메뉴 건너뛰기




Volumn 7, Issue 1, 2015, Pages 49-65

Ricin trafficking in cells

Author keywords

Chaperone; ER cytosol retrotranslocation; ERP2; HRD1; P24 proteins; Proteasome; Ricin; RPT

Indexed keywords

CALRETICULIN; CHAPERONE; CHOLESTEROL; COAT PROTEIN COMPLEX II; DITHIOTHREITOL; DYNAMIN; GAG PROTEIN; HEAT SHOCK COGNATE PROTEIN 70; PROTEASOME; RICIN; SPHINGOLIPID;

EID: 84921771734     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins7010049     Document Type: Article
Times cited : (72)

References (81)
  • 1
    • 0042311010 scopus 로고    scopus 로고
    • Role of lipids in the retrograde pathway of ricin intoxication
    • Spilsberg, B.; van Meer, G.; Sandvig, K. Role of lipids in the retrograde pathway of ricin intoxication. Traffic 2003, 4, 544-552.
    • (2003) Traffic , vol.4 , pp. 544-552
    • Spilsberg, B.1    van Meer, G.2    Sandvig, K.3
  • 3
    • 0017074398 scopus 로고
    • Kinetics of binding of the toxic lectins abrin and ricin to surface receptors of human cells
    • Sandvig, K.; Olsnes, S.; Pihl, A. Kinetics of binding of the toxic lectins abrin and ricin to surface receptors of human cells. J. Biol. Chem. 1976, 251, 3977-3984.
    • (1976) J. Biol. Chem , vol.251 , pp. 3977-3984
    • Sandvig, K.1    Olsnes, S.2    Pihl, A.3
  • 4
    • 0031868419 scopus 로고    scopus 로고
    • Expression of mutant dynamin protects cells against diphtheria toxin but not against ricin
    • Simpson, J.C.; Smith, D.C.; Roberts, L.M.; Lord, J.M. Expression of mutant dynamin protects cells against diphtheria toxin but not against ricin. Exp. Cell. Res. 1998, 239, 293-300.
    • (1998) Exp. Cell. Res , vol.239 , pp. 293-300
    • Simpson, J.C.1    Smith, D.C.2    Roberts, L.M.3    Lord, J.M.4
  • 5
    • 0022005540 scopus 로고
    • Inhibition of coated pit formation in Hep2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin toxin
    • Moya, M.; Dautry-Varsat, A.; Goud, B.; Louvard, D.; Boquet, P. Inhibition of coated pit formation in Hep2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin toxin. J. Cell. Biol. 1985, 101, 548-559.
    • (1985) J. Cell. Biol , vol.101 , pp. 548-559
    • Moya, M.1    Dautry-Varsat, A.2    Goud, B.3    Louvard, D.4    Boquet, P.5
  • 6
    • 0023837074 scopus 로고
    • Inhibition of endocytosis from coated pits by acidification of the cytosol
    • Sandvig, K.; Olsnes, S.; Petersen, O.W.; van Deurs, B. Inhibition of endocytosis from coated pits by acidification of the cytosol. J. Cell. Biochem. 1988, 36, 73-81.
    • (1988) J. Cell. Biochem , vol.36 , pp. 73-81
    • Sandvig, K.1    Olsnes, S.2    Petersen, O.W.3    van Deurs, B.4
  • 7
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves, P.J.; Callewaert, N.; Contreras, R.; Khorana, H.G. Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. USA 2002, 99, 13419-13424.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 13
    • 0030929658 scopus 로고    scopus 로고
    • Retrograde transporrt of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol
    • Rapak, A.; Falnes, P.O.; Olsnes, S. Retrograde transporrt of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol. Proc. Natl. Acad. Sci. USA 1997, 94, 3783-3788.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3783-3788
    • Rapak, A.1    Falnes, P.O.2    Olsnes, S.3
  • 14
    • 0033607688 scopus 로고    scopus 로고
    • Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol
    • Wesche, J.; Rapak, A.; Olsnes, S. Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol. J. Biol. Chem. 1999, 274, 34443-34449.
    • (1999) J. Biol. Chem , vol.274 , pp. 34443-34449
    • Wesche, J.1    Rapak, A.2    Olsnes, S.3
  • 15
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins
    • Endo, Y.; Mitsui, K.; Motizuki, M.; Tsurugi, K. The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J. Biol. Chem. 1987, 262, 5908-5912.
    • (1987) J. Biol. Chem , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 16
    • 84857866006 scopus 로고    scopus 로고
    • Ricin and Shiga toxins: Effects on host cell signal transduction
    • Jandhyala, D.M.; Thorpe, C.M.; Magun, B. Ricin and Shiga toxins: effects on host cell signal transduction. Curr. Top. Microbiol. Immunol. 2012, 357, 41-65.
    • (2012) Curr. Top. Microbiol. Immunol , vol.357 , pp. 41-65
    • Jandhyala, D.M.1    Thorpe, C.M.2    Magun, B.3
  • 17
    • 84857826373 scopus 로고    scopus 로고
    • The induction of apoptosis by Shiga toxins and ricin
    • Tesh, V.L. The induction of apoptosis by Shiga toxins and ricin. Curr. Top. Microbiol. Immunol. 2012, 357, 137-178.
    • (2012) Curr. Top. Microbiol. Immunol , vol.357 , pp. 137-178
    • Tesh, V.L.1
  • 18
    • 0032498544 scopus 로고    scopus 로고
    • Expression of mutant dynamin inhibits toxicity and transport of endocytosed ricin to the Golgi apparatus
    • Llorente, A.; Rapak, A.; Schmid, S.L.; van Deurs, B.; Sandvig, K. Expression of mutant dynamin inhibits toxicity and transport of endocytosed ricin to the Golgi apparatus. J. Cell. Biol. 1998, 140, 553-563.
    • (1998) J. Cell. Biol , vol.140 , pp. 553-563
    • Llorente, A.1    Rapak, A.2    Schmid, S.L.3    van Deurs, B.4    Sandvig, K.5
  • 19
    • 0033634889 scopus 로고    scopus 로고
    • Endosome to Golgi transport of ricin is regulated by cholesterol
    • Grimmer, S.; Iversen, T.G.; van Deurs, B.; Sandvig, K. Endosome to Golgi transport of ricin is regulated by cholesterol. Mol. Biol. Cell. 2000, 11, 4205-4216.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4205-4216
    • Grimmer, S.1    Iversen, T.G.2    van Deurs, B.3    Sandvig, K.4
  • 20
    • 0035831558 scopus 로고    scopus 로고
    • An interaction between ricin and calreticulin that may have implications for toxin trafficking
    • Day, P.J.; Owens, S.R.; Wesche, J.; Olsnes, S.; Roberts, L.M.; Lord, J.M. An interaction between ricin and calreticulin that may have implications for toxin trafficking. J. Biol. Chem. 2001, 276, 7202-7208.
    • (2001) J. Biol. Chem , vol.276 , pp. 7202-7208
    • Day, P.J.1    Owens, S.R.2    Wesche, J.3    Olsnes, S.4    Roberts, L.M.5    Lord, J.M.6
  • 22
    • 33646423848 scopus 로고    scopus 로고
    • Transport of ricin from endosomes to the Golgi apparatus is regulated by Rab6A and Rab6A’
    • Utskarpen, A.; Slagsvold, H.H.; Iversen, T.G.; Walchli, S.; Sandvig, K. Transport of ricin from endosomes to the Golgi apparatus is regulated by Rab6A and Rab6A’. Traffic 2006, 7, 663-672.
    • (2006) Traffic , vol.7 , pp. 663-672
    • Utskarpen, A.1    Slagsvold, H.H.2    Iversen, T.G.3    Walchli, S.4    Sandvig, K.5
  • 23
    • 33747058472 scopus 로고    scopus 로고
    • Depletion of sphingolipids facilitates endosome to Golgi transport of ricin
    • Grimmer, S.; Spilsberg, B.; Hanada, K.; Sandvig, K. Depletion of sphingolipids facilitates endosome to Golgi transport of ricin. Traffic 2006, 7, 1243-1253.
    • (2006) Traffic , vol.7 , pp. 1243-1253
    • Grimmer, S.1    Spilsberg, B.2    Hanada, K.3    Sandvig, K.4
  • 24
    • 77749249684 scopus 로고    scopus 로고
    • Interplay between toxin transport and flotillin localization
    • Pust, S.; Dyve, A.B.; Torgersen, M.L.; van Deurs, B.; Sandvig, K. Interplay between toxin transport and flotillin localization. PLoS One 2010, 5, doi:10.1371/journal.pone.0008844.
    • (2010) PLoS One , vol.5
    • Pust, S.1    Dyve, A.B.2    Torgersen, M.L.3    van Deurs, B.4    Sandvig, K.5
  • 25
    • 0035150144 scopus 로고    scopus 로고
    • Endosome to Golgi transport of ricin is independent of clathrin and of the Rab9- and Rab11-GTPases
    • Iversen, T.G.; Skretting, G.; Llorente, A.; Nicoziani, P.; van Deurs, B.; Sandvig, K. Endosome to Golgi transport of ricin is independent of clathrin and of the Rab9- and Rab11-GTPases. Mol. Biol. Cell. 2001, 12, 2099-2107.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2099-2107
    • Iversen, T.G.1    Skretting, G.2    Llorente, A.3    Nicoziani, P.4    van Deurs, B.5    Sandvig, K.6
  • 27
    • 0023239830 scopus 로고
    • Delivery of internalized ricin from endosomes to cisternal Golgi elements is a discontinuous, temperature-sensitive process
    • Van Deurs, B.; Petersen, O.W.; Olsnes, S.; Sandvig, K. Delivery of internalized ricin from endosomes to cisternal Golgi elements is a discontinuous, temperature-sensitive process. Exp. Cell. Res. 1987, 171, 137-152.
    • (1987) Exp. Cell. Res , vol.171 , pp. 137-152
    • Van Deurs, B.1    Petersen, O.W.2    Olsnes, S.3    Sandvig, K.4
  • 29
    • 0024288476 scopus 로고
    • Separation of ricin A- and B-chains after dithiothreitol reduction
    • Emmanuel, F.; Turpin, E.; Alfsen, A.; Frenoy, J.P. Separation of ricin A- and B-chains after dithiothreitol reduction. Anal. Biochem. 1988, 173, 134-141.
    • (1988) Anal. Biochem , vol.173 , pp. 134-141
    • Emmanuel, F.1    Turpin, E.2    Alfsen, A.3    Frenoy, J.P.4
  • 30
    • 0029379790 scopus 로고
    • Catalytic and cytotoxic activities of recombinant ricin A chain mutants with charged residues added at the carboxyl terminus
    • Simpson, J.C.; Roberts, L.M.; Lord, J.M. Catalytic and cytotoxic activities of recombinant ricin A chain mutants with charged residues added at the carboxyl terminus. Protein Expr. Purif. 1995, 6, 665-670.
    • (1995) Protein Expr. Purif , vol.6 , pp. 665-670
    • Simpson, J.C.1    Roberts, L.M.2    Lord, J.M.3
  • 31
    • 84857880542 scopus 로고    scopus 로고
    • How ricin and Shiga toxin reach the cytosol of target cells: Retrotranslocation from the endoplasmic reticulum
    • Spooner, R.A.; Lord, J.M. How ricin and Shiga toxin reach the cytosol of target cells: Retrotranslocation from the endoplasmic reticulum. Curr. Top. Microbiol. Immunol. 2012, 357, 19-40.
    • (2012) Curr. Top. Microbiol. Immunol , vol.357 , pp. 19-40
    • Spooner, R.A.1    Lord, J.M.2
  • 33
    • 84857746992 scopus 로고    scopus 로고
    • Reductive activation of type 2 ribosome-inactivating proteins is promoted by transmembrane thioredoxin-related protein
    • Pasetto, M.; Barison, E.; Castagna, M.; della Cristina, P.; Anselmi, C.; Colombatti, M. Reductive activation of type 2 ribosome-inactivating proteins is promoted by transmembrane thioredoxin-related protein. J. Biol. Chem. 2012, 287, 7367-7373.
    • (2012) J. Biol. Chem , vol.287 , pp. 7367-7373
    • Pasetto, M.1    Barison, E.2    Castagna, M.3    della Cristina, P.4    Anselmi, C.5    Colombatti, M.6
  • 35
    • 33749656178 scopus 로고    scopus 로고
    • Thermal inactivation of ricin using infant formula as a food matrix
    • Jackson, L.S.; Tolleson, W.H.; Chirtel, S.J. Thermal inactivation of ricin using infant formula as a food matrix. J. Agric. Food Chem. 2006, 54, 7300-7304.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 7300-7304
    • Jackson, L.S.1    Tolleson, W.H.2    Chirtel, S.J.3
  • 36
    • 0027138758 scopus 로고
    • Endosomal proteolysis precedes ricin A-chain toxicity in macrophages
    • Fiani, M.L.; Blum, J.S.; Stahl, P.D. Endosomal proteolysis precedes ricin A-chain toxicity in macrophages. Arch. Biochem. Biophys. 1993, 307, 225-230.
    • (1993) Arch. Biochem. Biophys , vol.307 , pp. 225-230
    • Fiani, M.L.1    Blum, J.S.2    Stahl, P.D.3
  • 37
    • 0025719150 scopus 로고
    • Proteolytic cleavage of ricin A chain in endosomal vesicles. Evidence for the action of endosomal proteases at both neutral and acidic pH
    • Blum, J.S.; Fiani, M.L.; Stahl, P.D. Proteolytic cleavage of ricin A chain in endosomal vesicles. Evidence for the action of endosomal proteases at both neutral and acidic pH. J. Biol. Chem. 1991, 266, 22091-22095.
    • (1991) J. Biol. Chem , vol.266 , pp. 22091-22095
    • Blum, J.S.1    Fiani, M.L.2    Stahl, P.D.3
  • 40
    • 77955106651 scopus 로고    scopus 로고
    • Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum
    • Li, S.; Spooner, R.A.; Allen, S.C.; Guise, C.P.; Ladds, G.; Schnöder, T.; Schmitt, M.J.; Lord, J.M.; Roberts, L.M. Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum. Mol. Biol. Cell. 2010, 21, 2543-2554.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2543-2554
    • Li, S.1    Spooner, R.A.2    Allen, S.C.3    Guise, C.P.4    Ladds, G.5    Schnöder, T.6    Schmitt, M.J.7    Lord, J.M.8    Roberts, L.M.9
  • 41
    • 77957817389 scopus 로고    scopus 로고
    • Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol
    • Taylor, M.; Navarro-Garcia, F.; Huerta, J.; Burress, H.; Massey, S.; Ireton, K.; Teter, K. Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol. J. Biol. Chem. 2010, 285, 31261-31267.
    • (2010) J. Biol. Chem , vol.285 , pp. 31261-31267
    • Taylor, M.1    Navarro-Garcia, F.2    Huerta, J.3    Burress, H.4    Massey, S.5    Ireton, K.6    Teter, K.7
  • 42
    • 84891096975 scopus 로고    scopus 로고
    • Novel class of potential therapeutics that target ricin retrograde translocation
    • Redmann, V.; Gardner, T.; Lau, Z.; Morohashi, K.; Felsenfeld, D.; Tortorella, D. Novel class of potential therapeutics that target ricin retrograde translocation. Toxins 2014, 6, 33-53.
    • (2014) Toxins , vol.6 , pp. 33-53
    • Redmann, V.1    Gardner, T.2    Lau, Z.3    Morohashi, K.4    Felsenfeld, D.5    Tortorella, D.6
  • 43
    • 33745395593 scopus 로고    scopus 로고
    • EDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol
    • Slominska-Wojewodzka, M.; Gregers, T.F.; Walchli, S.; Sandvig, K. EDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol. Mol. Biol. Cell. 2006, 17, 1664-1675.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1664-1675
    • Slominska-Wojewodzka, M.1    Gregers, T.F.2    Walchli, S.3    Sandvig, K.4
  • 44
    • 84892176396 scopus 로고    scopus 로고
    • The role of EDEM2 compared with EDEM1 in ricin transport from the endoplasmic reticulum to the cytosol
    • Slominska-Wojewodzka, M.; Pawlik, A.; Sokolowska, I.; Antoniewicz, J.; Wegrzyn, G.; Sandvig, K. The role of EDEM2 compared with EDEM1 in ricin transport from the endoplasmic reticulum to the cytosol. Biochem. J. 2014, 457, 485-496.
    • (2014) Biochem. J , vol.457 , pp. 485-496
    • Slominska-Wojewodzka, M.1    Pawlik, A.2    Sokolowska, I.3    Antoniewicz, J.4    Wegrzyn, G.5    Sandvig, K.6
  • 45
    • 79956042755 scopus 로고    scopus 로고
    • A single point mutation in ricin A-chain increases toxin degradation and inhibits EDEM1-dependent ER retrotranslocation
    • Sokolowska, I.; Walchli, S.; Wegrzyn, G.; Sandvig, K.; Slominska-Wojewodzka, M. A single point mutation in ricin A-chain increases toxin degradation and inhibits EDEM1-dependent ER retrotranslocation. Biochem. J. 2011, 436, 371-385.
    • (2011) Biochem. J , vol.436 , pp. 371-385
    • Sokolowska, I.1    Walchli, S.2    Wegrzyn, G.3    Sandvig, K.4    Slominska-Wojewodzka, M.5
  • 47
    • 67849130558 scopus 로고    scopus 로고
    • TOPCONS: Consensus prediction of membrane protein topology
    • Bernsel, A.; Viklund, H.; Hennerdal, A.; Elofsson, A. TOPCONS: Consensus prediction of membrane protein topology. Nucleic Acids Res. 2009, 37, W465-W468.
    • (2009) Nucleic Acids Res , vol.37 , pp. W465-W468
    • Bernsel, A.1    Viklund, H.2    Hennerdal, A.3    Elofsson, A.4
  • 48
    • 79954493200 scopus 로고    scopus 로고
    • Rapid membrane protein topology prediction
    • Hennerdal, A.; Elofsson, A. Rapid membrane protein topology prediction. Bioinformatics 2011, 27, 1322-1323.
    • (2011) Bioinformatics , vol.27 , pp. 1322-1323
    • Hennerdal, A.1    Elofsson, A.2
  • 49
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith, M.H.; Ploegh, H.L.; Weissman, J.S. Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum. Science 2011, 334, 1086-1090.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 50
    • 35448960024 scopus 로고    scopus 로고
    • The isolation and characterization of temperature-dependent ricin A chain molecules in Saccharomyces cerevisiae
    • Allen, S.C.; Moore, K.A.; Marsden, C.J.; Fulop, V.; Moffat, K.G.; Lord, J.M.; Ladds, G.; Roberts, L.M. The isolation and characterization of temperature-dependent ricin A chain molecules in Saccharomyces cerevisiae. FEBS J. 2007, 274, 5586-5599.
    • (2007) FEBS J , vol.274 , pp. 5586-5599
    • Allen, S.C.1    Moore, K.A.2    Marsden, C.J.3    Fulop, V.4    Moffat, K.G.5    Lord, J.M.6    Ladds, G.7    Roberts, L.M.8
  • 51
    • 44449144592 scopus 로고    scopus 로고
    • Ricin inhibits activation of the unfolded protein response by preventing splicing of the HAC1 mRNA
    • Parikh, B.A.; Tortora, A.; Li, X.P.; Tumer, N.E. Ricin inhibits activation of the unfolded protein response by preventing splicing of the HAC1 mRNA. J. Biol. Chem. 2008, 283, 6145-6153.
    • (2008) J. Biol. Chem , vol.283 , pp. 6145-6153
    • Parikh, B.A.1    Tortora, A.2    Li, X.P.3    Tumer, N.E.4
  • 52
    • 70450225048 scopus 로고    scopus 로고
    • ER exit sites-Localization and control of COPII vesicle formation
    • Budnik, A.; Stephens, D.J. ER exit sites-Localization and control of COPII vesicle formation. FEBS Lett. 2009, 583, 3796-3803.
    • (2009) FEBS Lett , vol.583 , pp. 3796-3803
    • Budnik, A.1    Stephens, D.J.2
  • 53
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
    • Vashist, S.; Kim, W.; Belden, W.J.; Spear, E.D.; Barlowe, C.; Ng, D.T. Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J. Cell. Biol. 2001, 155, 355-368.
    • (2001) J. Cell. Biol , vol.155 , pp. 355-368
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5    Ng, D.T.6
  • 54
    • 48249138088 scopus 로고    scopus 로고
    • Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated Degradation
    • Wakana, Y.; Takai, S.; Nakajima, K.; Tani, K.; Yamamoto, A.; Watson, P.; Stephens, D.J.; Hauri, H.P.; Tagaya, M. Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated Degradation. Mol. Biol. Cell. 2008, 19, 1825-1836.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1825-1836
    • Wakana, Y.1    Takai, S.2    Nakajima, K.3    Tani, K.4    Yamamoto, A.5    Watson, P.6    Stephens, D.J.7    Hauri, H.P.8    Tagaya, M.9
  • 55
    • 79951510404 scopus 로고    scopus 로고
    • p24 Proteins from the same subfamily are functionally nonredundant
    • Strating, J.R.; Bouw, G.; Hafmans, T.G.; Martens, G.J. p24 Proteins from the same subfamily are functionally nonredundant. Biochimie 2011, 93, 528-532.
    • (2011) Biochimie , vol.93 , pp. 528-532
    • Strating, J.R.1    Bouw, G.2    Hafmans, T.G.3    Martens, G.J.4
  • 56
    • 70149084008 scopus 로고    scopus 로고
    • The p24 family and selective transport processes at the ER-Golgi interface
    • Strating, J.R.; Martens, G.J. The p24 family and selective transport processes at the ER-Golgi interface. Biol. Cell 2009, 101, 495-509.
    • (2009) Biol. Cell , vol.101 , pp. 495-509
    • Strating, J.R.1    Martens, G.J.2
  • 58
    • 0030015550 scopus 로고    scopus 로고
    • Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations
    • Elrod-Erickson, M.J.; Kaiser, C.A. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol. Biol. Cell. 1996, 7, 1043-1058.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1043-1058
    • Elrod-Erickson, M.J.1    Kaiser, C.A.2
  • 61
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page, R.D. TreeView: An application to display phylogenetic trees on personal computers. Compt. Appl. Biosci. 1996, 12, 357-358.
    • (1996) Compt. Appl. Biosci , vol.12 , pp. 357-358
    • Page, R.D.1
  • 62
    • 0036047057 scopus 로고    scopus 로고
    • The GOLD domain, a novel protein module involved in Golgi function and secretion
    • Anantharaman, V.; Aravind, L. The GOLD domain, a novel protein module involved in Golgi function and secretion. Genome Biol. 2002, 3, doi:10.1186/gb-2002-3-5-research0023.
    • (2002) Genome Biol , vol.3
    • Anantharaman, V.1    Aravind, L.2
  • 63
    • 0034708445 scopus 로고    scopus 로고
    • Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway
    • Ciufo, L.F.; Boyd, A. Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway. J. Biol. Chem. 2000, 275, 8382-8388.
    • (2000) J. Biol. Chem , vol.275 , pp. 8382-8388
    • Ciufo, L.F.1    Boyd, A.2
  • 64
    • 12444339783 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat
    • Contreras, I.; Yang, Y.; Robinson, D.G.; Aniento, F. Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat. Plant. Cell Physiol. 2004, 45, 1779-1786.
    • (2004) Plant. Cell Physiol , vol.45 , pp. 1779-1786
    • Contreras, I.1    Yang, Y.2    Robinson, D.G.3    Aniento, F.4
  • 66
    • 84867229684 scopus 로고    scopus 로고
    • N-glycosylation does not affect the catalytic activity of ricin a chain but stimulates cytotoxicity by promoting its transport out of the endoplasmic reticulum
    • Yan, Q.; Li, X.P.; Tumer, N.E. N-glycosylation does not affect the catalytic activity of ricin a chain but stimulates cytotoxicity by promoting its transport out of the endoplasmic reticulum. Traffic 2012, 13, 1508-1521.
    • (2012) Traffic , vol.13 , pp. 1508-1521
    • Yan, Q.1    Li, X.P.2    Tumer, N.E.3
  • 67
    • 0029147513 scopus 로고
    • Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex
    • Simpson, J.C.; Dascher, C.; Roberts, L.M.; Lord, J.M.; Balch, W.E. Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex. J. Biol. Chem. 1995, 270, 20078-20083.
    • (1995) J. Biol. Chem , vol.270 , pp. 20078-20083
    • Simpson, J.C.1    Dascher, C.2    Roberts, L.M.3    Lord, J.M.4    Balch, W.E.5
  • 69
    • 77949351438 scopus 로고    scopus 로고
    • Modularity of the Hrd1 ERAD complex underlies its diverse client range
    • Kanehara, K.; Xie, W.; Ng, D.T. Modularity of the Hrd1 ERAD complex underlies its diverse client range. J. Cell. Biol. 2010, 188, 707-716.
    • (2010) J. Cell. Biol , vol.188 , pp. 707-716
    • Kanehara, K.1    Xie, W.2    Ng, D.T.3
  • 70
    • 79958695548 scopus 로고    scopus 로고
    • Dislocation of ricin toxin A chains in human cells utilizes selective cellular factors
    • Redmann, V.; Oresic, K.; Tortorella, L.L.; Cook, J.P.; Lord, M.; Tortorella, D. Dislocation of ricin toxin A chains in human cells utilizes selective cellular factors. J. Biol. Chem. 2011, 286, 21231-21238.
    • (2011) J. Biol. Chem , vol.286 , pp. 21231-21238
    • Redmann, V.1    Oresic, K.2    Tortorella, L.L.3    Cook, J.P.4    Lord, M.5    Tortorella, D.6
  • 71
    • 84864051812 scopus 로고    scopus 로고
    • Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p
    • Li, S.; Spooner, R.A.; Hampton, R.Y.; Lord, J.M.; Roberts, L.M. Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p. PLoS One 2012, 7, doi:10.1371/journal.pone.0041119.
    • (2012) PLoS One , vol.7
    • Li, S.1    Spooner, R.A.2    Hampton, R.Y.3    Lord, J.M.4    Roberts, L.M.5
  • 72
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • Sato, B.K.; Schulz, D.; Do, P.H.; Hampton, R.Y. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol. Cell. 2009, 34, 212-222.
    • (2009) Mol. Cell , vol.34 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 73
    • 0030886889 scopus 로고    scopus 로고
    • Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
    • Hazes, B.; Read, R.J. Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells. Biochemistry 1997, 36, 11051-11054.
    • (1997) Biochemistry , vol.36 , pp. 11051-11054
    • Hazes, B.1    Read, R.J.2
  • 74
    • 33845991518 scopus 로고    scopus 로고
    • Determinants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase
    • Bazirgan, O.A.; Garza, R.M.; Hampton, R.Y. Determinants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase. J. Biol. Chem. 2006, 281, 38989-39001.
    • (2006) J. Biol. Chem , vol.281 , pp. 38989-39001
    • Bazirgan, O.A.1    Garza, R.M.2    Hampton, R.Y.3
  • 76
    • 30344460667 scopus 로고    scopus 로고
    • The role of p97/Cdc48p in endoplasmic reticulum-associated degradation: From the immune system to yeast
    • Bar-Nun, S. The role of p97/Cdc48p in endoplasmic reticulum-associated degradation: From the immune system to yeast. Curr. Top. Microbiol. Immunol. 2005, 300, 95-125.
    • (2005) Curr. Top. Microbiol. Immunol , vol.300 , pp. 95-125
    • Bar-Nun, S.1
  • 77
    • 79953722543 scopus 로고    scopus 로고
    • Ubiquitylation in ERAD: Reversing to go forward?
    • Tsai, Y.C.; Weissman, A.M. Ubiquitylation in ERAD: Reversing to go forward? PLoS Biol. 2011, 9, doi:10.1371/journal.pbio.1001038.
    • (2011) PLoS Biol , vol.9
    • Tsai, Y.C.1    Weissman, A.M.2
  • 79
    • 43149093941 scopus 로고    scopus 로고
    • A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates
    • Lipson, C.; Alalouf, G.; Bajorek, M.; Rabinovich, E.; Atir-Lande, A.; Glickman, M.; Bar-Nun, S. A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates. J. Biol. Chem. 2008, 283, 7166-7175.
    • (2008) J. Biol. Chem , vol.283 , pp. 7166-7175
    • Lipson, C.1    Alalouf, G.2    Bajorek, M.3    Rabinovich, E.4    Atir-Lande, A.5    Glickman, M.6    Bar-Nun, S.7
  • 80
    • 0037066109 scopus 로고    scopus 로고
    • The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol
    • Deeks, E.D.; Cook, J.P.; Day, P.J.; Smith, D.C.; Roberts, L.M.; Lord, J.M. The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol. Biochemistry 2002, 41, 3405-3413.
    • (2002) Biochemistry , vol.41 , pp. 3405-3413
    • Deeks, E.D.1    Cook, J.P.2    Day, P.J.3    Smith, D.C.4    Roberts, L.M.5    Lord, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.