메뉴 건너뛰기




Volumn 10, Issue 8, 2011, Pages 3372-3385

Oleate-induced beta cell dysfunction and apoptosis: A proteomic approach to glucolipotoxicity by an unsaturated fatty acid

Author keywords

beta cells; lipotoxicity; oleate; proteomics; type 2 diabetes

Indexed keywords

ACETYL COENZYME A; ADENOSINE TRIPHOSPHATE; CHAPERONE; GLUCOSE; GLUCOSE REGULATED PROTEIN 78; INSULIN; MESSENGER RNA; OLEIC ACID; PROTEASOME; REACTIVE OXYGEN METABOLITE; UBIQUITIN; UNSATURATED FATTY ACID;

EID: 79961238766     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr101290n     Document Type: Article
Times cited : (20)

References (58)
  • 1
    • 0037219411 scopus 로고    scopus 로고
    • β-cell deficit and increased β-cell apoptosis in humans with type 2 diabetes
    • DOI 10.2337/diabetes.52.1.102
    • Butler, A. E.; Janson, J.; Bonner-Weir, S. Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes Diabetes 2003, 52, 102-110 (Pubitemid 36042113)
    • (2003) Diabetes , vol.52 , Issue.1 , pp. 102-110
    • Butler, A.E.1    Janson, J.2    Bonner-Weir, S.3    Ritzel, R.4    Rizza, R.A.5    Butler, P.C.6
  • 2
  • 3
    • 33748992313 scopus 로고    scopus 로고
    • Adipocytokines: Mediators linking adipose tissue, inflammation and immunity
    • DOI 10.1038/nri1937, PII NRI1937
    • Tilg, H.; Moschen, A. R. Adipocytokines: mediators linking adipose tissue, inflammation and immunity Nat. Rev. Immunol. 2006, 6, 772-783 (Pubitemid 44453463)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.10 , pp. 772-783
    • Tilg, H.1    Moschen, A.R.2
  • 4
    • 44849116310 scopus 로고    scopus 로고
    • The perfect storm: Obesity, adipocyte dysfunction, and metabolic consequences
    • DOI 10.1373/clinchem.2007.100156
    • de Ferranti, S.; Mozaffarian, D. The perfect storm: obesity, adipocyte dysfunction, and metabolic consequences Clin. Chem. 2008, 54, 945-955 (Pubitemid 351793400)
    • (2008) Clinical Chemistry , vol.54 , Issue.6 , pp. 945-955
    • De Ferranti, S.1    Mozaffarian, D.2
  • 5
    • 0029151863 scopus 로고
    • Lipotoxicity in the pathogenesis of obesity-dependent NIDDM. Genetic and clinical implications
    • Unger, R. H. Lipotoxicity in the pathogenesis of obesity-dependent NIDDM. Genetic and clinical implications Diabetes 1995, 44, 863-870
    • (1995) Diabetes , vol.44 , pp. 863-870
    • Unger, R.H.1
  • 6
    • 0036896505 scopus 로고    scopus 로고
    • Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: Role in beta-cell adaptation and failure in the etiology of diabetes
    • Prentki, M.; Joly, E.; El-Assaad, W. Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: role in beta-cell adaptation and failure in the etiology of diabetes Diabetes 2002, 51 (Suppl 3) S405-S413
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 3
    • Prentki, M.1    Joly, E.2    El-Assaad, W.3
  • 7
    • 34547888676 scopus 로고    scopus 로고
    • Mechanisms involved in the cytotoxic and cytoprotective actions of saturated versus monounsaturated long-chain fatty acids in pancreatic β-cells
    • DOI 10.1677/JOE-07-0082
    • Diakogiannaki, E.; Dhayal, S.; Childs, C. E. Mechanisms involved in the cytotoxic and cytoprotective actions of saturated versus monounsaturated long-chain fatty acids in pancreatic beta-cells J. Endocrinol. 2007, 194, 283-291 (Pubitemid 47249667)
    • (2007) Journal of Endocrinology , vol.194 , Issue.2 , pp. 283-291
    • Diakogiannaki, E.1    Dhayal, S.2    Childs, C.E.3    Calder, P.C.4    Welters, H.J.5    Morgan, N.G.6
  • 8
    • 42149111577 scopus 로고    scopus 로고
    • Structural requirements for the cytoprotective actions of mono-unsaturated fatty acids in the pancreatic β-cell line, BRIN-BD11
    • DOI 10.1038/bjp.2008.43, PII BJP200843
    • Dhayal, S.; Welters, H. J.; Morgan, N. G. Structural requirements for the cytoprotective actions of mono-unsaturated fatty acids in the pancreatic beta-cell line, BRIN-BD11 Br. J. Pharmacol. 2008, 153, 1718-1727 (Pubitemid 351536000)
    • (2008) British Journal of Pharmacology , vol.153 , Issue.8 , pp. 1718-1727
    • Dhayal, S.1    Welters, H.J.2    Morgan, N.G.3
  • 10
    • 0037230114 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is involved in apoptosis induced by serum withdrawal and fatty acids in the β-cell line INS-1
    • DOI 10.1210/en.2001-211282
    • Maestre, I.; Jordan, J.; Calvo, S. Mitochondrial dysfunction is involved in apoptosis induced by serum withdrawal and fatty acids in the beta-cell line INS-1 Endocrinology 2003, 144, 335-345 (Pubitemid 36076123)
    • (2003) Endocrinology , vol.144 , Issue.1 , pp. 335-345
    • Maestre, I.1    Jordan, J.2    Calvo, S.3    Reig, J.A.4    Cena, V.5    Soria, B.6    Prentki, M.7    Roche, E.8
  • 11
    • 33745116619 scopus 로고    scopus 로고
    • Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic β-cell apoptosis
    • DOI 10.1210/en.2005-1494
    • Karaskov, E.; Scott, C.; Zhang, L. Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis Endocrinology 2006, 147, 3398-3407 (Pubitemid 43901131)
    • (2006) Endocrinology , vol.147 , Issue.7 , pp. 3398-3407
    • Karaskov, E.1    Scott, C.2    Zhang, L.3    Teodoro, T.4    Ravazzola, M.5    Volchuk, A.6
  • 12
    • 49649084031 scopus 로고    scopus 로고
    • Initiation and execution of lipotoxic ER stress in pancreatic beta-cells
    • Cunha, D. A.; Hekerman, P.; Ladriere, L. Initiation and execution of lipotoxic ER stress in pancreatic beta-cells J. Cell Sci. 2008, 121, 2308-2318
    • (2008) J. Cell Sci. , vol.121 , pp. 2308-2318
    • Cunha, D.A.1    Hekerman, P.2    Ladriere, L.3
  • 13
    • 33646856191 scopus 로고    scopus 로고
    • Chronic effects of different non-esterified fatty acids on pancreatic islets of rats
    • DOI 10.1385/ENDO:29:1:169
    • Wang, Y.; Wang, P. Y.; Takashi, K. Chronic effects of different non-esterified fatty acids on pancreatic islets of rats Endocrine 2006, 29, 169-173 (Pubitemid 43780361)
    • (2006) Endocrine , vol.29 , Issue.1 , pp. 169-173
    • Wang, Y.1    Wang, P.-Y.2    Takashi, K.3
  • 16
    • 49249115161 scopus 로고    scopus 로고
    • Long-term exposure of mouse pancreatic islets to oleate or palmitate results in reduced glucose-induced somatostatin and oversecretion of glucagon
    • Collins, S. C.; Salehi, A.; Eliasson, L. Long-term exposure of mouse pancreatic islets to oleate or palmitate results in reduced glucose-induced somatostatin and oversecretion of glucagon Diabetologia 2008, 51, 1689-1693
    • (2008) Diabetologia , vol.51 , pp. 1689-1693
    • Collins, S.C.1    Salehi, A.2    Eliasson, L.3
  • 17
    • 0036230225 scopus 로고    scopus 로고
    • Expression profiling of palmitate- and oleate-regulated genes provides novel insights into the effects of chronic lipid exposure on pancreatic β-cell function
    • Busch, A. K.; Cordery, D.; Denyer, G. S. Expression profiling of palmitate- and oleate-regulated genes provides novel insights into the effects of chronic lipid exposure on pancreatic beta-cell function Diabetes 2002, 51, 977-987 (Pubitemid 34438339)
    • (2002) Diabetes , vol.51 , Issue.4 , pp. 977-987
    • Busch, A.K.1    Cordery, D.2    Denyer, G.S.3    Biden, T.J.4
  • 18
    • 34748899652 scopus 로고    scopus 로고
    • Evaluation of the SELDI-TOF MS technique for protein profiling of pancreatic islets exposed to glucose and oleate
    • DOI 10.1002/pmic.200601019
    • Ortsater, H.; Sundsten, T.; Lin, J. M. Evaluation of the SELDI-TOF MS technique for protein profiling of pancreatic islets exposed to glucose and oleate Proteomics 2007, 7, 3105-3115 (Pubitemid 47477954)
    • (2007) Proteomics , vol.7 , Issue.17 , pp. 3105-3115
    • Ortsater, H.1    Sundsten, T.2    Lin, J.-M.3    Bergsten, P.4
  • 19
    • 0842291578 scopus 로고    scopus 로고
    • Glucose Sensitivity and Metabolism-Secretion Coupling Studied during Two-Year Continuous Culture in INS-1E Insulinoma Cells
    • DOI 10.1210/en.2003-1099
    • Merglen, A.; Theander, S.; Rubi, B. Glucose sensitivity and metabolism-secretion coupling studied during two-year continuous culture in INS-1E insulinoma cells Endocrinology 2004, 145, 667-678 (Pubitemid 38183809)
    • (2004) Endocrinology , vol.145 , Issue.2 , pp. 667-678
    • Merglen, A.1    Theander, S.2    Rubi, B.3    Chaffard, G.4    Wollheim, C.B.5    Maechler, P.6
  • 20
    • 0026550830 scopus 로고
    • Establishment of 2-mercaptoethanol-dependent differentiated insulin-secreting cell lines
    • Asfari, M.; Janjic, D.; Meda, P. Establishment of 2-mercaptoethanol- dependent differentiated insulin-secreting cell lines Endocrinology 1992, 130, 167-178
    • (1992) Endocrinology , vol.130 , pp. 167-178
    • Asfari, M.1    Janjic, D.2    Meda, P.3
  • 21
    • 0029797603 scopus 로고    scopus 로고
    • Glucose promotes survival of rat pancreatic β cells by activating synthesis of proteins which suppress a constitutive apoptotic program
    • Hoorens, A.; Van de, C. M.; Kloppel, G. Glucose promotes survival of rat pancreatic beta cells by activating synthesis of proteins which suppress a constitutive apoptotic program J. Clin. Invest. 1996, 98, 1568-1574 (Pubitemid 26327866)
    • (1996) Journal of Clinical Investigation , vol.98 , Issue.7 , pp. 1568-1574
    • Hoorens, A.1    Van De Casteele, M.2    Kloppel, G.3    Pipeleers, D.4
  • 22
    • 38349025873 scopus 로고    scopus 로고
    • Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells: New insights into the pathways involved
    • D'Hertog, W.; Overbergh, L.; Lage, K. Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells: new insights into the pathways involved Mol. Cell. Proteomics 2007, 6, 2180-2199
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2180-2199
    • D'Hertog, W.1    Overbergh, L.2    Lage, K.3
  • 23
    • 38349025873 scopus 로고    scopus 로고
    • Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells: New insights into the pathways involved
    • D'Hertog, W.; Overbergh, L.; Lage, K. Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells: new insights into the pathways involved Mol. Cell. Proteomics 2007, 6, 2180-2199
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2180-2199
    • D'Hertog, W.1    Overbergh, L.2    Lage, K.3
  • 25
    • 0022369416 scopus 로고
    • Standardization of insulin secretion from pancreatic islets: Validation of a DNA assay
    • Hopcroft, D. W.; Mason, D. R.; Scott, R. S. Standardization of insulin secretion from pancreatic islets: validation of a DNA assay Horm. Metab. Res. 1985, 17, 559-561 (Pubitemid 16125286)
    • (1985) Hormone and Metabolic Research , vol.17 , Issue.11 , pp. 559-561
    • Hopcroft, D.W.1    Mason, D.R.2    Scott, R.S.3
  • 26
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. A new mathematical model for relative quantification in real-time RT-PCR Nucleic Acids Res. 2001, 29, e45
    • (2001) Nucleic Acids Res. , vol.29 , pp. 45
    • Pfaffl, M.W.1
  • 27
  • 28
    • 77949302911 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha (PPARalpha) protects against oleate-induced INS-1E beta cell dysfunction by preserving carbohydrate metabolism
    • Frigerio, F.; Brun, T.; Bartley, C. Peroxisome proliferator-activated receptor alpha (PPARalpha) protects against oleate-induced INS-1E beta cell dysfunction by preserving carbohydrate metabolism Diabetologia 2010, 53, 331-340
    • (2010) Diabetologia , vol.53 , pp. 331-340
    • Frigerio, F.1    Brun, T.2    Bartley, C.3
  • 29
    • 33947510911 scopus 로고    scopus 로고
    • Selective inhibition of eukaryotic translation initiation factor 2α dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic β-cell dysfunction and apoptosis
    • DOI 10.1074/jbc.M607627200
    • Cnop, M.; Ladriere, L.; Hekerman, P. Selective inhibition of eukaryotic translation initiation factor 2 alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis J. Biol. Chem. 2007, 282, 3989-3997 (Pubitemid 47084497)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 3989-3997
    • Cnop, M.1    Ladriere, L.2    Hekerman, P.3    Ortis, F.4    Cardozo, A.K.5    Dogusan, Z.6    Flamez, D.7    Boyce, M.8    Yuan, J.9    Eizirik, D.L.10
  • 31
    • 0032861252 scopus 로고    scopus 로고
    • Lipid rather than glucose metabolism is implicated in altered insulin secretion caused by oleate in INS-1 cells
    • Segall, L.; Lameloise, N.; Assimacopoulos-Jeannet, F. Lipid rather than glucose metabolism is implicated in altered insulin secretion caused by oleate in INS-1 cells Am. J. Physiol. 1999, 277, E521-E528
    • (1999) Am. J. Physiol. , vol.277
    • Segall, L.1    Lameloise, N.2    Assimacopoulos-Jeannet, F.3
  • 32
    • 0022375444 scopus 로고
    • +-channels in pancreatic β-cells are regulated by intracellular ATP
    • DOI 10.1007/BF00595682
    • Rorsman, P.; Trube, G. Glucose dependent K+-channels in pancreatic beta-cells are regulated by intracellular ATP Pflugers Arch. 1985, 405, 305-309 (Pubitemid 16202499)
    • (1985) Pflugers Archiv European Journal of Physiology , vol.405 , Issue.4 , pp. 305-309
    • Rorsman, P.1    Trube, G.2
  • 34
    • 33645530700 scopus 로고    scopus 로고
    • Regulation of the insulin gene by glucose and fatty acids
    • Poitout, V.; Hagman, D.; Stein, R. Regulation of the insulin gene by glucose and fatty acids J. Nutr. 2006, 136, 873-876
    • (2006) J. Nutr. , vol.136 , pp. 873-876
    • Poitout, V.1    Hagman, D.2    Stein, R.3
  • 35
    • 77957795415 scopus 로고    scopus 로고
    • ATP-citrate lyase reduction mediates palmitate-induced apoptosis in pancreatic beta-cells
    • Chu, K. Y.; Lin, Y.; Hendel, A. ATP-citrate lyase reduction mediates palmitate-induced apoptosis in pancreatic beta-cells J. Biol. Chem. 2010, 285, 32606-32615
    • (2010) J. Biol. Chem. , vol.285 , pp. 32606-32615
    • Chu, K.Y.1    Lin, Y.2    Hendel, A.3
  • 36
    • 0842284799 scopus 로고    scopus 로고
    • Beta-cell glucose toxicity, lipotoxicity, and chronic oxidative stress in type 2 diabetes
    • Robertson, R. P.; Harmon, J.; Tran, P. O. Beta-cell glucose toxicity, lipotoxicity, and chronic oxidative stress in type 2 diabetes Diabetes 2004, 53 (Suppl 1) S119-S124
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Robertson, R.P.1    Harmon, J.2    Tran, P.O.3
  • 37
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas, E.; Davies, K. J. Mitochondrial free radical generation, oxidative stress, and aging Free Radic. Biol. Med. 2000, 29, 222-230
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 38
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • DOI 10.1074/jbc.M210269200
    • Han, D.; Antunes, F.; Canali, R. Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol J. Biol. Chem. 2003, 278, 5557-5563 (Pubitemid 36800797)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 39
    • 29344468832 scopus 로고    scopus 로고
    • Voltage-dependent anion channel (VDAC) as mitochondrial governator - Thinking outside the box
    • DOI 10.1016/j.bbadis.2005.10.006, PII S0925443905001523, Mitochondria in Diseases and Therapeutics
    • Lemasters, J. J.; Holmuhamedov, E. Voltage-dependent anion channel (VDAC) as mitochondrial governator - thinking outside the box Biochim. Biophys. Acta 2006, 1762, 181-190 (Pubitemid 43006024)
    • (2006) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1762 , Issue.2 , pp. 181-190
    • Lemasters, J.J.1    Holmuhamedov, E.2
  • 40
    • 77049126374 scopus 로고    scopus 로고
    • Closure of VDAC causes oxidative stress and accelerates the Ca(2+)-induced mitochondrial permeability transition in rat liver mitochondria
    • Tikunov, A.; Johnson, C. B.; Pediaditakis, P. Closure of VDAC causes oxidative stress and accelerates the Ca(2+)-induced mitochondrial permeability transition in rat liver mitochondria Arch. Biochem. Biophys. 2010, 495, 174-181
    • (2010) Arch. Biochem. Biophys. , vol.495 , pp. 174-181
    • Tikunov, A.1    Johnson, C.B.2    Pediaditakis, P.3
  • 41
    • 25144476923 scopus 로고    scopus 로고
    • Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3
    • Brand, M. D.; Esteves, T. C. Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3 Cell Metab 2005, 2, 85-93
    • (2005) Cell Metab , vol.2 , pp. 85-93
    • Brand, M.D.1    Esteves, T.C.2
  • 42
    • 0032991716 scopus 로고    scopus 로고
    • Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets
    • DOI 10.2337/diabetes.48.7.1482
    • Chan, C. B.; MacDonald, P. E.; Saleh, M. C. Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets Diabetes 1999, 48, 1482-1486 (Pubitemid 29297315)
    • (1999) Diabetes , vol.48 , Issue.7 , pp. 1482-1486
    • Chan, C.B.1    MacDonald, P.E.2    Saleh, M.C.3    Johns, D.C.4    Marban, E.5    Wheeler, M.B.6
  • 43
    • 0036829870 scopus 로고    scopus 로고
    • Uncoupling protein 2 knockout mice have enhanced insulin secretory capacity after a high-fat diet
    • Joseph, J. W.; Koshkin, V.; Zhang, C. Y. Uncoupling protein 2 knockout mice have enhanced insulin secretory capacity after a high-fat diet Diabetes 2002, 51, 3211-3219 (Pubitemid 35246967)
    • (2002) Diabetes , vol.51 , Issue.11 , pp. 3211-3219
    • Joseph, J.W.1    Koshkin, V.2    Zhang, C.-Y.3    Wang, J.4    Lowell, B.B.5    Chan, C.B.6    Wheeler, M.B.7
  • 44
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss, G.; Kim, V. N.; Kataoka, N. Messenger-RNA-binding proteins and the messages they carry Nat. Rev. Mol. Cell Biol. 2002, 3, 195-205
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 45
    • 70350425204 scopus 로고    scopus 로고
    • Protein kinase C-delta mediates down-regulation of heterogeneous nuclear ribonucleoprotein K protein: Involvement in apoptosis induction
    • Gao, F. H.; Wu, Y. L.; Zhao, M. Protein kinase C-delta mediates down-regulation of heterogeneous nuclear ribonucleoprotein K protein: involvement in apoptosis induction Exp. Cell Res. 2009, 315, 3250-3258
    • (2009) Exp. Cell Res. , vol.315 , pp. 3250-3258
    • Gao, F.H.1    Wu, Y.L.2    Zhao, M.3
  • 47
    • 74849135072 scopus 로고    scopus 로고
    • Proteomic analysis of cell lines expressing small hepatitis B surface antigen revealed decreased glucose-regulated protein 78 kDa expression in association with higher susceptibility to apoptosis
    • Zhao, C.; Zhang, W.; Tian, X. Proteomic analysis of cell lines expressing small hepatitis B surface antigen revealed decreased glucose-regulated protein 78 kDa expression in association with higher susceptibility to apoptosis J. Med. Virol. 2010, 82, 14-22
    • (2010) J. Med. Virol. , vol.82 , pp. 14-22
    • Zhao, C.1    Zhang, W.2    Tian, X.3
  • 48
    • 34447559956 scopus 로고    scopus 로고
    • Downregulation of hnRNP C1/C2 by siRNA sensitizes HeLa cells to various stresses
    • Hossain, M. N.; Fuji, M.; Miki, K. Downregulation of hnRNP C1/C2 by siRNA sensitizes HeLa cells to various stresses Mol. Cell. Biochem. 2007, 296, 151-157
    • (2007) Mol. Cell. Biochem. , vol.296 , pp. 151-157
    • Hossain, M.N.1    Fuji, M.2    Miki, K.3
  • 49
    • 69249087295 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-xS splice isoform
    • Revil, T.; Pelletier, J.; Toutant, J. Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-xS splice isoform J. Biol. Chem. 2009, 284, 21458-21467
    • (2009) J. Biol. Chem. , vol.284 , pp. 21458-21467
    • Revil, T.1    Pelletier, J.2    Toutant, J.3
  • 50
    • 58249102282 scopus 로고    scopus 로고
    • HnRNP A1 regulates UV-induced NF-kappaB signalling through destabilization of cIAP1 mRNA
    • Zhao, T. T.; Graber, T. E.; Jordan, L. E. hnRNP A1 regulates UV-induced NF-kappaB signalling through destabilization of cIAP1 mRNA Cell Death Differ. 2009, 16, 244-252
    • (2009) Cell Death Differ. , vol.16 , pp. 244-252
    • Zhao, T.T.1    Graber, T.E.2    Jordan, L.E.3
  • 51
    • 48349132088 scopus 로고    scopus 로고
    • Concomitant transitory up-regulation of X-linked inhibitor of apoptosis protein (XIAP) and the heterogeneous nuclear ribonucleoprotein C1-C2 in surviving cells during neuronal apoptosis
    • Spahn, A.; Blondeau, N.; Heurteaux, C. Concomitant transitory up-regulation of X-linked inhibitor of apoptosis protein (XIAP) and the heterogeneous nuclear ribonucleoprotein C1-C2 in surviving cells during neuronal apoptosis Neurochem. Res. 2008, 33, 1859-1868
    • (2008) Neurochem. Res. , vol.33 , pp. 1859-1868
    • Spahn, A.1    Blondeau, N.2    Heurteaux, C.3
  • 52
    • 57749114764 scopus 로고    scopus 로고
    • Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step
    • Lee, J. N.; Zhang, X.; Feramisco, J. D. Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step J. Biol. Chem. 2008, 283, 33772-33783
    • (2008) J. Biol. Chem. , vol.283 , pp. 33772-33783
    • Lee, J.N.1    Zhang, X.2    Feramisco, J.D.3
  • 53
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • DOI 10.1038/sj.emboj.7601970, PII 7601970
    • Liberek, K.; Lewandowska, A.; Zietkiewicz, S. Chaperones in control of protein disaggregation EMBO J. 2008, 27, 328-335 (Pubitemid 351161659)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 54
    • 33749318236 scopus 로고    scopus 로고
    • 2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death
    • DOI 10.2337/db05-1566
    • Marzban, L.; Rhodes, C. J.; Steiner, D. F. Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death Diabetes 2006, 55, 2192-2201 (Pubitemid 44743615)
    • (2006) Diabetes , vol.55 , Issue.8 , pp. 2192-2201
    • Marzban, L.1    Rhodes, C.J.2    Steiner, D.F.3    Haataja, L.4    Halban, P.A.5    Verchere, C.B.6
  • 55
    • 0035854775 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin
    • Vaughan, P. S.; Leszyk, J. D.; Vaughan, K. T. Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin J. Biol. Chem. 2001, 276, 26171-26179
    • (2001) J. Biol. Chem. , vol.276 , pp. 26171-26179
    • Vaughan, P.S.1    Leszyk, J.D.2    Vaughan, K.T.3
  • 56
    • 0033044418 scopus 로고    scopus 로고
    • Microtubules and signal transduction
    • DOI 10.1016/S0955-0674(99)80010-6
    • Gundersen, G. G.; Cook, T. A. Microtubules and signal transduction Curr. Opin. Cell Biol. 1999, 11, 81-94 (Pubitemid 29084135)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.1 , pp. 81-94
    • Gundersen, G.G.1    Cook, T.A.2
  • 57
    • 0027493180 scopus 로고
    • Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein
    • DOI 10.1038/365459a0
    • Pleasure, I. T.; Black, M. M.; Keen, J. H. Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein Nature 1993, 365, 459-462 (Pubitemid 23311044)
    • (1993) Nature , vol.365 , Issue.6445 , pp. 459-462
    • Pleasure, I.T.1    Black, M.M.2    Keen, J.H.3
  • 58
    • 0029752048 scopus 로고    scopus 로고
    • Transport vesicle docking: SNAREs and associates
    • DOI 10.1146/annurev.cellbio.12.1.441
    • Pfeffer, S. R. Transport vesicle docking: SNAREs and associates Annu. Rev. Cell Dev. Biol. 1996, 12, 441-461 (Pubitemid 26422721)
    • (1996) Annual Review of Cell and Developmental Biology , vol.12 , pp. 441-461
    • Pfeffer, S.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.