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Volumn 44, Issue 5, 2009, Pages 735-741

The proteolytic activity of insulin-degrading enzyme: A mass spectrometry study

Author keywords

ATP; IDE; Insulin; MALDI; Mass spectrometry; Metal; Oligomer

Indexed keywords

AMYLOIDOGENIC PEPTIDES; ATP; CLEAVAGE PATTERNS; CLEAVAGE SITES; CONCENTRATION RATIO; DESORPTION IONIZATION; ENVIRONMENTAL FACTORS; IDE; INSULIN-DEGRADING ENZYMES; MALDI; PROTEOLYTIC ACTIVITIES; REACTION TIME; TRIPHOSPHATE;

EID: 66249126847     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1550     Document Type: Article
Times cited : (31)

References (29)
  • 2
    • 0035399887 scopus 로고    scopus 로고
    • Insulin-degrading enzyme: Embarking on amyloid destruction
    • I. V. Kurochkin. Insulin-degrading enzyme: embarking on amyloid destruction. Trends in Biochemical Sciences 2001, 26, 421.
    • (2001) Trends in Biochemical Sciences , vol.26 , pp. 421
    • Kurochkin, I.V.1
  • 4
    • 0037219221 scopus 로고    scopus 로고
    • D. G. Cook, J. B. Leverenz, P. J. McMillan, J. J. Kulstad, S. Ericksen, R. A. Roth, G. D. Schellenberg, L. W. Jin, K. S. Kovacina, S. Craft. Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele. American Journal of Pathology 2003, 162, 313.
    • D. G. Cook, J. B. Leverenz, P. J. McMillan, J. J. Kulstad, S. Ericksen, R. A. Roth, G. D. Schellenberg, L. W. Jin, K. S. Kovacina, S. Craft. Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele. American Journal of Pathology 2003, 162, 313.
  • 6
    • 33750302461 scopus 로고    scopus 로고
    • Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
    • Y. Shen,A. Joachimiak, M. R. Rosner, W.-J. Tang. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006, 443, 870.
    • (2006) Nature , vol.443 , pp. 870
    • Shen, Y.1    Joachimiak, A.2    Rosner, M.R.3    Tang, W.-J.4
  • 9
    • 0348010388 scopus 로고    scopus 로고
    • Substrate activation of insulin degrading enzyme (insulysin), A potential target for drug development
    • E. S. Song, M. A. Juliano, L. Juliano, L. B. Hersh. Substrate activation of insulin degrading enzyme (insulysin), A potential target for drug development. Journal of Biological Chemistry 2003, 278, 49789.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 49789
    • Song, E.S.1    Juliano, M.A.2    Juliano, L.3    Hersh, L.B.4
  • 10
    • 39749194421 scopus 로고    scopus 로고
    • Immunocapture-based fluoromet- ric assay for the measurement of insulin-degrading enzyme activity in brain tissue homogenates
    • J. S. Miners, P. G. Kehoe, S. Love. Immunocapture-based fluoromet- ric assay for the measurement of insulin-degrading enzyme activity in brain tissue homogenates. Journal of Neuroscience Methods 2008, 169, 177.
    • (2008) Journal of Neuroscience Methods , vol.169 , pp. 177
    • Miners, J.S.1    Kehoe, P.G.2    Love, S.3
  • 12
    • 0025160114 scopus 로고
    • Identification of residues in the insulin molecule important for binding to insulin-degrading enzyme
    • J. A. Affholter, M. A. Cascieri, M. L. Bayne, J. Brange, M. Casaretto, R. A. Roth. Identification of residues in the insulin molecule important for binding to insulin-degrading enzyme. Biochemistry 1990, 29, 7727.
    • (1990) Biochemistry , vol.29 , pp. 7727
    • Affholter, J.A.1    Cascieri, M.A.2    Bayne, M.L.3    Brange, J.4    Casaretto, M.5    Roth, R.A.6
  • 13
    • 0023851990 scopus 로고
    • Effect of iodination site on binding of radiolabeled ligand by insulin antibodies and insulin autoantibodies
    • J. L. Diaz, T. J. Wilkin. Effect of iodination site on binding of radiolabeled ligand by insulin antibodies and insulin autoantibodies. ClinicalChemistry1988, 34, 356.
    • (1988) ClinicalChemistry , vol.34 , pp. 356
    • Diaz, J.L.1    Wilkin, T.J.2
  • 14
    • 52449135535 scopus 로고    scopus 로고
    • How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin
    • G. Grasso, E. Rizzarelli, G. Spoto. How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin. Biochimica et Biophysica Acta 2008, 1784, 1122.
    • (2008) Biochimica et Biophysica Acta , vol.1784 , pp. 1122
    • Grasso, G.1    Rizzarelli, E.2    Spoto, G.3
  • 15
    • 38149007269 scopus 로고    scopus 로고
    • AP-MALDI/MS complete characterization of insulin fragments produced by the interaction of IDE with bovine insulin
    • G.Grasso, E. Rizzarelli, G.Spoto. AP-MALDI/MS complete characterization of insulin fragments produced by the interaction of IDE with bovine insulin. Journal of Mass Spectrometry 2007, 42, 1590.
    • (2007) Journal of Mass Spectrometry , vol.42 , pp. 1590
    • Grasso, G.1    Rizzarelli, E.2    Spoto, G.3
  • 18
    • 0024062933 scopus 로고
    • Insulin degradation: Mechanisms, products, and significance
    • W. C. Duckworth. Insulin degradation: mechanisms, products, and significance. Endocrine Reviews 1988, 9, 319.
    • (1988) Endocrine Reviews , vol.9 , pp. 319
    • Duckworth, W.C.1
  • 19
    • 2342630585 scopus 로고    scopus 로고
    • Atmospheric pressure MALDI with pulsed dynamic focusing for high-efficiency transmission of ions into a mass spectrometer
    • P. V. Tan, V. V. Laiko, V. M. Doroshenko. Atmospheric pressure MALDI with pulsed dynamic focusing for high-efficiency transmission of ions into a mass spectrometer. Analytical Chemistry 2004, 76, 2462.
    • (2004) Analytical Chemistry , vol.76 , pp. 2462
    • Tan, P.V.1    Laiko, V.V.2    Doroshenko, V.M.3
  • 22
    • 0029843563 scopus 로고    scopus 로고
    • Identification of γ - endorphin-generating enzyme as insulin-degrading enzyme
    • A. Safavi, B.C. Miller, L. Cottam, L. B. Hersh. Identification of γ - endorphin-generating enzyme as insulin-degrading enzyme. Biochemistry1996, 35, 14318.
    • (1996) Biochemistry , vol.35 , pp. 14318
    • Safavi, A.1    Miller, B.C.2    Cottam, L.3    Hersh, L.B.4
  • 25
    • 0035884102 scopus 로고    scopus 로고
    • Evaluation of the efficiency of in-gel digestion of proteins by peptide isotopic labeling and MALDI mass spectrometry
    • A. Shevchenko. Evaluation of the efficiency of in-gel digestion of proteins by peptide isotopic labeling and MALDI mass spectrometry. Analytical Biochemistry 2001, 296, 279.
    • (2001) Analytical Biochemistry , vol.296 , pp. 279
    • Shevchenko, A.1
  • 26
    • 39749188801 scopus 로고    scopus 로고
    • Twenty years of metallo-neurobiology: Where to now?
    • A. I. Bush, C. C. Curtain. Twenty years of metallo-neurobiology: where to now? European Biophysics Journal 2008, 37, 241.
    • (2008) European Biophysics Journal , vol.37 , pp. 241
    • Bush, A.I.1    Curtain, C.C.2
  • 27
    • 0031763979 scopus 로고    scopus 로고
    • Regulation of multicatalytic enzyme activity by insulin and the insulin-degrading enzyme
    • F. G. Hamel, R. Bennett, W. C. Duckworth. Regulation of multicatalytic enzyme activity by insulin and the insulin-degrading enzyme. Endocrinology 1998, 139, 4061.
    • (1998) Endocrinology , vol.139 , pp. 4061
    • Hamel, F.G.1    Bennett, R.2    Duckworth, W.C.3
  • 28
    • 0023690510 scopus 로고
    • Insulin-metal ion interactions: The binding of divalent cations to insulin hexamers and tetramers and the assembly of insulin hexamers
    • F. D. Coffman, M.F.Dunn. Insulin-metal ion interactions: the binding of divalent cations to insulin hexamers and tetramers and the assembly of insulin hexamers. Biochemistry 1988, 27, 6179.
    • (1988) Biochemistry , vol.27 , pp. 6179
    • Coffman, F.D.1    Dunn, M.F.2
  • 29


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.