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Volumn 8, Issue 4, 2011, Pages 495-504

Unraveling pancreatic islet biology by quantitative proteomics

Author keywords

diabetes; insulin resistance; pancreatic b cells; pancreatic islets; quantitative proteomics; signaling pathway

Indexed keywords

GLUCOSE; PROTEOME;

EID: 80051761567     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/epr.11.39     Document Type: Review
Times cited : (11)

References (87)
  • 1
    • 0029020475 scopus 로고
    • An immunocytochemical and morphometric study of the rat pancreatic islets
    • Elayat AA, el-Naggar MM, Tahir M. An immunocytochemical and morphometric study of the rat pancreatic islets. J. Anat. 186(Pt 3), 629-637 (1995).
    • (1995) J. Anat. , vol.186 , Issue.PART 3 , pp. 629-637
    • Elayat, A.A.1    El-Naggar, M.M.2    Tahir, M.3
  • 3
    • 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 AE, Janson J, Bonner-Weir S, Ritzel R, Rizza RA, Butler PC. b cell deficit and increased b-cell apoptosis in humans with Type 2 diabetes. Diabetes 5 (1), 102-110 (2003). (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
  • 4
    • 33746207753 scopus 로고    scopus 로고
    • Type 1 diabetes: Pathogenesis and prevention
    • DOI 10.1503/cmaj.060244
    • Gillespie KM. Type 1 diabetes: Pathogenesis and prevention. CMAJ 175(2), 165-170 (2006). (Pubitemid 44126252)
    • (2006) Canadian Medical Association Journal , vol.175 , Issue.2 , pp. 165-170
    • Gillespie, K.M.1
  • 6
    • 18244370762 scopus 로고    scopus 로고
    • Inflammation, stress and diabetes
    • Wellen KE, Hotamisligil GS. Inflammation, stress and diabetes. J Clin. Invest. 115(5), 1111-1119 (2005).
    • (2005) J Clin. Invest. , vol.115 , Issue.5 , pp. 1111-1119
    • Wellen, K.E.1    Hotamisligil, G.S.2
  • 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 CE, Calder PC, Welters HJ, Morgan NG. Mechanisms involved in the cytotoxic and cytoprotective actions of saturated versus monounsaturated long-chain fatty acids in pancreatic b-cells. J. Endocrinol. 194(2), 283-291 (2007). (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
  • 10
    • 69549126592 scopus 로고    scopus 로고
    • Pancreatic islet amyloidosis, b-cell apoptosis and a-cell proliferation are determinants of islet remodeling in Type-2 diabetic baboons
    • Guardado-Mendoza R, Davalli AM, Chavez AO et al. Pancreatic islet amyloidosis, b-cell apoptosis and a-cell proliferation are determinants of islet remodeling in Type-2 diabetic baboons. Proc. Natl Acad. Sci. USA 106(33), 13992-13997 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.33 , pp. 13992-13997
    • Guardado-Mendoza, R.1    Davalli, A.M.2    Chavez, A.O.3
  • 11
    • 79954570143 scopus 로고    scopus 로고
    • The glial glutamate transporter 1 (GLT1) is expressed by pancreatic b-cells and prevents glutamate-induced b-cell death
    • Di Cairano ES, Davalli AM, Perego L et al. The glial glutamate transporter 1 (GLT1) is expressed by pancreatic b-cells and prevents glutamate-induced b-cell death. J Biol. Chem. 286(16), 14007-14018 (2011).
    • (2011) J Biol. Chem. , vol.286 , Issue.16 , pp. 14007-14018
    • Di Cairano, E.S.1    Davalli, A.M.2    Perego, L.3
  • 12
    • 55149110908 scopus 로고    scopus 로고
    • Transgenic mice overexpressing human G97 R IRS-1 show impaired insulin action and insulin secretion
    • Hribal ML, Tornei F, Pujol A et al. Transgenic mice overexpressing human G97 R IRS-1 show impaired insulin action and insulin secretion. J Cell Mol. Med. 12(5B), 2096-2106 (2008).
    • (2008) J Cell Mol. Med. , vol.12 , Issue.5 B , pp. 2096-2106
    • Hribal, M.L.1    Tornei, F.2    Pujol, A.3
  • 14
    • 53049108033 scopus 로고    scopus 로고
    • Characterization of the mouse pancreatic islet proteome and comparative analysis with other mouse tissues
    • The first extensive profiling of the mouse islet proteome by 2D-liquid chromotography (LC)-MS/MS.
    • Petyuk VA, Qian WJ, Hinault C et al. Characterization of the mouse pancreatic islet proteome and comparative analysis with other mouse tissues. J. Proteome Res. 7(8), 3114-3126 (2008). The first extensive profiling of the mouse islet proteome by 2D-liquid chromotography (LC)-MS/MS.
    • (2008) J. Proteome Res. , vol.7 , Issue.8 , pp. 3114-3126
    • Petyuk, V.A.1    Qian, W.J.2    Hinault, C.3
  • 15
    • 79955427809 scopus 로고    scopus 로고
    • Detection of differential proteomes associated with the development of Type 2 diabetes in the Zucker rat model using the iTRAQ technique
    • A LC-MS/MS based quantitative proteomic study on islets comparing control and diabetic rat models to identify factors associated with the development of diabetes.
    • Han D, Moon S, Kim H et al. Detection of differential proteomes associated with the development of Type 2 diabetes in the Zucker rat model using the iTRAQ technique. J Proteome Res. 10(2), 564-577 (2010). A LC-MS/MS based quantitative proteomic study on islets comparing control and diabetic rat models to identify factors associated with the development of diabetes.
    • (2010) J Proteome Res. , vol.10 , Issue.2 , pp. 564-577
    • Han, D.1    Moon, S.2    Kim, H.3
  • 16
    • 73149110595 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of single pancreatic islets
    • High-sensitivity LC-MS/MS proteomics at the single islet level.
    • Waanders LF, Chwalek K, Monetti M, Kumar C, Lammert E, Mann M. Quantitative proteomic analysis of single pancreatic islets. Proc. Natl Acad. Sci. USA 106(45), 18902-18907 (2009). High-sensitivity LC-MS/MS proteomics at the single islet level.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.45 , pp. 18902-18907
    • Waanders, L.F.1    Chwalek, K.2    Monetti, M.3    Kumar, C.4    Lammert, E.5    Mann, M.6
  • 17
    • 50249094538 scopus 로고    scopus 로고
    • The identification of potential factors associated with the development of Type 2 diabetes: A quantitative proteomics approach
    • An extensive quantitative proteomic study on islets from a diabetic model.
    • Lu H, Yang Y, Allister EM, Wijesekara N, Wheeler MB. The identification of potential factors associated with the development of Type 2 diabetes: A quantitative proteomics approach. Mol. Cell. Proteomics 7(8), 1434-1451 (2008). An extensive quantitative proteomic study on islets from a diabetic model.
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.8 , pp. 1434-1451
    • Lu, H.1    Yang, Y.2    Allister, E.M.3    Wijesekara, N.4    Wheeler, M.B.5
  • 18
    • 24744460787 scopus 로고    scopus 로고
    • Proteomic analysis of differential protein expression in response to epidermal growth factor in neonatal porcine pancreatic cell monolayers
    • EGF-stimulated intracellular signaling relevant to islet development revealed by differential proteomics.
    • Hong OK, Suh SH, Kwon HS et al. Proteomic analysis of differential protein expression in response to epidermal growth factor in neonatal porcine pancreatic cell monolayers. J. Cell Biochem. 95(4), 769-781 (2005). EGF-stimulated intracellular signaling relevant to islet development revealed by differential proteomics.
    • (2005) J. Cell Biochem. , vol.95 , Issue.4 , pp. 769-781
    • Hong, O.K.1    Suh, S.H.2    Kwon, H.S.3
  • 19
    • 33845997409 scopus 로고    scopus 로고
    • Proteomic screening of glucose-responsive and glucose non-responsive MIN-6 beta cells reveals differential expression of proteins involved in protein folding, secretion and oxidative stress
    • DOI 10.1002/pmic.200600298
    • Dowling P, O'Driscoll L, O'Sullivan F et al. Proteomic screening of glucose-responsive and glucose nonresponsive MIN-6 b cells reveals differential expression of proteins involved in protein folding, secretion and oxidative stress. Proteomics 6(24), 6578-6587 (2006). Differential protein expressions relevant to glucose-stimulated response in b-cell line. (Pubitemid 46048396)
    • (2006) Proteomics , vol.6 , Issue.24 , pp. 6578-6587
    • Dowling, P.1    O'Driscoll, L.2    O'Sullivan, F.3    Dowd, A.4    Henry, M.5    Jeppesen, P.B.6    Meleady, P.7    Clynes, M.8
  • 20
    • 17844369439 scopus 로고    scopus 로고
    • Integrating global proteomic and genomic expression profiles generated from islet α cells: Opportunities and challenges to deriving reliable biological inferences
    • DOI 10.1074/mcp.R500011-MCP200
    • Maziarz M, Chung C, Drucker DJ, Emili A. Integrating global proteomic and genomic expression profiles generated from islet a cells: Opportunities and challenges to deriving reliable biological inferences. Mol. Cell. Proteomics 4(4), 458-474 (2005). (Pubitemid 40590565)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.4 , pp. 458-474
    • Maziarz, M.1    Chung, C.2    Drucker, D.J.3    Emili, A.4
  • 21
    • 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 et al. Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells: New insights into the pathways involved. Mol. Cell. Proteomics 6(12), 2180-2199 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.12 , pp. 2180-2199
    • D'Hertog, W.1    Overbergh, L.2    Lage, K.3
  • 23
    • 33749587601 scopus 로고    scopus 로고
    • Mitochondrial protein patterns correlating with impaired insulin secretion from INS-1E cells exposed to elevated glucose concentrations
    • DOI 10.1002/pmic.200600137
    • Nyblom HK, Thorn K, Ahmed M, Bergsten P. Mitochondrial protein patterns correlating with impaired insulin secretion from INS-1E cells exposed to elevated glucose concentrations. Proteomics 6(19), 5193-5198 (2006). (Pubitemid 44547159)
    • (2006) Proteomics , vol.6 , Issue.19 , pp. 5193-5198
    • Nyblom, H.K.1    Thorn, K.2    Ahmed, M.3    Bergsten, P.4
  • 24
    • 60849132750 scopus 로고    scopus 로고
    • Proteins associated with immunopurified granules from a model pancreatic islet b-cell system: Proteomic snapshot of an endocrine secretory granule
    • Proteome profiling of purified secretory granules from the INS-1E b-cell model.
    • Hickey AJ, Bradley JW, Skea GL et al. Proteins associated with immunopurified granules from a model pancreatic islet b-cell system: Proteomic snapshot of an endocrine secretory granule. J. Proteome Res. 8(1), 178-186 (2009). Proteome profiling of purified secretory granules from the INS-1E b-cell model.
    • (2009) J. Proteome Res. , vol.8 , Issue.1 , pp. 178-186
    • Hickey, A.J.1    Bradley, J.W.2    Skea, G.L.3
  • 25
    • 33845885784 scopus 로고    scopus 로고
    • Protein profiling of pancreatic islets
    • DOI 10.1586/14789450.3.6.665
    • Ortsater H, Bergsten P. Protein profiling of pancreatic islets. Expert Rev. Proteomics 3(6), 665-675 (2006). (Pubitemid 46021202)
    • (2006) Expert Review of Proteomics , vol.3 , Issue.6 , pp. 665-675
    • Ortsater, H.1    Bergsten, P.2
  • 27
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS. Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 18(11), 2071-2077 (1997). (Pubitemid 27501267)
    • (1997) Electrophoresis , vol.18 , Issue.11 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 28
    • 77952711951 scopus 로고    scopus 로고
    • Proteomics and islet research
    • Ahmed M. Proteomics and islet research. Adv. Exp. Med. Biol. 654, 363-390 (2010).
    • (2010) Adv. Exp. Med. Biol. , vol.654 , pp. 363-390
    • Ahmed, M.1
  • 29
    • 57749171580 scopus 로고    scopus 로고
    • Proteomics in diabetes research
    • Sundsten T, Ortsater H. Proteomics in diabetes research. Mol. Cell Endocrinol. 297(1-2), 93-103 (2009).
    • (2009) Mol. Cell Endocrinol. , vol.297 , Issue.1-2 , pp. 93-103
    • Sundsten, T.1    Ortsater, H.2
  • 30
    • 41149165737 scopus 로고    scopus 로고
    • Type 2 diabetes: Gaining insight into the disease process using proteomics
    • DOI 10.1002/prca.200780093
    • Maris M, Overbergh L, Mathieu C. Type 2 diabetes: Gaining insight into the disease process using proteomics. Proteomics Clin. Appl. 2(3), 312-326 (2008). (Pubitemid 351425362)
    • (2008) Proteomics - Clinical Applications , vol.2 , Issue.3 , pp. 312-326
    • Maris, M.1    Overbergh, L.2    Mathieu, C.3
  • 31
  • 33
    • 46049087000 scopus 로고    scopus 로고
    • Proteomic and transcriptomic analysis for streptozotocin-induced diabetic rat pancreas in response to fungal polysaccharide treatments
    • Kim SW, Hwang HJ, Baek YM, Lee SH, Hwang HS, Yun JW. Proteomic and transcriptomic analysis for streptozotocin-induced diabetic rat pancreas in response to fungal polysaccharide treatments. Proteomics 8(11), 2344-2361 (2008).
    • (2008) Proteomics , vol.8 , Issue.11 , pp. 2344-2361
    • Kim, S.W.1    Hwang, H.J.2    Baek, Y.M.3    Lee, S.H.4    Hwang, H.S.5    Yun, J.W.6
  • 35
    • 38549143790 scopus 로고    scopus 로고
    • Proteomic analysis of mouse islets after multiple low-dose streptozotocin injection
    • Proteomic study of pancreatic islets revealed proteins relevant to b-cell failure.
    • Xie X, Li S, Liu S, Lu Y, Shen P, Ji J. Proteomic analysis of mouse islets after multiple low-dose streptozotocin injection. Biochim. Biophys. Acta. 1784(2), 276-284 (2008). Proteomic study of pancreatic islets revealed proteins relevant to b-cell failure.
    • (2008) Biochim. Biophys. Acta. , vol.1784 , Issue.2 , pp. 276-284
    • Xie, X.1    Li, S.2    Liu, S.3    Lu, Y.4    Shen, P.5    Ji, J.6
  • 37
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold R, Mann M. Mass spectrometry-based proteomics. Nature 422(6928), 198-207 (2003). (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 38
    • 33750728385 scopus 로고    scopus 로고
    • Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications
    • DOI 10.1074/mcp.M600162-MCP200
    • Qian WJ, Jacobs JM, Liu T, Camp DG 2nd, Smith RD. Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications. Mol. Cell. Proteomics 5(10), 1727-1744 (2006). (Pubitemid 44696109)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.10 , pp. 1727-1744
    • Qian, W.-J.1    Jacobs, J.M.2    Liu, T.3    Camp II, D.G.4    Smith, R.D.5
  • 39
    • 78650087650 scopus 로고    scopus 로고
    • Protein markers for insulin-producing b cells with higher glucose sensitivity
    • Martens GA, Jiang L, Verhaeghen K et al. Protein markers for insulin-producing b cells with higher glucose sensitivity. PLoS One 5(12), e14214 (2010).
    • (2010) PLoS One , vol.5 , Issue.12
    • Martens, G.A.1    Jiang, L.2    Verhaeghen, K.3
  • 40
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • DOI 10.1021/ac0498563
    • Liu H, Sadygov RG, Yates JR 3rd. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76(14), 4193-4201 (2004). (Pubitemid 38943698)
    • (2004) Analytical Chemistry , vol.76 , Issue.14 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 41
    • 78149381050 scopus 로고    scopus 로고
    • Improved LC-MS/MS spectral counting statistics by recovering low-scoring spectra matched to confidently identified peptide sequences
    • Zhou JY, Schepmoes AA, Zhang X et al. Improved LC-MS/MS spectral counting statistics by recovering low-scoring spectra matched to confidently identified peptide sequences. J. Proteome Res. 9(11), 5698-5704 (2010).
    • (2010) J. Proteome Res. , vol.9 , Issue.11 , pp. 5698-5704
    • Zhou, J.Y.1    Schepmoes, A.A.2    Zhang, X.3
  • 43
  • 46
    • 34548136221 scopus 로고    scopus 로고
    • VIPER: An advanced software package to support high-throughput LC-MS peptide identification
    • DOI 10.1093/bioinformatics/btm281
    • Monroe ME, Tolic N, Jaitly N, Shaw JL, Adkins JN, Smith RD. VIPER: An advanced software package to support high-throughput LC-MS peptide identification. Bioinformatics 3(15), 2021-2023 (2007). (Pubitemid 47299846)
    • (2007) Bioinformatics , vol.23 , Issue.15 , pp. 2021-2023
    • Monroe, M.E.1    Tolic, N.2    Jaitly, N.3    Shaw, J.L.4    Adkins, J.N.5    Smith, R.D.6
  • 47
    • 26844492976 scopus 로고    scopus 로고
    • A software suite for the generation and comparison of peptide arrays from sets of data collected by liquid chromatography-mass spectrometry
    • DOI 10.1074/mcp.M500141-MCP200
    • Li XJ, Yi EC, Kemp CJ, Zhang H, Aebersold R. A software suite for the generation and comparison of peptide arrays from sets of data collected by liquid chromatography-mass spectrometry. Mol. Cell. Proteomics 4(9), 1328-1340 (2005). (Pubitemid 41448720)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1328-1340
    • Li, X.-J.1    Yi, E.C.2    Kemp, C.J.3    Zhang, H.4    Aebersold, R.5
  • 49
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 6(12), 1367-1137 (2008).
    • (2008) Nat. Biotechnol. , vol.6 , Issue.12 , pp. 1367-1137
    • Cox, J.1    Mann, M.2
  • 50
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong SE, Mann M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1(5), 252-262 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.5 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 51
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1(5), 376-386 (2002).
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3
  • 53
    • 66749156510 scopus 로고    scopus 로고
    • A simple procedure for effective quenching of trypsin activity and prevention of 18O-labeling back-exchange
    • Petritis BO, Qian WJ, Camp DG 2nd, Smith RD. A simple procedure for effective quenching of trypsin activity and prevention of 18O-labeling back-exchange. J. Proteome Res. 8(5), 2157-2163 (2009).
    • (2009) J. Proteome Res. , vol.8 , Issue.5 , pp. 2157-2163
    • Petritis, B.O.1    Qian, W.J.2    Camp II, D.G.3    Smith, R.D.4
  • 54
    • 60849084471 scopus 로고    scopus 로고
    • Large-scale multiplexed quantitative discovery proteomics enabled by the use of an (18)O-labeled 'universal' reference sample
    • Qian WJ, Liu T, Petyuk VA et al. Large-scale multiplexed quantitative discovery proteomics enabled by the use of an (18)O-labeled 'universal' reference sample. J. Proteome Res. 8(1), 2290-2299 (2009).
    • (2009) J. Proteome Res. , vol.8 , Issue.1 , pp. 2290-2299
    • Qian, W.J.1    Liu, T.2    Petyuk, V.A.3
  • 55
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross PL, Huang YN, Marchese JN et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 3(12), 1154-1169 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.12 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3
  • 57
    • 65249105457 scopus 로고    scopus 로고
    • Detection of differential proteomes of human b-cells during islet-like differentiation using iTRAQ labeling
    • Jin J, Park J, Kim K et al. Detection of differential proteomes of human b-cells during islet-like differentiation using iTRAQ labeling. J. Proteome Res. 8(3), 1393-1403 (2009).
    • (2009) J. Proteome Res. , vol.8 , Issue.3 , pp. 1393-1403
    • Jin, J.1    Park, J.2    Kim, K.3
  • 58
    • 77955159809 scopus 로고    scopus 로고
    • Peptide labeling with isobaric tags yields higher identification rates using iTRAQ 4-plex compared with TMT 6-plex and iTRAQ 8-plex on LTQ Orbitrap
    • Pichler P, Kocher T, Holzmann J et al. Peptide labeling with isobaric tags yields higher identification rates using iTRAQ 4-plex compared with TMT 6-plex and iTRAQ 8-plex on LTQ Orbitrap. Anal. Chem. 8(15), 6549-6558 (2010).
    • (2010) Anal. Chem. , vol.8 , Issue.15 , pp. 6549-6558
    • Pichler, P.1    Kocher, T.2    Holzmann, J.3
  • 59
    • 16844382825 scopus 로고    scopus 로고
    • Glucose-induced changes of multiple mouse islet proteins analysed by two-dimensional gel electrophoresis and mass spectrometry
    • DOI 10.1007/s00125-004-1661-7
    • Ahmed M, Bergsten P. Glucose-induced changes of multiple mouse islet proteins analysed by 2D gel electrophoresis and mass spectrometry. Diabetologia 48(3), 477-485 (2005). (Pubitemid 40487295)
    • (2005) Diabetologia , vol.48 , Issue.3 , pp. 477-485
    • Ahmed, M.1    Bergsten, P.2
  • 60
    • 20844435281 scopus 로고    scopus 로고
    • Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry
    • DOI 10.1021/pr050024a
    • Ahmed M, Forsberg J, Bergsten P. Protein profiling of human pancreatic islets by 2D gel electrophoresis and mass spectrometry. J. Proteome Res. 4(3), 931-940 (2005). (Pubitemid 40863282)
    • (2005) Journal of Proteome Research , vol.4 , Issue.3 , pp. 931-940
    • Ahmed, M.1    Forsberg, J.2    Bergsten, P.3
  • 62
    • 63449085198 scopus 로고    scopus 로고
    • Detailed transcriptome atlas of the pancreatic b cell
    • Kutlu B, Burdick D, Baxter D et al. Detailed transcriptome atlas of the pancreatic b cell. BMC Med. Genomics 3 (2009).
    • (2009) BMC Med. Genomics , vol.3
    • Kutlu, B.1    Burdick, D.2    Baxter, D.3
  • 63
    • 0026504568 scopus 로고
    • Identification of glucose response proteins in two biological models of b-cell adaptation to chronic high glucose exposure
    • Collins H, Najafi H, Buettger C, Rombeau J, Settle RG, Matschinsky FM. Identification of glucose response proteins in two biological models of b-cell adaptation to chronic high glucose exposure. J. Biol. Chem. 67(2), 1357-1366 (1992).
    • (1992) J. Biol. Chem. , vol.67 , Issue.2 , pp. 1357-1366
    • Collins, H.1    Najafi, H.2    Buettger, C.3    Rombeau, J.4    Settle, R.G.5    Matschinsky, F.M.6
  • 64
    • 0024999376 scopus 로고
    • High-resolution 2D polyacrylamide gel electrophoresis reveals a glucose-response protein of 65 kDa in pancreatic islet cells
    • Collins HW, Buettger C, Matschinsky F. High-resolution 2D polyacrylamide gel electrophoresis reveals a glucose-response protein of 65 kDa in pancreatic islet cells. Proc. Natl Acad. Sci. USA 87(14), 5494-5498 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , Issue.14 , pp. 5494-5498
    • Collins, H.W.1    Buettger, C.2    Matschinsky, F.3
  • 66
    • 0028971041 scopus 로고
    • Pharmacological characterization of SR 48692 sensitive neurotensin receptor in human pancreatic cancer cells, MIA PaCa-2
    • Yamada M, Ohata H, Momose K, Richelson E. Pharmacological characterization of SR 48692 sensitive neurotensin receptor in human pancreatic cancer cells, MIA PaCa-2. Res. Commun. Mol. Pathol. Pharmacol. 90(1), 37-47 (1995).
    • (1995) Res. Commun. Mol. Pathol. Pharmacol. , vol.90 , Issue.1 , pp. 37-47
    • Yamada, M.1    Ohata, H.2    Momose, K.3    Richelson, E.4
  • 67
    • 0035668779 scopus 로고    scopus 로고
    • A choice of death - The signal-transduction of immune-mediated beta-cell apoptosis
    • DOI 10.1007/s001250100021
    • Eizirik DL, Mandrup-Poulsen T. A choice of death - the signal-transduction of immune-mediated b-cell apoptosis. Diabetologia 44(12), 2115-2133 (2001). (Pubitemid 34015464)
    • (2001) Diabetologia , vol.44 , Issue.12 , pp. 2115-2133
    • Eizirik, D.L.1    Mandrup-Poulsen, T.2
  • 69
    • 8344271936 scopus 로고    scopus 로고
    • Cell lines derived from pancreatic islets
    • DOI 10.1016/j.mce.2004.04.017, PII S0303720704002217, Endocrine Cell Lines
    • Hohmeier HE, Newgard CB. Cell lines derived from pancreatic islets. Mol. Cell Endocrinol. 228(1-2), 121-128 (2004). (Pubitemid 39482523)
    • (2004) Molecular and Cellular Endocrinology , vol.228 , Issue.1-2 , pp. 121-128
    • Hohmeier, H.E.1    Newgard, C.B.2
  • 70
    • 0028954346 scopus 로고
    • 2D gel electrophoresis of rat islet proteins. Interleukin 1 b-induced changes in protein expression are reduced by l-arginine depletion and nicotinamide
    • Andersen HU, Larsen PM, Fey SJ, Karlsen AE, Mandrup-Poulsen T, Nerup J. 2D gel electrophoresis of rat islet proteins. Interleukin 1 b-induced changes in protein expression are reduced by l-arginine depletion and nicotinamide. Diabetes 44(4), 400-407 (1995).
    • (1995) Diabetes , vol.44 , Issue.4 , pp. 400-407
    • Andersen, H.U.1    Larsen, P.M.2    Fey, S.J.3    Karlsen, A.E.4    Mandrup-Poulsen, T.5    Nerup, J.6
  • 72
    • 33646040686 scopus 로고    scopus 로고
    • Immune-mediated b-cell destruction in vitro and in vivo-A pivotal role for galectin-3
    • Karlsen AE, Storling ZM, Sparre T et al. Immune-mediated b-cell destruction in vitro and in vivo-A pivotal role for galectin-3. Biochem. Biophys. Res. Commun. 344(1), 406-415 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , Issue.1 , pp. 406-415
    • Karlsen, A.E.1    Storling, Z.M.2    Sparre, T.3
  • 73
    • 77957372670 scopus 로고    scopus 로고
    • Galectin-3 is a candidate biomarker for amyotrophic lateral sclerosis: Discovery by a proteomics approach
    • Zhou JY, Afjehi-Sadat L, Asress S et al. Galectin-3 is a candidate biomarker for amyotrophic lateral sclerosis: Discovery by a proteomics approach. J. Proteome Res. 9(10), 5133-5141 (2010).
    • (2010) J. Proteome Res. , vol.9 , Issue.10 , pp. 5133-5141
    • Zhou, J.Y.1    Afjehi-Sadat, L.2    Asress, S.3
  • 75
    • 26844447225 scopus 로고    scopus 로고
    • Differentially expressed proteins in the pancreas of diet-induced diabetic mice
    • DOI 10.1074/mcp.M500016-MCP200
    • Qiu L, List EO, Kopchick JJ. Differentially expressed proteins in the pancreas of diet-induced diabetic mice. Mol. Cell. Proteomics 4(9), 1311-1318 (2005). (Pubitemid 41448718)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1311-1318
    • Qiu, L.1    List, E.O.2    Kopchick, J.J.3
  • 76
    • 77449154126 scopus 로고    scopus 로고
    • Molecular and metabolic evidence for mitochondrial defects associated with b-cell dysfunction in a mouse model of Type 2 diabetes
    • Lu H, Koshkin V, Allister EM, Gyulkhandanyan AV, Wheeler MB. Molecular and metabolic evidence for mitochondrial defects associated with b-cell dysfunction in a mouse model of Type 2 diabetes. Diabetes 59(2), 448-459 (2010).
    • (2010) Diabetes , vol.59 , Issue.2 , pp. 448-459
    • Lu, H.1    Koshkin, V.2    Allister, E.M.3    Gyulkhandanyan, A.V.4    Wheeler, M.B.5
  • 77
    • 0036652155 scopus 로고    scopus 로고
    • Effect of rosiglitazone on the differential expression of diabetes-associated proteins in pancreatic islets of C57Bl/6 lep/lep mice
    • Sanchez JC, Converset V, Nolan A et al. Effect of rosiglitazone on the differential expression of diabetes-associated proteins in pancreatic islets of C57Bl/6 lep/lep mice. Mol. Cell. Proteomics 1(7), 509-516 (2002).
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.7 , pp. 509-516
    • Sanchez, J.C.1    Converset, V.2    Nolan, A.3
  • 78
    • 71549166982 scopus 로고    scopus 로고
    • Apoptotic, regenerative and immune-related signaling in human islets from Type 2 diabetes individuals
    • Proteomic change in human islets from Type 2 diabetes patients.
    • Nyblom HK, Bugliani M, Fung E et al. Apoptotic, regenerative and immune-related signaling in human islets from Type 2 diabetes individuals. J. Proteome Res. 8(12), 5650-5656 (2009). Proteomic change in human islets from Type 2 diabetes patients.
    • (2009) J. Proteome Res. , vol.8 , Issue.12 , pp. 5650-5656
    • Nyblom, H.K.1    Bugliani, M.2    Fung, E.3
  • 79
    • 79957566487 scopus 로고    scopus 로고
    • Pancreatic islet transplantation
    • Noguchi H. Pancreatic islet transplantation. World J Gastrointest. Surg. 1(1), 16-20 (2009).
    • (2009) World J Gastrointest. Surg. , vol.1 , Issue.1 , pp. 16-20
    • Noguchi, H.1
  • 80
    • 64049098927 scopus 로고    scopus 로고
    • Discovery of a human peptide sequence signaling islet neogenesis
    • Levetan CS, Upham LV, Deng S et al. Discovery of a human peptide sequence signaling islet neogenesis. Endocr. Pract. 14(9), 1075-1083 (2008).
    • (2008) Endocr. Pract. , vol.14 , Issue.9 , pp. 1075-1083
    • Levetan, C.S.1    Upham, L.V.2    Deng, S.3
  • 81
    • 36249011487 scopus 로고    scopus 로고
    • Effects of glitazones in the treatment of diabetes and/or hyperlipidaemia: Glycaemic control and plasma lipid levels
    • DOI 10.1111/j.1472-8206.2007.00532.x
    • Verges B. Effects of glitazones in the treatment of diabetes and/or hyperlipidaemia: Glycaemic control and plasma lipid levels. Fundam. Clin. Pharmacol. 21(Suppl. 2), 15-18 (2007). (Pubitemid 350132289)
    • (2007) Fundamental and Clinical Pharmacology , vol.21 , Issue.SUPPL. 2 , pp. 15-18
    • Verges, B.1
  • 82
    • 66149089175 scopus 로고    scopus 로고
    • Combined pulsed-Q dissociation and electron transfer dissociation for identification and quantification of iTRAQ-labeled phosphopeptides
    • Yang F, Wu S, Stenoien DL et al. Combined pulsed-Q dissociation and electron transfer dissociation for identification and quantification of iTRAQ-labeled phosphopeptides. Anal. Chem. 81(10), 4137-4143 (2009).
    • (2009) Anal. Chem. , vol.81 , Issue.10 , pp. 4137-4143
    • Yang, F.1    Wu, S.2    Stenoien, D.L.3
  • 83
    • 43449106831 scopus 로고    scopus 로고
    • Redox proteomics: Understanding oxidative stress in the progression of age-related neurodegenerative disorders
    • DOI 10.1586/14789450.5.2.157
    • Butterfield DA, Sultana R. Redox proteomics: Understanding oxidative stress in the progression of age-related neurodegenerative disorders. Expert Rev. Proteomics 5(2), 157-160 (2008). (Pubitemid 351670922)
    • (2008) Expert Review of Proteomics , vol.5 , Issue.2 , pp. 157-160
    • Butterfield, D.A.1    Sultana, R.2
  • 85
    • 61349200777 scopus 로고    scopus 로고
    • Using mass spectrometry to identify ubiquitin and ubiquitin-like protein conjugation sites
    • Jeram SM, Srikumar T, Pedrioli PG, Raught B. Using mass spectrometry to identify ubiquitin and ubiquitin-like protein conjugation sites. Proteomics 9(4), 922-934 (2009).
    • (2009) Proteomics , vol.9 , Issue.4 , pp. 922-934
    • Jeram, S.M.1    Srikumar, T.2    Pedrioli, P.G.3    Raught, B.4
  • 86
    • 34848892777 scopus 로고    scopus 로고
    • Emerging role of SUMO in pancreatic β-cells
    • DOI 10.1055/s-2007-985372
    • Ehninger A, Mziaut H, Solimena M. Emerging role of SUMO in pancreatic b-cells. Horm. Metab. Res. 39(9), 658-664 (2007). (Pubitemid 47492649)
    • (2007) Hormone and Metabolic Research , vol.39 , Issue.9 , pp. 658-664
    • Ehninger, A.1    Mziaut, H.2    Solimena, M.3
  • 87
    • 79953184687 scopus 로고    scopus 로고
    • Enhanced sensitivity for selected reaction monitoring-mass spectrometry-based targeted proteomics using a dual-stage electrodynamic ion funnel interface
    • Hossain M, Kaleta DT, Robinson EW et al. Enhanced sensitivity for selected reaction monitoring-mass spectrometry-based targeted proteomics using a dual-stage electrodynamic ion funnel interface. Mol. Cell. Proteomics 10(2), M000062-MCP201 (2010).
    • (2010) Mol. Cell. Proteomics , vol.10 , Issue.2
    • Hossain, M.1    Kaleta, D.T.2    Robinson, E.W.3


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