메뉴 건너뛰기




Volumn 5, Issue 3, 2013, Pages

The contribution of systematic approaches to characterizing the proteins and functions of the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

MULTIPROTEIN COMPLEX; PROTEOME;

EID: 84874743524     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a013284     Document Type: Article
Times cited : (11)

References (155)
  • 4
    • 84857612880 scopus 로고    scopus 로고
    • Protein folding and quality control in the ER
    • Araki K, Nagata K. 2011. Protein folding and quality control in the ER. Cold Spring Harb Perspect Biol 3: a007526.
    • (2011) Cold Spring Harb Perspect Biol , vol.a007526 , pp. 3
    • Araki, K.1    Nagata, K.2
  • 5
    • 33644857820 scopus 로고    scopus 로고
    • Genomic association of the proteasome demonstrates overlapping gene regulatory activity with transcription factor substrates
    • Auld KL, Brown CR, Casolari JM, Komili S, Silver PA. 2006. Genomic association of the proteasome demonstrates overlapping gene regulatory activity with transcription factor substrates. Mol Cell 21: 861-871.
    • (2006) Mol Cell , vol.21 , pp. 861-871
    • Auld, K.L.1    Brown, C.R.2    Casolari, J.M.3    Komili, S.4    Silver, P.A.5
  • 12
    • 80555144827 scopus 로고    scopus 로고
    • N-linked global glycan profiling by nanoLC mass spectrometry
    • Bereman MS, Muddiman DC. 2011. N-linked global glycan profiling by nanoLC mass spectrometry. Methods Mol Biol 790: 87-97.
    • (2011) Methods Mol Biol , vol.790 , pp. 87-97
    • Bereman, M.S.1    Muddiman, D.C.2
  • 15
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman I, Bulleid NJ. 2011. Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem 80: 71-99.
    • (2011) Annu Rev Biochem , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 16
    • 84856625798 scopus 로고    scopus 로고
    • High-resolution view of the yeast meiotic program revealed by ribosome profiling
    • Brar GA, Yassour M, Friedman N, Regev A, Ingolia NT, Weissman JS. 2012. High-resolution view of the yeast meiotic program revealed by ribosome profiling. Science 335: 552-557.
    • (2012) Science , vol.335 , pp. 552-557
    • Brar, G.A.1    Yassour, M.2    Friedman, N.3    Regev, A.4    Ingolia, N.T.5    Weissman, J.S.6
  • 17
    • 72949098092 scopus 로고    scopus 로고
    • Explorations in topologydelving underneath the surface of genetic interaction maps
    • Breker M, Schuldiner M. 2009. Explorations in topologydelving underneath the surface of genetic interaction maps. Mol Biosyst 5: 1473-1481.
    • (2009) Mol Biosyst , vol.5 , pp. 1473-1481
    • Breker, M.1    Schuldiner, M.2
  • 18
    • 84874713274 scopus 로고    scopus 로고
    • Sphingolipid homeostasis in the endoplasmic reticulum and beyond
    • doi: 10.1101/cshperspect.a013326
    • Breslow DK. 2013. Sphingolipid homeostasis in the endoplasmic reticulum and beyond. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a013326.
    • (2013) Cold Spring Harb Perspect Biol
    • Breslow, D.K.1
  • 19
    • 78649373124 scopus 로고    scopus 로고
    • Membranes in balance: Mechanisms of sphingolipid homeostasis
    • Breslow DK, Weissman JS. 2010. Membranes in balance: Mechanisms of sphingolipid homeostasis. Mol Cell 40: 267-279.
    • (2010) Mol Cell , vol.40 , pp. 267-279
    • Breslow, D.K.1    Weissman, J.S.2
  • 22
    • 0028215472 scopus 로고
    • Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae
    • Burns N, Grimwade B, Ross-Macdonald PB, Choi EY, Finberg K, Roeder GS, Snyder M. 1994. Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae. Genes Dev 8: 1087-1105.
    • (1994) Genes Dev , vol.8 , pp. 1087-1105
    • Burns, N.1    Grimwade, B.2    Ross-Macdonald, P.B.3    Choi, E.Y.4    Finberg, K.5    Roeder, G.S.6    Snyder, M.7
  • 25
    • 0033637082 scopus 로고    scopus 로고
    • Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway
    • Casagrande R, Stern P, Diehn M, Shamu C, Osario M, Zuniga M, Brown PO, Ploegh H. 2000. Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway. Mol Cell 5: 729-735.
    • (2000) Mol Cell , vol.5 , pp. 729-735
    • Casagrande, R.1    Stern, P.2    Diehn, M.3    Shamu, C.4    Osario, M.5    Zuniga, M.6    Brown, P.O.7    Ploegh, H.8
  • 26
    • 34447550255 scopus 로고    scopus 로고
    • Managing and exploiting stress in the antibody factory
    • Cenci S, Sitia R. 2007. Managing and exploiting stress in the antibody factory. FEBS Lett 581: 3652-3657.
    • (2007) FEBS Lett , vol.581 , pp. 3652-3657
    • Cenci, S.1    Sitia, R.2
  • 28
    • 80054723502 scopus 로고    scopus 로고
    • Advanced methods for highthroughput microscopy screening of genetically modified yeast libraries
    • Cohen Y, Schuldiner M. 2011. Advanced methods for highthroughput microscopy screening of genetically modified yeast libraries. Methods Mol Biol 781: 127-159.
    • (2011) Methods Mol Biol , vol.781 , pp. 127-159
    • Cohen, Y.1    Schuldiner, M.2
  • 29
    • 33747367151 scopus 로고    scopus 로고
    • A strategy for extracting and analyzing large-scale quantitative epistatic interaction data
    • Collins SR, Schuldiner M, Krogan NJ, Weissman JS. 2006. A strategy for extracting and analyzing large-scale quantitative epistatic interaction data. Genome Biol 7: R63.
    • (2006) Genome Biol , vol.7
    • Collins, S.R.1    Schuldiner, M.2    Krogan, N.J.3    Weissman, J.S.4
  • 30
    • 70349318145 scopus 로고    scopus 로고
    • Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control
    • Copic A, Dorrington M, Pagant S, Barry J, Lee MC, Singh I, Hartman JL 4th, Miller EA. 2009. Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control. Genetics 182: 757-769.
    • (2009) Genetics , vol.182 , pp. 757-769
    • Copic, A.1    Dorrington, M.2    Pagant, S.3    Barry, J.4    Lee, M.C.5    Singh, I.6    Hartman IV, J.L.7    Miller, E.A.8
  • 32
    • 34547947625 scopus 로고    scopus 로고
    • A molecular caliper mechanism for determining very long-chain fatty acid length
    • Denic V, Weissman JS. 2007. A molecular caliper mechanism for determining very long-chain fatty acid length. Cell 130: 663-677.
    • (2007) Cell , vol.130 , pp. 663-677
    • Denic, V.1    Weissman, J.S.2
  • 33
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies RJ, Schekman R. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J Cell Biol 105: 633-645.
    • (1987) J Cell Biol , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 34
    • 50049119791 scopus 로고    scopus 로고
    • Thematic Review Series: Sphingolipids. New insights into sphingolipid metabolism and function in budding yeast
    • Dickson RC. 2008. Thematic Review Series: Sphingolipids. New insights into sphingolipid metabolism and function in budding yeast. J Lipid Res 49: 909-921.
    • (2008) J Lipid Res , vol.49 , pp. 909-921
    • Dickson, R.C.1
  • 35
    • 0035158456 scopus 로고    scopus 로고
    • Aux1p/ Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae
    • Du Y, Pypaert M, Novick P, Ferro-Novick S. 2001. Aux1p/ Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae. Mol Biol Cell 12: 2614-2628.
    • (2001) Mol Biol Cell , vol.12 , pp. 2614-2628
    • Du, Y.1    Pypaert, M.2    Novick, P.3    Ferro-Novick, S.4
  • 36
    • 4344664038 scopus 로고    scopus 로고
    • Dynamics and inheritance of the endoplasmic reticulum
    • Du Y, Ferro-Novick S, Novick P. 2004. Dynamics and inheritance of the endoplasmic reticulum. J Cell Sci 117: 2871- 2878.
    • (2004) J Cell Sci , vol.117 , pp. 2871
    • Du, Y.1    Ferro-Novick, S.2    Novick, P.3
  • 37
    • 33749364913 scopus 로고    scopus 로고
    • Ptc1p regulates cortical ER inheritance via Slt2p
    • Du Y, Walker L, Novick P, Ferro-Novick S. 2006. Ptc1p regulates cortical ER inheritance via Slt2p. EMBO J 25: 4413-4422.
    • (2006) EMBO J , vol.25 , pp. 4413-4422
    • Du, Y.1    Walker, L.2    Novick, P.3    Ferro-Novick, S.4
  • 38
    • 33644945987 scopus 로고    scopus 로고
    • Characterization of the yeast ionome: A genome-wide analysis of nutrient mineral and trace element homeostasis in Saccharomyces cerevisiae
    • Eide DJ, Clark S, Nair TM, Gehl M, Gribskov M, Guerinot ML, Harper JF. 2005. Characterization of the yeast ionome: A genome-wide analysis of nutrient mineral and trace element homeostasis in Saccharomyces cerevisiae. Genome Biol 6: R77.
    • (2005) Genome Biol , vol.6
    • Eide, D.J.1    Clark, S.2    Nair, T.M.3    Gehl, M.4    Gribskov, M.5    Guerinot, M.L.6    Harper, J.F.7
  • 40
    • 80755153578 scopus 로고    scopus 로고
    • Staying in touch: The molecular era of organelle contact sites
    • Elbaz Y, Schuldiner M. 2011. Staying in touch: The molecular era of organelle contact sites. Trends Biochem Sci 36: 616-623.
    • (2011) Trends Biochem Sci , vol.36 , pp. 616-623
    • Elbaz, Y.1    Schuldiner, M.2
  • 41
    • 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
  • 42
    • 14044255694 scopus 로고    scopus 로고
    • Ice2p is important for the distribution and structure of the cortical ER network in Saccharomyces cerevisiae
    • Estrada de Martin P, Du Y, Novick P, Ferro-Novick S. 2005. Ice2p is important for the distribution and structure of the cortical ER network in Saccharomyces cerevisiae. J Cell Sci 118: 65-77.
    • (2005) J Cell Sci , vol.118 , pp. 65-77
    • Estrada de Martin, P.1    Du, Y.2    Novick, P.3    Ferro-Novick, S.4
  • 43
    • 66349117317 scopus 로고    scopus 로고
    • Membrane phospholipid synthesis and endoplasmic reticulum function
    • Fagone P, Jackowski S. 2009. Membrane phospholipid synthesis and endoplasmic reticulum function. J Lipid Res 50: S311-S316.
    • (2009) J Lipid Res , vol.50
    • Fagone, P.1    Jackowski, S.2
  • 44
    • 62149124046 scopus 로고    scopus 로고
    • Quantitative high-throughput analysis of synthetic genetic interactions in Caenorhabditis elegans by RNA interference
    • Fortunato A. 2009. Quantitative high-throughput analysis of synthetic genetic interactions in Caenorhabditis elegans by RNA interference. Genomics 93: 392-396.
    • (2009) Genomics , vol.93 , pp. 392-396
    • Fortunato, A.1
  • 47
    • 40749160804 scopus 로고    scopus 로고
    • Lipid remodeling of GPI-anchored proteins and its function
    • Fujita M, Jigami Y. 2008. Lipid remodeling of GPI-anchored proteins and its function. Biochim Biophys Acta 1780: 410-420.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 410-420
    • Fujita, M.1    Jigami, Y.2
  • 50
    • 33747375103 scopus 로고    scopus 로고
    • Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae
    • Gaspar ML, Aregullin MA, Jesch SA, Henry SA. 2006. Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae. J Biol Chem 281: 22773-22785.
    • (2006) J Biol Chem , vol.281 , pp. 22773-22785
    • Gaspar, M.L.1    Aregullin, M.A.2    Jesch, S.A.3    Henry, S.A.4
  • 51
    • 0346331895 scopus 로고    scopus 로고
    • Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response
    • Gass JN, Gunn KE, Sriburi R, Brewer JW. 2004. Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response. Trends Immunol 25: 17-24.
    • (2004) Trends Immunol , vol.25 , pp. 17-24
    • Gass, J.N.1    Gunn, K.E.2    Sriburi, R.3    Brewer, J.W.4
  • 52
    • 78049518892 scopus 로고    scopus 로고
    • An overview of sphingolipid metabolism: From synthesis to breakdown
    • Gault CR, Obeid LM, Hannun YA. 2010. An overview of sphingolipid metabolism: From synthesis to breakdown. Adv Exp Med Biol 688: 1-23.
    • (2010) Adv Exp Med Biol , vol.688 , pp. 1-23
    • Gault, C.R.1    Obeid, L.M.2    Hannun, Y.A.3
  • 57
    • 77649219141 scopus 로고    scopus 로고
    • Persistent ER stress induces the spliced leader RNA silencing pathway (SLS), leading to programmed cell death in Trypanosoma brucei
    • Goldshmidt H, Matas D, Kabi A, Carmi S, Hope R, Michaeli S. 2010. Persistent ER stress induces the spliced leader RNA silencing pathway (SLS), leading to programmed cell death in Trypanosoma brucei. PLoS Pathog 6: e1000731.
    • (2010) PLoS Pathog , vol.6
    • Goldshmidt, H.1    Matas, D.2    Kabi, A.3    Carmi, S.4    Hope, R.5    Michaeli, S.6
  • 62
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton RY, Gardner RG, Rine J. 1996. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell 7: 2029-2044.
    • (1996) Mol Biol Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 63
    • 60849132182 scopus 로고    scopus 로고
    • Localization of gene products using a chromosomally tagged GFP-fusion library in the fission yeast Schizosaccharomyces pombe
    • Hayashi A, Ding DQ, Tsutsumi C, Chikashige Y, Masuda H, Haraguchi T, Hiraoka Y. 2009. Localization of gene products using a chromosomally tagged GFP-fusion library in the fission yeast Schizosaccharomyces pombe. Genes Cells 14: 217-225.
    • (2009) Genes Cells , vol.14 , pp. 217-225
    • Hayashi, A.1    Ding, D.Q.2    Tsutsumi, C.3    Chikashige, Y.4    Masuda, H.5    Haraguchi, T.6    Hiraoka, Y.7
  • 64
    • 84857424979 scopus 로고    scopus 로고
    • Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae
    • Henry SA, Kohlwein SD, Carman GM. 2012. Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae. Genetics 190: 317-349.
    • (2012) Genetics , vol.190 , pp. 317-349
    • Henry, S.A.1    Kohlwein, S.D.2    Carman, G.M.3
  • 65
    • 84861539173 scopus 로고    scopus 로고
    • A systematic approach to pair secretory cargo receptors with their cargo suggests a mechanism for cargo selection by erv14
    • Herzig Y, Sharpe HJ, Elbaz Y, Munro S, Schuldiner M. 2012. A systematic approach to pair secretory cargo receptors with their cargo suggests a mechanism for cargo selection by erv14. PLoS Biol 10: e1001329.
    • (2012) PLoS Biol , vol.10
    • Herzig, Y.1    Sharpe, H.J.2    Elbaz, Y.3    Munro, S.4    Schuldiner, M.5
  • 68
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • Hollien J, Weissman JS. 2006. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313: 104-107.
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 69
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe T, Matuschewski K, Rape M, Schlenker S, Ulrich HD, Jentsch S. 2000. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102: 577-586.
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 70
    • 79953289737 scopus 로고    scopus 로고
    • Mapping of signaling networks through synthetic genetic interaction analysis by RNAi
    • Horn T, Sandmann T, Fischer B, Axelsson E, Huber W, Boutros M. 2011. Mapping of signaling networks through synthetic genetic interaction analysis by RNAi. Nat Methods 8: 341-346.
    • (2011) Nat Methods , vol.8 , pp. 341-346
    • Horn, T.1    Sandmann, T.2    Fischer, B.3    Axelsson, E.4    Huber, W.5    Boutros, M.6
  • 71
    • 0142027805 scopus 로고    scopus 로고
    • Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes
    • Horton JD, Shah NA, Warrington JA, Anderson NN, Park SW, Brown MS, Goldstein JL. 2003. Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes. Proc Natl Acad Sci 100: 12027-12032.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 12027-12032
    • Horton, J.D.1    Shah, N.A.2    Warrington, J.A.3    Anderson, N.N.4    Park, S.W.5    Brown, M.S.6    Goldstein, J.L.7
  • 72
    • 0020049833 scopus 로고
    • Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation
    • Huffaker TC, Robbins PW. 1982. Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation. J Biol Chem 257: 3203-3210.
    • (1982) J Biol Chem , vol.257 , pp. 3203-3210
    • Huffaker, T.C.1    Robbins, P.W.2
  • 74
    • 0027409423 scopus 로고
    • Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy
    • Inoue N, Kinoshita T, Orii T, Takeda J. 1993. Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy. J Biol Chem 268: 6882-6885.
    • (1993) J Biol Chem , vol.268 , pp. 6882-6885
    • Inoue, N.1    Kinoshita, T.2    Orii, T.3    Takeda, J.4
  • 75
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito T, Chiba T, Ozawa R, Yoshida M, Hattori M, Sakaki Y. 2001. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci 98: 4569-4574.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4    Hattori, M.5    Sakaki, Y.6
  • 76
    • 33646018341 scopus 로고    scopus 로고
    • Fatty acid elongases in mammals: Their regulation and roles in metabolism
    • Jakobsson A, Westerberg R, Jacobsson A. 2006. Fatty acid elongases in mammals: Their regulation and roles in metabolism. Prog Lipid Res 45: 237-249.
    • (2006) Prog Lipid Res , vol.45 , pp. 237-249
    • Jakobsson, A.1    Westerberg, R.2    Jacobsson, A.3
  • 78
    • 15744368614 scopus 로고    scopus 로고
    • Genome-wide analysis reveals inositol, not choline, as the major effector of Ino2p-Ino4p and unfolded protein response target gene expression in yeast
    • Jesch SA, Zhao X, Wells MT, Henry SA. 2005. Genome-wide analysis reveals inositol, not choline, as the major effector of Ino2p-Ino4p and unfolded protein response target gene expression in yeast. J Biol Chem 280: 9106-9118.
    • (2005) J Biol Chem , vol.280 , pp. 9106-9118
    • Jesch, S.A.1    Zhao, X.2    Wells, M.T.3    Henry, S.A.4
  • 79
    • 33747735581 scopus 로고    scopus 로고
    • Multiple endoplasmic reticulum-to-nucleus signaling pathways coordinate phospholipid metabolism with gene expression by distinct mechanisms
    • Jesch SA, Liu P, Zhao X, Wells MT, Henry SA. 2006. Multiple endoplasmic reticulum-to-nucleus signaling pathways coordinate phospholipid metabolism with gene expression by distinct mechanisms. J Biol Chem 281: 24070- 24083.
    • (2006) J Biol Chem , vol.281 , pp. 24070
    • Jesch, S.A.1    Liu, P.2    Zhao, X.3    Wells, M.T.4    Henry, S.A.5
  • 82
    • 33746616385 scopus 로고    scopus 로고
    • A global topology map of the Saccharomyces cerevisiae membrane proteome
    • Kim H, Melen K, Osterberg M, von Heijne G. 2006. A global topology map of the Saccharomyces cerevisiae membrane proteome. Proc Natl Acad Sci 103: 11142-11147.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 11142-11147
    • Kim, H.1    Melen, K.2    Osterberg, M.3    von Heijne, G.4
  • 87
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee AH, Iwakoshi NN, Glimcher LH. 2003. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23: 7448-7459.
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 88
    • 0028906887 scopus 로고
    • Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae-A review
    • Lees ND, Skaggs B, Kirsch DR, Bard M. 1995. Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae-A review. Lipids 30: 221-226.
    • (1995) Lipids , vol.30 , pp. 221-226
    • Lees, N.D.1    Skaggs, B.2    Kirsch, D.R.3    Bard, M.4
  • 89
    • 33746525415 scopus 로고    scopus 로고
    • Systematic mapping of genetic interactions in Caenorhabditis elegans identifies common modifiers of diverse signaling pathways
    • Lehner B, Crombie C, Tischler J, Fortunato A, Fraser AG. 2006. Systematic mapping of genetic interactions in Caenorhabditis elegans identifies common modifiers of diverse signaling pathways. Nat Genet 38: 896-903.
    • (2006) Nat Genet , vol.38 , pp. 896-903
    • Lehner, B.1    Crombie, C.2    Tischler, J.3    Fortunato, A.4    Fraser, A.G.5
  • 90
    • 0029006987 scopus 로고
    • Isolation and characterization of yeast glycosylphosphatidylinositol anchoring mutants
    • Leidich SD, Drapp DA, Orlean P. 1995a. Isolation and characterization of yeast glycosylphosphatidylinositol anchoring mutants. Methods Enzymol 250: 560-571.
    • (1995) Methods Enzymol , vol.250 , pp. 560-571
    • Leidich, S.D.1    Drapp, D.A.2    Orlean, P.3
  • 91
    • 0028998118 scopus 로고
    • Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol. Cloning of the GPI2 gene
    • Leidich SD, Kostova Z, Latek RR, Costello LC, Drapp DA, Gray W, Fassler JS, Orlean P. 1995b. Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol. Cloning of the GPI2 gene. J Biol Chem 270: 13029-13035.
    • (1995) J Biol Chem , vol.270 , pp. 13029-13035
    • Leidich, S.D.1    Kostova, Z.2    Latek, R.R.3    Costello, L.C.4    Drapp, D.A.5    Gray, W.6    Fassler, J.S.7    Orlean, P.8
  • 94
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin JH, Walter P, Yen TS. 2008. Endoplasmic reticulum stress in disease pathogenesis. Annu Rev Pathol 3: 399-425.
    • (2008) Annu Rev Pathol , vol.3 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Yen, T.S.3
  • 96
    • 35948950693 scopus 로고    scopus 로고
    • Inheritance of cortical ER in yeast is required for normal septin organization
    • Loewen CJ, Young BP, Tavassoli S, Levine TP. 2007. Inheritance of cortical ER in yeast is required for normal septin organization. J Cell Biol 179: 467-483.
    • (2007) J Cell Biol , vol.179 , pp. 467-483
    • Loewen, C.J.1    Young, B.P.2    Tavassoli, S.3    Levine, T.P.4
  • 97
    • 0037327305 scopus 로고    scopus 로고
    • Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes
    • Martinez IM, Chrispeels MJ. 2003. Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes. Plant Cell 15: 561-576.
    • (2003) Plant Cell , vol.15 , pp. 561-576
    • Martinez, I.M.1    Chrispeels, M.J.2
  • 99
    • 56349087407 scopus 로고    scopus 로고
    • Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions
    • Merksamer PI, Trusina A, Papa FR. 2008. Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135: 933-947.
    • (2008) Cell , vol.135 , pp. 933-947
    • Merksamer, P.I.1    Trusina, A.2    Papa, F.R.3
  • 101
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock G, De Angelis DA, Rothman JE. 1998. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394: 192-195.
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    de Angelis, D.A.2    Rothman, J.E.3
  • 104
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • Morelle W, Michalski JC. 2007. Analysis of protein glycosylation by mass spectrometry. Nat Protoc 2: 1585-1602.
    • (2007) Nat Protoc , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.C.2
  • 105
    • 71949098172 scopus 로고    scopus 로고
    • Signalling pathways in the unfolded protein response: Development from yeast to mammals
    • Mori K. 2009. Signalling pathways in the unfolded protein response: Development from yeast to mammals. J Biochem 146: 743-750.
    • (2009) J Biochem , vol.146 , pp. 743-750
    • Mori, K.1
  • 107
    • 0000756130 scopus 로고
    • Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae
    • Novick P, Schekman R. 1979. Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci 76: 1858-1862.
    • (1979) Proc Natl Acad Sci , vol.76 , pp. 1858-1862
    • Novick, P.1    Schekman, R.2
  • 108
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick P, Field C, Schekman R. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21: 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 109
    • 0019424489 scopus 로고
    • Order of events in the yeast secretory pathway
    • Novick P, Ferro S, Schekman R. 1981. Order of events in the yeast secretory pathway. Cell 25: 461-469.
    • (1981) Cell , vol.25 , pp. 461-469
    • Novick, P.1    Ferro, S.2    Schekman, R.3
  • 110
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada T, Yoshida H, Akazawa R, Negishi M, Mori K. 2002. Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem J 366: 585-594.
    • (2002) Biochem J , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 111
    • 84855966721 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress in metabolic disease and other disorders
    • Ozcan L, Tabas I. 2012. Role of endoplasmic reticulum stress in metabolic disease and other disorders. Annu Rev Med 63: 317-328.
    • (2012) Annu Rev Med , vol.63 , pp. 317-328
    • Ozcan, L.1    Tabas, I.2
  • 114
    • 84858636070 scopus 로고    scopus 로고
    • In vivo determination of organellar pH using a universal wavelengthbased confocal microscopy approach
    • Pineda Rodo A, Vachova L, Palkova Z. 2012. In vivo determination of organellar pH using a universal wavelengthbased confocal microscopy approach. PLoS ONE 7: e33229.
    • (2012) PLoS ONE , vol.7
    • Pineda Rodo, A.1    Vachova, L.2    Palkova, Z.3
  • 117
    • 33846964132 scopus 로고    scopus 로고
    • Insight into transcription factor gene duplication from Caenorhabditis elegans Promoterome-driven expression patterns
    • Reece-Hoyes JS, Shingles J, Dupuy D, Grove CA, Walhout AJ, Vidal M, Hope IA. 2007. Insight into transcription factor gene duplication from Caenorhabditis elegans Promoterome-driven expression patterns. BMC Genomics 8: 27.
    • (2007) BMC Genomics , vol.8 , pp. 27
    • Reece-Hoyes, J.S.1    Shingles, J.2    Dupuy, D.3    Grove, C.A.4    Walhout, A.J.5    Vidal, M.6    Hope, I.A.7
  • 118
    • 84856769427 scopus 로고    scopus 로고
    • Getting the whole picture: Combining throughput with content in microscopy
    • Rimon N, Schuldiner M. 2011. Getting the whole picture: Combining throughput with content in microscopy. J Cell Sci 124: 3743-3751.
    • (2011) J Cell Sci , vol.124 , pp. 3743-3751
    • Rimon, N.1    Schuldiner, M.2
  • 119
    • 35848940244 scopus 로고    scopus 로고
    • Highthroughput genetic interaction mapping in the fission yeast Schizosaccharomyces pombe
    • Roguev A, Wiren M, Weissman JS, Krogan NJ. 2007. Highthroughput genetic interaction mapping in the fission yeast Schizosaccharomyces pombe. Nat Methods 4: 861-866.
    • (2007) Nat Methods , vol.4 , pp. 861-866
    • Roguev, A.1    Wiren, M.2    Weissman, J.S.3    Krogan, N.J.4
  • 120
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE. 1994. Mechanisms of intracellular protein transport. Nature 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 121
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman JE, Orci L. 1992. Molecular dissection of the secretory pathway. Nature 355: 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 123
    • 0141866789 scopus 로고    scopus 로고
    • Genome expression analysis in yeast reveals novel transcriptional regulation by inositol and choline and new regulatory functions for Opi1p, Ino2p, and Ino4p
    • Santiago TC, Mamoun CB. 2003. Genome expression analysis in yeast reveals novel transcriptional regulation by inositol and choline and new regulatory functions for Opi1p, Ino2p, and Ino4p. J Biol Chem 278: 38723- 38730.
    • (2003) J Biol Chem , vol.278 , pp. 38723
    • Santiago, T.C.1    Mamoun, C.B.2
  • 126
    • 2342431029 scopus 로고    scopus 로고
    • The Hera database and its use in the characterization of endoplasmic reticulum proteins
    • Scott M, Lu G, Hallett M, Thomas DY. 2004. The Hera database and its use in the characterization of endoplasmic reticulum proteins. Bioinformatics 20: 937-944.
    • (2004) Bioinformatics , vol.20 , pp. 937-944
    • Scott, M.1    Lu, G.2    Hallett, M.3    Thomas, D.Y.4
  • 127
    • 33745606008 scopus 로고    scopus 로고
    • Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans
    • Shen X, Ellis RE, Sakaki K, Kaufman RJ. 2005. Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans. PLoS Genet 1: e37.
    • (2005) PLoS Genet , vol.1
    • Shen, X.1    Ellis, R.E.2    Sakaki, K.3    Kaufman, R.J.4
  • 129
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith MH, Ploegh H., Weissman JS. 2011. Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum. Science 334: 1086-1090.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.2    Weissman, J.S.3
  • 131
    • 0038182336 scopus 로고    scopus 로고
    • Triacylglycerol biosynthesis in yeast
    • Sorger D, Daum G. 2003. Triacylglycerol biosynthesis in yeast. Appl Microbiol Biotechnol 61: 289-299.
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 289-299
    • Sorger, D.1    Daum, G.2
  • 132
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar I, Korostensky C, Johnsson N, te Heesen S. 1998. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc Natl Acad Sci 95: 5187-5192.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    te Heesen, S.4
  • 133
    • 44449095717 scopus 로고    scopus 로고
    • Proteomic analysis of mouse brain microsomes: Identification and bioinformatic characterization of endoplasmic reticulum proteins in the mammalian central nervous system
    • Stevens SM Jr, Duncan RS, Koulen P, Prokai L. 2008. Proteomic analysis of mouse brain microsomes: identification and bioinformatic characterization of endoplasmic reticulum proteins in the mammalian central nervous system. J Proteome Res 7: 1046-1054.
    • (2008) J Proteome Res , vol.7 , pp. 1046-1054
    • Stevens Jr., S.M.1    Duncan, R.S.2    Koulen, P.3    Prokai, L.4
  • 134
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas I, Ron D. 2011. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat Cell Biol 13: 184-190.
    • (2011) Nat Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 135
    • 0027310539 scopus 로고
    • Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria
    • Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T. 1993. Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell 73: 703-711.
    • (1993) Cell , vol.73 , pp. 703-711
    • Takeda, J.1    Miyata, T.2    Kawagoe, K.3    Iida, Y.4    Endo, Y.5    Fujita, T.6    Takahashi, M.7    Kitani, T.8    Kinoshita, T.9
  • 138
    • 33644807842 scopus 로고    scopus 로고
    • Synthetic genetic array analysis in Saccharomyces cerevisiae
    • Tong AH, Boone C. 2006. Synthetic genetic array analysis in Saccharomyces cerevisiae. Methods Mol Biol 313: 171-192.
    • (2006) Methods Mol Biol , vol.313 , pp. 171-192
    • Tong, A.H.1    Boone, C.2
  • 141
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101: 249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 143
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien RY. 1998. The green fluorescent protein. Annu Rev Biochem 67: 509-544.
    • (1998) Annu Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 146
    • 0037767632 scopus 로고    scopus 로고
    • Cell growth selection system to detect extracellular and transmembrane protein interactions
    • Urech DM, Lichtlen P, Barberis A. 2003. Cell growth selection system to detect extracellular and transmembrane protein interactions. Biochim Biophys Acta 1622: 117-127.
    • (2003) Biochim Biophys Acta , vol.1622 , pp. 117-127
    • Urech, D.M.1    Lichtlen, P.2    Barberis, A.3
  • 147
    • 1542465944 scopus 로고    scopus 로고
    • Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism
    • Vance JE. 2003. Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism. Prog Nucleic Acid Res Mol Biol 75: 69-111.
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.75 , pp. 69-111
    • Vance, J.E.1
  • 148
    • 79959263110 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and glucose homeostasis
    • Wagner M, Moore DD. 2011. Endoplasmic reticulum stress and glucose homeostasis. Curr Opin Clin Nutr Metab Care 14: 367-373.
    • (2011) Curr Opin Clin Nutr Metab Care , vol.14 , pp. 367-373
    • Wagner, M.1    Moore, D.D.2
  • 149
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P, Ron D. 2011. The unfolded protein response: From stress pathway to homeostatic regulation. Science 334: 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 151
    • 18844391758 scopus 로고    scopus 로고
    • Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: Topological features and in vivo interactions
    • Yan A, Wu E, Lennarz WJ. 2005. Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: Topological features and in vivo interactions. Proc Natl Acad Sci 102: 7121-7126.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 7121-7126
    • Yan, A.1    Wu, E.2    Lennarz, W.J.3
  • 155
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang K, Kaufman RJ. 2008. From endoplasmic-reticulum stress to the inflammatory response. Nature 454: 455-462.
    • (2008) Nature , vol.454 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.