메뉴 건너뛰기




Volumn 162, Issue 1, 2002, Pages 29-43

Role of the unfolded protein response pathway in regulation of INO1 and in the sec14 bypass mechanism in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL;

EID: 0036743487     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (51)

References (52)
  • 1
    • 0018940962 scopus 로고
    • Yeast mutant defective in phosphatidylserine synthase
    • Atkinson, K., S. Fogel and S. A. Henry, 1980 Yeast mutant defective in phosphatidylserine synthase. J. Biol. Chem. 255: 6653-6661.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6653-6661
    • Atkinson, K.1    Fogel, S.2    Henry, S.A.3
  • 2
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • Bankaitis, V. A., D. E. Malehorn, S. D. Emr and R. Greene, 1989 The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J. Cell Biol. 108: 1271-1281.
    • (1989) J. Cell Biol. , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 3
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast for Golgi function
    • Bankaitis, V., J. Aitkin, A. Cleves and W. Dowhan, 1990 An essential role for a phospholipid transfer protein in yeast for Golgi function. Nature 347: 561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.1    Aitkin, J.2    Cleves, A.3    Dowhan, W.4
  • 4
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M., H. Zeng, F. Urano, J. H. Till, S. R. Hubbard et al al., 2002 IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415: 92-96.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5
  • 5
    • 0024324794 scopus 로고
    • Phospholipid biosynthesis in yeast
    • Carman, G. M., and S. A. Henry, 1989 Phospholipid biosynthesis in yeast. Annu. Rev. Biochem. 58: 635-669.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 635-669
    • Carman, G.M.1    Henry, S.A.2
  • 6
    • 0031282636 scopus 로고    scopus 로고
    • Translational attenuation mediated by an mRNA intron
    • Chapman, R. E., and P. Walter, 1997 Translational attenuation mediated by an mRNA intron. Curr. Biol. 7: 850-859.
    • (1997) Curr. Biol. , vol.7 , pp. 850-859
    • Chapman, R.E.1    Walter, P.2
  • 7
    • 0026073075 scopus 로고
    • Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein
    • Cleves, A. E., T. P. McGee, E. A. Whitters, K. M. Champion, J. R. Aitken et al., 1991 Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cell 64: 789-800.
    • (1991) Cell , vol.64 , pp. 789-800
    • Cleves, A.E.1    McGee, T.P.2    Whitters, E.A.3    Champion, K.M.4    Aitken, J.R.5
  • 8
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox, J. S., and P. Walter, 1996 A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87: 391-404.
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 9
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox, J. S., C. E. Shamu, and P. Walter, 1993 Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73: 1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 10
    • 0030879870 scopus 로고    scopus 로고
    • The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane
    • Cox, J. S., R. E. Chapman, and P. Walter, 1997 The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol. Biol. Cell 8: 1805-1814.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1805-1814
    • Cox, J.S.1    Chapman, R.E.2    Walter, P.3
  • 11
    • 0016739154 scopus 로고
    • Inositol-requiring mutants of Saccharomyces cerevisiae
    • Culbertson, M. R., and S. A. Henry, 1975. Inositol-requiring mutants of Saccharomyces cerevisiae. Genetics 80: 23-40.
    • (1975) Genetics , vol.80 , pp. 23-40
    • Culbertson, M.R.1    Henry, S.A.2
  • 12
    • 0019877154 scopus 로고
    • myo-Inositol-1-phosphate synthase: Characteristics of the enzyme and identification of its structural gene in yeast
    • Donahue, T. F., and S. A. Henry, 1981 myo-Inositol-1-phosphate synthase: characteristics of the enzyme and identification of its structural gene in yeast. J. Biol. Chem. 256: 7077-7085.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7077-7085
    • Donahue, T.F.1    Henry, S.A.2
  • 13
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander, R., E. Jarosch, J. Urban, C. Volkwein and T. Sommer, 2000 A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat. Cell Biol. 2: 379-384.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 14
    • 0029963923 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae
    • Greenberg, M. L., and J. M. Lopes, 1996 Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae. Microbiol. Rev. 60: 1-20.
    • (1996) Microbiol. Rev. , vol.60 , pp. 1-20
    • Greenberg, M.L.1    Lopes, J.M.2
  • 15
    • 0019988791 scopus 로고
    • Characterization of a yeast regulatory, mutant constitutive for inositol1-phosphate synthase
    • Greenberg, M., P. Goldwasser and S. A. Henry, 1982 Characterization of a yeast regulatory, mutant constitutive for inositol1-phosphate synthase. Mol. Gen. Genet. 186: 157-163.
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 157-163
    • Greenberg, M.1    Goldwasser, P.2    Henry, S.A.3
  • 17
    • 0029818842 scopus 로고    scopus 로고
    • The role of phosphatidylcholine biosynthesis in the regulation of the INO1 gene of yeast
    • Griac, P., M. Swede and S. A. Henry, 1996 The role of phosphatidylcholine biosynthesis in the regulation of the INO1 gene of yeast. J. Biol. Chem. 271: 25692-25698.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25692-25698
    • Griac, P.1    Swede, M.2    Henry, S.A.3
  • 18
    • 0031610424 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid metabolism: Yeast as a model eukayote
    • edited by W. E. Cohn and K. Moldave. Academic Press, San Diego
    • Henry, S. A., and J. L. Patton-Vogt, 1998 Genetic regulation of phospholipid metabolism: yeast as a model eukayote, pp. 133-179 in Progress in Nucleic Acid Research and Molecular Biology, edited by W. E. Cohn and K. Moldave. Academic Press, San Diego.
    • (1998) Progress in Nucleic Acid Research and Molecular Biology , pp. 133-179
    • Henry, S.A.1    Patton-Vogt, J.L.2
  • 20
    • 0022799260 scopus 로고
    • Expression of the Saccharomyces cerevisiae inositol-1-phosphate synthase (INO1) gene is regulated by factors that affect phospholipid synthesis
    • Hirsch, J. P., and S. A. Henry, 1986 Expression of the Saccharomyces cerevisiae inositol-1-phosphate synthase (INO1) gene is regulated by factors that affect phospholipid synthesis. Mol. Cell. Biol. 6: 3320-3328.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3320-3328
    • Hirsch, J.P.1    Henry, S.A.2
  • 21
    • 0037128926 scopus 로고    scopus 로고
    • Induction of secretory pathway components in yeast is associated with increased stability of their mRNA
    • Hyde, M., L. Block-Alper, J. Felix, P. Webster and D. I. Meyer, 2002 Induction of secretory pathway components in yeast is associated with increased stability of their mRNA. J. Cell Biol. 156: 993-1001.
    • (2002) J. Cell Biol. , vol.156 , pp. 993-1001
    • Hyde, M.1    Block-Alper, L.2    Felix, J.3    Webster, P.4    Meyer, D.I.5
  • 22
    • 0030808558 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response
    • Kawahara, T., H. Yanagi, T. Yara and K. Mori, 1997 Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response. Mol. Biol. Cell 8: 1845-1862.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1845-1862
    • Kawahara, T.1    Yanagi, H.2    Yara, T.3    Mori, K.4
  • 23
    • 0024279590 scopus 로고
    • Regulation of phospholipid biosynthesis in Saccharomyces cerevisiae by inositol. Inositol is an inhibitor of phosphatidylserine synthase activity
    • Kelley, M. J., A. M. Bailis, S. A. Henry and G. M. Carman, 1988 Regulation of phospholipid biosynthesis in Saccharomyces cerevisiae by inositol. Inositol is an inhibitor of phosphatidylserine synthase activity. J. Biol. Chem. 263: 18078-18085.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18078-18085
    • Kelley, M.J.1    Bailis, A.M.2    Henry, S.A.3    Carman, G.M.4
  • 24
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno, K., K. Normington, J. Sambrook, M. J. Gething and K. Mori, 1993 The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell. Biol. 13: 877-890.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething, M.J.4    Mori, K.5
  • 25
    • 0025755893 scopus 로고
    • Analysis of sequences in the INO1 promoter that are involved in its regulation by phospholipid precursors
    • Lopes, J. M., J. P. Hirsch, P. A. Chorco, K. L. Schulze and S. A. Henry, 1991 Analysis of sequences in the INO1 promoter that are involved in its regulation by phospholipid precursors. Nucleic Acids Res. 19: 1687-1693.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1687-1693
    • Lopes, J.M.1    Hirsch, J.P.2    Chorco, P.A.3    Schulze, K.L.4    Henry, S.A.5
  • 26
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • McCracken, A. A., and J. L. Brodsky, 1996 Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132: 291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 27
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori, K., A. Sant, K. Kohno, K. Normington, M. J. Gething et al., 1992 A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J. 11: 2583-2593.
    • (1992) EMBO J. , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5
  • 28
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • Mori, K., W. Ma, M. J. Gethinc. and J. F. Sambrook, 1993 A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74: 743-756.
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gethinc, M.J.3    Sambrook, J.F.4
  • 29
    • 0034712734 scopus 로고    scopus 로고
    • mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response
    • Mori, K., N. Ogawa, T. Kawahara, S. Yanagi and T. Yura, 2000 mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response. Proc. Natl. Acad. Sci. USA 97: 4660-4665.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4660-4665
    • Mori, K.1    Ogawa, N.2    Kawahara, T.3    Yanagi, S.4    Yura, T.5
  • 30
    • 0034632033 scopus 로고    scopus 로고
    • The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
    • Ng, D. T., E. D. Spear and P. Walter, 2000 The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J. Cell Biol. 150: 77-88.
    • (2000) J. Cell Biol. , vol.150 , pp. 77-88
    • Ng, D.T.1    Spear, E.D.2    Walter, P.3
  • 31
    • 0026710871 scopus 로고    scopus 로고
    • IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae
    • Nikawa, J. I., and S. Yamashita, 1999 IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae. Mol. Microbiol. 6: 1441-1446.
    • (1999) Mol. Microbiol. , vol.6 , pp. 1441-1446
    • Nikawa, J.I.1    Yamashita, S.2
  • 32
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory, pathway
    • Novick, P., C. Field and R. Schekman, 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
  • 33
    • 0019424489 scopus 로고
    • Order of events in the yeast secretory pathway
    • Novick, P., S. Ferro and R. Schekman, 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
  • 34
    • 0030861295 scopus 로고    scopus 로고
    • Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidylcholine turn-over and INO1 regulation
    • Patton-Vogt, J. L., P. Griac, A. Sreenivas, V. Bruno, S. Dowd et al., 1997 Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidylcholine turn-over and INO1 regulation. J. Biol. Chem. 272: 90873-90883.
    • (1997) J. Biol. Chem. , vol.272 , pp. 90873-90883
    • Patton-Vogt, J.L.1    Griac, P.2    Sreenivas, A.3    Bruno, V.4    Dowd, S.5
  • 35
    • 0034650851 scopus 로고    scopus 로고
    • An essential role in liver development for transcription factor XBP-1
    • Reimold, A. M., A. Etkin, I. Clauss, A. Perkins D. S. Friend et al., 2000 An essential role in liver development for transcription factor XBP-1. Genes Dev. 14: 152-157.
    • (2000) Genes Dev. , vol.14 , pp. 152-157
    • Reimold, A.M.1    Etkin, A.2    Clauss, I.3    Perkins, A.4    Friend, D.S.5
  • 39
    • 0035812716 scopus 로고    scopus 로고
    • Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response
    • Ruegsegger, U., J. H. Leber and P. Walter, 2001 Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Cell 107: 103-114.
    • (2001) Cell , vol.107 , pp. 103-114
    • Ruegsegger, U.1    Leber, J.H.2    Walter, P.3
  • 41
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphoulation of the Ite1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C. E., and P. Walter, 1996 Oligomerization and phosphoulation of the Ite1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15: 3028-3039.
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 43
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • Sidrauski, C., and P. Walter, 1997 The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90: 1031-1039.
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 44
    • 0032479169 scopus 로고    scopus 로고
    • A role for phospholipase D1 (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast
    • Sreenivas, A., J. L. Patton-Vogt, V. Bruno, P. Griac: and S. A. Henry, 1998 A role for phospholipase D1 (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast. J. Biol. Chem. 273: 16635-16638.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16635-16638
    • Sreenivas, A.1    Patton-Vogt, J.L.2    Bruno, V.3    Griac, P.4    Henry, S.A.5
  • 45
    • 0015518138 scopus 로고
    • In vitro studies of phospholipid biosynthesis in Saccharomyces cerevisiae
    • Steiner, M. R., and R. L. Lester, 1972 In vitro studies of phospholipid biosynthesis in Saccharomyces cerevisiae. Biochim. Biophys. Acta 260: 222-243.
    • (1972) Biochim. Biophys. Acta , vol.260 , pp. 222-243
    • Steiner, M.R.1    Lester, R.L.2
  • 46
    • 0024256676 scopus 로고
    • Saccharomyces cerevisiae cho2 mutants are deficient in phospholipid methylation and cross-pathway regulation of inositol synthesis
    • Summers, E. F., V. A. Letts, P. McGraw and S. A. Henry, 1988 Saccharomyces cerevisiae cho2 mutants are deficient in phospholipid methylation and cross-pathway regulation of inositol synthesis. Genetics 120: 909-922.
    • (1988) Genetics , vol.120 , pp. 909-922
    • Summers, E.F.1    Letts, V.A.2    McGraw, P.3    Henry, S.A.4
  • 47
    • 0026553117 scopus 로고
    • Strategies for generating phospholipid synthesis mutants in yeast
    • edited by D. E. Vance and E. A. Dennis. Academic Press, San Diego
    • Swede, M. J., K. A. Hudak, J. M. Lopes and S. A. Henry, 1992 Strategies for generating phospholipid synthesis mutants in yeast, pp. 21-34 in Methods in Enzymology: Phospholipid Biosynthesis, edited by D. E. Vance and E. A. Dennis. Academic Press, San Diego.
    • (1992) Methods in Enzymology: Phospholipid Biosynthesis , pp. 21-34
    • Swede, M.J.1    Hudak, K.A.2    Lopes, J.M.3    Henry, S.A.4
  • 48
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers, K. J., C. K. Patil, L. Wodicka, D. J. Lockhart, J. S. Weissman et al., 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
  • 49
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endophasmic reticulum protein folding
    • Vashist, S., W. Kim, W. J. Belden, E. D. SPEAR, C. Barlowe et al., 2001 Distinct retrieval and retention mechanisms are required for the quality control of endophasmic reticulum protein folding. J. Cell Biol. 155: 355-367.
    • (2001) J. Cell Biol. , vol.155 , pp. 355-367
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5
  • 50
    • 0030918921 scopus 로고    scopus 로고
    • Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome
    • Webb, G. C., J. Zhang, S. J. Garlow, A. Wesp, H. Riezman et al., 1997 Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome. Mol. Biol. Cell 8: 871-895.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 871-895
    • Webb, G.C.1    Zhang, J.2    Garlow, S.J.3    Wesp, A.4    Riezman, H.5
  • 51
    • 0032514738 scopus 로고    scopus 로고
    • Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects
    • Xie, Z., M. Fang, M. Rivas, A. J. Faulkner, P. Sterweis et al., 1998 Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects. Proc. Natl. Acad. Sci. USA 95: 12346-12351.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12346-12351
    • Xie, Z.1    Fang, M.2    Rivas, M.3    Faulkner, A.J.4    Sterweis, P.5
  • 52
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H., T. Matsui, A. Yamamoto, T. Okada and K. Mori, 2001 XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107: 881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.