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Volumn 7, Issue 4, 2012, Pages

A redox-sensitive luciferase assay for determining the localization and topology of endoplasmic reticulum proteins

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LUCIFERASE; MEMBRANE PROTEIN; PROTEIN HERP; PROTEIN HRD1; UNCLASSIFIED DRUG;

EID: 84859942953     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035628     Document Type: Article
Times cited : (9)

References (22)
  • 1
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
    • Buchberger A, Bukau B, Sommer T, (2010) Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell 40: 238-252.
    • (2010) Mol Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 2
    • 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 Cell Biol 4: 181-191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 5
    • 63049127493 scopus 로고    scopus 로고
    • Topology of mammalian isoprenylcysteine carboxyl methyltransferase determined in live cells with a fluorescent probe
    • Wright LP, Court H, Mor A, Ahearn IM, Casey PJ, et al. (2009) Topology of mammalian isoprenylcysteine carboxyl methyltransferase determined in live cells with a fluorescent probe. Mol Cell Biol 29: 1826-1833.
    • (2009) Mol Cell Biol , vol.29 , pp. 1826-1833
    • Wright, L.P.1    Court, H.2    Mor, A.3    Ahearn, I.M.4    Casey, P.J.5
  • 6
    • 58849150788 scopus 로고    scopus 로고
    • Non-invasive topology analysis of membrane proteins in the secretory pathway
    • Brach T, Soyk S, Muller C, Hinz G, Hell R, et al. (2009) Non-invasive topology analysis of membrane proteins in the secretory pathway. Plant J 57: 534-541.
    • (2009) Plant J , vol.57 , pp. 534-541
    • Brach, T.1    Soyk, S.2    Muller, C.3    Hinz, G.4    Hell, R.5
  • 7
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy I, Michnick SW, (2006) A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat Methods 3: 977-979.
    • (2006) Nat Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 8
    • 33646357780 scopus 로고    scopus 로고
    • Fluorescence protease protection of GFP chimeras to reveal protein topology and subcellular localization
    • Lorenz H, Hailey DW, Lippincott-Schwartz J, (2006) Fluorescence protease protection of GFP chimeras to reveal protein topology and subcellular localization. Nat Methods 3: 205-210.
    • (2006) Nat Methods , vol.3 , pp. 205-210
    • Lorenz, H.1    Hailey, D.W.2    Lippincott-Schwartz, J.3
  • 9
    • 14044250981 scopus 로고    scopus 로고
    • Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo
    • Tannous BA, Kim DE, Fernandez JL, Weissleder R, Breakefield XO, (2005) Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo. Mol Ther 11: 435-443.
    • (2005) Mol Ther , vol.11 , pp. 435-443
    • Tannous, B.A.1    Kim, D.E.2    Fernandez, J.L.3    Weissleder, R.4    Breakefield, X.O.5
  • 10
    • 39349083349 scopus 로고    scopus 로고
    • A highly sensitive assay for monitoring the secretory pathway and ER stress
    • Badr CE, Hewett JW, Breakefield XO, Tannous BA, (2007) A highly sensitive assay for monitoring the secretory pathway and ER stress. PLoS One 2: e571.
    • (2007) PLoS One , vol.2
    • Badr, C.E.1    Hewett, J.W.2    Breakefield, X.O.3    Tannous, B.A.4
  • 11
    • 77955093961 scopus 로고    scopus 로고
    • Biophysical characterization of highly active recombinant Gaussia luciferase expressed in Escherichia coli
    • Rathnayaka T, Tawa M, Sohya S, Yohda M, Kuroda Y, (2010) Biophysical characterization of highly active recombinant Gaussia luciferase expressed in Escherichia coli. Biochim Biophys Acta 1804: 1902-1907.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1902-1907
    • Rathnayaka, T.1    Tawa, M.2    Sohya, S.3    Yohda, M.4    Kuroda, Y.5
  • 12
    • 36048997217 scopus 로고    scopus 로고
    • Identification of two catalytic domains in a luciferase secreted by the copepod Gaussia princeps
    • Inouye S, Sahara Y, (2008) Identification of two catalytic domains in a luciferase secreted by the copepod Gaussia princeps. Biochem Biophys Res Commun 365: 96-101.
    • (2008) Biochem Biophys Res Commun , vol.365 , pp. 96-101
    • Inouye, S.1    Sahara, Y.2
  • 13
    • 0029048360 scopus 로고
    • Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+
    • Ou WJ, Bergeron JJ, Li Y, Kang CY, Thomas DY, (1995) Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+. J Biol Chem 270: 18051-18059.
    • (1995) J Biol Chem , vol.270 , pp. 18051-18059
    • Ou, W.J.1    Bergeron, J.J.2    Li, Y.3    Kang, C.Y.4    Thomas, D.Y.5
  • 14
    • 71549167617 scopus 로고    scopus 로고
    • Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome
    • Becker T, Bhushan S, Jarasch A, Armache JP, Funes S, et al. (2009) Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome. Science 326: 1369-1373.
    • (2009) Science , vol.326 , pp. 1369-1373
    • Becker, T.1    Bhushan, S.2    Jarasch, A.3    Armache, J.P.4    Funes, S.5
  • 15
    • 76149098224 scopus 로고    scopus 로고
    • Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates
    • Bernasconi R, Galli C, Calanca V, Nakajima T, Molinari M, (2010) Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates. J Cell Biol 188: 223-235.
    • (2010) J Cell Biol , vol.188 , pp. 223-235
    • Bernasconi, R.1    Galli, C.2    Calanca, V.3    Nakajima, T.4    Molinari, M.5
  • 16
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame K, Agarwala KL, Kato H, Miyata T, (2000) Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J Biol Chem 275: 32846-32853.
    • (2000) J Biol Chem , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 17
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL, (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9: 944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 18
    • 0035815754 scopus 로고    scopus 로고
    • Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation
    • Deak PM, Wolf DH, (2001) Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem 276: 10663-10669.
    • (2001) J Biol Chem , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 19
    • 70350337095 scopus 로고    scopus 로고
    • Fluorescent proteins: a cell biologist's user guide
    • Snapp EL, (2009) Fluorescent proteins: a cell biologist's user guide. Trends Cell Biol 19: 649-655.
    • (2009) Trends Cell Biol , vol.19 , pp. 649-655
    • Snapp, E.L.1
  • 20
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
    • Dayel MJ, Hom EF, Verkman AS, (1999) Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys J 76: 2843-2851.
    • (1999) Biophys J , vol.76 , pp. 2843-2851
    • Dayel, M.J.1    Hom, E.F.2    Verkman, A.S.3
  • 21
    • 49749114828 scopus 로고    scopus 로고
    • Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments
    • Lohman JR, Remington SJ, (2008) Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments. Biochemistry 47: 8678-8688.
    • (2008) Biochemistry , vol.47 , pp. 8678-8688
    • Lohman, J.R.1    Remington, S.J.2
  • 22
    • 79960420766 scopus 로고    scopus 로고
    • Real-time monitoring of redox changes in the mammalian endoplasmic reticulum
    • van Lith M, Tiwari S, Pediani J, Milligan G, Bulleid NJ, (2011) Real-time monitoring of redox changes in the mammalian endoplasmic reticulum. J Cell Sci 124: 2349-2356.
    • (2011) J Cell Sci , vol.124 , pp. 2349-2356
    • van Lith, M.1    Tiwari, S.2    Pediani, J.3    Milligan, G.4    Bulleid, N.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.