메뉴 건너뛰기




Volumn 17, Issue 10, 2012, Pages 1348-1361

Cell-permeable, small-molecule activators of the insulin-degrading enzyme

Author keywords

A ; activator; Alzheimer disease; IDE; protease

Indexed keywords

AMYLOID BETA PROTEIN; INSULIN; INSULINASE; PHEROMONE;

EID: 84869053378     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057112451921     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 33847662852 scopus 로고    scopus 로고
    • Soluble Protein Oligomers in Neurodegeneration: Lessons from the Alzheimer's Amyloid Beta-Peptide
    • Haass C., Selkoe D.J.. Soluble Protein Oligomers in Neurodegeneration: Lessons from the Alzheimer's Amyloid Beta-Peptide. Nat. Rev. Mol. Cell. Biol. 2007 ; 8 (2). 101-112
    • (2007) Nat. Rev. Mol. Cell. Biol , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 2
    • 84655160768 scopus 로고    scopus 로고
    • Are Amyloid-Degrading Enzymes Viable Therapeutic Targets in Alzheimer's Disease?
    • Nalivaeva N.N., Beckett C., Belyaev N.D., Turner A.J.. Are Amyloid-Degrading Enzymes Viable Therapeutic Targets in Alzheimer's Disease?. J. Neurochem. 2012 ; 120 (Suppl. 1). 167-185
    • (2012) J. Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 167-185
    • Nalivaeva, N.N.1    Beckett, C.2    Belyaev, N.D.3    Turner, A.J.4
  • 4
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced Proteolysis of Beta-Amyloid in APP Transgenic Mice Prevents Plaque Formation, Secondary Pathology, and Premature Death
    • Leissring M.A., Farris W., Chang A.Y., Walsh D.M., Wu X., Sun X., Frosch M.P., Selkoe D.J.. Enhanced Proteolysis of Beta-Amyloid in APP Transgenic Mice Prevents Plaque Formation, Secondary Pathology, and Premature Death. Neuron. 2003 ; 40 (6). 1087-1093
    • (2003) Neuron , vol.40 , Issue.6 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 7
    • 0029022718 scopus 로고
    • Insulysin and Pitrilysin: Insulin-Degrading Enzymes of Mammals and Bacteria
    • Becker A.B., Roth R.A.. Insulysin and Pitrilysin: Insulin-Degrading Enzymes of Mammals and Bacteria. Methods Enzymol. 1995 ; 248: 693-703
    • (1995) Methods Enzymol , vol.248 , pp. 693-703
    • Becker, A.B.1    Roth, R.A.2
  • 8
    • 33646543361 scopus 로고    scopus 로고
    • The Closed Structure of Presequence Protease PreP Forms a Unique 10,000 Angstroms3 Chamber for Proteolysis
    • Johnson K.A., Bhushan S., Stahl A., Hallberg B.M., Frohn A., Glaser E., Eneqvist T.. The Closed Structure of Presequence Protease PreP Forms a Unique 10,000 Angstroms3 Chamber for Proteolysis. Embo J. 2006 ; 25 (9). 1977-1986
    • (2006) Embo J , vol.25 , Issue.9 , pp. 1977-1986
    • Johnson, K.A.1    Bhushan, S.2    Stahl, A.3    Hallberg, B.M.4    Frohn, A.5    Glaser, E.6    Eneqvist, T.7
  • 9
    • 33750302461 scopus 로고    scopus 로고
    • Structures of Human Insulin-Degrading Enzyme Reveal a New Substrate Recognition Mechanism
    • Shen Y., Joachimiak A., Rosner M.R., Tang W.J.. Structures of Human Insulin-Degrading Enzyme Reveal a New Substrate Recognition Mechanism. Nature. 2006 ; 443 (7113). 870-874
    • (2006) Nature , vol.443 , Issue.7113 , pp. 870-874
    • Shen, Y.1    Joachimiak, A.2    Rosner, M.R.3    Tang, W.J.4
  • 10
    • 23044439856 scopus 로고    scopus 로고
    • Yeast as a Tractable Genetic System for Functional Studies of the Insulin-Degrading Enzyme
    • Kim S., Lapham A., Freedman C., Reed T., Schmidt W.. Yeast as a Tractable Genetic System for Functional Studies of the Insulin-Degrading Enzyme. J. Biol. Chem. 2005 ; 280 (30). 27481-27490
    • (2005) J. Biol. Chem , vol.280 , Issue.30 , pp. 27481-27490
    • Kim, S.1    Lapham, A.2    Freedman, C.3    Reed, T.4    Schmidt, W.5
  • 11
    • 33747178174 scopus 로고    scopus 로고
    • A Common Genetic System for Functional Studies of Pitrilysin and Related M16A Proteases
    • Alper B.J., Nienow T.E., Schmidt W.K.. A Common Genetic System for Functional Studies of Pitrilysin and Related M16A Proteases. Biochem. J. 2006 ; 398 (1). 145-152
    • (2006) Biochem. J , vol.398 , Issue.1 , pp. 145-152
    • Alper, B.J.1    Nienow, T.E.2    Schmidt, W.K.3
  • 12
    • 9244250417 scopus 로고    scopus 로고
    • Cleavage of Various Peptides with Pitrilysin from Escherichia coli: Kinetic Analyses Using Beta-Endorphin and Its Derivatives
    • Cornista J., Ikeuchi S., Haruki M., Kohara A., Takano K., Morikawa M., Kanaya S.. Cleavage of Various Peptides with Pitrilysin from Escherichia coli: Kinetic Analyses Using Beta-Endorphin and Its Derivatives. Biosci. Biotechnol. Biochem. 2004 ; 68 (10). 2128-2137
    • (2004) Biosci. Biotechnol. Biochem , vol.68 , Issue.10 , pp. 2128-2137
    • Cornista, J.1    Ikeuchi, S.2    Haruki, M.3    Kohara, A.4    Takano, K.5    Morikawa, M.6    Kanaya, S.7
  • 13
    • 70449675029 scopus 로고    scopus 로고
    • Yeast Ste23p Shares Functional Similarities with Mammalian Insulin-Degrading Enzymes
    • Alper B., Rowse J., Schmidt W.. Yeast Ste23p Shares Functional Similarities with Mammalian Insulin-Degrading Enzymes. Yeast. 2009 ; 26 (11). 595-610
    • (2009) Yeast , vol.26 , Issue.11 , pp. 595-610
    • Alper, B.1    Rowse, J.2    Schmidt, W.3
  • 14
    • 11144234853 scopus 로고    scopus 로고
    • ATP Effects on Insulin-Degrading Enzyme Are Mediated Primarily through Its Triphosphate Moiety
    • Song E.S., Juliano M.A., Juliano L., Fried M.G., Wagner S.L., Hersh L.B.. ATP Effects on Insulin-Degrading Enzyme Are Mediated Primarily through Its Triphosphate Moiety. J. Biol. Chem. 2004 ; 279 (52). 54216-54220
    • (2004) J. Biol. Chem , vol.279 , Issue.52 , pp. 54216-54220
    • Song, E.S.1    Juliano, M.A.2    Juliano, L.3    Fried, M.G.4    Wagner, S.L.5    Hersh, L.B.6
  • 17
    • 0034668893 scopus 로고    scopus 로고
    • Intracellular ATP Increases Capsaicin-Activated Channel Activity by Interacting with Nucleotide-Binding Domains
    • Kwak J., Wang M.H., Hwang S.W., Kim T.Y., Lee S.Y., Oh U.. Intracellular ATP Increases Capsaicin-Activated Channel Activity by Interacting with Nucleotide-Binding Domains. J. Neurosci. 2000 ; 20 (22). 8298-8304
    • (2000) J. Neurosci , vol.20 , Issue.22 , pp. 8298-8304
    • Kwak, J.1    Wang, M.H.2    Hwang, S.W.3    Kim, T.Y.4    Lee, S.Y.5    Oh, U.6
  • 19
    • 0034327206 scopus 로고    scopus 로고
    • Human Ras-Converting Enzyme (hRCE1) Endoproteolytic Activity on K-Ras-Derived Peptides
    • Hollander I., Frommer E., Mallon R.. Human Ras-Converting Enzyme (hRCE1) Endoproteolytic Activity on K-Ras-Derived Peptides. Anal. Biochem. 2000 ; 286 (1). 129-137
    • (2000) Anal. Biochem , vol.286 , Issue.1 , pp. 129-137
    • Hollander, I.1    Frommer, E.2    Mallon, R.3
  • 21
    • 59249100307 scopus 로고    scopus 로고
    • A Capillary Electrophoresis Method for Evaluation of Aß Proteolysis in Vitro
    • Alper B., Schmidt W.. A Capillary Electrophoresis Method for Evaluation of Aß Proteolysis In Vitro. J. Neurosci. Methods. 2009 ; 178: 40-45
    • (2009) J. Neurosci. Methods , vol.178 , pp. 40-45
    • Alper, B.1    Schmidt, W.2
  • 22
    • 0025119656 scopus 로고
    • Insulin-Degrading Enzyme: Stable Expression of the Human Complementary DNA, Characterization of Its Protein Product, and Chromosomal Mapping of the Human and Mouse Genes
    • Affholter J.A., Hsieh C.L., Francke U., Roth R.A.. Insulin-Degrading Enzyme: Stable Expression of the Human Complementary DNA, Characterization of Its Protein Product, and Chromosomal Mapping of the Human and Mouse Genes. Mol. Endocrinol. 1990 ; 4 (8). 1125-1135
    • (1990) Mol. Endocrinol , vol.4 , Issue.8 , pp. 1125-1135
    • Affholter, J.A.1    Hsieh, C.L.2    Francke, U.3    Roth, R.A.4
  • 23
    • 0024319166 scopus 로고
    • The Basal Component of the Nematode Dense-Body Is Vinculin
    • Barstead R.J., Waterston R.H.. The Basal Component of the Nematode Dense-Body Is Vinculin. J. Biol. Chem. 1989 ; 264 (17). 10177-10185
    • (1989) J. Biol. Chem , vol.264 , Issue.17 , pp. 10177-10185
    • Barstead, R.J.1    Waterston, R.H.2
  • 24
    • 1942422761 scopus 로고    scopus 로고
    • Update on NCI in Vitro Drug Screen Utilities
    • Holbeck S.L.. Update on NCI In Vitro Drug Screen Utilities. Eur. J. Cancer. 2004 ; 40 (6). 785-793
    • (2004) Eur. J. Cancer , vol.40 , Issue.6 , pp. 785-793
    • Holbeck, S.L.1
  • 25
    • 43049089747 scopus 로고    scopus 로고
    • Identification of Promiscuous Small Molecule Activators in High-Throughput Enzyme Activation Screens
    • Goode D.R., Totten R.K., Heeres J.T., Hergenrother P.J.. Identification of Promiscuous Small Molecule Activators in High-Throughput Enzyme Activation Screens. J. Med. Chem. 2008 ; 51 (8). 2346-2349
    • (2008) J. Med. Chem , vol.51 , Issue.8 , pp. 2346-2349
    • Goode, D.R.1    Totten, R.K.2    Heeres, J.T.3    Hergenrother, P.J.4
  • 26
    • 0020040057 scopus 로고
    • Isolation and Genetic Analysis of Saccharomyces cerevisiae Mutants Supersensitive to G1 Arrest by a Factor and Alpha Factor Pheromones
    • Chan R.K., Otte C.A.. Isolation and Genetic Analysis of Saccharomyces cerevisiae Mutants Supersensitive to G1 Arrest by a Factor and Alpha Factor Pheromones. Mol. Cell. Biol. 1982 ; 2 (1). 11-20
    • (1982) Mol. Cell. Biol , vol.2 , Issue.1 , pp. 11-20
    • Chan, R.K.1    Otte, C.A.2
  • 27
    • 0023974052 scopus 로고
    • The a-Factor Pheromone of Saccharomyces cerevisiae Is Essential for Mating
    • Michaelis S., Herskowitz I.. The a-Factor Pheromone of Saccharomyces cerevisiae Is Essential for Mating. Mol. Cell. Biol. 1988 ; 8 (3). 1309-1318
    • (1988) Mol. Cell. Biol , vol.8 , Issue.3 , pp. 1309-1318
    • Michaelis, S.1    Herskowitz, I.2
  • 28
    • 0028879135 scopus 로고
    • Role of Yeast Insulin-Degrading Enzyme Homologs in Propheromone Processing and Bud Site Selection
    • Adames N., Blundell K., Ashby M.N., Boone C.. Role of Yeast Insulin-Degrading Enzyme Homologs in Propheromone Processing and Bud Site Selection. Science. 1995 ; 270: 464-467
    • (1995) Science , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 29
    • 0026703547 scopus 로고
    • A Simple and Efficient Procedure for Transformation of Yeasts
    • Elble R.. A Simple and Efficient Procedure for Transformation of Yeasts. BioTechniques. 1992 ; 13: 18-20
    • (1992) BioTechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 30
    • 0024669291 scopus 로고
    • A System of Shuttle Vectors and Yeast Host Strains Designed for Efficient Manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R.S., Hieter P.. A System of Shuttle Vectors and Yeast Host Strains Designed for Efficient Manipulation of DNA in Saccharomyces cerevisiae. Genetics. 1989 ; 122 (1). 19-27
    • (1989) Genetics , vol.122 , Issue.1 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 31
    • 0031055072 scopus 로고    scopus 로고
    • Biogenesis of the Saccharomyces cerevisiae Mating Pheromone a-Factor
    • Chen P., Sapperstein S.K., Choi J.D., Michaelis S.. Biogenesis of the Saccharomyces cerevisiae Mating Pheromone a-Factor. J. Cell. Biol. 1997 ; 136 (2). 251-269
    • (1997) J. Cell. Biol , vol.136 , Issue.2 , pp. 251-269
    • Chen, P.1    Sapperstein, S.K.2    Choi, J.D.3    Michaelis, S.4
  • 32
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and Computational Approaches to Estimate Solubility and Permeability in Drug Discovery and Development Settings
    • Lipinski C., Lombardo F., Dominy B., Feeney P.. Experimental and Computational Approaches to Estimate Solubility and Permeability in Drug Discovery and Development Settings. Adv. Drug Del. Rev. 1997 ; 23: 3-25
    • (1997) Adv. Drug Del. Rev , vol.23 , pp. 3-25
    • Lipinski, C.1    Lombardo, F.2    Dominy, B.3    Feeney, P.4
  • 33
    • 0035861547 scopus 로고    scopus 로고
    • The Multispanning Membrane Protein Ste24p Catalyzes CAAX Proteolysis and NH2-Terminal Processing of the Yeast a-Factor Precursor
    • Tam A., Schmidt W.K., Michaelis S.. The Multispanning Membrane Protein Ste24p Catalyzes CAAX Proteolysis and NH2-Terminal Processing of the Yeast a-Factor Precursor. J. Biol. Chem. 2001 ; 276 (50). 46798-46806
    • (2001) J. Biol. Chem , vol.276 , Issue.50 , pp. 46798-46806
    • Tam, A.1    Schmidt, W.K.2    Michaelis, S.3
  • 35
    • 0032496368 scopus 로고    scopus 로고
    • Amyloidogenic Determinant as a Substrate Recognition Motif of Insulin-Degrading Enzyme
    • Kurochkin I.V.. Amyloidogenic Determinant as a Substrate Recognition Motif of Insulin-Degrading Enzyme. FEBS Lett. 1998 ; 427 (2). 153-156
    • (1998) FEBS Lett , vol.427 , Issue.2 , pp. 153-156
    • Kurochkin, I.V.1
  • 36
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the Brain's Amyloid Cobwebs
    • Selkoe D.J.. Clearing the Brain's Amyloid Cobwebs. Neuron. 2001 ; 32 (2). 177-180
    • (2001) Neuron , vol.32 , Issue.2 , pp. 177-180
    • Selkoe, D.J.1
  • 39
    • 0032855482 scopus 로고    scopus 로고
    • Ethodological and Chemical Factors Affecting Amyloid Beta Peptide Amyloidogenicity
    • Zagorski M., Yang J., Shao H., Ma K., Zeng H., Hong A. M. ethodological and Chemical Factors Affecting Amyloid Beta Peptide Amyloidogenicity. Methods Enzymol. 1999 ; 309: 189-204
    • (1999) Methods Enzymol , vol.309 , pp. 189-204
    • Zagorski, M.1    Yang, J.2    Shao, H.3    Ma, K.4    Zeng, H.5    Hong, A.M.6
  • 40
    • 0141621234 scopus 로고    scopus 로고
    • Kinetics of Amyloid Beta-Protein Degradation Determined by Novel Fluorescence- and Fluorescence Polarization-Based Assays
    • Leissring M.A., Lu A., Condron M.M., Teplow D.B., Stein R.L., Farris W., Selkoe D.J.. Kinetics of Amyloid Beta-Protein Degradation Determined by Novel Fluorescence- and Fluorescence Polarization-Based Assays. J. Biol. Chem. 2003 ; 278 (39). 37314-37320
    • (2003) J. Biol. Chem , vol.278 , Issue.39 , pp. 37314-37320
    • Leissring, M.A.1    Lu, A.2    Condron, M.M.3    Teplow, D.B.4    Stein, R.L.5    Farris, W.6    Selkoe, D.J.7
  • 41
    • 77249169281 scopus 로고    scopus 로고
    • Turning Enzymes on with Small Molecules
    • Zorn J.A., Wells J.A.. Turning Enzymes ON with Small Molecules. Nat. Chem. Biol. 2010 ; 6 (3). 179-187
    • (2010) Nat. Chem. Biol , vol.6 , Issue.3 , pp. 179-187
    • Zorn, J.A.1    Wells, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.