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Volumn 21, Issue , 2015, Pages 154-166

Protein-binding function of RNA-dependent protein kinase promotes proliferation through TRAF2/RIP1/NF-κB/c-Myc pathway in pancreatic β cells

Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; MYC PROTEIN; PROTEIN KINASE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RECEPTOR INTERACTING SERINE THREONINE PROTEIN KINASE 1; RNA DEPENDENT PROTEIN KINASE; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 5; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UNCLASSIFIED DRUG; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN BINDING; PROTEIN KINASE R; RALBP1 PROTEIN, MOUSE; TUMOR NECROSIS FACTOR;

EID: 84935875147     PISSN: 10761551     EISSN: 15283658     Source Type: Journal    
DOI: 10.2119/molmed.2014.00235     Document Type: Article
Times cited : (9)

References (79)
  • 1
    • 33845627785 scopus 로고    scopus 로고
    • Impact of protein kinase PKR in cell biology: From antiviral to antiproliferative action
    • Garcia MA, et al. (2006) Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action. Microbiol. Mol. Biol. Rev. 70:1032-60.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 1032-1060
    • Garcia, M.A.1
  • 2
    • 84856101167 scopus 로고    scopus 로고
    • The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest
    • Bennett RL, et al. (2012) The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest. Cell Cycle. 11:407-17.
    • (2012) Cell Cycle , vol.11 , pp. 407-417
    • Bennett, R.L.1
  • 3
    • 84902213434 scopus 로고    scopus 로고
    • Activation of the PKR/eIF2alpha signaling cascade inhibits replication of Newcastle disease virus
    • Zhang S, et al. (2014) Activation of the PKR/eIF2alpha signaling cascade inhibits replication of Newcastle disease virus. Virol. J. 11:62.
    • (2014) Virol. J , vol.11 , pp. 62
    • Zhang, S.1
  • 4
    • 84901045220 scopus 로고    scopus 로고
    • The impact of PKR activation: From neurodegeneration to cancer
    • Marchal JA, et al. (2014) The impact of PKR activation: from neurodegeneration to cancer. FASEB J. 28:1965-74.
    • (2014) FASEB J , vol.28 , pp. 1965-1974
    • Marchal, J.A.1
  • 5
    • 0029122270 scopus 로고
    • Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferoninduced enzyme RNA-dependent protein kinase
    • Barber GN, Jagus R, Meurs EF, Hovanessian AG, Katze MG. (1995) Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferoninduced enzyme RNA-dependent protein kinase. J. Biol. Chem. 270:17423-8.
    • (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
  • 7
    • 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, Nunez G. (2013) The protein kinase PKR is critical for LPS-induced iNOS production but dispensable for inflammasome activation in macrophages. Eur. J. Immunol. 43:1147-52.
    • (2013) Eur. J. Immunol , vol.43 , pp. 1147-1152
    • He, Y.1    Franchi, L.2    Nunez, G.3
  • 8
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNAdependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • Nakamura T, et al. (2010) Double-stranded RNAdependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell. 140:338-48.
    • (2010) Cell , vol.140 , pp. 338-348
    • Nakamura, T.1
  • 9
    • 84867827691 scopus 로고    scopus 로고
    • Double-stranded RNA-activated protein kinase is a key modulator of insulin sensitivity in physiological conditions and in obesity in mice
    • Carvalho-Filho MA, et al. (2012) Double-stranded RNA-activated protein kinase is a key modulator of insulin sensitivity in physiological conditions and in obesity in mice. Endocrinology. 153:5261-74.
    • (2012) Endocrinology , vol.153 , pp. 5261-5274
    • Carvalho-Filho, M.A.1
  • 10
    • 84889680862 scopus 로고    scopus 로고
    • Modulation of doublestranded RNA-activated protein kinase in insulin sensitive tissues of obese humans
    • Carvalho BM, et al. (2013) Modulation of doublestranded RNA-activated protein kinase in insulin sensitive tissues of obese humans. Obesity (Silver Spring). 21:2452-7.
    • (2013) Obesity (Silver Spring) , vol.21 , pp. 2452-2457
    • Carvalho, B.M.1
  • 11
    • 84893155439 scopus 로고    scopus 로고
    • Small-molecule inhibitors of PKR improve glucose homeostasis in obese diabetic mice
    • Nakamura T, Arduini A, Baccaro B, Furuhashi M, Hotamisligil GS. (2014) Small-molecule inhibitors of PKR improve glucose homeostasis in obese diabetic mice. Diabetes. 63:526-34.
    • (2014) Diabetes , vol.63 , pp. 526-534
    • Nakamura, T.1    Arduini, A.2    Baccaro, B.3    Furuhashi, M.4    Hotamisligil, G.S.5
  • 12
    • 84893695281 scopus 로고    scopus 로고
    • Activation of double-stranded RNA-dependent protein kinase inhibits proliferation of pancreatic beta-cells
    • Chen SS, et al. (2014) Activation of double-stranded RNA-dependent protein kinase inhibits proliferation of pancreatic beta-cells. Biochem. Biophys. Res. Commun. 443:814-20.
    • (2014) Biochem. Biophys. Res. Commun , vol.443 , pp. 814-820
    • Chen, S.S.1
  • 14
    • 2942620924 scopus 로고    scopus 로고
    • TRAF family proteins link PKR with NF-kappa B activation
    • Gil J, et al. (2004) TRAF family proteins link PKR with NF-kappa B activation. Mol. Cell. Biol. 24:4502-12.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 4502-4512
    • Gil, J.1
  • 15
    • 30544447047 scopus 로고    scopus 로고
    • Critical role of TRAF3 in the Toll-like receptor-dependent and-independent antiviral response
    • Oganesyan G, et al. (2006) Critical role of TRAF3 in the Toll-like receptor-dependent and-independent antiviral response. Nature. 439:208-11.
    • (2006) Nature , vol.439 , pp. 208-211
    • Oganesyan, G.1
  • 17
    • 33745627468 scopus 로고    scopus 로고
    • Molecular basis for PKR activation by PACT or dsRNA
    • Li S, et al. (2006) Molecular basis for PKR activation by PACT or dsRNA. Proc. Natl. Acad. Sci. U. S. A. 103:10005-10.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 10005-10010
    • Li, S.1
  • 18
    • 0035475338 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factors (TRAFs)
    • Bradley JR, Pober JS. (2001) Tumor necrosis factor receptor-associated factors (TRAFs). Oncogene. 20:6482-91.
    • (2001) Oncogene , vol.20 , pp. 6482-6491
    • Bradley, J.R.1    Pober, J.S.2
  • 19
    • 84878816379 scopus 로고    scopus 로고
    • TRAF molecules in cell signaling and in human diseases
    • Xie P. (2013) TRAF molecules in cell signaling and in human diseases. J. Mol. Signal 8:7.
    • (2013) J. Mol. Signal , vol.8 , pp. 7
    • Xie, P.1
  • 20
    • 84883347520 scopus 로고    scopus 로고
    • The protein kinase double-stranded RNA-dependent (PKR) enhances protection against disease cause by a non-viral pathogen
    • Ogolla PS, et al. (2013) The protein kinase double-stranded RNA-dependent (PKR) enhances protection against disease cause by a non-viral pathogen. PLoS Pathog. 9:e1003557.
    • (2013) PLoS Pathog , vol.9
    • Ogolla, P.S.1
  • 21
    • 33847394078 scopus 로고    scopus 로고
    • Evidence that TNF-TNFR1-TRADD-TRAF2-RIP-TAK1-IKK pathway mediates constitutive NF-kappaB activation and proliferation in human head and neck squamous cell carcinoma
    • Jackson-Bernitsas DG, et al. (2007) Evidence that TNF-TNFR1-TRADD-TRAF2-RIP-TAK1-IKK pathway mediates constitutive NF-kappaB activation and proliferation in human head and neck squamous cell carcinoma. Oncogene. 26:1385-97.
    • (2007) Oncogene , vol.26 , pp. 1385-1397
    • Jackson-Bernitsas, D.G.1
  • 22
    • 0035898611 scopus 로고    scopus 로고
    • Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR
    • Ung TL, Cao C, Lu J, Ozato K, Dever TE. (2001) Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR. EMBO J. 20:3728-37.
    • (2001) EMBO J , vol.20 , pp. 3728-3737
    • Ung, T.L.1    Cao, C.2    Lu, J.3    Ozato, K.4    Dever, T.E.5
  • 23
    • 84881116306 scopus 로고    scopus 로고
    • Elevated toll-like receptor 3 inhibits pancreatic beta-cell proliferation through G1 phase cell cycle arrest
    • Wang Y, et al. (2013) Elevated toll-like receptor 3 inhibits pancreatic beta-cell proliferation through G1 phase cell cycle arrest. Mol. Cell. Endocrinol. 377:112-22.
    • (2013) Mol. Cell. Endocrinol , vol.377 , pp. 112-122
    • Wang, Y.1
  • 24
    • 84935830379 scopus 로고
    • Guide for the Care and Use of Laboratory Animals
    • (NIH publication; no. 85-23)
    • Institute of Laboratory Animal Resources (U. S.), Committee on Care and Use of Laboratory Animals. (1985) Guide for the Care and Use of Laboratory Animals. Rev. 1985. Bethesda (MD): NIH. 83 pp. (NIH publication; no. 85-23).
    • (1985) Rev. 1985. Bethesda (MD): NIH
  • 25
    • 0035033889 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 prevents cytokinemediated dysfunction and cytotoxicity in pancreatic islets and beta-cells
    • Han X, Sun Y, Scott S, Bleich D. (2001) Tissue inhibitor of metalloproteinase-1 prevents cytokinemediated dysfunction and cytotoxicity in pancreatic islets and beta-cells. Diabetes. 50:1047-55.
    • (2001) Diabetes , vol.50 , pp. 1047-1055
    • Han, X.1    Sun, Y.2    Scott, S.3    Bleich, D.4
  • 26
    • 70349327410 scopus 로고    scopus 로고
    • Transfection of rat pancreatic islet tissue by polymeric gene vectors
    • Kang HC, Bae YH. (2009) Transfection of rat pancreatic islet tissue by polymeric gene vectors. Diabetes Technol. Ther. 11:443-9.
    • (2009) Diabetes Technol. Ther , vol.11 , pp. 443-449
    • Kang, H.C.1    Bae, Y.H.2
  • 27
    • 84883261205 scopus 로고    scopus 로고
    • Early activation of nSMase2/ceramide pathway in astrocytes is involved in ischemia-associated neuronal damage via inflammation in rat hippocampi
    • Gu L, et al. (2013) Early activation of nSMase2/ceramide pathway in astrocytes is involved in ischemia-associated neuronal damage via inflammation in rat hippocampi. J. Neuroinflammation. 10:109.
    • (2013) J. Neuroinflammation , vol.10 , pp. 109
    • Gu, L.1
  • 28
    • 57249094223 scopus 로고    scopus 로고
    • Activation of liver X receptors inhibits pancreatic islet beta cell proliferation through cell cycle arrest
    • Meng ZX, et al. (2009) Activation of liver X receptors inhibits pancreatic islet beta cell proliferation through cell cycle arrest. Diabetologia. 52:125-35.
    • (2009) Diabetologia , vol.52 , pp. 125-135
    • Meng, Z.X.1
  • 29
    • 62449159500 scopus 로고    scopus 로고
    • Double-stranded RNAdependent protein kinase-dependent apoptosis induction by a novel small compound
    • Hu W, et al. (2009) Double-stranded RNAdependent protein kinase-dependent apoptosis induction by a novel small compound. J. Pharmacol. Exp. Ther. 328:866-72.
    • (2009) J. Pharmacol. Exp. Ther , vol.328 , pp. 866-872
    • Hu, W.1
  • 30
    • 0027787072 scopus 로고
    • 2-Aminopurine inhibits the double-stranded RNA-dependent protein kinase both in vitro and in vivo
    • Hu Y, Conway TW. (1993) 2-Aminopurine inhibits the double-stranded RNA-dependent protein kinase both in vitro and in vivo. J. Interferon. Res. 13:323-8.
    • (1993) J. Interferon. Res , vol.13 , pp. 323-328
    • Hu, Y.1    Conway, T.W.2
  • 31
    • 33847687194 scopus 로고    scopus 로고
    • Molecular regulation of pancreatic beta-cell mass development, maintenance, and expansion
    • Ackermann AM, Gannon M. (2007) Molecular regulation of pancreatic beta-cell mass development, maintenance, and expansion. J. Mol. Endocrinol. 38:193-206.
    • (2007) J. Mol. Endocrinol , vol.38 , pp. 193-206
    • Ackermann, A.M.1    Gannon, M.2
  • 32
    • 84901301607 scopus 로고    scopus 로고
    • Mangiferin facilitates islet regeneration and beta-cell proliferation through upregulation of cell cycle and beta-cell regeneration regulators
    • Wang HL, et al. (2014) Mangiferin facilitates islet regeneration and beta-cell proliferation through upregulation of cell cycle and beta-cell regeneration regulators. Int. J. Mol. Sci. 15:9016-35.
    • (2014) Int. J. Mol. Sci , vol.15 , pp. 9016-9035
    • Wang, H.L.1
  • 33
    • 33847236171 scopus 로고    scopus 로고
    • Genetic deletion of PKR abrogates TNF-induced activation of IkappaBalpha kinase, JNK, Akt and cell proliferation but potentiates p44/p42 MAPK and p38 MAPK activation
    • Takada Y, et al. (2007) Genetic deletion of PKR abrogates TNF-induced activation of IkappaBalpha kinase, JNK, Akt and cell proliferation but potentiates p44/p42 MAPK and p38 MAPK activation. Oncogene. 26:1201-12.
    • (2007) Oncogene , vol.26 , pp. 1201-1212
    • Takada, Y.1
  • 34
    • 80053345327 scopus 로고    scopus 로고
    • CMyc is a principal upstream driver of beta-cell proliferation in rat insulinoma cell lines and is an effective mediator of human beta-cell replication
    • Karslioglu E, et al. (2011) CMyc is a principal upstream driver of beta-cell proliferation in rat insulinoma cell lines and is an effective mediator of human beta-cell replication. Mol. Endocrinol. 25:1760-72.
    • (2011) Mol. Endocrinol , vol.25 , pp. 1760-1772
    • Karslioglu, E.1
  • 35
    • 84871878351 scopus 로고    scopus 로고
    • PERK is required in the adult pancreas and is essential for maintenance of glucose homeostasis
    • Gao Y, et al. (2012) PERK is required in the adult pancreas and is essential for maintenance of glucose homeostasis. Mol. Cell. Biol. 32:5129-39.
    • (2012) Mol. Cell. Biol , vol.32 , pp. 5129-5139
    • Gao, Y.1
  • 36
    • 0035032028 scopus 로고    scopus 로고
    • Involvement of nuclear factor kappaB in c-Myc induction by tubulin polymerization inhibitors
    • Bourgarel-Rey V, et al. (2001) Involvement of nuclear factor kappaB in c-Myc induction by tubulin polymerization inhibitors. Mol. Pharmacol. 59:1165-70.
    • (2001) Mol. Pharmacol , vol.59 , pp. 1165-1170
    • Bourgarel-Rey, V.1
  • 37
    • 0030666532 scopus 로고    scopus 로고
    • Expression of the neoplastic phenotype by human thyroid carcinoma cell lines requires NFkappaB p65 protein expression
    • Visconti R, et al. (1997) Expression of the neoplastic phenotype by human thyroid carcinoma cell lines requires NFkappaB p65 protein expression. Oncogene. 15:1987-94.
    • (1997) Oncogene , vol.15 , pp. 1987-1994
    • Visconti, R.1
  • 38
    • 0036570010 scopus 로고    scopus 로고
    • Activation of the nuclear transcription factor kappaB (NFkappaB) and differential gene expression in U87 glioma cells after exposure to the cytoprotector amifostine
    • Kataoka Y, Murley JS, Khodarev NN, Weichselbaum RR, Grdina DJ. (2002) Activation of the nuclear transcription factor kappaB (NFkappaB) and differential gene expression in U87 glioma cells after exposure to the cytoprotector amifostine. Int. J. Radiat. Oncol. Biol. Phys. 53:180-9.
    • (2002) Int. J. Radiat. Oncol. Biol. Phys , vol.53 , pp. 180-189
    • Kataoka, Y.1    Murley, J.S.2    Khodarev, N.N.3    Weichselbaum, R.R.4    Grdina, D.J.5
  • 39
    • 79951601376 scopus 로고    scopus 로고
    • The NF. B pathway inhibitors Bay 11-7082 and parthenolide induce programmed cell death in anucleated erythrocytes
    • Ghashghaeinia M, et al. (2011) The NF. B pathway inhibitors Bay 11-7082 and parthenolide induce programmed cell death in anucleated erythrocytes. Cell. Physiol. Biochem. 27:45-54.
    • (2011) Cell. Physiol. Biochem , vol.27 , pp. 45-54
    • Ghashghaeinia, M.1
  • 40
    • 82255173951 scopus 로고    scopus 로고
    • Lipopolysaccharide-enhanced early proliferation of insulin secreting NIT-1 cell is associated with nuclear factor-kappaB-mediated inhibition of caspase 3 cleavage
    • Liu SY, et al. (2011) Lipopolysaccharide-enhanced early proliferation of insulin secreting NIT-1 cell is associated with nuclear factor-kappaB-mediated inhibition of caspase 3 cleavage. Chin. Med J. (Engl.) 124:3652-6.
    • (2011) Chin. Med J. (Engl.) , vol.124 , pp. 3652-3656
    • Liu, S.Y.1
  • 41
    • 84931847670 scopus 로고    scopus 로고
    • Ubiquitinmediated NFkappaB degradation pathway
    • 2014, Oct 27 [Epub ahead of print]
    • Xu H, You M, Shi H, Hou Y. (2014) Ubiquitinmediated NFkappaB degradation pathway. Cell Mol. Immunol. 2014, Oct 27 [Epub ahead of print].
    • (2014) Cell Mol. Immunol
    • Xu, H.1    You, M.2    Shi, H.3    Hou, Y.4
  • 42
    • 40749090052 scopus 로고    scopus 로고
    • IkappaB kinase beta (IKKbeta/IKK2/IKBKB)-a key molecule in signaling to the transcription factor NF-kappaB
    • Schmid JA, Birbach A. (2008) IkappaB kinase beta (IKKbeta/IKK2/IKBKB)-a key molecule in signaling to the transcription factor NF-kappaB. Cytokine Growth Factor Rev. 19:157-65.
    • (2008) Cytokine Growth Factor Rev , vol.19 , pp. 157-165
    • Schmid, J.A.1    Birbach, A.2
  • 44
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ. (2006) Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell. 22:245-57.
    • (2006) Mol. Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 45
    • 79952831701 scopus 로고    scopus 로고
    • Emerging complexity of protein ubiquitination in the NF-kappaB pathway
    • Habelhah H. (2010) Emerging complexity of protein ubiquitination in the NF-kappaB pathway. Genes Cancer. 1:735-47.
    • (2010) Genes Cancer , vol.1 , pp. 735-747
    • Habelhah, H.1
  • 46
    • 53849106114 scopus 로고    scopus 로고
    • Glucolipotoxicity of the pancreatic beta-cell: Myth or reality? Biochem
    • Poitout V. (2008) Glucolipotoxicity of the pancreatic beta-cell: myth or reality? Biochem. Soc. Trans. 36:901-4.
    • (2008) Soc. Trans , vol.36 , pp. 901-904
    • Poitout, V.1
  • 47
    • 84879495791 scopus 로고    scopus 로고
    • Chronic glucolipotoxic conditions in pancreatic islets impair insulin secretion due to dysregulated calcium dynamics, glucose responsiveness and mitochondrial activity
    • Somesh BP, et al. (2013) Chronic glucolipotoxic conditions in pancreatic islets impair insulin secretion due to dysregulated calcium dynamics, glucose responsiveness and mitochondrial activity. BMC Cell. Biol. 14:31.
    • (2013) BMC Cell. Biol , vol.14 , pp. 31
    • Somesh, B.P.1
  • 48
    • 84862809326 scopus 로고    scopus 로고
    • Glucolipotoxicity in pancreatic beta-Cells
    • Kim JW, Yoon KH. (2011) Glucolipotoxicity in pancreatic beta-Cells. Diabetes Metab. J. 35:444-50.
    • (2011) Diabetes Metab. J , vol.35 , pp. 444-450
    • Kim, J.W.1    Yoon, K.H.2
  • 49
    • 43549108142 scopus 로고    scopus 로고
    • Glucolipotoxicity: Fuel excess and beta-cell dysfunction
    • Poitout V, Robertson RP. (2008) Glucolipotoxicity: fuel excess and beta-cell dysfunction. Endocr. Rev. 29:351-66.
    • (2008) Endocr. Rev , vol.29 , pp. 351-366
    • Poitout, V.1    Robertson, R.P.2
  • 50
    • 84872681503 scopus 로고    scopus 로고
    • Pro-inflammatory cytokines related to severity and mortality in type 2 diabetes patients with soft tissue infection
    • [Article in Spanish]
    • Garcia-Elorriaga G, et al. 2012. Pro-inflammatory cytokines related to severity and mortality in type 2 diabetes patients with soft tissue infection. [Article in Spanish] Rev. Med. Inst. Mex. Seguro Soc. 50:237-41.
    • (2012) Rev. Med. Inst. Mex. Seguro Soc , vol.50 , pp. 237-241
    • Garcia-Elorriaga, G.1
  • 52
    • 84914181252 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 stimulates insulin secretion via inhibiting RhoA/ROCK signaling and disassembling glucotoxicity-induced stress fibers
    • Kong X, et al. (2014) Glucagon-like peptide 1 stimulates insulin secretion via inhibiting RhoA/ROCK signaling and disassembling glucotoxicity-induced stress fibers. Endocrinology. 155:4676-85.
    • (2014) Endocrinology , vol.155 , pp. 4676-4685
    • Kong, X.1
  • 54
    • 84886923440 scopus 로고    scopus 로고
    • Pdx-1 activates islet alphaand beta-cell proliferation via a mechanism regulated by transient receptor potential cation channels 3 and 6 and extracellular signal-regulated kinases 1 and 2
    • Hayes HL, et al. (2013) Pdx-1 activates islet alphaand beta-cell proliferation via a mechanism regulated by transient receptor potential cation channels 3 and 6 and extracellular signal-regulated kinases 1 and 2. Mol. Cell. Biol. 33:4017-29.
    • (2013) Mol. Cell. Biol , vol.33 , pp. 4017-4029
    • Hayes, H.L.1
  • 55
    • 79953650081 scopus 로고    scopus 로고
    • Molecular mechanism of pancreatic beta-cell adaptive proliferation: Studies during pregnancy in rats and in vitro
    • Chen G, Liu C, Xue Y, Mao X, Xu K. (2011) Molecular mechanism of pancreatic beta-cell adaptive proliferation: studies during pregnancy in rats and in vitro. Endocrine. 39:118-27.
    • (2011) Endocrine , vol.39 , pp. 118-127
    • Chen, G.1    Liu, C.2    Xue, Y.3    Mao, X.4    Xu, K.5
  • 56
    • 0035810051 scopus 로고    scopus 로고
    • Activation of the I kappa B alpha kinase (IKK) complex by double-stranded RNAbinding defective and catalytic inactive mutants of the interferon-inducible protein kinase PKR
    • Ishii T, Kwon H, Hiscott J, Mosialos G, Koromilas AE. (2001) Activation of the I kappa B alpha kinase (IKK) complex by double-stranded RNAbinding defective and catalytic inactive mutants of the interferon-inducible protein kinase PKR. Oncogene. 20:1900-12.
    • (2001) Oncogene , vol.20 , pp. 1900-1912
    • Ishii, T.1    Kwon, H.2    Hiscott, J.3    Mosialos, G.4    Koromilas, A.E.5
  • 57
    • 0034082457 scopus 로고    scopus 로고
    • PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex
    • Bonnet MC, Weil R, Dam E, Hovanessian AG, Meurs EF. (2000) PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex. Mol. Cell. Biol. 20:4532-42.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4532-4542
    • Bonnet, M.C.1    Weil, R.2    Dam, E.3    Hovanessian, A.G.4    Meurs, E.F.5
  • 58
    • 84880045947 scopus 로고    scopus 로고
    • Poly I:C induces a protective antiviral immune response in the Pacific oyster (Crassostrea gigas) against subsequent challenge with Ostreid herpesvirus (OsHV-1 muvar)
    • Green TJ, Montagnani C. (2013) Poly I:C induces a protective antiviral immune response in the Pacific oyster (Crassostrea gigas) against subsequent challenge with Ostreid herpesvirus (OsHV-1 muvar). Fish Shellfish Immunol. 35:382-8.
    • (2013) Fish Shellfish Immunol , vol.35 , pp. 382-388
    • Green, T.J.1    Montagnani, C.2
  • 59
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV. (1996) TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity. 4:387-96.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 60
    • 0033002994 scopus 로고    scopus 로고
    • Mutant cells that do not respond to interleukin-1 (IL-1) reveal a novel role for IL-1 receptor-associated kinase
    • Li X, et al. (1999) Mutant cells that do not respond to interleukin-1 (IL-1) reveal a novel role for IL-1 receptor-associated kinase. Mol. Cell. Biol. 19:4643-52.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4643-4652
    • Li, X.1
  • 61
    • 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 SH, Gunnery S, Choe JK, Mathews MB. (2002) Neoplastic progression in melanoma and colon cancer is associated with increased expression and activity of the interferon-inducible protein kinase, PKR. Oncogene. 21:8741-8.
    • (2002) Oncogene , vol.21 , pp. 8741-8748
    • Kim, S.H.1    Gunnery, S.2    Choe, J.K.3    Mathews, M.B.4
  • 62
    • 0034702174 scopus 로고    scopus 로고
    • Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR
    • Kim SH, Forman AP, Mathews MB, Gunnery S. (2000) Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR. Oncogene. 19:3086-94.
    • (2000) Oncogene , vol.19 , pp. 3086-3094
    • Kim, S.H.1    Forman, A.P.2    Mathews, M.B.3    Gunnery, S.4
  • 63
    • 84881480185 scopus 로고    scopus 로고
    • Cell death/proliferation roles for nc886, a non-coding RNA, in the protein kinase R pathway in cholangiocarcinoma
    • Kunkeaw N, et al. (2013) Cell death/proliferation roles for nc886, a non-coding RNA, in the protein kinase R pathway in cholangiocarcinoma. Oncogene. 32:3722-31.
    • (2013) Oncogene , vol.32 , pp. 3722-3731
    • Kunkeaw, N.1
  • 65
    • 0344731406 scopus 로고    scopus 로고
    • Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the alpha subunit of eukaryotic translation initiation factor 2 and NF-kappaB
    • Gil J, Alcami J, Esteban M. (1999) Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the alpha subunit of eukaryotic translation initiation factor 2 and NF-kappaB. Mol. Cell. Biol. 19:4653-63.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4653-4663
    • Gil, J.1    Alcami, J.2    Esteban, M.3
  • 66
    • 33750577982 scopus 로고    scopus 로고
    • Nuclear factor-kappaB regulates beta-cell death: A critical role for A20 in beta-cell protection
    • Liuwantara D, et al. (2006) Nuclear factor-kappaB regulates beta-cell death: a critical role for A20 in beta-cell protection. Diabetes. 55:2491-501.
    • (2006) Diabetes , vol.55 , pp. 2491-2501
    • Liuwantara, D.1
  • 67
    • 84885001378 scopus 로고    scopus 로고
    • Blockage of progesterone receptor effectively protects pancreatic islet beta cell viability
    • Zhou R, et al. (2013) Blockage of progesterone receptor effectively protects pancreatic islet beta cell viability. Steroids. 78:987-95.
    • (2013) Steroids , vol.78 , pp. 987-995
    • Zhou, R.1
  • 68
    • 84873837649 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination modulates mixed lineage kinase-3 interaction with JIP1 scaffold protein in cytokineinduced pancreatic beta cell death
    • Humphrey RK, et al. (2013) Lysine 63-linked ubiquitination modulates mixed lineage kinase-3 interaction with JIP1 scaffold protein in cytokineinduced pancreatic beta cell death. J. Biol. Chem. 288:2428-40.
    • (2013) J. Biol. Chem , vol.288 , pp. 2428-2440
    • Humphrey, R.K.1
  • 69
    • 81055145273 scopus 로고    scopus 로고
    • Crucial role for TNF receptor-associated factor 2 (TRAF2) in regulating NFkappaB2 signaling that contributes to autoimmunity
    • Lin WJ, et al. (2011) Crucial role for TNF receptor-associated factor 2 (TRAF2) in regulating NFkappaB2 signaling that contributes to autoimmunity. Proc. Natl. Acad. Sci. U. S. A. 108:18354-9.
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , pp. 18354-18359
    • Lin, W.J.1
  • 70
    • 84869099031 scopus 로고    scopus 로고
    • APPL1 regulates basal NF-kappaB activity by stabilizing NIK
    • Hupalowska A, Pyrzynska B, Miaczynska M. (2012) APPL1 regulates basal NF-kappaB activity by stabilizing NIK. J. Cell Sci. 125:4090-102.
    • (2012) J. Cell Sci , vol.125 , pp. 4090-4102
    • Hupalowska, A.1    Pyrzynska, B.2    Miaczynska, M.3
  • 71
    • 79954566704 scopus 로고    scopus 로고
    • Cucurbitacin B suppresses the transactivation activity of RelA/p65
    • Jin HR, Jin X, Dat NT, Lee JJ. (2011) Cucurbitacin B suppresses the transactivation activity of RelA/p65. J. Cell. Biochem. 112:1643-50.
    • (2011) J. Cell. Biochem , vol.112 , pp. 1643-1650
    • Jin, H.R.1    Jin, X.2    Dat, N.T.3    Lee, J.J.4
  • 72
    • 84871862001 scopus 로고    scopus 로고
    • Downregulation of TRAF2 mediates NIK-induced pancreatic cancer cell proliferation and tumorigenicity
    • Doppler H, Liou GY, Storz P. (2013) Downregulation of TRAF2 mediates NIK-induced pancreatic cancer cell proliferation and tumorigenicity. PloS One. 8:e53676.
    • (2013) PloS One , vol.8
    • Doppler, H.1    Liou, G.Y.2    Storz, P.3
  • 73
    • 84898657121 scopus 로고    scopus 로고
    • Suppressive role of miR-502-5p in breast cancer via downregulation of TRAF2
    • Sun LL, et al. (2014) Suppressive role of miR-502-5p in breast cancer via downregulation of TRAF2. Oncol. Rep. 31:2085-92.
    • (2014) Oncol. Rep , vol.31 , pp. 2085-2092
    • Sun, L.L.1
  • 74
    • 84859602197 scopus 로고    scopus 로고
    • De-ubiquitinating protease USP2a targets RIP1 and TRAF2 to mediate cell death by TNF
    • Mahul-Mellier AL, et al. (2012) De-ubiquitinating protease USP2a targets RIP1 and TRAF2 to mediate cell death by TNF. Cell Death Differ. 19:891-9.
    • (2012) Cell Death Differ , vol.19 , pp. 891-899
    • Mahul-Mellier, A.L.1
  • 75
    • 84864389178 scopus 로고    scopus 로고
    • NEMO inhibits programmed necrosis in an NFkappaB-independent manner by restraining RIP1
    • O'Donnell MA, Hase H, Legarda D, Ting AT. (2012) NEMO inhibits programmed necrosis in an NFkappaB-independent manner by restraining RIP1. PloS One. 7:e41238.
    • (2012) PloS One , vol.7
    • O'Donnell, M.A.1    Hase, H.2    Legarda, D.3    Ting, A.T.4
  • 76
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes
    • Ozcan U, et al. (2004) Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science. 306:457-61.
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1
  • 77
    • 84919643292 scopus 로고    scopus 로고
    • Identification of small molecules that protect pancreatic beta cells against endoplasmic reticulum stress-induced cell death
    • Tran K, et al. (2014) Identification of small molecules that protect pancreatic beta cells against endoplasmic reticulum stress-induced cell death. ACS Chem. Biol. 9:2796-806.
    • (2014) ACS Chem. Biol , vol.9 , pp. 2796-2806
    • Tran, K.1
  • 79
    • 0037013147 scopus 로고    scopus 로고
    • Suppression of Myc-induced apoptosis in beta cells exposes multiple oncogenic properties of Myc and triggers carcinogenic progression
    • Pelengaris S, Khan M, Evan GI. (2002) Suppression of Myc-induced apoptosis in beta cells exposes multiple oncogenic properties of Myc and triggers carcinogenic progression. Cell. 109:321-34.
    • (2002) Cell , vol.109 , pp. 321-334
    • Pelengaris, S.1    Khan, M.2    Evan, G.I.3


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