. Nature 1996, 384:481-484.
    • (1996) Nature , vol.384 , pp. 481-484
    • Chardin, P.1    Paris, S.2    Antonny, B.3    Robineau, S.4    Berauddufour, S.5    Jackson, C.L.6
  • 19
    • 0027274897 scopus 로고
    • A 102 kda subunit of a Golgi-associated particle has homology to beta-subunits of trimeric G-proteins
    • Harrison-Lavoie KJ, Lewis VA, Hynes GM, Collison KS, Nutland E, Willison KR: A 102 kda subunit of a Golgi-associated particle has homology to beta-subunits of trimeric G-proteins. EMBO J 1993, 12:2847-2853.
    • (1993) EMBO J , vol.12 , pp. 2847-2853
    • Harrison-Lavoie, K.J.1    Lewis, V.A.2    Hynes, G.M.3    Collison, K.S.4    Nutland, E.5    Willison, K.R.6
  • 20
    • 0030889062 scopus 로고    scopus 로고
    • Distinct compartmentalization of TGN46 and β1,4-galactosyltransferase in HeLa cells
    • Prescott AR, Lucocq JM, James J, Lister JM, Ponnambalam S: Distinct compartmentalization of TGN46 and β1,4-galactosyltransferase in HeLa cells. Eur J Cell Biol 1997, 72:238-246.
    • (1997) Eur J Cell Biol , vol.72 , pp. 238-246
    • Prescott, A.R.1    Lucocq, J.M.2    James, J.3    Lister, J.M.4    Ponnambalam, S.5
  • 22
    • 0029892506 scopus 로고    scopus 로고
    • Cloning, expression, and localization of 230-kDa phosphatidylinositol 4-kinase
    • Nakagawa T, Goto K, Kondo H: Cloning, expression, and localization of 230-kDa phosphatidylinositol 4-kinase. J Biol Chem 1996, 271:12088-12094.
    • (1996) J Biol Chem , vol.271 , pp. 12088-12094
    • Nakagawa, T.1    Goto, K.2    Kondo, H.3
  • 23
    • 0028213802 scopus 로고
    • A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein
    • Jiang B, Brown JL, Sheraton J, Fortin N, Bussey H: A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein. Yeast 1994, 10:341-353.
    • (1994) Yeast , vol.10 , pp. 341-353
    • Jiang, B.1    Brown, J.L.2    Sheraton, J.3    Fortin, N.4    Bussey, H.5
  • 24
    • 0028048619 scopus 로고
    • SWH1 from yeast encodes a candidate nuclear factor-containing ankyrin repeats and showing homology to mammalian oxysterol-binding protein
    • Schmalix WA, Bandlow W: SWH1 from yeast encodes a candidate nuclear factor-containing ankyrin repeats and showing homology to mammalian oxysterol-binding protein. Biochim Biophys Acta 1994, 1219:205-210.
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 205-210
    • Schmalix, W.A.1    Bandlow, W.2
  • 25
    • 0025674154 scopus 로고
    • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
    • Donaldson JG, Lippincott-Schwartz J, Bloom GS, Kreis TE, Klausner RD: Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J Cell Biol 1990, 111:2295-2306.
    • (1990) J Cell Biol , vol.111 , pp. 2295-2306
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Bloom, G.S.3    Kreis, T.E.4    Klausner, R.D.5
  • 27
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Fesik SW: Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 1994, 371:168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 29
    • 0029924329 scopus 로고    scopus 로고
    • Crystal-structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen LO, Perisic O, Cheung R, Katan M, Williams RL: Crystal-structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 1996, 380:595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 30
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
    • Rameh LE, Tolias KF, Duckworth BC, Cantley LC: A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 1997, 390:192-196.
    • (1997) Nature , vol.390 , pp. 192-196
    • Rameh, L.E.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 31
    • 10544219605 scopus 로고    scopus 로고
    • Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Brutons tyrosine kinase
    • Salim K, Bottomley MJ, Querfurth E, Zvelebil MJ, Gout I, Scaife R, et al.: Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Brutons tyrosine kinase. EMBO J 1996, 15:6241-6250.
    • (1996) EMBO J , vol.15 , pp. 6241-6250
    • Salim, K.1    Bottomley, M.J.2    Querfurth, E.3    Zvelebil, M.J.4    Gout, I.5    Scaife, R.6
  • 32
    • 0031002348 scopus 로고    scopus 로고
    • The role of the PH domain in the signal-dependent membrane targeting of Sos
    • Chen RH, CorbalanGarcia S, BarSagi D: The role of the PH domain in the signal-dependent membrane targeting of Sos. EMBO J 1997, 16:1351-1359.
    • (1997) EMBO J , vol.16 , pp. 1351-1359
    • Chen, R.H.1    CorbalanGarcia, S.2    BarSagi, D.3
  • 34
    • 0030782261 scopus 로고    scopus 로고
    • Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex
    • Cluett EB, Kuismanen E, Machamer CE: Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex. Mol Biol Cell 1997, 8:2233-2240.
    • (1997) Mol Biol Cell , vol.8 , pp. 2233-2240
    • Cluett, E.B.1    Kuismanen, E.2    Machamer, C.E.3
  • 35
    • 0027389279 scopus 로고
    • Comparison of the levels of inositol metabolites in transformed hematopoietic-cells and their normal counterparts
    • Bunce CM, French PJ, Allen P, Mountford JC, Moor B, Greaves MF, et al.: Comparison of the levels of inositol metabolites in transformed hematopoietic-cells and their normal counterparts. Biochem J 1993, 289:667-673.
    • (1993) Biochem J , vol.289 , pp. 667-673
    • Bunce, C.M.1    French, P.J.2    Allen, P.3    Mountford, J.C.4    Moor, B.5    Greaves, M.F.6
  • 36
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C δ1 binds with high affinity to phosphatidylinositol 4,5- Bisphosphate in bilayer membranes
    • Garcia P, Gupta R, Shah S, Morris AJ, Rudge SA, Scarlata S, et al.: The pleckstrin homology domain of phospholipase C δ1 binds with high affinity to phosphatidylinositol 4,5- bisphosphate in bilayer membranes. Biochemistry 1995, 34:16228-16234.
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6
  • 37
    • 15144349594 scopus 로고    scopus 로고
    • High affinity binding of the pleckstrin homology domain of mSos1 to phosphatidylinositol (4,5)-bisphosphate
    • Kubiseski TJ, Chook YM, Parris WE, Rozakis-Adcock M, Pawson T: High affinity binding of the pleckstrin homology domain of mSos1 to phosphatidylinositol (4,5)-bisphosphate. J Biol Chem 1997, 272:1799-1804.
    • (1997) J Biol Chem , vol.272 , pp. 1799-1804
    • Kubiseski, T.J.1    Chook, Y.M.2    Parris, W.E.3    Rozakis-Adcock, M.4    Pawson, T.5
  • 38
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon MA, Ferguson KM, O'Brien R, Sigler PB, Schlessinger J: Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc Natl Acad Sci USA 1995, 92:10472-10476.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 39
    • 0031006326 scopus 로고    scopus 로고
    • Regulatory recruitment of signalling molecules to the cell membrane by pleckstrin-homology domains
    • Lemmon MA, Falasca M, Ferguson KM, Schlessinger J: Regulatory recruitment of signalling molecules to the cell membrane by pleckstrin-homology domains. Trends Cell Biol 1997, 7:237-242.
    • (1997) Trends Cell Biol , vol.7 , pp. 237-242
    • Lemmon, M.A.1    Falasca, M.2    Ferguson, K.M.3    Schlessinger, J.4
  • 40
    • 0029416974 scopus 로고
    • Phospholipase C δ 1 requires a pleckstrin homology domain for interaction with the plasma membrane
    • Paterson HF, Savopoulos JW, Perisic O, Cheung R, Ellis MV, Williams RL, et al.: Phospholipase C δ 1 requires a pleckstrin homology domain for interaction with the plasma membrane. Biochem J 1995, 312:661-666.
    • (1995) Biochem J , vol.312 , pp. 661-666
    • Paterson, H.F.1    Savopoulos, J.W.2    Perisic, O.3    Cheung, R.4    Ellis, M.V.5    Williams, R.L.6
  • 41
    • 0030820924 scopus 로고    scopus 로고
    • A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
    • Rameh LE, Arvidsson AK, Carraway KL, Couvillon AD, Rathbun G, Crompton A, et al.: A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J Biol Chem 1997, 272:22059-22066.
    • (1997) J Biol Chem , vol.272 , pp. 22059-22066
    • Rameh, L.E.1    Arvidsson, A.K.2    Carraway, K.L.3    Couvillon, A.D.4    Rathbun, G.5    Crompton, A.6
  • 42
    • 0030884527 scopus 로고    scopus 로고
    • Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin
    • Domin J, Pages F, Volinia S, Rittenhouse SE, Zvelebil MJ, Stein RC, et al.: Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin. Biochem J 1997, 326:139-147.
    • (1997) Biochem J , vol.326 , pp. 139-147
    • Domin, J.1    Pages, F.2    Volinia, S.3    Rittenhouse, S.E.4    Zvelebil, M.J.5    Stein, R.C.6
  • 43
    • 0030783603 scopus 로고    scopus 로고
    • Heterologous pleckstrin homology domains do not couple IRS-1 to the insulin receptor
    • Burks DJ, Pons S, Towery H, Smith-Hall J, Myers M, Yenush L, et al.: Heterologous pleckstrin homology domains do not couple IRS-1 to the insulin receptor. J Biol Chem 1997, 272:27716-27721.
    • (1997) J Biol Chem , vol.272 , pp. 27716-27721
    • Burks, D.J.1    Pons, S.2    Towery, H.3    Smith-Hall, J.4    Myers, M.5    Yenush, L.6
  • 45
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic-receptor kinase requires coordinate interaction with G(βγ) subunits and lipid
    • Pitcher JA, Touhara K, Payne ES, Lefkowitz RJ: Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic-receptor kinase requires coordinate interaction with G(βγ) subunits and lipid. J Biol Chem 1995, 270:11707-11710.
    • (1995) J Biol Chem , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 47
    • 0345012707 scopus 로고
    • Structural relationships between clthrin assembly proteins from the Golgi and the plasma-membrane
    • Ahle S, Mann A, Eichelsbacher U, Ungewickell E: Structural relationships between clthrin assembly proteins from the Golgi and the plasma-membrane. EMBO J 1988, 7:919-929.
    • (1988) EMBO J , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, U.3    Ungewickell, E.4
  • 48
    • 0026752711 scopus 로고
    • Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic-reticulum
    • Napier RM, Fowke LC, Hawes C, Lewis M, Pelham HRB: Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic-reticulum. J Cell Sci 1992, 102:261-271.
    • (1992) J Cell Sci , vol.102 , pp. 261-271
    • Napier, R.M.1    Fowke, L.C.2    Hawes, C.3    Lewis, M.4    Pelham, H.R.B.5
  • 49
    • 0028032480 scopus 로고
    • Cloning and characterization of a human phosphatidylinositol 4-kinase
    • Wong K, Cantley LC: Cloning and characterization of a human phosphatidylinositol 4-kinase. J Biol Chem 1994, 269:28878-28884.
    • (1994) J Biol Chem , vol.269 , pp. 28878-28884
    • Wong, K.1    Cantley, L.C.2
  • 50
    • 0029617615 scopus 로고
    • Structure of the high-affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB: Structure of the high-affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 1995, 83:1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 51
    • 0027979837 scopus 로고
    • A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae
    • Yoshida S, Goebl M, Ohya Y, Nakano A, Anraku Y: A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae. J Biol Chem 1994, 269:1166-1172.
    • (1994) J Biol Chem , vol.269 , pp. 1166-1172
    • Yoshida, S.1    Goebl, M.2    Ohya, Y.3    Nakano, A.4    Anraku, Y.5
  • 52
    • 0030452512 scopus 로고    scopus 로고
    • Mutations that suppress the thermosensitivity of green fluorescent protein
    • Siemering KR, Golbik R, Sever R, Haseloff J: Mutations that suppress the thermosensitivity of green fluorescent protein. Curr Biol 1996, 6:1653-1663.
    • (1996) Curr Biol , vol.6 , pp. 1653-1663
    • Siemering, K.R.1    Golbik, R.2    Sever, R.3    Haseloff, J.4
  • 53
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S, Pelham HRB: A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987, 48:899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 54
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro S: An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J 1995, 14:4695-4704.
    • (1995) EMBO J , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 55
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille C, Hui N, Hunte F, Kieckbusch R, Berger EG, Warren G: Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J Cell Sci 1995, 108:1617-1627.
    • (1995) J Cell Sci , vol.108 , pp. 1617-1627
    • Rabouille, C.1    Hui, N.2    Hunte, F.3    Kieckbusch, R.4    Berger, E.G.5    Warren, G.6
  • 56
    • 0000708640 scopus 로고
    • Purification of rat liver Golgi stacks
    • Edited by Celis JE. Orlando, Florida: Academic Press
    • Slusarewicz P, Hui N, Warren G: Purification of rat liver Golgi stacks In Cell Biology: a Laboratory Handbook Vol. 1. Edited by Celis JE. Orlando, Florida: Academic Press; 1994:509-516.
    • (1994) Cell Biology: A Laboratory Handbook Vol. 1 , vol.1 , pp. 509-516
    • Slusarewicz, P.1    Hui, N.2    Warren, G.3
  • 57
    • 0030054722 scopus 로고    scopus 로고
    • Binding of the vesicle docking protein p115 to Golgi membranes is inhibited under mitotic conditions
    • Levine TP, Rabouille C, Kieckbusch RH, Warren G: Binding of the vesicle docking protein p115 to Golgi membranes is inhibited under mitotic conditions. J Biol Chem 1996, 271:17304-17311.
    • (1996) J Biol Chem , vol.271 , pp. 17304-17311
    • Levine, T.P.1    Rabouille, C.2    Kieckbusch, R.H.3    Warren, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.