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Volumn 4, Issue 5, 2003, Pages 651-661

P58 IPK , a plant ortholog of double-stranded RNA-dependent protein kinase PKR inhibitor, functions in firal pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; INITIATION FACTOR; PROTEIN KINASE INHIBITOR; PROTEIN P58; UNCLASSIFIED DRUG;

EID: 0038668784     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1534-5807(03)00125-4     Document Type: Article
Times cited : (84)

References (41)
  • 1
    • 0031789863 scopus 로고    scopus 로고
    • Tobacco mosaic virus helicase domain induces necrosis in N gene-carrying tobacco in the absence of virus replication
    • Abbink T.E.M. Tjernberg P.A. Bol J.F. Linthorst J.M. Tobacco mosaic virus helicase domain induces necrosis in N gene-carrying tobacco in the absence of virus replication Mol. Plant Microbe Interact. 11 1998 1242-1246
    • (1998) Mol. Plant Microbe Interact. , vol.11 , pp. 1242-1246
    • Abbink, T.E.M.1    Tjernberg, P.A.2    Bol, J.F.3    Linthorst, J.M.4
  • 2
    • 0033119713 scopus 로고    scopus 로고
    • Fast forward genetics based on virus-induced gene silencing
    • Baulcombe D.C. Fast forward genetics based on virus-induced gene silencing Curr. Opin. Plant Biol. 2 1999 109-113
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 109-113
    • Baulcombe, D.C.1
  • 4
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dependent protein kinase PKR: Structure and function
    • Clemens M.J. Elia A. The double-stranded RNA-dependent protein kinase PKR: Structure and function J. Interferon Cytokine Res. 17 1997 503-524
    • (1997) J. Interferon Cytokine Res. , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 5
    • 0024288651 scopus 로고
    • Tobacco mosaic virus infection stimulates the phosphorylation of a plant protein associated with double-stranded RNA-dependent protein kinase activity
    • Crum C.J. Hu J. Hiddinga H.J. Roth D.A. Tobacco mosaic virus infection stimulates the phosphorylation of a plant protein associated with double-stranded RNA-dependent protein kinase activity J. Biol. Chem. 263 1988 13440-13443
    • (1988) J. Biol. Chem. , vol.263 , pp. 13440-13443
    • Crum, C.J.1    Hu, J.2    Hiddinga, H.J.3    Roth, D.A.4
  • 6
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl J.L. Jones J.D.G. Plant pathogens and integrated defence responses to infection Nature 411 2001 826-833
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.G.2
  • 7
    • 0033213918 scopus 로고    scopus 로고
    • Translation initiation: Adept at adapting
    • Dever T.E. Translation initiation: adept at adapting Trends Biochem. Sci. 24 1999 398-403
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 398-403
    • Dever, T.E.1
  • 9
    • 0029118217 scopus 로고
    • Abrogation of translation initiation factor eIF2 phosphorylation causes malignant transformation of NIH 3T3 cells
    • Donze O. Jagus R. Koromilas A.E. Hershey J.W.B. Sonenberg N. Abrogation of translation initiation factor eIF2 phosphorylation causes malignant transformation of NIH 3T3 cells EMBO J. 14 1995 3828-3834
    • (1995) EMBO J. , vol.14 , pp. 3828-3834
    • Donze, O.1    Jagus, R.2    Koromilas, A.E.3    Hershey, J.W.B.4    Sonenberg, N.5
  • 11
    • 0000152068 scopus 로고    scopus 로고
    • Interaction trap cloning with yeast
    • B. D. Hames, S. J. Higgins, & H. Hames (Eds.), Oxford: Oxford University Press
    • Finley R.L. Brent R. Interaction trap cloning with yeast Hames B.D. Higgins S.J. Hames H. Gene Probes: A Practical Approach 1996 169-201 Oxford University Press Oxford
    • (1996) Gene Probes: A Practical Approach , pp. 169-201
    • Finley, R.L.1    Brent, R.2
  • 12
    • 0345164384 scopus 로고    scopus 로고
    • Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase
    • Gale M. Katze M.G. Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase Pharmacol. Ther. 78 1998 29-46
    • (1998) Pharmacol. Ther. , vol.78 , pp. 29-46
    • Gale, M.1    Katze, M.G.2
  • 13
    • 8944219769 scopus 로고    scopus 로고
    • IPK and vaccinia virus K3L is mediated by unique domains: Implications for kinase regulation
    • IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation Mol. Cell. Biol. 16 1996 4172-4181
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4172-4181
    • Gale, M.J.1    Tan, S.-L.2    Wambach, M.3    Katze, M.G.4
  • 15
    • 0344731406 scopus 로고    scopus 로고
    • Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the a subunit of eukaryotic translation initiation factor 2 and NF-κB
    • Gil J. Alcami J. Esteban M. Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the a subunit of eukaryotic translation initiation factor 2 and NF-κB Mol. Cell. Biol. 19 1999 4653-4663
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4653-4663
    • Gil, J.1    Alcami, J.2    Esteban, M.3
  • 16
    • 0034084338 scopus 로고    scopus 로고
    • Induction of apoptosis by the dsRNA-dependent protein kinase (PKR): Mechanism of action
    • Gil J. Esteban M. Induction of apoptosis by the dsRNA-dependent protein kinase (PKR): Mechanism of action Apoptosis 5 2000 107-114
    • (2000) Apoptosis , vol.5 , pp. 107-114
    • Gil, J.1    Esteban, M.2
  • 17
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P. Zhang Y. Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase Nature 397 1999 271-274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 18
    • 0031769602 scopus 로고    scopus 로고
    • Changing patterns of localization of the tobacco mosaic virus movement protein and replicase to the endoplasmic reticulum and microtubules during infection
    • Heinlein M. Padgett H.S. Gens J.S. Pickard B.G. Casper S.J. Epel B.L. Beachy R.N. Changing patterns of localization of the tobacco mosaic virus movement protein and replicase to the endoplasmic reticulum and microtubules during infection Plant Cell 10 1998 1107-1120
    • (1998) Plant Cell , vol.10 , pp. 1107-1120
    • Heinlein, M.1    Padgett, H.S.2    Gens, J.S.3    Pickard, B.G.4    Casper, S.J.5    Epel, B.L.6    Beachy, R.N.7
  • 19
    • 0023695807 scopus 로고
    • Viroid-induced phosphorylation of a host protein related to a dsRNA-dependent protein kinase
    • Hiddinga H.J. Crum C.J. Roth D.A. Viroid-induced phosphorylation of a host protein related to a dsRNA-dependent protein kinase Science 241 1985 451-453
    • (1985) Science , vol.241 , pp. 451-453
    • Hiddinga, H.J.1    Crum, C.J.2    Roth, D.A.3
  • 20
    • 0028695223 scopus 로고
    • The eIF-2 alpha kinases: Regulators of protein synthesis in starvation and stress
    • Hinnebusch A.G. The eIF-2 alpha kinases: regulators of protein synthesis in starvation and stress Sem. Cell Biol. 5 1994 417-426
    • (1994) Sem. Cell Biol. , vol.5 , pp. 417-426
    • Hinnebusch, A.G.1
  • 21
    • 0034881650 scopus 로고    scopus 로고
    • Tobamovirus replicase coding region is involved in cell-to-cell movement
    • Hirashima K. Watanabe Y. Tobamovirus replicase coding region is involved in cell-to-cell movement J. Virol. 75 2001 8831-8836
    • (2001) J. Virol. , vol.75 , pp. 8831-8836
    • Hirashima, K.1    Watanabe, Y.2
  • 22
    • 0000435517 scopus 로고
    • Inheritance of resistance to tobacco-mosaic disease in tobacco
    • Holmes F.O. Inheritance of resistance to tobacco-mosaic disease in tobacco Phytopathology 28 1938 553-561
    • (1938) Phytopathology , vol.28 , pp. 553-561
    • Holmes, F.O.1
  • 23
    • 0036715591 scopus 로고    scopus 로고
    • Viruses and interferon: A fight for supremacy
    • Katze M.G. He Y. Gale M. Viruses and interferon: a fight for supremacy Nat. Rev. Immunol. 2 2002 675-687
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 675-687
    • Katze, M.G.1    He, Y.2    Gale, M.3
  • 24
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls Genes Dev. 13 1999 1211-1233
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 25
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley W.L. The J-domain family and the recruitment of chaperone power Trends Biochem. Sci. 23 1998 222-227
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 26
    • 0028998441 scopus 로고
    • Tetratrico peptide repeat interactions: To TPR or not to TPR?
    • Lamb J.R. Tugendreich S. Hieter P. Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends Biochem. Sci. 20 1995 257-259
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 27
    • 0029328380 scopus 로고
    • Identification of a plant-encoded analog of PKR, the mammalian double-stranded RNA-dependent protein kinase
    • Langland J.O. Jin S. Jacobs B.L. Roth D.A. Identification of a plant-encoded analog of PKR, the mammalian double-stranded RNA-dependent protein kinase Plant Physiol. 108 1995 1259-1267
    • (1995) Plant Physiol. , vol.108 , pp. 1259-1267
    • Langland, J.O.1    Jin, S.2    Jacobs, B.L.3    Roth, D.A.4
  • 28
    • 0027949937 scopus 로고
    • The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • Lee T.G. Tang N. Thompson S. Miller J. Katze M.G. The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins Mol. Cell. Biol. 14 1994 2331-2342
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 29
    • 0035984050 scopus 로고    scopus 로고
    • Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to tobacco mosaic virus
    • Liu Y. Schiff M. Serino G. Deng X.-W. Dinesh-Kumar S.P. Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to tobacco mosaic virus Plant Cell 14 2002 1483-1496
    • (2002) Plant Cell , vol.14 , pp. 1483-1496
    • Liu, Y.1    Schiff, M.2    Serino, G.3    Deng, X.-W.4    Dinesh-Kumar, S.P.5
  • 30
    • 0036015061 scopus 로고    scopus 로고
    • Tobacco Rar1, EDS1 and NPR1/NIM1 like genes are required for N-mediated resistance to tobacco mosaic virus
    • Liu Y. Schiff M. Marathe R. Dinesh-Kumar S.P. Tobacco Rar1, EDS1 and NPR1/NIM1 like genes are required for N-mediated resistance to tobacco mosaic virus Plant J. 30 2002 415-429
    • (2002) Plant J. , vol.30 , pp. 415-429
    • Liu, Y.1    Schiff, M.2    Marathe, R.3    Dinesh-Kumar, S.P.4
  • 32
    • 0033624975 scopus 로고    scopus 로고
    • IPK , a novel cochaperone containing tetratricopeptide repeats and a J-domain with oncogenic potential
    • IPK , a novel cochaperone containing tetratricopeptide repeats and a J-domain with oncogenic potential Cell. Mol. Life Sci. 57 2000 311-322
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 311-322
    • Melville, M.W.1    Katze, M.G.2    Tan, S.-L.3
  • 33
    • 0030759411 scopus 로고    scopus 로고
    • Identification of the TMV replicase sequence that activates the N gene-mediated hypersensitive response
    • Padgett H.S. Watanabe Y. Beachy R.N. Identification of the TMV replicase sequence that activates the N gene-mediated hypersensitive response Mol. Plant Microbe Interact. 10 1997 709-715
    • (1997) Mol. Plant Microbe Interact. , vol.10 , pp. 709-715
    • Padgett, H.S.1    Watanabe, Y.2    Beachy, R.N.3
  • 34
    • 0029923279 scopus 로고    scopus 로고
    • Rapsyn's knobs and holes: Eight tetratricopeptide repeats
    • Ponting C.C.P. Phillips C. Rapsyn's knobs and holes: eight tetratricopeptide repeats Biochem. J. 314 1996 1053-1056
    • (1996) Biochem. J. , vol.314 , pp. 1053-1056
    • Ponting, C.C.P.1    Phillips, C.2
  • 35
    • 0032530963 scopus 로고    scopus 로고
    • Tobacco mosaic virus infection induces severe morphological changes of the endoplasmic reticulum
    • Reichel C. Beachy R.N. Tobacco mosaic virus infection induces severe morphological changes of the endoplasmic reticulum Proc. Natl. Acad. Sci. USA 95 1999 11169-11174
    • (1999) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11169-11174
    • Reichel, C.1    Beachy, R.N.2
  • 36
    • 0033559493 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex
    • Roy B. Lee A.S. The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex Nucleic Acids Res. 27 1999 1437-1443
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1437-1443
    • Roy, B.1    Lee, A.S.2
  • 37
    • 3643145804 scopus 로고    scopus 로고
    • Initiation and maintenance of virus-induced gene silencing
    • Ruiz M.T. Voinnet O. Baulcombe D.C. Initiation and maintenance of virus-induced gene silencing Plant Cell 10 1998 937-946
    • (1998) Plant Cell , vol.10 , pp. 937-946
    • Ruiz, M.T.1    Voinnet, O.2    Baulcombe, D.C.3
  • 38
    • 0030915143 scopus 로고    scopus 로고
    • Formation of plant RNA virus replication complexes on membranes: Role of an endoplasmic reticulum-targeted viral protein
    • Schaad M.C. Jensen P.E. Carrington J.C. Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein EMBO J. 16 1997 4049-4059
    • (1997) EMBO J. , vol.16 , pp. 4049-4059
    • Schaad, M.C.1    Jensen, P.E.2    Carrington, J.C.3
  • 41
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan W. Frank C.L. Korth M.J. Sopher B.L. Novoa I. Ron D. Katze M.G. Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK Proc. Natl. Acad. Sci. USA 99 2002 15920-15925
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15920-15925
    • Yan, W.1    Frank, C.L.2    Korth, M.J.3    Sopher, B.L.4    Novoa, I.5    Ron, D.6    Katze, M.G.7


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