메뉴 건너뛰기




Volumn 16, Issue 10, 2015, Pages 1027-1038

Inhibitors of Protein Translocation Across the ER Membrane

Author keywords

Antigen cross presentation; Endoplasmic reticulum; ER associated degradation; Membrane protein integration; Protein secretion; Protein translocation; Sec61 channel

Indexed keywords

CALMODULIN INHIBITOR; CHAPERONE; CYCLODEPSIPEPTIDE; EXOTOXIN; LACTONE DERIVATIVE; LANTHANUM; MEMBRANE PROTEIN; STEROL; ANTINEOPLASTIC AGENT; CARRIER PROTEIN;

EID: 84941601044     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12308     Document Type: Review
Times cited : (20)

References (76)
  • 1
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • Wicker W, Schekman R. Protein translocation across biological membranes. Science 2005;310:1452-1456.
    • (2005) Science , vol.310 , pp. 1452-1456
    • Wicker, W.1    Schekman, R.2
  • 2
    • 0036009896 scopus 로고    scopus 로고
    • New apratoxins of marine cyanobacterial origin from guam and palau
    • Luesch H, Yoshida WY, Moore RE, Paul VJ. New apratoxins of marine cyanobacterial origin from guam and palau. Bioorg Med Chem 2002;10:1973-1978.
    • (2002) Bioorg Med Chem , vol.10 , pp. 1973-1978
    • Luesch, H.1    Yoshida, W.Y.2    Moore, R.E.3    Paul, V.J.4
  • 4
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Römisch K. Endoplasmic reticulum-associated degradation. Annu Rev Cell Dev Biol 2005;21:435-456.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 435-456
    • Römisch, K.1
  • 5
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park E, Rapoport TA. Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu Rev Biophys 2012;41:21-40.
    • (2012) Annu Rev Biophys , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 6
    • 84455178968 scopus 로고    scopus 로고
    • A calmodulin-dependent translocation pathway for small secretory proteins
    • Shao S, Hegde RS. A calmodulin-dependent translocation pathway for small secretory proteins. Cell 2011;147:1576-1588.
    • (2011) Cell , vol.147 , pp. 1576-1588
    • Shao, S.1    Hegde, R.S.2
  • 7
    • 84863934536 scopus 로고    scopus 로고
    • Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation
    • Lakkaraju AK, Thankappan R, Mary C, Garrison JL, Taunton J, Strub K. Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation. Mol Biol Cell 2012;23:2712-2722.
    • (2012) Mol Biol Cell , vol.23 , pp. 2712-2722
    • Lakkaraju, A.K.1    Thankappan, R.2    Mary, C.3    Garrison, J.L.4    Taunton, J.5    Strub, K.6
  • 8
    • 0021677233 scopus 로고
    • Design and synthesis of a consensus signal sequence that inhibits protein translocation into rough microsomal vesicles
    • Austen BM, Hermon-Taylor J, Kaderbhai MA, Ridd DH. Design and synthesis of a consensus signal sequence that inhibits protein translocation into rough microsomal vesicles. Biochem J 1984;224:317-325.
    • (1984) Biochem J , vol.224 , pp. 317-325
    • Austen, B.M.1    Hermon-Taylor, J.2    Kaderbhai, M.A.3    Ridd, D.H.4
  • 10
    • 0035847010 scopus 로고    scopus 로고
    • Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis
    • Fewell SW, Day BW, Brodsky JL. Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis. J Biol Chem 2001;276:910-914.
    • (2001) J Biol Chem , vol.276 , pp. 910-914
    • Fewell, S.W.1    Day, B.W.2    Brodsky, J.L.3
  • 12
    • 64249149363 scopus 로고    scopus 로고
    • Post-translational import of protein into the endoplasmic reticulum of a trypanosome: an in vitro system for discovery of anti-trypanosomal chemical entities
    • Patham B, Duffy J, Lane A, Davis RC, Wipf P, Fewell SW, Brodsky JL, Mensa-Wilmot K. Post-translational import of protein into the endoplasmic reticulum of a trypanosome: an in vitro system for discovery of anti-trypanosomal chemical entities. Biochem J 2009;419:507-517.
    • (2009) Biochem J , vol.419 , pp. 507-517
    • Patham, B.1    Duffy, J.2    Lane, A.3    Davis, R.C.4    Wipf, P.5    Fewell, S.W.6    Brodsky, J.L.7    Mensa-Wilmot, K.8
  • 14
    • 0018606687 scopus 로고
    • Equisetin, an antibiotic from Fusarium equiseti NRRL 5537, identified as a derivative of N-methyl-2,4-pyrollidone
    • Vesonder RF, Tjarks LW, Rohwedder WK, Burmeister HR, Laugal JA. Equisetin, an antibiotic from Fusarium equiseti NRRL 5537, identified as a derivative of N-methyl-2, 4-pyrollidone. J Antibiot 1979;32:759-761.
    • (1979) J Antibiot , vol.32 , pp. 759-761
    • Vesonder, R.F.1    Tjarks, L.W.2    Rohwedder, W.K.3    Burmeister, H.R.4    Laugal, J.A.5
  • 17
    • 67650144829 scopus 로고    scopus 로고
    • Lanthanum ions inhibit the mammalian Sec61 complex in its channel dynamics and protein transport activity
    • Erdmann F, Jung M, Eyrisch S, Lang S, Helms V, Wagner R, Zimmermann R. Lanthanum ions inhibit the mammalian Sec61 complex in its channel dynamics and protein transport activity. FEBS Lett 2009;583:2359-2364.
    • (2009) FEBS Lett , vol.583 , pp. 2359-2364
    • Erdmann, F.1    Jung, M.2    Eyrisch, S.3    Lang, S.4    Helms, V.5    Wagner, R.6    Zimmermann, R.7
  • 18
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: an energetic perspective
    • Andersen OS, Koeppe RE. Bilayer thickness and membrane protein function: an energetic perspective. Annu Rev Biophys Biomol Struct 2007;36:107-130.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe, R.E.2
  • 19
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R, Ursell T, Wiggins P, Sens P. Emerging roles for lipids in shaping membrane-protein function. Nature 2009;459:379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 20
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher MS, Munro S. Cholesterol and the Golgi apparatus. Science 1993;261:1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 21
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe HJ, Stevens TJ, Munro S. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 2010;142:158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 22
    • 51649107357 scopus 로고    scopus 로고
    • To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane topology
    • Bogdanov M, Xie J, Heacock P, Dowhan W. To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane topology. J Cell Biol 2008;182:925-935.
    • (2008) J Cell Biol , vol.182 , pp. 925-935
    • Bogdanov, M.1    Xie, J.2    Heacock, P.3    Dowhan, W.4
  • 23
    • 0035834729 scopus 로고    scopus 로고
    • Inhibition of protein translocation across the endoplasmic reticulum membrane by sterols
    • Nilsson IM, Ohvo-Rekilä H, Slotte JP, Johnson AE, von Heijne G. Inhibition of protein translocation across the endoplasmic reticulum membrane by sterols. J Biol Chem 2001;276:41748-41754.
    • (2001) J Biol Chem , vol.276 , pp. 41748-41754
    • Nilsson, I.M.1    Ohvo-Rekilä, H.2    Slotte, J.P.3    Johnson, A.E.4    von Heijne, G.5
  • 24
    • 84935866871 scopus 로고    scopus 로고
    • Lipid-protein interplay and lateral organization of biomembranes
    • Nyholm TK. Lipid-protein interplay and lateral organization of biomembranes. Chem Phys Lipids 2015;189:48-55.
    • (2015) Chem Phys Lipids , vol.189 , pp. 48-55
    • Nyholm, T.K.1
  • 25
  • 26
    • 0028083959 scopus 로고
    • Apparent inhibition of chloroplast protein import by cold temperatures is due to energetic considerations not membrane fluidity
    • Leheny EA, Theg SM. Apparent inhibition of chloroplast protein import by cold temperatures is due to energetic considerations not membrane fluidity. Plant Cell 1994;6:427-437.
    • (1994) Plant Cell , vol.6 , pp. 427-437
    • Leheny, E.A.1    Theg, S.M.2
  • 27
    • 0041669436 scopus 로고    scopus 로고
    • Protein translocation across the endoplasmic reticulum membrane in cold-adapted organisms
    • Römisch K, Collie N, Soto N, Logue J, Lindsay M, Scheper W, Cheng C-HC. Protein translocation across the endoplasmic reticulum membrane in cold-adapted organisms. J Cell Sci 2003;116:2875-2883.
    • (2003) J Cell Sci , vol.116 , pp. 2875-2883
    • Römisch, K.1    Collie, N.2    Soto, N.3    Logue, J.4    Lindsay, M.5    Scheper, W.6    Cheng, C.-H.7
  • 28
    • 84860481321 scopus 로고    scopus 로고
    • Pleiotropic effects of membrane cholesterol upon translocation of protein across the endoplasmic reticulum membrane
    • Yamamoto H, Fujita H, Kida Y, Sakaguchi M. Pleiotropic effects of membrane cholesterol upon translocation of protein across the endoplasmic reticulum membrane. Biochemistry 2012;51:3596-3605.
    • (2012) Biochemistry , vol.51 , pp. 3596-3605
    • Yamamoto, H.1    Fujita, H.2    Kida, Y.3    Sakaguchi, M.4
  • 31
    • 4344578601 scopus 로고    scopus 로고
    • Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids
    • Li Y, Ge M, Ciani L, Kuriakose G, Westover EJ, Dura M, Covey DF, Freed JH, Maxfield FR, Lytton J, Tabas I. Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids. J Biol Chem 2004;279:37030-37039.
    • (2004) J Biol Chem , vol.279 , pp. 37030-37039
    • Li, Y.1    Ge, M.2    Ciani, L.3    Kuriakose, G.4    Westover, E.J.5    Dura, M.6    Covey, D.F.7    Freed, J.H.8    Maxfield, F.R.9    Lytton, J.10    Tabas, I.11
  • 32
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky JL. Cleaning up: ER-associated degradation to the rescue. Cell 2012;151:1163-1167.
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 33
    • 0033725154 scopus 로고    scopus 로고
    • Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
    • Koopmann JO, Albring J, Hüter E, Bulbuc N, Spee P, Neefjes J, Hämmerling GJ, Momburg F. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel. Immunity 2000;13:117-127.
    • (2000) Immunity , vol.13 , pp. 117-127
    • Koopmann, J.O.1    Albring, J.2    Hüter, E.3    Bulbuc, N.4    Spee, P.5    Neefjes, J.6    Hämmerling, G.J.7    Momburg, F.8
  • 34
    • 33749522738 scopus 로고    scopus 로고
    • A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
    • Ackerman AL, Giodini A, Cresswell P. A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells. Immunity 2006;25:607-617.
    • (2006) Immunity , vol.25 , pp. 607-617
    • Ackerman, A.L.1    Giodini, A.2    Cresswell, P.3
  • 37
    • 0028135639 scopus 로고
    • Pharmacological modulation of endothelial cell-associated adhesion molecule expression: implications for future treatment of dermatological diseases
    • Foster CA, Dreyfuss M, Mandak B, Meingassner JG, Naegeli HU, Nussbaumer A, Oberer L, Scheel G, Swoboda EM. Pharmacological modulation of endothelial cell-associated adhesion molecule expression: implications for future treatment of dermatological diseases. J Dermatol 1994;21:847-854.
    • (1994) J Dermatol , vol.21 , pp. 847-854
    • Foster, C.A.1    Dreyfuss, M.2    Mandak, B.3    Meingassner, J.G.4    Naegeli, H.U.5    Nussbaumer, A.6    Oberer, L.7    Scheel, G.8    Swoboda, E.M.9
  • 38
    • 0026683256 scopus 로고
    • ICAM-1 expression in a spontaneously transformed human keratinocyte cell line: characterization by a simple cell-ELISA assay
    • Winiski AP, Foster CA. ICAM-1 expression in a spontaneously transformed human keratinocyte cell line: characterization by a simple cell-ELISA assay. J Invest Dermatol 1992;99:48-52.
    • (1992) J Invest Dermatol , vol.99 , pp. 48-52
    • Winiski, A.P.1    Foster, C.A.2
  • 40
    • 0037094115 scopus 로고    scopus 로고
    • Solution-phase parallel synthesis of a pharmacophore library of HUN-7293 analogues: a general chemical mutagenesis approach to defining structure-function properties of naturally occurring cyclic (depsi)peptides
    • Chen Y, Bilban M, Foster CA, Boger DL. Solution-phase parallel synthesis of a pharmacophore library of HUN-7293 analogues: a general chemical mutagenesis approach to defining structure-function properties of naturally occurring cyclic (depsi)peptides. J Am Chem Soc 2002;124:5431-5440.
    • (2002) J Am Chem Soc , vol.124 , pp. 5431-5440
    • Chen, Y.1    Bilban, M.2    Foster, C.A.3    Boger, D.L.4
  • 42
    • 33750081430 scopus 로고    scopus 로고
    • The translocation inhibitor CAM741 interferes with vascular cell adhesion molecule 1 signal peptide insertion at the translocon
    • Harant H, Lettner N, Hofer L, Oberhauser B, de Vries JE, Lindley IJ. The translocation inhibitor CAM741 interferes with vascular cell adhesion molecule 1 signal peptide insertion at the translocon. J Biol Chem 2006;281:30492-30502.
    • (2006) J Biol Chem , vol.281 , pp. 30492-30502
    • Harant, H.1    Lettner, N.2    Hofer, L.3    Oberhauser, B.4    de Vries, J.E.5    Lindley, I.J.6
  • 44
    • 22444450987 scopus 로고    scopus 로고
    • A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
    • Garrison JL, Kunkel EJ, Hegde RS, Taunton J. A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum. Nature 2005;436:285-289.
    • (2005) Nature , vol.436 , pp. 285-289
    • Garrison, J.L.1    Kunkel, E.J.2    Hegde, R.S.3    Taunton, J.4
  • 45
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang SW, Rane NS, Kim SJ, Garrison JL, Taunton J, Hegde RS. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 2006;127:999-1013.
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 48
    • 84876074679 scopus 로고    scopus 로고
    • Cotransin induces accumulation of a cytotoxic clusterin variant that cotranslationally rerouted to the cytosol
    • Choi I, Kim J, Park JY, Kang SW. Cotransin induces accumulation of a cytotoxic clusterin variant that cotranslationally rerouted to the cytosol. Exp Cell Res 2013;319:1073-1082.
    • (2013) Exp Cell Res , vol.319 , pp. 1073-1082
    • Choi, I.1    Kim, J.2    Park, J.Y.3    Kang, S.W.4
  • 50
    • 84898761276 scopus 로고    scopus 로고
    • An allosteric Sec61 inhibitor traps nascent transmembrane helices at the lateral gate
    • MacKinnon AL, Paavilainen VO, Sharma A, Hegde RS, Taunton J. An allosteric Sec61 inhibitor traps nascent transmembrane helices at the lateral gate. Elife 2014;3:e01483.
    • (2014) Elife , vol.3 , pp. e01483
    • MacKinnon, A.L.1    Paavilainen, V.O.2    Sharma, A.3    Hegde, R.S.4    Taunton, J.5
  • 51
    • 36749047362 scopus 로고    scopus 로고
    • Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation
    • MacKinnon AL, Garrison JL, Hegde RS, Taunton J. Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation. J Am Chem Soc 2007;129:14560-14561.
    • (2007) J Am Chem Soc , vol.129 , pp. 14560-14561
    • MacKinnon, A.L.1    Garrison, J.L.2    Hegde, R.S.3    Taunton, J.4
  • 52
    • 0034833620 scopus 로고    scopus 로고
    • Total structure determination of apratoxin A, a potent novel cytotoxin from the marine cyanobacterium Lyngbya majuscula
    • Luesch H, Yoshida WY, Moore RE, Paul VJ, Corbett TH. Total structure determination of apratoxin A, a potent novel cytotoxin from the marine cyanobacterium Lyngbya majuscula. J Am Chem Soc 2001;123:5418-5423.
    • (2001) J Am Chem Soc , vol.123 , pp. 5418-5423
    • Luesch, H.1    Yoshida, W.Y.2    Moore, R.E.3    Paul, V.J.4    Corbett, T.H.5
  • 54
    • 67649861838 scopus 로고    scopus 로고
    • Apratoxin A reversibly inhibits the secretory pathway by preventing cotranslational translocation
    • Liu Y, Law BK, Luesch H. Apratoxin A reversibly inhibits the secretory pathway by preventing cotranslational translocation. Mol Pharmacol 2009;76:91-104.
    • (2009) Mol Pharmacol , vol.76 , pp. 91-104
    • Liu, Y.1    Law, B.K.2    Luesch, H.3
  • 55
    • 78651192970 scopus 로고
    • Potassium transport-linked swelling induced by valinomycin in liver mitochondria
    • Azzi A, Azzone GF. Potassium transport-linked swelling induced by valinomycin in liver mitochondria. Biochem J 1965;96:1C-2C.
    • (1965) Biochem J , vol.96 , pp. 1C-2C
    • Azzi, A.1    Azzone, G.F.2
  • 56
    • 33645540155 scopus 로고    scopus 로고
    • Selective cytotoxic activity of valinomycin against HT-29 human colon carcinoma cells via down-regulation of GRP78
    • Ryoo IJ, Park HR, Choo SJ, Hwang JH, Park YM, Bae KH, Shin-Ya K, Yoo ID. Selective cytotoxic activity of valinomycin against HT-29 human colon carcinoma cells via down-regulation of GRP78. Biol Pharm Bull 2006;29:817-820.
    • (2006) Biol Pharm Bull , vol.29 , pp. 817-820
    • Ryoo, I.J.1    Park, H.R.2    Choo, S.J.3    Hwang, J.H.4    Park, Y.M.5    Bae, K.H.6    Shin-Ya, K.7    Yoo, I.D.8
  • 57
    • 84879886715 scopus 로고    scopus 로고
    • Specific inhibition of hamster prion protein translocation by the dodecadepsipeptide valinomycin
    • Kim J, Choi I, Park JY, Kang SW. Specific inhibition of hamster prion protein translocation by the dodecadepsipeptide valinomycin. Exp Cell Res 2013;319:2049-2057.
    • (2013) Exp Cell Res , vol.319 , pp. 2049-2057
    • Kim, J.1    Choi, I.2    Park, J.Y.3    Kang, S.W.4
  • 58
    • 82955195439 scopus 로고    scopus 로고
    • Perturbation of intracellular K(+) homeostasis with valinomycin promotes cell death by mitochondrial swelling and autophagic processes
    • Klein B, Worndl K, Lutz-Meindl U, Kerschbaum HH. Perturbation of intracellular K(+) homeostasis with valinomycin promotes cell death by mitochondrial swelling and autophagic processes. Apoptosis 2011;16:1101-1117.
    • (2011) Apoptosis , vol.16 , pp. 1101-1117
    • Klein, B.1    Worndl, K.2    Lutz-Meindl, U.3    Kerschbaum, H.H.4
  • 59
    • 33947717668 scopus 로고    scopus 로고
    • The effect of the ionophore valinomycin on biomimetic solid supported lipid DPPTE/EPC membranes
    • Rose L, Jenkins ATA. The effect of the ionophore valinomycin on biomimetic solid supported lipid DPPTE/EPC membranes. Bioelectrochemistry 2007;70:387-393.
    • (2007) Bioelectrochemistry , vol.70 , pp. 387-393
    • Rose, L.1    Jenkins, A.T.A.2
  • 60
    • 7744237428 scopus 로고    scopus 로고
    • CADA, a novel CD4-targeted HIV inhibitor, is synergistic with various anti-HIV drugs in vitro
    • Vermeire K, Princen K, Hatse S, De Clercq E, Dey K, Bell TW, Schols D. CADA, a novel CD4-targeted HIV inhibitor, is synergistic with various anti-HIV drugs in vitro. AIDS 2004;18:2115-2125.
    • (2004) AIDS , vol.18 , pp. 2115-2125
    • Vermeire, K.1    Princen, K.2    Hatse, S.3    De Clercq, E.4    Dey, K.5    Bell, T.W.6    Schols, D.7
  • 62
    • 0037220770 scopus 로고    scopus 로고
    • The anti-HIV potency of cyclotriazadisulfonamide analogs is directly correlated with their ability to down-modulate the CD4 receptor
    • Vermeire K, Bell TW, Choi HJ, Jin Q, Samala MF, Sodoma A, De Clercq E, Schols D. The anti-HIV potency of cyclotriazadisulfonamide analogs is directly correlated with their ability to down-modulate the CD4 receptor. Mol Pharmacol 2003;63:203-210.
    • (2003) Mol Pharmacol , vol.63 , pp. 203-210
    • Vermeire, K.1    Bell, T.W.2    Choi, H.J.3    Jin, Q.4    Samala, M.F.5    Sodoma, A.6    De Clercq, E.7    Schols, D.8
  • 65
    • 61449255984 scopus 로고    scopus 로고
    • Mycolactone inhibits monocyte cytokine production by a posttranscriptional mechanism
    • Simmonds RE, Lali FV, Smallie T, Small PL, Foxwell BM. Mycolactone inhibits monocyte cytokine production by a posttranscriptional mechanism. J Immunol 2009;182:2194-2202.
    • (2009) J Immunol , vol.182 , pp. 2194-2202
    • Simmonds, R.E.1    Lali, F.V.2    Smallie, T.3    Small, P.L.4    Foxwell, B.M.5
  • 66
    • 84901374066 scopus 로고    scopus 로고
    • The pathogenic mechanism of the Mycobacterium ulcerance virulence factor, mycolactone, depends on blockade of protein translocation into the ER
    • Hall BS, Hill K, McKenna M, Ogbechi J, High S, Willis AE, Simmonds RE. The pathogenic mechanism of the Mycobacterium ulcerance virulence factor, mycolactone, depends on blockade of protein translocation into the ER. PLoS Pathog 2014;10:e1004061.
    • (2014) PLoS Pathog , vol.10 , pp. e1004061
    • Hall, B.S.1    Hill, K.2    McKenna, M.3    Ogbechi, J.4    High, S.5    Willis, A.E.6    Simmonds, R.E.7
  • 67
    • 1642505493 scopus 로고    scopus 로고
    • Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin
    • Fiebiger E, Hirsch C, Vyas JM, Gordon E, Ploegh HL, Tortorella D. Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin. Mol Biol Cell 2004;15:1635-1646.
    • (2004) Mol Biol Cell , vol.15 , pp. 1635-1646
    • Fiebiger, E.1    Hirsch, C.2    Vyas, J.M.3    Gordon, E.4    Ploegh, H.L.5    Tortorella, D.6
  • 68
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by eeyarestatin I
    • Wang Q, Li L, Ye Y. Inhibition of p97-dependent protein degradation by eeyarestatin I. J Biol Chem 2008;283:7445-7454.
    • (2008) J Biol Chem , vol.283 , pp. 7445-7454
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 71
    • 78649742954 scopus 로고    scopus 로고
    • The ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domainand a p97/VCP inhibitory group
    • Wang Q, Shinkre BA, Lee J, Weniger MA, Liu Y, Chen W, Wiestner A, Trenkle WC, Ye Y. The ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domainand a p97/VCP inhibitory group. PLoS One 2010;5:e15479.
    • (2010) PLoS One , vol.5 , pp. e15479
    • Wang, Q.1    Shinkre, B.A.2    Lee, J.3    Weniger, M.A.4    Liu, Y.5    Chen, W.6    Wiestner, A.7    Trenkle, W.C.8    Ye, Y.9
  • 73
    • 0034712930 scopus 로고    scopus 로고
    • The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane
    • Gillece P, Pilon M, Römisch K. The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 2000;97:4609-4614.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4609-4614
    • Gillece, P.1    Pilon, M.2    Römisch, K.3
  • 74
    • 0032969203 scopus 로고    scopus 로고
    • The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by shiga-like toxin-1 during retrograde transport from the Golgi complex to the endoplasmic reticulum
    • Jackson ME, Simpson JC, Girod A, Pepperkok R, Roberts LM, Lord JM. The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by shiga-like toxin-1 during retrograde transport from the Golgi complex to the endoplasmic reticulum. J Cell Sci 1999;112:467-475.
    • (1999) J Cell Sci , vol.112 , pp. 467-475
    • Jackson, M.E.1    Simpson, J.C.2    Girod, A.3    Pepperkok, R.4    Roberts, L.M.5    Lord, J.M.6
  • 76
    • 84901437696 scopus 로고    scopus 로고
    • Interaction of Pseudomonas aeruginosa exotoxin A with the human Sec61 complex suppresses passive calcium efflux from the endoplasmic reticulum
    • Schäuble N, Cavalie A, Zimmermann R, Jung M. Interaction of Pseudomonas aeruginosa exotoxin A with the human Sec61 complex suppresses passive calcium efflux from the endoplasmic reticulum. Channels (Austin) 2014;8:76-83.
    • (2014) Channels (Austin) , vol.8 , pp. 76-83
    • Schäuble, N.1    Cavalie, A.2    Zimmermann, R.3    Jung, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.