메뉴 건너뛰기




Volumn 28, Issue 5, 2014, Pages 1965-1974

The impact of PKR activation: From neurodegeneration to cancer

Author keywords

Apoptosis; Protein kinase R; Protein kinase R modulators

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INITIATION FACTOR 2ALPHA; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; METHIONYL AMINOPEPTIDASE 2; MICRORNA; PACT PROTEIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN; PROTEIN KINASE R; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 84901045220     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.13-248294     Document Type: Review
Times cited : (87)

References (137)
  • 3
    • 84864363275 scopus 로고    scopus 로고
    • Alzheimer disease controls cancer: Concerning the apoptogenic interaction of cell membranestanding type-1 VDAC and amyloid peptides via GxxxG motifs
    • Thinnes, F. P. (2012) Alzheimer disease controls cancer: concerning the apoptogenic interaction of cell membranestanding type-1 VDAC and amyloid peptides via GxxxG motifs. Mol. Genet. Metab. 106, 502-503
    • (2012) Mol. Genet. Metab. , vol.106 , pp. 502-503
    • Thinnes, F.P.1
  • 4
    • 78651488459 scopus 로고    scopus 로고
    • The role of protein kinase R in the interferon response
    • Pindel, A., and Sadler, A. (2011) The role of protein kinase R in the interferon response. J. Interferon Cytokine Res. 31, 59-70
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 59-70
    • Pindel, A.1    Sadler, A.2
  • 6
    • 0035800333 scopus 로고    scopus 로고
    • Signal integration via PKR
    • Williams, B. R. (2001) Signal integration via PKR. Sci. STKE 2001, re2
    • (2001) Sci. STKE , vol.2001
    • Williams, B.R.1
  • 7
  • 8
    • 0033230617 scopus 로고    scopus 로고
    • PKR: A sentinel kinase for cellular stress
    • Williams, B. R. (1999) PKR: a sentinel kinase for cellular stress. Oncogene 18, 6112-6120
    • (1999) Oncogene , vol.18 , pp. 6112-6120
    • Williams, B.R.1
  • 9
    • 84869414509 scopus 로고    scopus 로고
    • Specificity of the double-stranded RNAbinding domain from the RNA-activated protein kinase PKR for double-stranded RNA: Insights from thermodynamics and small-angle X-ray scattering
    • Patel, S., Blose, J. M., Sokoloski, J. E., Pollack, L., and Bevilacqua, P. C. (2012) Specificity of the double-stranded RNAbinding domain from the RNA-activated protein kinase PKR for double-stranded RNA: insights from thermodynamics and small-angle X-ray scattering. Biochemistry 51, 9312-9322
    • (2012) Biochemistry , vol.51 , pp. 9312-9322
    • Patel, S.1    Blose, J.M.2    Sokoloski, J.E.3    Pollack, L.4    Bevilacqua, P.C.5
  • 10
    • 70349305529 scopus 로고    scopus 로고
    • PKR, the double stranded RNA-dependent protein kinase as a critical target in Alzheimer's disease
    • Morel, M., Couturier, J., Lafay-Chebassier, C., Paccalin, M., and Page, G. (2009) PKR, the double stranded RNA-dependent protein kinase as a critical target in Alzheimer's disease. J. Cell. Mol. Med. 13, 1476-1488
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 1476-1488
    • Morel, M.1    Couturier, J.2    Lafay-Chebassier, C.3    Paccalin, M.4    Page, G.5
  • 11
    • 50249156475 scopus 로고    scopus 로고
    • The role of PACT in mediating gene induction, PKR activation, and apoptosis in response to diverse stimuli
    • Marques, J. T., White, C. L., Peters, G. A., Williams, B. R., and Sen, G. C. (2008) The role of PACT in mediating gene induction, PKR activation, and apoptosis in response to diverse stimuli. J. Interferon Cytokine Res. 28, 469-476
    • (2008) J. Interferon Cytokine Res. , vol.28 , pp. 469-476
    • Marques, J.T.1    White, C.L.2    Peters, G.A.3    Williams, B.R.4    Sen, G.C.5
  • 12
    • 84862517868 scopus 로고    scopus 로고
    • Increased interaction between PACT molecules in response to stress signals is required for PKR activation
    • Singh, M., and Patel, R. C. (2012) Increased interaction between PACT molecules in response to stress signals is required for PKR activation. J. Cell. Biochem. 113, 2754-2764
    • (2012) J. Cell. Biochem. , vol.113 , pp. 2754-2764
    • Singh, M.1    Patel, R.C.2
  • 15
    • 0034624770 scopus 로고    scopus 로고
    • Activation of NF-kappa B by the dsRNA-dependent protein kinase, PKR involves the i kappa B kinase complex
    • Gil, J., Alcami, J., and Esteban, M. (2000) Activation of NF-kappa B by the dsRNA-dependent protein kinase, PKR involves the I kappa B kinase complex. Oncogene 19, 1369-1378
    • (2000) Oncogene , vol.19 , pp. 1369-1378
    • Gil, J.1    Alcami, J.2    Esteban, M.3
  • 17
    • 66049147774 scopus 로고    scopus 로고
    • PKR, a p53 target gene, plays a crucial role in the tumor-suppressor function of p53
    • Yoon, C. H., Lee, E. S., Lim, D. S., and Bae, Y. S. (2009) PKR, a p53 target gene, plays a crucial role in the tumor-suppressor function of p53. Proc. Natl. Acad. Sci. U. S. A. 106, 7852-7857
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 7852-7857
    • Yoon, C.H.1    Lee, E.S.2    Lim, D.S.3    Bae, Y.S.4
  • 18
    • 84857708456 scopus 로고    scopus 로고
    • Enhanced phosphorylation of STAT-1 is dependent on double-stranded RNA-dependent protein kinase signaling in HLA-B27-expressing U937 monocytic cells
    • Ruuska, M., Sahlberg, A. S., Colbert, R. A., Granfors, K., and Penttinen, M. A. (2012) Enhanced phosphorylation of STAT-1 is dependent on double-stranded RNA-dependent protein kinase signaling in HLA-B27-expressing U937 monocytic cells. Arthritis Rheum. 64, 772-777
    • (2012) Arthritis Rheum. , vol.64 , pp. 772-777
    • Ruuska, M.1    Sahlberg, A.S.2    Colbert, R.A.3    Granfors, K.4    Penttinen, M.A.5
  • 19
    • 84868138734 scopus 로고    scopus 로고
    • Double-stranded RNAdependent protein kinase regulates the motility of breast cancer cells
    • Xu, M., Chen, G., Wang, S., Liao, M., Frank, J. A., Bower, K. A., Zhang, Z., Shi, X., and Luo, J. (2012) Double-stranded RNAdependent protein kinase regulates the motility of breast cancer cells. PLoS ONE 7, e47721
    • (2012) PLoS ONE , vol.7
    • Xu, M.1    Chen, G.2    Wang, S.3    Liao, M.4    Frank, J.A.5    Bower, K.A.6    Zhang, Z.7    Shi, X.8    Luo, J.9
  • 20
    • 0036892618 scopus 로고    scopus 로고
    • Involvement of double-stranded RNAdependent protein kinase and phosphorylation of eukaryotic initiation factor-2alpha in neuronal degeneration
    • Chang, R. C., Suen, K. C., Ma, C. H., Elyaman, W., Ng, H. K., and Hugon, J. (2002) Involvement of double-stranded RNAdependent protein kinase and phosphorylation of eukaryotic initiation factor-2alpha in neuronal degeneration. J. Neurochem. 83, 1215-1225
    • (2002) J. Neurochem. , vol.83 , pp. 1215-1225
    • Chang, R.C.1    Suen, K.C.2    Ma, C.H.3    Elyaman, W.4    Ng, H.K.5    Hugon, J.6
  • 21
    • 0348010382 scopus 로고    scopus 로고
    • Upstream signaling pathways leading to the activation of double-stranded RNA-dependent serine/threonine protein kinase in beta-amyloid peptide neurotoxicity
    • Suen, K. C., Yu, M. S., So, K. F., Chang, R. C., and Hugon, J. (2003) Upstream signaling pathways leading to the activation of double-stranded RNA-dependent serine/threonine protein kinase in beta-amyloid peptide neurotoxicity. J. Biol. Chem. 278, 49819-49827
    • (2003) J. Biol. Chem. , vol.278 , pp. 49819-49827
    • Suen, K.C.1    Yu, M.S.2    So, K.F.3    Chang, R.C.4    Hugon, J.5
  • 22
    • 1842562209 scopus 로고    scopus 로고
    • An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer's disease
    • Onuki, R., Bando, Y., Suyama, E., Katayama, T., Kawasaki, H., Baba, T., Tohyama, M., and Taira, K. (2004) An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer's disease. EMBO J. 23, 959-968
    • (2004) EMBO J. , vol.23 , pp. 959-968
    • Onuki, R.1    Bando, Y.2    Suyama, E.3    Katayama, T.4    Kawasaki, H.5    Baba, T.6    Tohyama, M.7    Taira, K.8
  • 23
    • 0035878553 scopus 로고    scopus 로고
    • Double-stranded RNAdependent protein kinase, PKR, binds preferentially to Huntington's disease (HD) transcripts and is activated in HD tissue
    • Peel, A. L., Rao, R. V., Cottrell, B. A., Hayden, M. R., Ellerby, L. M., and Bredesen, D. E. (2001) Double-stranded RNAdependent protein kinase, PKR, binds preferentially to Huntington's disease (HD) transcripts and is activated in HD tissue. Hum. Mol. Genet. 10, 1531-1538
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1531-1538
    • Peel, A.L.1    Rao, R.V.2    Cottrell, B.A.3    Hayden, M.R.4    Ellerby, L.M.5    Bredesen, D.E.6
  • 24
    • 9644303217 scopus 로고    scopus 로고
    • Double-strand RNA dependent protein kinase (PKR) is involved in the extrastriatal degeneration in Parkinson's disease and Huntington's disease
    • Bando, Y., Onuki, R., Katayama, T., Manabe, T., Kudo, T., Taira, K., and Tohyama, M. (2005) Double-strand RNA dependent protein kinase (PKR) is involved in the extrastriatal degeneration in Parkinson's disease and Huntington's disease. Neurochem. Int. 46, 11-18
    • (2005) Neurochem. Int. , vol.46 , pp. 11-18
    • Bando, Y.1    Onuki, R.2    Katayama, T.3    Manabe, T.4    Kudo, T.5    Taira, K.6    Tohyama, M.7
  • 25
    • 0842288218 scopus 로고    scopus 로고
    • PKR activation in neurodegenerative disease
    • Peel, A. L. (2004) PKR activation in neurodegenerative disease. J Neuropathol. Exp. Neurol. 63, 97-105
    • (2004) J Neuropathol. Exp. Neurol. , vol.63 , pp. 97-105
    • Peel, A.L.1
  • 26
    • 84884660617 scopus 로고    scopus 로고
    • Gene expression regulation by upstream open reading frames and human disease
    • Barbosa, C., Peixeiro, I., and Romao, L. (2013) Gene expression regulation by upstream open reading frames and human disease. PLoS Genet. 9, e1003529
    • (2013) PLoS Genet. , vol.9
    • Barbosa, C.1    Peixeiro, I.2    Romao, L.3
  • 28
    • 79251575329 scopus 로고    scopus 로고
    • Modulation of tau phosphorylation by the kinase PKR: Implications in Alzheimer's disease
    • Bose, A., Mouton-Liger, F., Paquet, C., Mazot, P., Vigny, M., Gray, F., and Hugon, J. (2011) Modulation of tau phosphorylation by the kinase PKR: implications in Alzheimer's disease. Brain Pathol. 21, 189-200
    • (2011) Brain Pathol. , vol.21 , pp. 189-200
    • Bose, A.1    Mouton-Liger, F.2    Paquet, C.3    Mazot, P.4    Vigny, M.5    Gray, F.6    Hugon, J.7
  • 29
    • 79959441142 scopus 로고    scopus 로고
    • Prevention of the beta-amyloid peptide-induced inflammatory process by inhibition of double-stranded RNA-dependent protein kinase in primary murine mixed co-cultures
    • Couturier, J., Paccalin, M., Morel, M., Terro, F., Milin, S., Pontcharraud, R., Fauconneau, B., and Page, G. (2011) Prevention of the beta-amyloid peptide-induced inflammatory process by inhibition of double-stranded RNA-dependent protein kinase in primary murine mixed co-cultures. J. Neuroinflammation 8, 72
    • (2011) J. Neuroinflammation , vol.8 , pp. 72
    • Couturier, J.1    Paccalin, M.2    Morel, M.3    Terro, F.4    Milin, S.5    Pontcharraud, R.6    Fauconneau, B.7    Page, G.8
  • 30
    • 84860285084 scopus 로고    scopus 로고
    • Pharmacological inhibition of PKR in APPswePS1dE9 mice transiently prevents inflammation at 12 months of age but increases Abeta42 levels in the late stages of the Alzheimer's disease
    • Couturier, J., Paccalin, M., Lafay-Chebassier, C., Chalon, S., Ingrand, I., Pinguet, J., Pontcharraud, R., Guillard, O., Fauconneau, B., and Page, G. (2012) Pharmacological inhibition of PKR in APPswePS1dE9 mice transiently prevents inflammation at 12 months of age but increases Abeta42 levels in the late stages of the Alzheimer's disease. Curr. Alzheimer Res. 9, 344-360
    • (2012) Curr. Alzheimer Res. , vol.9 , pp. 344-360
    • Couturier, J.1    Paccalin, M.2    Lafay-Chebassier, C.3    Chalon, S.4    Ingrand, I.5    Pinguet, J.6    Pontcharraud, R.7    Guillard, O.8    Fauconneau, B.9    Page, G.10
  • 32
    • 70350167138 scopus 로고    scopus 로고
    • Could PKR inhibition modulate human neurodegeneration?
    • Hugon, J., Paquet, C., and Chang, R. C. (2009) Could PKR inhibition modulate human neurodegeneration? Expert Rev. Neurother. 9, 1455-1457
    • (2009) Expert Rev. Neurother. , vol.9 , pp. 1455-1457
    • Hugon, J.1    Paquet, C.2    Chang, R.C.3
  • 34
    • 84873292476 scopus 로고    scopus 로고
    • Blocking the eIF2alpha kinase (PKR) enhances positive and negative forms of cortex-dependent taste memory
    • Stern, E., Chinnakkaruppan, A., David, O., Sonenberg, N., and Rosenblum, K. (2013) Blocking the eIF2alpha kinase (PKR) enhances positive and negative forms of cortex-dependent taste memory. J. Neurosci. 33, 2517-2525
    • (2013) J. Neurosci. , vol.33 , pp. 2517-2525
    • Stern, E.1    Chinnakkaruppan, A.2    David, O.3    Sonenberg, N.4    Rosenblum, K.5
  • 35
    • 84885070972 scopus 로고    scopus 로고
    • Small molecule modulators of eukaryotic initiation factor 2alpha kinases, the key regulators of protein synthesis
    • Joshi, M., Kulkarni, A., and Pal, J. K. (2013) Small molecule modulators of eukaryotic initiation factor 2alpha kinases, the key regulators of protein synthesis. Biochimie 95, 1980-1990
    • (2013) Biochimie , vol.95 , pp. 1980-1990
    • Joshi, M.1    Kulkarni, A.2    Pal, J.K.3
  • 36
    • 55949137191 scopus 로고    scopus 로고
    • A chemical compound commonly used to inhibit PKR, {8-(imidazol-4- ylmethylene)-6H-azolidino[5,4-g] benzothiazol-7-one}, protects neurons by inhibiting cyclin-dependent kinase
    • Chen, H. M., Wang, L., and D'Mello, S. R. (2008) A chemical compound commonly used to inhibit PKR, {8-(imidazol-4-ylmethylene)-6H-azolidino[5,4-g] benzothiazol-7-one}, protects neurons by inhibiting cyclin-dependent kinase. Eur. J. Neurosci. 28, 2003-2016
    • (2008) Eur. J. Neurosci. , vol.28 , pp. 2003-2016
    • Chen, H.M.1    Wang, L.2    D'Mello, S.R.3
  • 41
    • 80055091982 scopus 로고    scopus 로고
    • Fluazinam-induced apoptosis of SH-SY5Y cells is mediated by p53 and Bcl-2 family proteins
    • Lee, J. E., Kang, J. S., Shin, I. C., Lee, S. J., Hyun, D. H., Lee, K. S., and Koh, H. C. (2011) Fluazinam-induced apoptosis of SH-SY5Y cells is mediated by p53 and Bcl-2 family proteins. Neurotoxicology 32, 702-710
    • (2011) Neurotoxicology , vol.32 , pp. 702-710
    • Lee, J.E.1    Kang, J.S.2    Shin, I.C.3    Lee, S.J.4    Hyun, D.H.5    Lee, K.S.6    Koh, H.C.7
  • 43
    • 77955963832 scopus 로고    scopus 로고
    • P53-mediated neuronal cell death in ischemic brain injury
    • Hong, L. Z., Zhao, X. Y., and Zhang, H. L. (2010) p53-mediated neuronal cell death in ischemic brain injury. Neurosci. Bull. 26, 232-240
    • (2010) Neurosci. Bull. , vol.26 , pp. 232-240
    • Hong, L.Z.1    Zhao, X.Y.2    Zhang, H.L.3
  • 44
    • 84867649631 scopus 로고    scopus 로고
    • Inhibition of p53 transactivation functionally interacts with microtubule stabilization to suppress excitotoxicity-induced axon degeneration
    • Fujiwara, T., and Morimoto, K. (2012) Inhibition of p53 transactivation functionally interacts with microtubule stabilization to suppress excitotoxicity-induced axon degeneration. Biochem. Biophys. Res. Commun. 427, 100-106
    • (2012) Biochem. Biophys. Res. Commun. , vol.427 , pp. 100-106
    • Fujiwara, T.1    Morimoto, K.2
  • 45
    • 84857038779 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta inhibitors protect hippocampal neurons from radiation-induced apoptosis by regulating MDM2-p53 pathway
    • Thotala, D. K., Hallahan, D. E., and Yazlovitskaya, E. M. (2012) Glycogen synthase kinase 3beta inhibitors protect hippocampal neurons from radiation-induced apoptosis by regulating MDM2-p53 pathway. Cell Death Differ. 19, 387-396
    • (2012) Cell Death Differ. , vol.19 , pp. 387-396
    • Thotala, D.K.1    Hallahan, D.E.2    Yazlovitskaya, E.M.3
  • 46
    • 77953184918 scopus 로고    scopus 로고
    • HIF-1 antagonizes p53-mediated apoptosis through a secreted neuronal tyrosinase
    • Sendoel, A., Kohler, I., Fellmann, C., Lowe, S. W., and Hengartner, M. O. (2010) HIF-1 antagonizes p53-mediated apoptosis through a secreted neuronal tyrosinase. Nature 465, 577-583
    • (2010) Nature , vol.465 , pp. 577-583
    • Sendoel, A.1    Kohler, I.2    Fellmann, C.3    Lowe, S.W.4    Hengartner, M.O.5
  • 47
    • 63849206749 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors prevent p53-dependent and p53-independent Bax-mediated neuronal apoptosis through two distinct mechanisms
    • Uo, T., Veenstra, T. D., and Morrison, R. S. (2009) Histone deacetylase inhibitors prevent p53-dependent and p53-independent Bax-mediated neuronal apoptosis through two distinct mechanisms. J. Neurosci. 29, 2824-2832
    • (2009) J. Neurosci. , vol.29 , pp. 2824-2832
    • Uo, T.1    Veenstra, T.D.2    Morrison, R.S.3
  • 48
    • 77955709610 scopus 로고    scopus 로고
    • HDAC inhibition promotes neuronal outgrowth and counteracts growth cone collapse through CBP/p300 and P/CAF-dependent p53 acetylation
    • Gaub, P., Tedeschi, A., Puttagunta, R., Nguyen, T., Schmandke, A., and Di Giovanni, S. (2010) HDAC inhibition promotes neuronal outgrowth and counteracts growth cone collapse through CBP/p300 and P/CAF-dependent p53 acetylation. Cell Death Differ. 17, 1392-1408
    • (2010) Cell Death Differ. , vol.17 , pp. 1392-1408
    • Gaub, P.1    Tedeschi, A.2    Puttagunta, R.3    Nguyen, T.4    Schmandke, A.5    Di Giovanni, S.6
  • 50
    • 84870568314 scopus 로고    scopus 로고
    • SCYL1BP1 modulates neurite outgrowth and regeneration by regulating the Mdm2/p53 pathway
    • Liu, Y., Chen, Y., Lu, X., Wang, Y., Duan, Y., Cheng, C., and Shen, A. (2012) SCYL1BP1 modulates neurite outgrowth and regeneration by regulating the Mdm2/p53 pathway. Mol. Biol. Cell 23, 4506-4514
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4506-4514
    • Liu, Y.1    Chen, Y.2    Lu, X.3    Wang, Y.4    Duan, Y.5    Cheng, C.6    Shen, A.7
  • 51
    • 77954505297 scopus 로고    scopus 로고
    • Unfolded p53 in blood as a predictive signature signature of the transition from mild cognitive impairment to Alzheimer's disease
    • Lanni, C., Racchi, M., Stanga, S., Mazzini, G., Ranzenigo, A., Polotti, R., Memo, M., Govoni, S., and Uberti, D. (2010) Unfolded p53 in blood as a predictive signature signature of the transition from mild cognitive impairment to Alzheimer's disease. J. Alzheimers Dis. 20, 97-104
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 97-104
    • Lanni, C.1    Racchi, M.2    Stanga, S.3    Mazzini, G.4    Ranzenigo, A.5    Polotti, R.6    Memo, M.7    Govoni, S.8    Uberti, D.9
  • 52
    • 72549104579 scopus 로고    scopus 로고
    • P53-mediated G(1)/S checkpoint dysfunction in lymphocytes from Alzheimer's disease patients
    • Zhou, X., and Jia, J. (2010) P53-mediated G(1)/S checkpoint dysfunction in lymphocytes from Alzheimer's disease patients. Neurosci. Lett. 468, 320-325
    • (2010) Neurosci. Lett. , vol.468 , pp. 320-325
    • Zhou, X.1    Jia, J.2
  • 53
    • 77951046871 scopus 로고    scopus 로고
    • High sensitivity to carcinogens in the brain of a mouse model of Alzheimer's disease
    • Serrano, J., Fernandez, A. P., Martinez-Murillo, R., and Martinez, A. (2010) High sensitivity to carcinogens in the brain of a mouse model of Alzheimer's disease. Oncogene 29, 2165-2171
    • (2010) Oncogene , vol.29 , pp. 2165-2171
    • Serrano, J.1    Fernandez, A.P.2    Martinez-Murillo, R.3    Martinez, A.4
  • 54
    • 84874915777 scopus 로고    scopus 로고
    • Searching for predictive blood biomarkers: Misfolded p53 in mild cognitive impairment
    • Stanga, S., Lanni, C., Sinforiani, E., Mazzini, G., and Racchi, M. (2012) Searching for predictive blood biomarkers: misfolded p53 in mild cognitive impairment. Curr. Alzheimer Res. 9, 1191-1197
    • (2012) Curr. Alzheimer Res. , vol.9 , pp. 1191-1197
    • Stanga, S.1    Lanni, C.2    Sinforiani, E.3    Mazzini, G.4    Racchi, M.5
  • 55
    • 84860494301 scopus 로고    scopus 로고
    • Combination of p53(ser15) and p21/p21(thr145) in peripheral blood lymphocytes as potential Alzheimer's disease biomarkers
    • Tan, M., Wang, S., Song, J., and Jia, J. (2012) Combination of p53(ser15) and p21/p21(thr145) in peripheral blood lymphocytes as potential Alzheimer's disease biomarkers. Neurosci. Lett. 516, 226-231
    • (2012) Neurosci. Lett. , vol.516 , pp. 226-231
    • Tan, M.1    Wang, S.2    Song, J.3    Jia, J.4
  • 56
    • 0033614407 scopus 로고    scopus 로고
    • The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro
    • Cuddihy, A. R., Wong, A. H., Tam, N. W., Li, S., and Koromilas, A. E. (1999) The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro. Oncogene 18, 2690-2702
    • (1999) Oncogene , vol.18 , pp. 2690-2702
    • Cuddihy, A.R.1    Wong, A.H.2    Tam, N.W.3    Li, S.4    Koromilas, A.E.5
  • 57
    • 41249089202 scopus 로고    scopus 로고
    • PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation
    • Raven, J. F., Baltzis, D., Wang, S., Mounir, Z., Papadakis, A. I., Gao, H. Q., and Koromilas, A. E. (2008) PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation. J. Biol. Chem. 283, 3097-3108
    • (2008) J. Biol. Chem. , vol.283 , pp. 3097-3108
    • Raven, J.F.1    Baltzis, D.2    Wang, S.3    Mounir, Z.4    Papadakis, A.I.5    Gao, H.Q.6    Koromilas, A.E.7
  • 58
    • 70349323831 scopus 로고    scopus 로고
    • PKR, a cognitive decline biomarker, can regulate translation via two consecutive molecular targets p53 and Redd1 in lymphocytes of AD patients
    • Damjanac, M., Page, G., Ragot, S., Laborie, G., Gil, R., Hugon, J., and Paccalin, M. (2009) PKR, a cognitive decline biomarker, can regulate translation via two consecutive molecular targets p53 and Redd1 in lymphocytes of AD patients. J. Cell. Mol. Med. 13, 1823-1832
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 1823-1832
    • Damjanac, M.1    Page, G.2    Ragot, S.3    Laborie, G.4    Gil, R.5    Hugon, J.6    Paccalin, M.7
  • 59
    • 69749122264 scopus 로고    scopus 로고
    • Evidence of molecular links between PKR and mTOR signalling pathways in Abeta neurotoxicity: Role of p53, Redd1 and TSC2
    • Morel, M., Couturier, J., Pontcharraud, R., Gil, R., Fauconneau, B., Paccalin, M., and Page, G. (2009) Evidence of molecular links between PKR and mTOR signalling pathways in Abeta neurotoxicity: role of p53, Redd1 and TSC2. Neurobiol. Dis. 36, 151-161
    • (2009) Neurobiol. Dis. , vol.36 , pp. 151-161
    • Morel, M.1    Couturier, J.2    Pontcharraud, R.3    Gil, R.4    Fauconneau, B.5    Paccalin, M.6    Page, G.7
  • 60
    • 77952509193 scopus 로고    scopus 로고
    • Uncovering the PKR pathway's potential for treatment of tumors
    • Mounir, Z., and Koromilas, A. E. (2010) Uncovering the PKR pathway's potential for treatment of tumors. Future Oncol. 6, 643-645
    • (2010) Future Oncol. , vol.6 , pp. 643-645
    • Mounir, Z.1    Koromilas, A.E.2
  • 61
    • 0032967979 scopus 로고    scopus 로고
    • Abnormal levels and minimal activity of the dsRNA-activated protein kinase, PKR, in breast carcinoma cells
    • Savinova, O., Joshi, B., and Jagus, R. (1999) Abnormal levels and minimal activity of the dsRNA-activated protein kinase, PKR, in breast carcinoma cells. Int. J. Biochem. Cell Biol. 31, 175-189
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 175-189
    • Savinova, O.1    Joshi, B.2    Jagus, R.3
  • 64
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas, A. E., Roy, S., Barber, G. N., Katze, M. G., and Sonenberg, N. (1992) Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257, 1685-1689
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonenberg, N.5
  • 65
    • 0029122270 scopus 로고
    • Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase
    • Barber, G. N., Jagus, R., Meurs, E. F., Hovanessian, A. G., and Katze, M. G. (1995) Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase. J. Biol. Chem. 270, 17423-17428
    • (1995) J. Biol. Chem. , vol.270 , pp. 17423-17428
    • Barber, G.N.1    Jagus, R.2    Meurs, E.F.3    Hovanessian, A.G.4    Katze, M.G.5
  • 66
    • 0037048685 scopus 로고    scopus 로고
    • Caspase 9 activation by the dsRNA-dependent protein kinase, PKR: Molecular mechanism and relevance
    • Gil, J., Garcia, M. A., and Esteban, M. (2002) Caspase 9 activation by the dsRNA-dependent protein kinase, PKR: molecular mechanism and relevance. FEBS Lett. 529, 249-255
    • (2002) FEBS Lett. , vol.529 , pp. 249-255
    • Gil, J.1    Garcia, M.A.2    Esteban, M.3
  • 69
    • 0034075460 scopus 로고    scopus 로고
    • Levels, phosphorylation status and cellular localization of translational factor eIF2 in gastrointestinal carcinomas
    • Lobo, M. V., Martin, M. E., Perez, M. I., Alonso, F. J., Redondo, C., Alvarez, M. I., and Salinas, M. (2000) Levels, phosphorylation status and cellular localization of translational factor eIF2 in gastrointestinal carcinomas. Histochem. J. 32, 139-150
    • (2000) Histochem. J. , vol.32 , pp. 139-150
    • Lobo, M.V.1    Martin, M.E.2    Perez, M.I.3    Alonso, F.J.4    Redondo, C.5    Alvarez, M.I.6    Salinas, M.7
  • 70
    • 2342594006 scopus 로고    scopus 로고
    • The role of translation in neoplastic transformation from a pathologist's point of view
    • Rosenwald, I. B. (2004) The role of translation in neoplastic transformation from a pathologist's point of view. Oncogene 23, 3230-3247
    • (2004) Oncogene , vol.23 , pp. 3230-3247
    • Rosenwald, I.B.1
  • 74
    • 27644461968 scopus 로고    scopus 로고
    • Expression of double-stranded RNA-activated protein kinase (PKR) and its prognostic significance in lymph node negative rectal cancer
    • Kwon, H. C., Moon, C. H., Kim, S. H., Choi, H. J., Lee, H. S., Roh, M. S., Hwang, T. H., Kim, J. S., and Kim, H. J. (2005) Expression of double-stranded RNA-activated protein kinase (PKR) and its prognostic significance in lymph node negative rectal cancer. Jpn. J. Clin. Oncol. 35, 545-550
    • (2005) Jpn. J. Clin. Oncol. , vol.35 , pp. 545-550
    • Kwon, H.C.1    Moon, C.H.2    Kim, S.H.3    Choi, H.J.4    Lee, H.S.5    Roh, M.S.6    Hwang, T.H.7    Kim, J.S.8    Kim, H.J.9
  • 76
    • 0032189405 scopus 로고    scopus 로고
    • Aberrant expression of double-stranded RNA-dependent protein kinase in hepatocytes of chronic hepatitis and differentiated hepatocellular carcinoma
    • Shimada, A., Shiota, G., Miyata, H., Kamahora, T., Kawasaki, H., Shiraki, K., Hino, S., and Terada, T. (1998) Aberrant expression of double-stranded RNA-dependent protein kinase in hepatocytes of chronic hepatitis and differentiated hepatocellular carcinoma. Cancer Res. 58, 4434-4438
    • (1998) Cancer Res. , vol.58 , pp. 4434-4438
    • Shimada, A.1    Shiota, G.2    Miyata, H.3    Kamahora, T.4    Kawasaki, H.5    Shiraki, K.6    Hino, S.7    Terada, T.8
  • 78
    • 84885357375 scopus 로고    scopus 로고
    • PKR negatively regulates leukemia progression in association with PP2A activation, Bcl-2 inhibition and increased apoptosis
    • Cheng, X., Bennett, R. L., Liu, X., Byrne, M., and Stratford May, W. (2013) PKR negatively regulates leukemia progression in association with PP2A activation, Bcl-2 inhibition and increased apoptosis. Blood Cancer J. 3, e144
    • (2013) Blood Cancer J. , vol.3
    • Cheng, X.1    Bennett, R.L.2    Liu, X.3    Byrne, M.4    Stratford May, W.5
  • 79
    • 84877594165 scopus 로고    scopus 로고
    • PKR regulates proliferation, differentiation, and survival of murine hematopoietic stem/progenitor cells
    • Liu, X., Bennett, R. L., Cheng, X., Byrne, M., Reinhard, M. K., and May, W. S., Jr. (2013) PKR regulates proliferation, differentiation, and survival of murine hematopoietic stem/progenitor cells. Blood 121, 3364-3374
    • (2013) Blood , vol.121 , pp. 3364-3374
    • Liu, X.1    Bennett, R.L.2    Cheng, X.3    Byrne, M.4    Reinhard, M.K.5    May Jr., W.S.6
  • 80
    • 78650176190 scopus 로고    scopus 로고
    • Doxorubicin bypasses the cytoprotective effects of eIF2alpha phosphorylation and promotes PKRmediated cell death
    • Peidis, P., Papadakis, A. I., Muaddi, H., Richard, S., and Koromilas, A. E. (2011) Doxorubicin bypasses the cytoprotective effects of eIF2alpha phosphorylation and promotes PKRmediated cell death. Cell Death Differ. 18, 145-154
    • (2011) Cell Death Differ. , vol.18 , pp. 145-154
    • Peidis, P.1    Papadakis, A.I.2    Muaddi, H.3    Richard, S.4    Koromilas, A.E.5
  • 81
    • 84866636092 scopus 로고    scopus 로고
    • Increased expression of the dsRNAactivated protein kinase PKR in breast cancer promotes sensitivity to doxorubicin
    • Bennett, R. L., Carruthers, A. L., Hui, T., Kerney, K. R., Liu, X., and May, W. S., Jr. (2012) Increased expression of the dsRNAactivated protein kinase PKR in breast cancer promotes sensitivity to doxorubicin. PLoS ONE 7, e46040
    • (2012) PLoS ONE , vol.7
    • Bennett, R.L.1    Carruthers, A.L.2    Hui, T.3    Kerney, K.R.4    Liu, X.5    May Jr., W.S.6
  • 83
    • 0034537477 scopus 로고    scopus 로고
    • Protein expression of double-stranded RNA-activated protein kinase (PKR) in intrahepatic bile ducts in normal adult livers, fetal livers, primary biliary cirrhosis, hepatolithiasis and intrahepatic cholangiocarcinoma
    • Terada, T., Ueyama, J., Ukita, Y., and Ohta, T. (2000) Protein expression of double-stranded RNA-activated protein kinase (PKR) in intrahepatic bile ducts in normal adult livers, fetal livers, primary biliary cirrhosis, hepatolithiasis and intrahepatic cholangiocarcinoma. Liver 20, 450-457
    • (2000) Liver , vol.20 , pp. 450-457
    • Terada, T.1    Ueyama, J.2    Ukita, Y.3    Ohta, T.4
  • 84
    • 0033943112 scopus 로고    scopus 로고
    • Protein expression of double-stranded RNA-activated protein kinase in thyroid carcinomas: Correlations with histologic types, pathologic parameters, and Ki-67 labeling
    • Terada, T., Maeta, H., Endo, K., and Ohta, T. (2000) Protein expression of double-stranded RNA-activated protein kinase in thyroid carcinomas: correlations with histologic types, pathologic parameters, and Ki-67 labeling. Hum. Pathol. 31, 817-821
    • (2000) Hum. Pathol. , vol.31 , pp. 817-821
    • Terada, T.1    Maeta, H.2    Endo, K.3    Ohta, T.4
  • 85
    • 0344496152 scopus 로고    scopus 로고
    • Protein kinase R is increased and is functional in hepatitis C virus-related hepatocellular carcinoma
    • Hiasa, Y., Kamegaya, Y., Nuriya, H., Onji, M., Kohara, M., Schmidt, E. V., and Chung, R. T. (2003) Protein kinase R is increased and is functional in hepatitis C virus-related hepatocellular carcinoma. Am. J. Gastroenterol. 98, 2528-2534
    • (2003) Am. J. Gastroenterol. , vol.98 , pp. 2528-2534
    • Hiasa, Y.1    Kamegaya, Y.2    Nuriya, H.3    Onji, M.4    Kohara, M.5    Schmidt, E.V.6    Chung, R.T.7
  • 86
    • 0037069935 scopus 로고    scopus 로고
    • Neoplastic progression in melanoma and colon cancer is associated with increased expression and activity of the interferon-inducible protein kinase, PKR
    • Kim, S. H., Gunnery, S., Choe, J. K., and Mathews, M. B. (2002) Neoplastic progression in melanoma and colon cancer is associated with increased expression and activity of the interferon-inducible protein kinase, PKR. Oncogene 21, 8741-8748
    • (2002) Oncogene , vol.21 , pp. 8741-8748
    • Kim, S.H.1    Gunnery, S.2    Choe, J.K.3    Mathews, M.B.4
  • 87
    • 0029655361 scopus 로고    scopus 로고
    • Expression of the doublestranded RNA-dependent protein kinase (p68) in human breast tissues
    • Haines, G. K., Cajulis, R., Hayden, R., Duda, R., Talamonti, M., and Radosevich, J. A. (1996) Expression of the doublestranded RNA-dependent protein kinase (p68) in human breast tissues. Tumour Biol. 17, 5-12
    • (1996) Tumour Biol. , vol.17 , pp. 5-12
    • Haines, G.K.1    Cajulis, R.2    Hayden, R.3    Duda, R.4    Talamonti, M.5    Radosevich, J.A.6
  • 88
    • 28444482781 scopus 로고    scopus 로고
    • Expression of double-stranded RNA-activated protein kinase in small-size peripheral adenocarcinoma of the lung
    • Roh, M. S., Kwak, J. Y., Kim, S. J., Lee, H. W., Kwon, H. C., Hwang, T. H., Choi, P. J., and Hong, Y. S. (2005) Expression of double-stranded RNA-activated protein kinase in small-size peripheral adenocarcinoma of the lung. Pathol. Int. 55, 688-693
    • (2005) Pathol. Int. , vol.55 , pp. 688-693
    • Roh, M.S.1    Kwak, J.Y.2    Kim, S.J.3    Lee, H.W.4    Kwon, H.C.5    Hwang, T.H.6    Choi, P.J.7    Hong, Y.S.8
  • 89
    • 77649237309 scopus 로고    scopus 로고
    • NFkappaB and cancer: How intimate is this relationship
    • Prasad, S., Ravindran, J., and Aggarwal, B. B. (2010) NFkappaB and cancer: how intimate is this relationship. Mol. Cell. Biochem. 336, 25-37
    • (2010) Mol. Cell. Biochem. , vol.336 , pp. 25-37
    • Prasad, S.1    Ravindran, J.2    Aggarwal, B.B.3
  • 90
    • 35349014040 scopus 로고    scopus 로고
    • Knockdown of PKR expression by RNAi reduces pulmonary metastatic potential of B16-F10 melanoma cells in mice: Possible role of NF-kappaB
    • Delgado Andre, N., and De Lucca, F. L. (2007) Knockdown of PKR expression by RNAi reduces pulmonary metastatic potential of B16-F10 melanoma cells in mice: possible role of NF-kappaB. Cancer Lett. 258, 118-125
    • (2007) Cancer Lett. , vol.258 , pp. 118-125
    • Delgado Andre, N.1    De Lucca, F.L.2
  • 92
    • 84860880318 scopus 로고    scopus 로고
    • Age-associated chronic diseases require age-old medicine: Role of chronic inflammation
    • Prasad, S., Sung, B., and Aggarwal, B. B. (2012) Age-associated chronic diseases require age-old medicine: role of chronic inflammation. Prev. Med. 54(Supp.), S29-S37
    • (2012) Prev. Med. , vol.54 , Issue.SUPPL.
    • Prasad, S.1    Sung, B.2    Aggarwal, B.B.3
  • 93
    • 74049107328 scopus 로고    scopus 로고
    • Interaction of double-stranded RNA-dependent protein kinase (PKR) with the death receptor signaling pathway in amyloid beta (Abeta)-treated cells and in APPSLPS1 knock-in mice
    • Couturier, J., Morel, M., Pontcharraud, R., Gontier, V., Fauconneau, B., Paccalin, M., and Page, G. (2010) Interaction of double-stranded RNA-dependent protein kinase (PKR) with the death receptor signaling pathway in amyloid beta (Abeta)-treated cells and in APPSLPS1 knock-in mice. J. Biol. Chem. 285, 1272-1282
    • (2010) J. Biol. Chem. , vol.285 , pp. 1272-1282
    • Couturier, J.1    Morel, M.2    Pontcharraud, R.3    Gontier, V.4    Fauconneau, B.5    Paccalin, M.6    Page, G.7
  • 96
    • 84859498356 scopus 로고    scopus 로고
    • Increased cerebrospinal fluid levels of double-stranded RNA-dependent protein kinase in Alzheimer's disease
    • Mouton-Liger, F., Paquet, C., Dumurgier, J., Lapalus, P., Gray, F., Laplanche, J. L., and Hugon, J. (2012) Increased cerebrospinal fluid levels of double-stranded RNA-dependent protein kinase in Alzheimer's disease. Biol. Psychiatry 71, 829-835
    • (2012) Biol. Psychiatry , vol.71 , pp. 829-835
    • Mouton-Liger, F.1    Paquet, C.2    Dumurgier, J.3    Lapalus, P.4    Gray, F.5    Laplanche, J.L.6    Hugon, J.7
  • 99
    • 84876872146 scopus 로고    scopus 로고
    • The protein kinase PKR is critical for LPS-induced iNOS production but dispensable for inflammasome activation in macrophages
    • He, Y., Franchi, L., and Nunez, G. (2013) The protein kinase PKR is critical for LPS-induced iNOS production but dispensable for inflammasome activation in macrophages. Eur. J. Immunol. 43, 1147-1152
    • (2013) Eur. J. Immunol. , vol.43 , pp. 1147-1152
    • He, Y.1    Franchi, L.2    Nunez, G.3
  • 101
    • 77949889567 scopus 로고    scopus 로고
    • Constitutively active inflammasome in human melanoma cells mediating autoinflammation via caspase-1 processing and secretion of interleukin-1beta
    • Okamoto, M., Liu, W., Luo, Y., Tanaka, A., Cai, X., Norris, D. A., Dinarello, C. A., and Fujita, M. (2010) Constitutively active inflammasome in human melanoma cells mediating autoinflammation via caspase-1 processing and secretion of interleukin-1beta. J. Biol. Chem. 285, 6477-6488
    • (2010) J. Biol. Chem. , vol.285 , pp. 6477-6488
    • Okamoto, M.1    Liu, W.2    Luo, Y.3    Tanaka, A.4    Cai, X.5    Norris, D.A.6    Dinarello, C.A.7    Fujita, M.8
  • 103
    • 0033056848 scopus 로고    scopus 로고
    • RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling
    • Ito, T., Yang, M., and May, W. S. (1999) RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J. Biol. Chem. 274, 15427-15432
    • (1999) J. Biol. Chem. , vol.274 , pp. 15427-15432
    • Ito, T.1    Yang, M.2    May, W.S.3
  • 104
    • 0032480017 scopus 로고    scopus 로고
    • PACT, a protein activator of the interferon-induced protein kinase, PKR
    • Patel, R. C., and Sen, G. C. (1998) PACT, a protein activator of the interferon-induced protein kinase, PKR. EMBO J. 17, 4379-4390
    • (1998) EMBO J. , vol.17 , pp. 4379-4390
    • Patel, R.C.1    Sen, G.C.2
  • 106
    • 58149104379 scopus 로고    scopus 로고
    • Essential role of PACT-mediated PKR activation in tunicamycin-induced apoptosis
    • Singh, M., Fowlkes, V., Handy, I., Patel, C. V., and Patel, R. C. (2009) Essential role of PACT-mediated PKR activation in tunicamycin-induced apoptosis. J. Mol. Biol. 385, 457-468
    • (2009) J. Mol. Biol. , vol.385 , pp. 457-468
    • Singh, M.1    Fowlkes, V.2    Handy, I.3    Patel, C.V.4    Patel, R.C.5
  • 107
    • 67649781990 scopus 로고    scopus 로고
    • The double-stranded RNA-binding protein, PACT, is required for postnatal anterior pituitary proliferation
    • Peters, G. A., Seachrist, D. D., Keri, R. A., and Sen, G. C. (2009) The double-stranded RNA-binding protein, PACT, is required for postnatal anterior pituitary proliferation. Proc. Natl. Acad. Sci. U. S. A. 106, 10696-10701
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10696-10701
    • Peters, G.A.1    Seachrist, D.D.2    Keri, R.A.3    Sen, G.C.4
  • 109
    • 84865727711 scopus 로고    scopus 로고
    • The multiple functions of TRBP, at the hub of cell responses to viruses, stress, and cancer
    • Daniels, S. M., and Gatignol, A. (2012) The multiple functions of TRBP, at the hub of cell responses to viruses, stress, and cancer. Microbiol. Mol. Biol. Rev. 76, 652-666
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , pp. 652-666
    • Daniels, S.M.1    Gatignol, A.2
  • 110
    • 81255164734 scopus 로고    scopus 로고
    • The cellular TAR RNA binding protein, TRBP, promotes HIV-1 replication primarily by inhibiting the activation of double-stranded RNA-dependent kinase PKR
    • Sanghvi, V. R., and Steel, L. F. (2011) The cellular TAR RNA binding protein, TRBP, promotes HIV-1 replication primarily by inhibiting the activation of double-stranded RNA-dependent kinase PKR. J. Virol. 85, 12614-12621
    • (2011) J. Virol. , vol.85 , pp. 12614-12621
    • Sanghvi, V.R.1    Steel, L.F.2
  • 111
    • 79958158639 scopus 로고    scopus 로고
    • Stress-induced phosphorylation of PACT reduces its interaction with TRBP and leads to PKR activation
    • Singh, M., Castillo, D., Patel, C. V., and Patel, R. C. (2011) Stress-induced phosphorylation of PACT reduces its interaction with TRBP and leads to PKR activation. Biochemistry 50, 4550-4560
    • (2011) Biochemistry , vol.50 , pp. 4550-4560
    • Singh, M.1    Castillo, D.2    Patel, C.V.3    Patel, R.C.4
  • 114
    • 0031014063 scopus 로고    scopus 로고
    • Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR
    • Benkirane, M., Neuveut, C., Chun, R. F., Smith, S. M., Samuel, C. E., Gatignol, A., and Jeang, K. T. (1997) Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J. 16, 611-624
    • (1997) EMBO J. , vol.16 , pp. 611-624
    • Benkirane, M.1    Neuveut, C.2    Chun, R.F.3    Smith, S.M.4    Samuel, C.E.5    Gatignol, A.6    Jeang, K.T.7
  • 116
    • 0035898534 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR
    • Donze, O., Abbas-Terki, T., and Picard, D. (2001) The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J. 20, 3771-3780
    • (2001) EMBO J. , vol.20 , pp. 3771-3780
    • Donze, O.1    Abbas-Terki, T.2    Picard, D.3
  • 117
    • 0347721778 scopus 로고    scopus 로고
    • Doublestranded RNA-dependent protein kinase (pkr) is essential for thermotolerance, accumulation of HSP70, and stabilization of ARE-containing HSP70 mRNA during stress
    • Zhao, M., Tang, D., Lechpammer, S., Hoffman, A., Asea, A., Stevenson, M. A., and Calderwood, S. K. (2002) Doublestranded RNA-dependent protein kinase (pkr) is essential for thermotolerance, accumulation of HSP70, and stabilization of ARE-containing HSP70 mRNA during stress. J. Biol. Chem. 277, 44539-44547
    • (2002) J. Biol. Chem. , vol.277 , pp. 44539-44547
    • Zhao, M.1    Tang, D.2    Lechpammer, S.3    Hoffman, A.4    Asea, A.5    Stevenson, M.A.6    Calderwood, S.K.7
  • 118
    • 0037147247 scopus 로고    scopus 로고
    • The anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCC
    • Pang, Q., Christianson, T. A., Keeble, W., Koretsky, T., and Bagby, G. C. (2002) The anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCC. J. Biol. Chem. 277, 49638-49643
    • (2002) J. Biol. Chem. , vol.277 , pp. 49638-49643
    • Pang, Q.1    Christianson, T.A.2    Keeble, W.3    Koretsky, T.4    Bagby, G.C.5
  • 119
    • 0035881864 scopus 로고    scopus 로고
    • FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity
    • Pang, Q., Keeble, W., Christianson, T. A., Faulkner, G. R., and Bagby, G. C. (2001) FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity. EMBO J. 20, 4478-4489
    • (2001) EMBO J. , vol.20 , pp. 4478-4489
    • Pang, Q.1    Keeble, W.2    Christianson, T.A.3    Faulkner, G.R.4    Bagby, G.C.5
  • 121
    • 84875420225 scopus 로고    scopus 로고
    • MicroRNAs in cancers and neurodegenerative disorders
    • Saito, Y., and Saito, H. (2012) MicroRNAs in cancers and neurodegenerative disorders. Front. Genet. 3, 194
    • (2012) Front. Genet. , vol.3 , pp. 194
    • Saito, Y.1    Saito, H.2
  • 122
    • 79956202150 scopus 로고    scopus 로고
    • Precursor miR-886, a novel noncoding RNA repressed in cancer, associates with PKR and modulates its activity
    • Lee, K., Kunkeaw, N., Jeon, S. H., Lee, I., Johnson, B. H., Kang, G. Y., Bang, J. Y., Park, H. S., Leelayuwat, C., and Lee, Y. S. (2011) Precursor miR-886, a novel noncoding RNA repressed in cancer, associates with PKR and modulates its activity. RNA 17, 1076-1089
    • (2011) RNA , vol.17 , pp. 1076-1089
    • Lee, K.1    Kunkeaw, N.2    Jeon, S.H.3    Lee, I.4    Johnson, B.H.5    Kang, G.Y.6    Bang, J.Y.7    Park, H.S.8    Leelayuwat, C.9    Lee, Y.S.10
  • 123
    • 33746826546 scopus 로고    scopus 로고
    • The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases
    • Datta, B., Datta, R., Ghosh, A., and Majumdar, A. (2006) The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases. Arch Biochem. Biophys 452, 138-148
    • (2006) Arch Biochem. Biophys , vol.452 , pp. 138-148
    • Datta, B.1    Datta, R.2    Ghosh, A.3    Majumdar, A.4
  • 124
    • 0034719164 scopus 로고    scopus 로고
    • In vivo regulation of the dsRNA-dependent protein kinase PKR by the cellular glycoprotein p67
    • Gil, J., Esteban, M., and Roth, D. (2000) In vivo regulation of the dsRNA-dependent protein kinase PKR by the cellular glycoprotein p67. Biochemistry 39, 16016-16025
    • (2000) Biochemistry , vol.39 , pp. 16016-16025
    • Gil, J.1    Esteban, M.2    Roth, D.3
  • 125
    • 4444311427 scopus 로고    scopus 로고
    • Expression of methionine aminopeptidase 2, N-myristoyltransferase, and Nmyristoyltransferase inhibitor protein 71 in HT29
    • Selvakumar, P., Lakshmikuttyamma, A., Lawman, Z., Bonham, K., Dimmock, J. R., and Sharma, R. K. (2004) Expression of methionine aminopeptidase 2, N-myristoyltransferase, and Nmyristoyltransferase inhibitor protein 71 in HT29. Biochem. Biophys. Res. Commun. 322, 1012-1017
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 1012-1017
    • Selvakumar, P.1    Lakshmikuttyamma, A.2    Lawman, Z.3    Bonham, K.4    Dimmock, J.R.5    Sharma, R.K.6
  • 128
    • 0023878562 scopus 로고
    • The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2
    • Rowlands, A. G., Panniers, R., and Henshaw, E. C. (1988) The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J. Biol. Chem. 263, 5526-5533
    • (1988) J. Biol. Chem. , vol.263 , pp. 5526-5533
    • Rowlands, A.G.1    Panniers, R.2    Henshaw, E.C.3
  • 129
    • 1642553650 scopus 로고    scopus 로고
    • Defective translational control facilitates vesicular stomatitis virus oncolysis
    • Balachandran, S., and Barber, G. N. (2004) Defective translational control facilitates vesicular stomatitis virus oncolysis. Cancer Cell 5, 51-65
    • (2004) Cancer Cell , vol.5 , pp. 51-65
    • Balachandran, S.1    Barber, G.N.2
  • 130
    • 79751528879 scopus 로고    scopus 로고
    • Multiple forms of PKR present in the nuclei of acute leukemia cells represent an active kinase that is responsive to stress
    • Blalock, W. L., Bavelloni, A., Piazzi, M., Tagliavini, F., Faenza, I., Martelli, A. M., Follo, M. Y., and Cocco, L. (2011) Multiple forms of PKR present in the nuclei of acute leukemia cells represent an active kinase that is responsive to stress. Leukemia 25, 236-245
    • (2011) Leukemia , vol.25 , pp. 236-245
    • Blalock, W.L.1    Bavelloni, A.2    Piazzi, M.3    Tagliavini, F.4    Faenza, I.5    Martelli, A.M.6    Follo, M.Y.7    Cocco, L.8
  • 133
    • 0031899816 scopus 로고    scopus 로고
    • Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2
    • Romano, P. R., Garcia-Barrio, M. T., Zhang, X., Wang, Q., Taylor, D. R., Zhang, F., Herring, C., Mathews, M. B., Qin, J., and Hinnebusch, A. G. (1998) Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2. Mol. Cell. Biol. 18, 2282-2297
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2282-2297
    • Romano, P.R.1    Garcia-Barrio, M.T.2    Zhang, X.3    Wang, Q.4    Taylor, D.R.5    Zhang, F.6    Herring, C.7    Mathews, M.B.8    Qin, J.9    Hinnebusch, A.G.10
  • 134
    • 84873863319 scopus 로고    scopus 로고
    • Activation of doublestranded RNA-activated protein kinase (PKR) by interferonstimulated gene 15 (ISG15) modification down-regulates protein translation
    • Okumura, F., Okumura, A. J., Uematsu, K., Hatakeyama, S., Zhang, D. E., and Kamura, T. (2013) Activation of doublestranded RNA-activated protein kinase (PKR) by interferonstimulated gene 15 (ISG15) modification down-regulates protein translation. J. Biol. Chem. 288, 2839-2847
    • (2013) J. Biol. Chem. , vol.288 , pp. 2839-2847
    • Okumura, F.1    Okumura, A.J.2    Uematsu, K.3    Hatakeyama, S.4    Zhang, D.E.5    Kamura, T.6
  • 135
    • 22544487172 scopus 로고    scopus 로고
    • Human ISG15 conjugation targets both IFNinduced and constitutively expressed proteins functioning in diverse cellular pathways
    • Zhao, C., Denison, C., Huibregtse, J. M., Gygi, S., and Krug, R. M. (2005) Human ISG15 conjugation targets both IFNinduced and constitutively expressed proteins functioning in diverse cellular pathways. Proc. Natl. Acad. Sci. U. S. A. 102, 10200-10205
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 10200-10205
    • Zhao, C.1    Denison, C.2    Huibregtse, J.M.3    Gygi, S.4    Krug, R.M.5
  • 136
    • 25144477805 scopus 로고    scopus 로고
    • Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition
    • Dey, M., Cao, C., Dar, A. C., Tamura, T., Ozato, K., Sicheri, F., and Dever, T. E. (2005) Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition. Cell 122, 901-913
    • (2005) Cell , vol.122 , pp. 901-913
    • Dey, M.1    Cao, C.2    Dar, A.C.3    Tamura, T.4    Ozato, K.5    Sicheri, F.6    Dever, T.E.7
  • 137
    • 84887850498 scopus 로고    scopus 로고
    • Sumoylation in gene regulation, human disease, and therapeutic action
    • Yang, X. J., and Chiang, C. M. (2013) Sumoylation in gene regulation, human disease, and therapeutic action. F1000Prime Rep. 5, 45
    • (2013) F1000Prime Rep. , vol.5 , pp. 45
    • Yang, X.J.1    Chiang, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.