메뉴 건너뛰기




Volumn 146, Issue 10, 2005, Pages 4234-4249

Cholesterol and steroid synthesizing smooth endoplasmic reticulum of adrenocortical cells contains high levels of proteins associated with the translocation channel

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; OLIGOSACCHARIDE; SIGNAL PEPTIDE; TRANSLOCON;

EID: 24944507218     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/en.2005-0372     Document Type: Article
Times cited : (16)

References (114)
  • 1
    • 0036545889 scopus 로고    scopus 로고
    • Regulation of cholesterol supply for mineralocorticoid biosynthesis
    • Capponi AM 2002 Regulation of cholesterol supply for mineralocorticoid biosynthesis. Trends Endocrinol Metab 13:118-121
    • (2002) Trends Endocrinol Metab , vol.13 , pp. 118-121
    • Capponi, A.M.1
  • 2
    • 0019863261 scopus 로고
    • Analytical fractionation of human liver microsomal fractions: Localization of cholesterol and of the enzymes relevant to its metabolism
    • Colch
    • Balasubramaniam S, Mitropolos KA, Venkatesan S, Myant NB, Peters TJ, Postiglione A, Mancini M 1981 Analytical fractionation of human liver microsomal fractions: localization of cholesterol and of the enzymes relevant to its metabolism. Clin Sci (Colch) 60:435-439
    • (1981) Clin Sci , vol.60 , pp. 435-439
    • Balasubramaniam, S.1    Mitropolos, K.A.2    Venkatesan, S.3    Myant, N.B.4    Peters, T.J.5    Postiglione, A.6    Mancini, M.7
  • 3
    • 0030995458 scopus 로고    scopus 로고
    • Light and electron microscopic immunohistochemistry of the localization of adrenal steroidogenic enzymes
    • Ishimura K, Fujita H 1997 Light and electron microscopic immunohistochemistry of the localization of adrenal steroidogenic enzymes. Microsc Res Tech 36:445-453
    • (1997) Microsc Res Tech , vol.36 , pp. 445-453
    • Ishimura, K.1    Fujita, H.2
  • 4
    • 0015423510 scopus 로고
    • The development of smooth-surfaced endoplasmic reticulum in adrenal cortical cells of fetal guinea pigs
    • Black VH 1972 The development of smooth-surfaced endoplasmic reticulum in adrenal cortical cells of fetal guinea pigs. Am J Anat 135:381-418
    • (1972) Am J Anat , vol.135 , pp. 381-418
    • Black, V.H.1
  • 5
    • 0018688288 scopus 로고
    • A correlated thin-section and freeze-fracture analysis of guinea pig adrenocortical cells
    • Black VH, Robbins E, McNamara N, Huima T 1979 A correlated thin-section and freeze-fracture analysis of guinea pig adrenocortical cells. Am J Anat 156:453-504
    • (1979) Am J Anat , vol.156 , pp. 453-504
    • Black, V.H.1    Robbins, E.2    McNamara, N.3    Huima, T.4
  • 6
    • 0019137049 scopus 로고
    • Stereological analysis of the guinea pig adrenal: Effects of dexamethasone and ACTH treatment with emphasis on the inner cortex
    • Black VH, Russo JJ 1980 Stereological analysis of the guinea pig adrenal: effects of dexamethasone and ACTH treatment with emphasis on the inner cortex. Am J Anat 159:85-120
    • (1980) Am J Anat , vol.159 , pp. 85-120
    • Black, V.H.1    Russo, J.J.2
  • 7
    • 0023629763 scopus 로고
    • Effect of long-term inhibition of hydroxy-methylglutaryl coenzyme A reductase by mevinolin on the zona fasciculata of rat adrenal cortex. A combined morphometric and biochemical study
    • Rebuffat P, Mazzocchi G, Nussdorfer GG 1987 Effect of long-term inhibition of hydroxy-methylglutaryl coenzyme A reductase by mevinolin on the zona fasciculata of rat adrenal cortex. A combined morphometric and biochemical study. Virchows Arch B Cell Pathol Include Mol Pathol 54:67-72
    • (1987) Virchows Arch B Cell Pathol Include Mol Pathol , vol.54 , pp. 67-72
    • Rebuffat, P.1    Mazzocchi, G.2    Nussdorfer, G.G.3
  • 8
    • 0344416996 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum biogenesis in response to cytochrome P450 overproduction
    • Sandig G, Kargel E, Menzel R, Vogel F, Zimmer T, Schunck WH 1999 Regulation of endoplasmic reticulum biogenesis in response to cytochrome P450 overproduction. Drug Metab Rev 31:393-410
    • (1999) Drug Metab Rev , vol.31 , pp. 393-410
    • Sandig, G.1    Kargel, E.2    Menzel, R.3    Vogel, F.4    Zimmer, T.5    Schunck, W.H.6
  • 9
    • 0023202281 scopus 로고
    • Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum
    • Jingami H, Brown MS, Goldstein JL, Anderson RG, Luskey KL 1987 Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum. J Cell Biol 104:1693-1704
    • (1987) J Cell Biol , vol.104 , pp. 1693-1704
    • Jingami, H.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.4    Luskey, K.L.5
  • 10
    • 0017357697 scopus 로고
    • Regulation of cholesterol synthesis in rat adrenal gland through coordinate control of 3-hydroxy-3-methylglutaryl coenzyme A synthase and reductase activities
    • USA
    • Balasubramaniam S, Goldstein JL, Brown MS 1977 Regulation of cholesterol synthesis in rat adrenal gland through coordinate control of 3-hydroxy-3-methylglutaryl coenzyme A synthase and reductase activities. Proc Natl Acad Sci USA 74:1421-1425
    • (1977) Proc Natl Acad Sci , vol.74 , pp. 1421-1425
    • Balasubramaniam, S.1    Goldstein, J.L.2    Brown, M.S.3
  • 11
    • 0023856609 scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme A reductase in outer versus inner cortices of the guinea pig adrenal: Effects of adrenocorticotropin and dexamethasone
    • Black VH, Brody RI, Martin KO 1988 3-Hydroxy-3-methylglutaryl coenzyme A reductase in outer versus inner cortices of the guinea pig adrenal: effects of adrenocorticotropin and dexamethasone. Endocrinology 122:296-305
    • (1988) Endocrinology , vol.122 , pp. 296-305
    • Black, V.H.1    Brody, R.I.2    Martin, K.O.3
  • 12
  • 13
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • Johnson AE, van Waes M 1999 The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15:799-842
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 799-842
    • Johnson, A.E.1    Van Waes, M.2
  • 14
    • 0033490112 scopus 로고    scopus 로고
    • Surfing the Sec61 channel: Bidirectional protein translocation across the ER membrane
    • Romisch K 1999 Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J Cell Sci 112:4185-4191
    • (1999) J Cell Sci , vol.112 , pp. 4185-4191
    • Romisch, K.1
  • 15
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y, Rapoport 2002 Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3:246-255
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport3
  • 16
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in polypeptide translocation
    • Görlich D, Hartmann E, Prehn S, Rapoport TA 1992 A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature 357:47-52
    • (1992) Nature , vol.357 , pp. 47-52
    • Görlich, D.1    Hartmann, E.2    Prehn, S.3    Rapoport, T.A.4
  • 17
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich D, Rapoport TA 1993 Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75:615-630
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 20
    • 0031781639 scopus 로고    scopus 로고
    • The β subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation
    • Kalies KU, Rapoport TA, Hartmann E 1998 The β subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation. J Cell Biol 141:887-894
    • (1998) J Cell Biol , vol.141 , pp. 887-894
    • Kalies, K.U.1    Rapoport, T.A.2    Hartmann, E.3
  • 22
    • 0035341399 scopus 로고    scopus 로고
    • SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon
    • Fulga TA, Sinning I, Dobberstein B, Pool MR 2001 SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon. EMBO J 20:2338-2347
    • (2001) EMBO J , vol.20 , pp. 2338-2347
    • Fulga, T.A.1    Sinning, I.2    Dobberstein, B.3    Pool, M.R.4
  • 23
    • 0023192259 scopus 로고
    • A signal sequence receptor in the endoplasmic reticulum membrane
    • Wiedmann M, Kurzchalia TV, Hartmann E, Rapoport TA 1987 A signal sequence receptor in the endoplasmic reticulum membrane. Nature 328:830-833
    • (1987) Nature , vol.328 , pp. 830-833
    • Wiedmann, M.1    Kurzchalia, T.V.2    Hartmann, E.3    Rapoport, T.A.4
  • 24
    • 0022527444 scopus 로고
    • The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle
    • Kurzchalia TV, Wiedmann M, Girshovich AS, Bochkareva ES, Bielka H, Rapoport TA 1986 The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle. Nature 320:634-636
    • (1986) Nature , vol.320 , pp. 634-636
    • Kurzchalia, T.V.1    Wiedmann, M.2    Girshovich, A.S.3    Bochkareva, E.S.4    Bielka, H.5    Rapoport, T.A.6
  • 25
    • 0005614190 scopus 로고
    • Photocrosslinking of signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
    • USA
    • Krieg UC, Walter P, Johnson AE 1986 Photocrosslinking of signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc Natl Acad Sci USA 83:8604-8608
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 8604-8608
    • Krieg, U.C.1    Walter, P.2    Johnson, A.E.3
  • 27
    • 0029951178 scopus 로고    scopus 로고
    • Signal-seqeunce-dependent function of the TRAM protein during early phases of protein transport across the ER membrane
    • Voigt S, Jungnickel B, Hartmann E, Rapoport TA 1996 Signal-seqeunce- dependent function of the TRAM protein during early phases of protein transport across the ER membrane. J Cell Biol 134:25-35
    • (1996) J Cell Biol , vol.134 , pp. 25-35
    • Voigt, S.1    Jungnickel, B.2    Hartmann, E.3    Rapoport, T.A.4
  • 28
    • 0033552594 scopus 로고    scopus 로고
    • Stress-associated endoplasmic reticulum protein 1 (SERP1)/ribosome- associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation
    • Yamaguchi A, Hori O, Stern DM, Hartmann E, Ogawa S, Tohyama M 1999 Stress-associated endoplasmic reticulum protein 1 (SERP1)/ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. J Cell Biol 147:1195-1204
    • (1999) J Cell Biol , vol.147 , pp. 1195-1204
    • Yamaguchi, A.1    Hori, O.2    Stern, D.M.3    Hartmann, E.4    Ogawa, S.5    Tohyama, M.6
  • 31
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • Fons RD, Bogert BA, Hegde RS 2003 Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane. J Cell Biol 160:529-539
    • (2003) J Cell Biol , vol.160 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 32
    • 0032728066 scopus 로고    scopus 로고
    • Posttranslational protein translocation across the membrane of the endoplasmic reticulum
    • Rapoport TA, Matlack KE, Plath K, Misselwitz B, Staeck O 1999 Posttranslational protein translocation across the membrane of the endoplasmic reticulum. Biol Chem 380:1143-1150
    • (1999) Biol Chem , vol.380 , pp. 1143-1150
    • Rapoport, T.A.1    Matlack, K.E.2    Plath, K.3    Misselwitz, B.4    Staeck, O.5
  • 36
    • 0033738377 scopus 로고    scopus 로고
    • Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex
    • Wittke S, Dunnwald M, Johnsson N 2000 Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex. Mol Bio Cell 11:3859-3871
    • (2000) Mol Bio Cell , vol.11 , pp. 3859-3871
    • Wittke, S.1    Dunnwald, M.2    Johnsson, N.3
  • 37
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-a factor across the ER membrane
    • Matlack KE, Misselwitz B, Plath K, Rapoport TA 1999 BiP acts as a molecular ratchet during posttranslational transport of prepro-a factor across the ER membrane. Cell 97:553-564
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 38
    • 0012295328 scopus 로고
    • Purification of microsomal signal peptidase as a complex
    • USA
    • Evans EA, Gilmore R, Blobel G 1986 Purification of microsomal signal peptidase as a complex. Proc Natl Acad Sci USA 83:581-585
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 581-585
    • Evans, E.A.1    Gilmore, R.2    Blobel, G.3
  • 39
    • 0035951866 scopus 로고    scopus 로고
    • Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum
    • Chen X, Van Valkenburgh C, Liang H, Fang H, Green N 2001 Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum. J Biol Chem 276:2411-2416
    • (2001) J Biol Chem , vol.276 , pp. 2411-2416
    • Chen, X.1    Van Valkenburgh, C.2    Liang, H.3    Fang, H.4    Green, N.5
  • 40
    • 0030063873 scopus 로고    scopus 로고
    • Membrane topology of the 12- and 25-kDa subunits of the mammalian signal peptidase complex
    • Kalies KU, Hartmann E 1996 Membrane topology of the 12- and 25-kDa subunits of the mammalian signal peptidase complex. J Biol Chem 271:3925-3929
    • (1996) J Biol Chem , vol.271 , pp. 3925-3929
    • Kalies, K.U.1    Hartmann, E.2
  • 41
    • 0026716017 scopus 로고
    • Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48-kDa protein
    • Kelleher DJ, Kreibich G, Gilmore R 1992 Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48-kDa protein. Cell 69:55-65
    • (1992) Cell , vol.69 , pp. 55-65
    • Kelleher, D.J.1    Kreibich, G.2    Gilmore, R.3
  • 42
    • 0030922695 scopus 로고    scopus 로고
    • DAD1, the defender against apoptotic cell death, is a subunit of the mammalian oligosaccharyltransferase
    • USA
    • Kelleher DJ, Gilmore R 1997 DAD1, the defender against apoptotic cell death, is a subunit of the mammalian oligosaccharyltransferase. Proc Natl Acad Sci USA 94:4994
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 4994
    • Kelleher, D.J.1    Gilmore, R.2
  • 43
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R 2003 Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell 12:101-111
    • (2003) Mol Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 44
    • 0034635564 scopus 로고    scopus 로고
    • Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulum
    • Fu J, Kreibich G 2000 Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulum. J Biol Chem 275:3984-3990
    • (2000) J Biol Chem , vol.275 , pp. 3984-3990
    • Fu, J.1    Kreibich, G.2
  • 45
    • 0027082782 scopus 로고
    • The 48-kDa subunit of the mammalian oligosaccharyltransferase complex is homologous to the essential yeast protein WMP
    • Silberstein S, Kelleher DJ, Gilmore R 1992 The 48-kDa subunit of the mammalian oligosaccharyltransferase complex is homologous to the essential yeast protein WMP. J Biol Chem 267:23658-23683
    • (1992) J Biol Chem , vol.267 , pp. 23658-23683
    • Silberstein, S.1    Kelleher, D.J.2    Gilmore, R.3
  • 46
    • 0034434661 scopus 로고    scopus 로고
    • The oligosaccharyltransferase complex from pig liver: cDNA cloning, expression and functional characterization
    • Hardt B, Aparicio B, Bause E 2000 The oligosaccharyltransferase complex from pig liver: cDNA cloning, expression and functional characterization. Glycoconj J 17:767-779
    • (2000) Glycoconj J , vol.17 , pp. 767-779
    • Hardt, B.1    Aparicio, B.2    Bause, E.3
  • 47
    • 0032476047 scopus 로고    scopus 로고
    • DAD1 is required for the function and the structural integrity of the oligosaccharyltransferase complex
    • Sanjay A, Fu J, Kreibich G 1998 DAD1 is required for the function and the structural integrity of the oligosaccharyltransferase complex. J Biol Chem 273:26094-26099
    • (1998) J Biol Chem , vol.273 , pp. 26094-26099
    • Sanjay, A.1    Fu, J.2    Kreibich, G.3
  • 48
    • 0033819123 scopus 로고    scopus 로고
    • A subunit of the mammalian oligosaccharyltransferase, DAD1, interacts with Mcl-1, one of the bcl-2 protein family
    • Tokyo
    • Makishima T, Yoshimi M, Komiyama S, Hara N, Nishimoto T 2000 A subunit of the mammalian oligosaccharyltransferase, DAD1, interacts with Mcl-1, one of the bcl-2 protein family. J Biochem (Tokyo) 128:399-405
    • (2000) J Biochem , vol.128 , pp. 399-405
    • Makishima, T.1    Yoshimi, M.2    Komiyama, S.3    Hara, N.4    Nishimoto, T.5
  • 49
    • 0033860694 scopus 로고    scopus 로고
    • Evidence for interaction of yeast protein kinase C with several subunits of oligosaccharyl transferase
    • Park H, Lennarz WJ 2000 Evidence for interaction of yeast protein kinase C with several subunits of oligosaccharyl transferase. Glycobiology 10:737-744
    • (2000) Glycobiology , vol.10 , pp. 737-744
    • Park, H.1    Lennarz, W.J.2
  • 50
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A 2003 Quality control in the endoplasmic reticulum. Nat Rev Mol Biol 4:181-191
    • (2003) Nat Rev Mol Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 51
  • 52
    • 7444240833 scopus 로고    scopus 로고
    • The ER chaperone BiP is a master regulator of ER function
    • Hendershot LM 2004 The ER chaperone BiP is a master regulator of ER function. Mt Sinai J Med 71:289-297
    • (2004) Mt Sinai J Med , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 53
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman BD, Hendershot LM, Johnson AE 1998 BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92:747-758
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 54
    • 13444271726 scopus 로고    scopus 로고
    • The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum
    • Adler NN, Shen Y, Brodsky JL, Hendershot LM, Johnson AE 2005 The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. J Cell Biol 168:389-399
    • (2005) J Cell Biol , vol.168 , pp. 389-399
    • Adler, N.N.1    Shen, Y.2    Brodsky, J.L.3    Hendershot, L.M.4    Johnson, A.E.5
  • 55
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
    • Melnick J, Aviel S, Argon Y 1992 The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J Biol Chem 267:21303-21306
    • (1992) J Biol Chem , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 56
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi AJ 2000 Protein glucosylation and its role in protein folding. Annu Rev Biochem 69:69-93
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 57
    • 0035816569 scopus 로고    scopus 로고
    • The lectin-chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo
    • Danilczyk UG, Williams DB 2001 The lectin-chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo. J Biol Chem 276:25532-25540
    • (2001) J Biol Chem , vol.276 , pp. 25532-25540
    • Danilczyk, U.G.1    Williams, D.B.2
  • 58
    • 0022254927 scopus 로고
    • Immunochemical analysis of rough and smooth microsomes from rat liver
    • Hortsch M, Meyer DI 1985 Immunochemical analysis of rough and smooth microsomes from rat liver. Eur J Biochem 150:559-5665
    • (1985) Eur J Biochem , vol.150 , pp. 559-5665
    • Hortsch, M.1    Meyer, D.I.2
  • 59
    • 0025689948 scopus 로고
    • Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane
    • Vogel F, Hartmann E, Gorlich D, Rapoport TA 1990 Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane. Eur J Cell Biol 53:197-202
    • (1990) Eur J Cell Biol , vol.53 , pp. 197-202
    • Vogel, F.1    Hartmann, E.2    Gorlich, D.3    Rapoport, T.A.4
  • 60
    • 0017858332 scopus 로고
    • Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristic of rough microsomes
    • Kreibich G, Ulrich BL, Sabatini DD 1978 Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristic of rough microsomes. J Cell Biol 77:464-487
    • (1978) J Cell Biol , vol.77 , pp. 464-487
    • Kreibich, G.1    Ulrich, B.L.2    Sabatini, D.D.3
  • 61
    • 0020135043 scopus 로고
    • Identification of ribophorins in rough microsomal membranes from different organs of several species
    • Marcantonio EE, Grebenau RC, Sabatini DD, Kreibich G 1982 Identification of ribophorins in rough microsomal membranes from different organs of several species. Eur J Biochem 124:217-222
    • (1982) Eur J Biochem , vol.124 , pp. 217-222
    • Marcantonio, E.E.1    Grebenau, R.C.2    Sabatini, D.D.3    Kreibich, G.4
  • 62
    • 0021738720 scopus 로고
    • Segregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subfractions contain equimolar amounts of ribophorins and ribosomes
    • Marcantonio EE, Amar-Costesec A, Kreibich G 1984 Segregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subfractions contain equimolar amounts of ribophorins and ribosomes. J Cell Biol 99:2254-2259
    • (1984) J Cell Biol , vol.99 , pp. 2254-2259
    • Marcantonio, E.E.1    Amar-Costesec, A.2    Kreibich, G.3
  • 63
    • 0022005297 scopus 로고
    • Restriction of docking protein to the rough endoplasmic reticulum: Immunocytochemical localization in rat liver
    • Hortsch M, Griffiths G, Meyer DI 1985 Restriction of docking protein to the rough endoplasmic reticulum: immunocytochemical localization in rat liver. Eur J Cell Biol 38:271-279
    • (1985) Eur J Cell Biol , vol.38 , pp. 271-279
    • Hortsch, M.1    Griffiths, G.2    Meyer, D.I.3
  • 64
    • 0032527058 scopus 로고    scopus 로고
    • Induction of CP1A1, but not of CYP1A2, in adrenals of 3-methylcholanthrene-treated guinea pigs
    • Black VH, Wang A-F, Henry M, Shaw PM 1998 Induction of CP1A1, but not of CYP1A2, in adrenals of 3-methylcholanthrene-treated guinea pigs. Arch Biochem Biophys 354:197-205
    • (1998) Arch Biochem Biophys , vol.354 , pp. 197-205
    • Black, V.H.1    Wang, A.-F.2    Henry, M.3    Shaw, P.M.4
  • 65
    • 0020319756 scopus 로고
    • Hormone-dependent changes in peroxisomal enzyme activity in guinea pig adrenal
    • Russo JJ, Black V 1982 Hormone-dependent changes in peroxisomal enzyme activity in guinea pig adrenal. J Biol Chem 257:3883-3889
    • (1982) J Biol Chem , vol.257 , pp. 3883-3889
    • Russo, J.J.1    Black, V.2
  • 66
    • 0024507012 scopus 로고
    • A cytochrome P450 immunochemically related to P450c, d (P450I) localized to the smooth microsomes and inner zone of the guinea pig adrenal
    • Black VH, Barilla JR, Russo JJ, Martin KO 1989 A cytochrome P450 immunochemically related to P450c, d (P450I) localized to the smooth microsomes and inner zone of the guinea pig adrenal. Endocrinology 124:2480-2493
    • (1989) Endocrinology , vol.124 , pp. 2480-2493
    • Black, V.H.1    Barilla, J.R.2    Russo, J.J.3    Martin, K.O.4
  • 67
    • 0015540436 scopus 로고
    • An improved cell fractionation procedure for the preparation of rat liver membrane-bound ribosomes
    • Adelman MR, Blobel G, Sabatini DD 1973 An improved cell fractionation procedure for the preparation of rat liver membrane-bound ribosomes. J Cell Biol 56:191-205
    • (1973) J Cell Biol , vol.56 , pp. 191-205
    • Adelman, M.R.1    Blobel, G.2    Sabatini, D.D.3
  • 68
    • 0017710194 scopus 로고
    • Release of poly A(+) messenger RNA from rat liver rough microsomes upon disassembly of bound polysomes
    • Kruppa J, Sabatini DD 1977 Release of poly A(+) messenger RNA from rat liver rough microsomes upon disassembly of bound polysomes. J Cell Biol 74:414-427
    • (1977) J Cell Biol , vol.74 , pp. 414-427
    • Kruppa, J.1    Sabatini, D.D.2
  • 69
    • 0015549345 scopus 로고
    • Ribosome-membrane interaction. Nondestructive disassembly of rat liver rough microsomes into ribosomal and membranous components
    • Adelman MR, Blobel G, Sabatini DD 1973 Ribosome-membrane interaction. Nondestructive disassembly of rat liver rough microsomes into ribosomal and membranous components. J Cell Biol 56:206-229
    • (1973) J Cell Biol , vol.56 , pp. 206-229
    • Adelman, M.R.1    Blobel, G.2    Sabatini, D.D.3
  • 70
    • 0025163241 scopus 로고
    • Antiribophorin antibodies inhibit the targeting to the ER membrane of ribosomes containing nascent secretory polypeptides
    • Yu Y, Sabatini DD, Kreibich G 1990 Antiribophorin antibodies inhibit the targeting to the ER membrane of ribosomes containing nascent secretory polypeptides. J Cell Biol 111:1335-1342
    • (1990) J Cell Biol , vol.111 , pp. 1335-1342
    • Yu, Y.1    Sabatini, D.D.2    Kreibich, G.3
  • 71
    • 0025002582 scopus 로고
    • Immunodetectable cytochromes P450 I, II, and III in guinea pig adrenal - Hormone responsiveness and relationship to capacity for xenobiotic metabolism
    • Black VH 1990 Immunodetectable cytochromes P450 I, II, and III in guinea pig adrenal - hormone responsiveness and relationship to capacity for xenobiotic metabolism. Endocrinology 127:1153-1159
    • (1990) Endocrinology , vol.127 , pp. 1153-1159
    • Black, V.H.1
  • 72
    • 0028240848 scopus 로고
    • Estrogen, not testosterone, creates male predominance of a P4501-related cytochrome in adult guinea pig adrenals
    • Black VH 1994 Estrogen, not testosterone, creates male predominance of a P4501-related cytochrome in adult guinea pig adrenals. Endocrinology 135:299-306
    • (1994) Endocrinology , vol.135 , pp. 299-306
    • Black, V.H.1
  • 74
    • 0020414932 scopus 로고
    • Isolated guinea pig adrenocortical cells in vitro: Morphology and steroidogenesis in control and ACTH-treated cultures
    • Black VH, Mierlak J, Katz T, Miao P, Huima T, McNamara N 1982 Isolated guinea pig adrenocortical cells in vitro: morphology and steroidogenesis in control and ACTH-treated cultures. Am J Anat 165:225-2248
    • (1982) Am J Anat , vol.165 , pp. 225-2248
    • Black, V.H.1    Mierlak, J.2    Katz, T.3    Miao, P.4    Huima, T.5    McNamara, N.6
  • 75
    • 0021100147 scopus 로고
    • Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides
    • Welply JK, Shenbagamurthi P, Lennarz WJ, Naider F 1983 Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides. J Biol Chem 258:11856-11863
    • (1983) J Biol Chem , vol.258 , pp. 11856-11863
    • Welply, J.K.1    Shenbagamurthi, P.2    Lennarz, W.J.3    Naider, F.4
  • 76
    • 0023658351 scopus 로고
    • The rate of bulk flow from the endoplasmic reticulum to the cell surface
    • Wieland FT, Gleason ML, Serafini TA, Rothman JE 1987 The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50:289-300
    • (1987) Cell , vol.50 , pp. 289-300
    • Wieland, F.T.1    Gleason, M.L.2    Serafini, T.A.3    Rothman, J.E.4
  • 77
    • 0028067206 scopus 로고
    • Complete Golgi passage of glycotripeptides generated in the endoplasmic reticulum of mammalian cells
    • van Leyen K, Wieland F 1994 Complete Golgi passage of glycotripeptides generated in the endoplasmic reticulum of mammalian cells. FEBS Lett 352:211-21532
    • (1994) FEBS Lett , vol.352 , pp. 211-21532
    • Van Leyen, K.1    Wieland, F.2
  • 78
    • 0032506006 scopus 로고    scopus 로고
    • A general mechanism for regulation of access to the translocon: Competition for a membrane attachment site on ribosomes
    • USA
    • Möller I, Jung M, Beatrix B, Levy R, Kreibich G, Zimmermann R, Wiedmann M, Lauring B 1998 A general mechanism for regulation of access to the translocon: competition for a membrane attachment site on ribosomes. Proc Natl Acad Sci USA 95:13425-13430
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 13425-13430
    • Möller, I.1    Jung, M.2    Beatrix, B.3    Levy, R.4    Kreibich, G.5    Zimmermann, R.6    Wiedmann, M.7    Lauring, B.8
  • 79
    • 0029076816 scopus 로고
    • Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum
    • Lauring B, Sakai H, Kreibich G, Wiedmann M 1995 Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum. Proc Natl Acad Sci 92:5411-5415
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 5411-5415
    • Lauring, B.1    Sakai, H.2    Kreibich, G.3    Wiedmann, M.4
  • 80
    • 0022358406 scopus 로고
    • Bovine opsin has more than one signal sequence
    • Friedlander M, Blobel G 1985 Bovine opsin has more than one signal sequence. Nature 318:338-343
    • (1985) Nature , vol.318 , pp. 338-343
    • Friedlander, M.1    Blobel, G.2
  • 81
    • 0023936207 scopus 로고
    • Guanosine triphosphate promotes the posttranslational integration of opsin into the endoplasmic reticulum membrane
    • Hoffman KE, Gilmore R 1988 Guanosine triphosphate promotes the posttranslational integration of opsin into the endoplasmic reticulum membrane. J Biol Chem 263:4381-4385
    • (1988) J Biol Chem , vol.263 , pp. 4381-4385
    • Hoffman, K.E.1    Gilmore, R.2
  • 82
    • 0034110919 scopus 로고    scopus 로고
    • Translocation machinery for synthesis of integral membrane and secretory proteins in dendritic spines
    • Pierce JP, van Leyen K, McCarthy JB 2000 Translocation machinery for synthesis of integral membrane and secretory proteins in dendritic spines. Nat Neurosci 3:311-313
    • (2000) Nat Neurosci , vol.3 , pp. 311-313
    • Pierce, J.P.1    Van Leyen, K.2    McCarthy, J.B.3
  • 83
    • 0036000025 scopus 로고    scopus 로고
    • Targeting of rough endoplasmic reticulum membrane proteins in invertebrate neurons
    • Rolls MM, Hall DH, Victor M, Stelzer EHK, Rapoport TA 2002 Targeting of rough endoplasmic reticulum membrane proteins in invertebrate neurons. Mol Biol Cell 13:1778-1791
    • (2002) Mol Biol Cell , vol.13 , pp. 1778-1791
    • Rolls, M.M.1    Hall, D.H.2    Victor, M.3    Stelzer, E.H.K.4    Rapoport, T.A.5
  • 84
    • 0026656581 scopus 로고
    • The endoplasmic reticulum-sarcoplasmic reticulum connection: Distribution of endoplasmic reticulum markers in the sarcoplasmic reticulum of skeletal muscle fibers
    • USA
    • Volpe P, Villa A, Podini P, Martini A, Nori A, Panzeri MC, Meldolesi J 1992 The endoplasmic reticulum-sarcoplasmic reticulum connection: distribution of endoplasmic reticulum markers in the sarcoplasmic reticulum of skeletal muscle fibers. Proc Natl Acad Sci USA 89:6142-6146
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 6142-6146
    • Volpe, P.1    Villa, A.2    Podini, P.3    Martini, A.4    Nori, A.5    Panzeri, M.C.6    Meldolesi, J.7
  • 86
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann O, Walz B 2001 Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Intl Rev Cytol 205:149-214
    • (2001) Intl Rev Cytol , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 87
    • 0021752001 scopus 로고
    • A heuristic proposal for understanding steroidogenic processes
    • Lieberman S, Greenfield NJ, Wolfson A 1984 A heuristic proposal for understanding steroidogenic processes. Endocr Rev 5:128-148
    • (1984) Endocr Rev , vol.5 , pp. 128-148
    • Lieberman, S.1    Greenfield, N.J.2    Wolfson, A.3
  • 88
    • 24944500291 scopus 로고
    • Utilization of adrenal gland cholesterol for synthesis of cortisol by intact normal and ACTH-treated guinea pig
    • Werbin H, Chaikoff IL 1961 Utilization of adrenal gland cholesterol for synthesis of cortisol by intact normal and ACTH-treated guinea pig. Arch Biochem Biophys 93:476-484
    • (1961) Arch Biochem Biophys , vol.93 , pp. 476-484
    • Werbin, H.1    Chaikoff, I.L.2
  • 89
    • 0015457955 scopus 로고
    • Rates of adrenal cholesterol formation by the hamster, sheep, guinea pig and rat from labeled pyruvate, in vitro
    • Lloyd B 1972 Rates of adrenal cholesterol formation by the hamster, sheep, guinea pig and rat from labeled pyruvate, in vitro. Gen Comp Endocrinol 19:428-431
    • (1972) Gen Comp Endocrinol , vol.19 , pp. 428-431
    • Lloyd, B.1
  • 90
    • 0020533584 scopus 로고
    • Sterol synthesis in vivo in 18 tissues of the squirrel monkey, guinea pig, rabbit, hamster, and rat
    • Spady DK, Dietschy JM 1983 Sterol synthesis in vivo in 18 tissues of the squirrel monkey, guinea pig, rabbit, hamster, and rat. J Lipid Res 24:303-315
    • (1983) J Lipid Res , vol.24 , pp. 303-315
    • Spady, D.K.1    Dietschy, J.M.2
  • 91
    • 0022360706 scopus 로고
    • Rates of cholesterol synthesis and low-density lipoprotein uptake in the adrenal glands of the rat, hamster and rabbit in vivo
    • Spady DK, Dietschy JM 1985 Rates of cholesterol synthesis and low-density lipoprotein uptake in the adrenal glands of the rat, hamster and rabbit in vivo. Biochim Biophys Acta 836:167-175
    • (1985) Biochim Biophys Acta , vol.836 , pp. 167-175
    • Spady, D.K.1    Dietschy, J.M.2
  • 92
    • 0018577934 scopus 로고
    • Processing in vitro of placental peptide hormones by smooth microsomes
    • USA
    • Bielinska M, Rogers G, Rucinsky T, Boime I 1979 Processing in vitro of placental peptide hormones by smooth microsomes. Proc Natl Acad Sci USA 76:6152-6156
    • (1979) Proc Natl Acad Sci , vol.76 , pp. 6152-6156
    • Bielinska, M.1    Rogers, G.2    Rucinsky, T.3    Boime, I.4
  • 93
    • 0036940470 scopus 로고    scopus 로고
    • Cholesterol and steroid synthesizing smooth endoplasmic reticulum of adrenocortical cells contains high levels of translocation apparatus and oligosaccharyltransferase complex proteins
    • Black VH, Sanjay A, Van Leyen K, Möeller I, Lauring B, Kreibich G 2002 Cholesterol and steroid synthesizing smooth endoplasmic reticulum of adrenocortical cells contains high levels of translocation apparatus and oligosaccharyltransferase complex proteins. Endocr Res 28:425-430
    • (2002) Endocr Res , vol.28 , pp. 425-430
    • Black, V.H.1    Sanjay, A.2    Van Leyen, K.3    Möeller, I.4    Lauring, B.5    Kreibich, G.6
  • 94
    • 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 1998 Topology of SREBP cleavage-activating protein, a polytopic membrane protein with a sterol-sensing domain. J Biol Chem 273:17243-17250
    • (1998) J Biol Chem , vol.273 , pp. 17243-17250
    • Nohturfft, A.1    Brown, M.S.2    Goldstein, J.L.3
  • 95
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS 2002 Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 110:489-500
    • (2002) Cell , vol.110 , pp. 489-500
    • Yang, T.1    Espenshade, P.J.2    Wright, M.E.3    Yabe, D.4    Gong, Y.5    Aebersold, R.6    Goldstein, J.L.7    Brown, M.S.8
  • 97
    • 0036251153 scopus 로고    scopus 로고
    • SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver
    • Horton JD, Goldstein JL, Brown MS 2002 SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver. J Clin Invest 109:1125-1131
    • (2002) J Clin Invest , vol.109 , pp. 1125-1131
    • Horton, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 98
    • 0024601874 scopus 로고
    • Effects of age, adrenocorticotropin, and dexamethasone on a male-specific cytochrome P450 localized in the inner zone of the guinea pig adrenal
    • Black VH, Barilla JR, Martin KO 1989 Effects of age, adrenocorticotropin, and dexamethasone on a male-specific cytochrome P450 localized in the inner zone of the guinea pig adrenal. Endocrinology 124:2494-2498
    • (1989) Endocrinology , vol.124 , pp. 2494-2498
    • Black, V.H.1    Barilla, J.R.2    Martin, K.O.3
  • 99
    • 0030660267 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • USA
    • Hampton RY, Bhakta H 1997 Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci USA 94:12944-12948
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 100
    • 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 275:35840-35847
    • (2000) J Biol Chem , vol.275 , pp. 35840-35847
    • Ravid, T.1    Doolman, R.2    Avner, R.3    Harats, D.4    Roitelman, J.5
  • 102
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA 2004 A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429:841-847
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 103
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley BN, Ploegh HL 2004 A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429:834-840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 104
    • 4444313480 scopus 로고    scopus 로고
    • Checkpoints in ER-associated degradation: Excuse me, which way to the proteosome?
    • Ahner A, Brodsky JL 2004 Checkpoints in ER-associated degradation: excuse me, which way to the proteosome? Trends Cell Biol 14:474-478
    • (2004) Trends Cell Biol , vol.14 , pp. 474-478
    • Ahner, A.1    Brodsky, J.L.2
  • 105
    • 14244258608 scopus 로고    scopus 로고
    • Ribophorin I associates with a subset of membrane proteins after their integration at the sec61 translocon
    • Wilson CM, Kraft C, Duggan C, Ismail N, Crawshaw SG, High S 2005 Ribophorin I associates with a subset of membrane proteins after their integration at the sec61 translocon. J Biol Chem 280:4195-4206
    • (2005) J Biol Chem , vol.280 , pp. 4195-4206
    • Wilson, C.M.1    Kraft, C.2    Duggan, C.3    Ismail, N.4    Crawshaw, S.G.5    High, S.6
  • 106
    • 0035059281 scopus 로고    scopus 로고
    • Genomic-scale comparison of sequence- and structure-based methods of function prediction: Does structure provide additional insight?
    • Fetrow JS, Siew N, Di Gennaro JA, Martinez-Yamout M, Dyson HJ, Skolnick J 2001 Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10:1005-1014
    • (2001) Protein Sci , vol.10 , pp. 1005-1014
    • Fetrow, J.S.1    Siew, N.2    Di Gennaro, J.A.3    Martinez-Yamout, M.4    Dyson, H.J.5    Skolnick, J.6
  • 107
    • 0346158365 scopus 로고    scopus 로고
    • Making membrane proteins at the mammalian endoplasmic reticulum
    • Lecomte FJL, Ismail S, High S 2003 Making membrane proteins at the mammalian endoplasmic reticulum. Biochem Soc Trans 31:1248-1252
    • (2003) Biochem Soc Trans , vol.31 , pp. 1248-1252
    • Lecomte, F.J.L.1    Ismail, S.2    High, S.3
  • 108
    • 0037092503 scopus 로고    scopus 로고
    • Integral membrane protein biosynthesis: Why topology is hard to predict
    • Ott CM, Lingappa VR 2002 Integral membrane protein biosynthesis: why topology is hard to predict. J Cell Sci 115:2003-2009
    • (2002) J Cell Sci , vol.115 , pp. 2003-2009
    • Ott, C.M.1    Lingappa, V.R.2
  • 109
    • 0031963435 scopus 로고    scopus 로고
    • Differential intracellular sorting of immediate early gene mRNAs depends on signals in the mRNA sequence
    • Wallace CS, Lyford GL, Worley PF, Steward O 1998 Differential intracellular sorting of immediate early gene mRNAs depends on signals in the mRNA sequence. J Neurosci 18:26-3578
    • (1998) J Neurosci , vol.18 , pp. 26-3578
    • Wallace, C.S.1    Lyford, G.L.2    Worley, P.F.3    Steward, O.4
  • 110
    • 0036481454 scopus 로고    scopus 로고
    • Signal sequences control gating of the protein translocation channel in a substrate-specific manner
    • Kim SJ, Mitra C, Salernao JR, Hegde RS 2002 Signal sequences control gating of the protein translocation channel in a substrate-specific manner. Dev Cell 2:207-217
    • (2002) Dev Cell , vol.2 , pp. 207-217
    • Kim, S.J.1    Mitra, C.2    Salernao, J.R.3    Hegde, R.S.4
  • 111
    • 0032904215 scopus 로고    scopus 로고
    • Regulation of protein biogenesis at the endoplasmic reticulum membrane
    • Hegde RS, Lingappa VR 1999 Regulation of protein biogenesis at the endoplasmic reticulum membrane. Trends Cell Biol 9:132-137
    • (1999) Trends Cell Biol , vol.9 , pp. 132-137
    • Hegde, R.S.1    Lingappa, V.R.2
  • 112
    • 0037189518 scopus 로고    scopus 로고
    • Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon after termination of protein synthesis
    • Potter MD, Nicchitta CV 2002 Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon after termination of protein synthesis. J Biol Chem 277:23314-23320
    • (2002) J Biol Chem , vol.277 , pp. 23314-23320
    • Potter, M.D.1    Nicchitta, C.V.2
  • 113
  • 114
    • 13244269851 scopus 로고    scopus 로고
    • Lipid-mediated, reversible misfolding of a sterol-sensing domain protein
    • Shearer AG, Hampton RY 2005 Lipid-mediated, reversible misfolding of a sterol-sensing domain protein. EMBO J 24:149-159
    • (2005) EMBO J , vol.24 , pp. 149-159
    • Shearer, A.G.1    Hampton, R.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.