메뉴 건너뛰기




Volumn 466, Issue 2, 2015, Pages 192-195

Insulin-degrading enzyme is activated by the C-terminus of α-synuclein

Author keywords

Amyloid; Insulin degrading enzyme; Parkinson's disease; Proteolysis; Synuclein

Indexed keywords

ALPHA SYNUCLEIN; AMYLIN; AMYLOID; INSULINASE; RECOMBINANT ENZYME;

EID: 84942295055     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.09.002     Document Type: Article
Times cited : (24)

References (25)
  • 1
    • 84858632761 scopus 로고    scopus 로고
    • Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective
    • J.R. Brender, S. Salamekh, and A. Ramamoorthy Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective Acc. Chem. Res. 45 3 2012 454 462
    • (2012) Acc. Chem. Res. , vol.45 , Issue.3 , pp. 454-462
    • Brender, J.R.1    Salamekh, S.2    Ramamoorthy, A.3
  • 2
    • 80155209561 scopus 로고    scopus 로고
    • Misfolded proteins in Alzheimer's disease and type II diabetes
    • A.S. DeToma, and et al. Misfolded proteins in Alzheimer's disease and type II diabetes Chem. Soc. Rev. 41 2 2012 608 621
    • (2012) Chem. Soc. Rev. , vol.41 , Issue.2 , pp. 608-621
    • DeToma, A.S.1
  • 3
    • 84907220929 scopus 로고    scopus 로고
    • Differences between amyloid-beta aggregation in solution and on the membrane: Insights into elucidation of the mechanistic details of Alzheimer's disease
    • S.A. Kotler, and et al. Differences between amyloid-beta aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease Chem. Soc. Rev. 43 19 2014 6692 6700
    • (2014) Chem. Soc. Rev. , vol.43 , Issue.19 , pp. 6692-6700
    • Kotler, S.A.1
  • 4
    • 84902105470 scopus 로고    scopus 로고
    • Search of Aggregation Pathways of IAPP and other amyloidogenic proteins: Finding answers through NMR spectroscopy
    • H.R. Patel, and et al. Search of Aggregation Pathways of IAPP and other amyloidogenic proteins: finding answers through NMR spectroscopy J. Phys. Chem. Lett. 5 11 2014 1864 1870
    • (2014) J. Phys. Chem. Lett. , vol.5 , Issue.11 , pp. 1864-1870
    • Patel, H.R.1
  • 5
    • 0032608987 scopus 로고    scopus 로고
    • Pathobiology of the Lewy body
    • J.E. Galvin, and et al. Pathobiology of the Lewy body Adv. Neurol. 80 1999 313 324
    • (1999) Adv. Neurol. , vol.80 , pp. 313-324
    • Galvin, J.E.1
  • 6
    • 79952742454 scopus 로고    scopus 로고
    • In vivo demonstration that alpha-synuclein oligomers are toxic
    • U. S. A.
    • B. Winner, et al., In vivo demonstration that alpha-synuclein oligomers are toxic. Proc. Natl. Acad. Sci. U. S. A. 108 (10) 4194-4199.
    • Proc. Natl. Acad. Sci. , vol.108 , Issue.10 , pp. 4194-4199
    • Winner, B.1
  • 7
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • D. Eliezer, and et al. Conformational properties of alpha-synuclein in its free and lipid-associated states J. Mol. Biol. 307 4 2001 1061 1073
    • (2001) J. Mol. Biol. , vol.307 , Issue.4 , pp. 1061-1073
    • Eliezer, D.1
  • 8
    • 0021111565 scopus 로고
    • A high molecular weight metalloendoprotease from the cytosol of mammalian cells
    • R.J. Kirschner, and A.L. Goldberg A high molecular weight metalloendoprotease from the cytosol of mammalian cells J. Biol. Chem. 258 2 1983 967 976
    • (1983) J. Biol. Chem. , vol.258 , Issue.2 , pp. 967-976
    • Kirschner, R.J.1    Goldberg, A.L.2
  • 9
    • 0031690490 scopus 로고    scopus 로고
    • Insulin degradation: Progress and potential
    • W.C. Duckworth, R.G. Bennett, and F.G. Hamel Insulin degradation: progress and potential Endocr. Rev. 19 5 1998 608 624
    • (1998) Endocr. Rev. , vol.19 , Issue.5 , pp. 608-624
    • Duckworth, W.C.1    Bennett, R.G.2    Hamel, F.G.3
  • 10
    • 34249888775 scopus 로고    scopus 로고
    • Genome-wide association analysis identifies loci for type 2 diabetes and triglyceride levels
    • Diabetes Genetics Initiative of Broad Institute of Harvard
    • Diabetes Genetics Initiative of Broad Institute of Harvard and MIT, and et al. Genome-wide association analysis identifies loci for type 2 diabetes and triglyceride levels Science 316 5829 2007 1331 1336
    • (2007) Science , vol.316 , Issue.5829 , pp. 1331-1336
    • Mit1
  • 11
    • 34249885875 scopus 로고    scopus 로고
    • A genome-wide association study of type 2 diabetes in Finns detects multiple susceptibility variants
    • L.J. Scott, and et al. A genome-wide association study of type 2 diabetes in Finns detects multiple susceptibility variants Science 316 5829 2007 1341 1345
    • (2007) Science , vol.316 , Issue.5829 , pp. 1341-1345
    • Scott, L.J.1
  • 12
    • 84878253079 scopus 로고    scopus 로고
    • The type 2 diabetes-associated gene ide is required for insulin secretion and suppression of alpha-synuclein levels in beta-cells
    • P. Steneberg, and et al. The type 2 diabetes-associated gene ide is required for insulin secretion and suppression of alpha-synuclein levels in beta-cells Diabetes 62 6 2013 2004 2014
    • (2013) Diabetes , vol.62 , Issue.6 , pp. 2004-2014
    • Steneberg, P.1
  • 13
    • 0037390039 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo
    • W. Farris, and et al. Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo Proc. Natl. Acad. Sci. U. S. A. 100 7 2003 4162 4167
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.7 , pp. 4162-4167
    • Farris, W.1
  • 14
    • 33750302461 scopus 로고    scopus 로고
    • Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
    • Y. Shen, and et al. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism Nature 443 7113 2006 870 874
    • (2006) Nature , vol.443 , Issue.7113 , pp. 870-874
    • Shen, Y.1
  • 15
    • 47749114576 scopus 로고    scopus 로고
    • The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid beta peptide: Implications for Alzheimer disease pathogenesis
    • R.E. Llovera, and et al. The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid beta peptide: implications for Alzheimer disease pathogenesis J. Biol. Chem. 283 25 2008 17039 17048
    • (2008) J. Biol. Chem. , vol.283 , Issue.25 , pp. 17039-17048
    • Llovera, R.E.1
  • 16
    • 62449140977 scopus 로고    scopus 로고
    • The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: A biological perspective
    • M.B. de Tullio, L. Morelli, and E.M. Castano The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: a biological perspective Prion 2 2 2008 51 56
    • (2008) Prion , vol.2 , Issue.2 , pp. 51-56
    • De Tullio, M.B.1    Morelli, L.2    Castano, E.M.3
  • 17
    • 84938523810 scopus 로고    scopus 로고
    • Insulin-degrading enzyme prevents alpha-synuclein fibril formation in a nonproteolytical manner
    • S.K. Sharma, and et al. Insulin-degrading enzyme prevents alpha-synuclein fibril formation in a nonproteolytical manner Sci. Rep. 5 2015 12531
    • (2015) Sci. Rep. , vol.5 , pp. 12531
    • Sharma, S.K.1
  • 18
    • 84857438892 scopus 로고    scopus 로고
    • Mechanisms of protein oligomerization: Inhibitor of functional amyloids templates alpha-synuclein fibrillation
    • I. Horvath, and et al. Mechanisms of protein oligomerization: inhibitor of functional amyloids templates alpha-synuclein fibrillation J. Am. Chem. Soc. 134 7 2012 3439 3444
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.7 , pp. 3439-3444
    • Horvath, I.1
  • 19
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • H. Naiki, and et al. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1 Anal. Biochem. 177 2 1989 244 249
    • (1989) Anal. Biochem. , vol.177 , Issue.2 , pp. 244-249
    • Naiki, H.1
  • 20
    • 34548505012 scopus 로고    scopus 로고
    • Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE
    • H. Im, and et al. Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE J. Biol. Chem. 282 35 2007 25453 25463
    • (2007) J. Biol. Chem. , vol.282 , Issue.35 , pp. 25453-25463
    • Im, H.1
  • 21
    • 73149099387 scopus 로고    scopus 로고
    • Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme
    • Q. Guo, and et al. Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme J. Mol. Biol. 395 2 2010 430 443
    • (2010) J. Mol. Biol. , vol.395 , Issue.2 , pp. 430-443
    • Guo, Q.1
  • 22
    • 57049166021 scopus 로고    scopus 로고
    • Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme
    • E. Malito, and et al. Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme Biochemistry 47 48 2008 12822 12834
    • (2008) Biochemistry , vol.47 , Issue.48 , pp. 12822-12834
    • Malito, E.1
  • 23
    • 84930659235 scopus 로고    scopus 로고
    • Direct correlation between ligand-induced α-synuclein oligomers and amyloid-like fibril growth
    • M. Nors Perdersen, and et al. Direct correlation between ligand-induced α-synuclein oligomers and amyloid-like fibril growth Sci. Rep. 5 2015 10422
    • (2015) Sci. Rep. , vol.5 , pp. 10422
    • Nors Perdersen, M.1
  • 24
    • 79953206595 scopus 로고    scopus 로고
    • The neurotransmitter serotonin interrupts alpha-synuclein amyloid maturation
    • S.F. Falsone, and et al. The neurotransmitter serotonin interrupts alpha-synuclein amyloid maturation Biochim. Biophys. Acta 1814 5 2011 553 561
    • (2011) Biochim. Biophys. Acta , vol.1814 , Issue.5 , pp. 553-561
    • Falsone, S.F.1
  • 25
    • 84876102518 scopus 로고    scopus 로고
    • Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic abeta peptide aggregates
    • M.B. de Tullio, and et al. Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic abeta peptide aggregates PLoS One 8 4 2013 e59113
    • (2013) PLoS One , vol.8 , Issue.4 , pp. e59113
    • De Tullio, M.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.