메뉴 건너뛰기




Volumn 49, Issue 49, 2010, Pages 10371-10380

Hydralazine modifies Aβ fibril formation and prevents modification by lipids in vitro

Author keywords

[No Author keywords available]

Indexed keywords

4-HYDROXY-2-NONENAL; ALZHEIMER'S DISEASE PATHOLOGIES; BLOOD-BRAIN BARRIER; DISEASE PROGRESSION; DRUG DEVELOPMENT; DRUG DISCOVERY; FIBRIL FORMATION; FOOD AND DRUG ADMINISTRATION; HYDRALAZINE; HYDRAZIDE GROUPS; IN-VITRO; LIPID MODIFICATIONS; MISFOLDING; OXIDATIVE DAMAGE; POTENTIAL DRUG; PROTECTION ASSAY; PROTEIN MODIFICATIONS; SIDE EFFECT; SMOOTH MUSCLE RELAXANT; WESTERN BLOTTING;

EID: 78650114682     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101249p     Document Type: Article
Times cited : (22)

References (85)
  • 1
    • 0034516988 scopus 로고    scopus 로고
    • Toward a comprehensive theory for Alzheimer's disease-Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein
    • Selkoe, D. J. (2000) Toward a comprehensive theory for Alzheimer's disease-Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein Ann. N.Y. Acad. Sci. 924, 17-25
    • (2000) Ann. N.Y. Acad. Sci. , vol.924 , pp. 17-25
    • Selkoe, D.J.1
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 297, 353
    • (2002) Science , vol.297 , pp. 353
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery, W. R. and Carney, J. M. (1999) Oxidative alterations in Alzheimer's disease Brain Pathol. 9, 133-146
    • (1999) Brain Pathol. , vol.9 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 4
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W. R. (1997) Oxidative stress hypothesis in Alzheimer's disease Free Radical Biol. Med. 23, 134-147
    • (1997) Free Radical Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 6
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • Christen, Y (2000) Oxidative stress and Alzheimer disease Am. J. Clin. Nutr. 71, 621s-6629
    • (2000) Am. J. Clin. Nutr. , vol.71
    • Christen, Y.1
  • 7
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress
    • Butterfield, D. A. and Lauderback, C. M. (2002) Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress Free Radical Biol. Med. 32, 1050-1060
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 8
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • Butterfield, D. A., Castegna, A., Lauderback, C. M., and Drake, J. (2002) Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death Neurobiol. Aging 23, 655-664
    • (2002) Neurobiol. Aging , vol.23 , pp. 655-664
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 9
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
    • Selkoe, D. J. (2008) Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior Behav. Brain Res. 192, 106-113
    • (2008) Behav. Brain Res. , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 11
    • 1842519391 scopus 로고    scopus 로고
    • Alzheimer's amyloid beta-peptide (1-42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide
    • Butterfield, D. A. and Bush, A. I. (2004) Alzheimer's amyloid beta-peptide (1-42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide Neurobiol. Aging 25, 563-568
    • (2004) Neurobiol. Aging , vol.25 , pp. 563-568
    • Butterfield, D.A.1    Bush, A.I.2
  • 14
    • 34248219460 scopus 로고    scopus 로고
    • Membrane-mediated amyloidogenesis and the promotion of oxidative lipid damage by amyloid beta proteins
    • Murray, I. V. J., Liu, L., Komatsu, H., Uryu, K., Xiao, G., Lawson, J. A., and Axelsen, P. H. (2007) Membrane-mediated amyloidogenesis and the promotion of oxidative lipid damage by amyloid beta proteins J. Biol. Chem. 282, 9335-9345
    • (2007) J. Biol. Chem. , vol.282 , pp. 9335-9345
    • Murray, I.V.J.1    Liu, L.2    Komatsu, H.3    Uryu, K.4    Xiao, G.5    Lawson, J.A.6    Axelsen, P.H.7
  • 15
    • 14844304305 scopus 로고    scopus 로고
    • Oxidation of cholesterol by amyloid precursor protein and beta-amyloid peptide
    • Nelson, T. J. and Alkon, D. L. (2005) Oxidation of cholesterol by amyloid precursor protein and beta-amyloid peptide J. Biol. Chem. 280, 7377-7387
    • (2005) J. Biol. Chem. , vol.280 , pp. 7377-7387
    • Nelson, T.J.1    Alkon, D.L.2
  • 18
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith, M. A., Harris, P. L. R., Sayre, L. M., and Perry, G (1997) Iron accumulation in Alzheimer disease is a source of redox-generated free radicals Proc. Natl. Acad. Sci. U.S.A. 94, 9866-9868
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.R.2    Sayre, L.M.3    Perry, G.4
  • 20
    • 0035872487 scopus 로고    scopus 로고
    • Copper in disorders with neurological symptoms: Alzheimer's, Menkes, and Wilson diseases
    • Strausak, D., Mercer, J. F. B., Dieter, H. H., Stremmel, W., and Multhaup, G. (2001) Copper in disorders with neurological symptoms: Alzheimer's, Menkes, and Wilson diseases Brain. Res. Bull. 55, 175-185
    • (2001) Brain. Res. Bull. , vol.55 , pp. 175-185
    • Strausak, D.1    Mercer, J.F.B.2    Dieter, H.H.3    Stremmel, W.4    Multhaup, G.5
  • 21
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong, J., Atwood, C. S., Anderson, V. E., Siedlak, S. L., Smith, M. A., Perry, G., and Carey, P. R. (2003) Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence Biochemistry 42, 2768-2773
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 22
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid [beta] peptide
    • Smith, D. G., Cappai, R., and Barnham, K. J. (2007) The redox chemistry of the Alzheimer's disease amyloid [beta] peptide Biochim. Biophys. Acta 1768, 1976-1990
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 23
    • 67651020783 scopus 로고    scopus 로고
    • Amyloid plaques in PSAPP mice bind less metal than plaques in human Alzheimer's disease
    • Leskovjan, A. C., Lanzirotti, A., and Miller, L. M. (2009) Amyloid plaques in PSAPP mice bind less metal than plaques in human Alzheimer's disease Neuroimage 47, 1215-1220
    • (2009) Neuroimage , vol.47 , pp. 1215-1220
    • Leskovjan, A.C.1    Lanzirotti, A.2    Miller, L.M.3
  • 24
    • 63349095579 scopus 로고    scopus 로고
    • A novel approach to the identification and quantitative elemental analysis of amyloid deposits-Insights into the pathology of Alzheimer's disease
    • Rajendran, R., Minqin, R., Ynsa, M. D., Casadesus, G., Smith, M. A., Perry, G., Halliwell, B., and Watt, F. (2009) A novel approach to the identification and quantitative elemental analysis of amyloid deposits-Insights into the pathology of Alzheimer's disease Biochem. Biophys. Res. Commun. 382, 91-95
    • (2009) Biochem. Biophys. Res. Commun. , vol.382 , pp. 91-95
    • Rajendran, R.1    Minqin, R.2    Ynsa, M.D.3    Casadesus, G.4    Smith, M.A.5    Perry, G.6    Halliwell, B.7    Watt, F.8
  • 25
    • 0037444553 scopus 로고    scopus 로고
    • In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy
    • McLellan, M. E., Kajdasz, S. T., Hyman, B. T., and Bacskai, B. J. (2003) In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy J. Neurosci. 23, 2212-2217
    • (2003) J. Neurosci. , vol.23 , pp. 2212-2217
    • McLellan, M.E.1    Kajdasz, S.T.2    Hyman, B.T.3    Bacskai, B.J.4
  • 26
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • Sayre, L. M., Perry, G., Harris, P. L. R., Liu, Y. H., Schubert, K. A., and Smith, M. A. (2000) In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals J. Neurochem. 74, 270-279
    • (2000) J. Neurochem. , vol.74 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.R.3    Liu, Y.H.4    Schubert, K.A.5    Smith, M.A.6
  • 27
    • 0034129716 scopus 로고    scopus 로고
    • The antihypertensive hydralazine is an efficient scavenger of acrolein
    • Burcham, P. C., Kerr, P. G., and Fontaine, F. R. (2000) The antihypertensive hydralazine is an efficient scavenger of acrolein Redox Rep. 5, 47-49
    • (2000) Redox Rep. , vol.5 , pp. 47-49
    • Burcham, P.C.1    Kerr, P.G.2    Fontaine, F.R.3
  • 28
    • 4243088697 scopus 로고    scopus 로고
    • Aldehyde-sequestering drugs: Tools for studying protein damage by lipid peroxidation products
    • Burcham, P. C., Kaminskas, L. M., Fontaine, F. R., Petersen, D. R., and Pyke, S. M. (2002) Aldehyde-sequestering drugs: tools for studying protein damage by lipid peroxidation products Toxicology 181-182, 229-236
    • (2002) Toxicology , vol.181-182 , pp. 229-236
    • Burcham, P.C.1    Kaminskas, L.M.2    Fontaine, F.R.3    Petersen, D.R.4    Pyke, S.M.5
  • 29
    • 1342308332 scopus 로고    scopus 로고
    • Protein adduct-trapping by hydrazinophthalazine drugs: Mechanisms of cytoprotection against acrolein-mediated toxicity
    • Burcham, P. C., Fontaine, F. R., Kaminskas, L. M., Petersen, D. R., and Pyke, S. M. (2004) Protein adduct-trapping by hydrazinophthalazine drugs: Mechanisms of cytoprotection against acrolein-mediated toxicity Mol. Pharmacol. 65, 655-664
    • (2004) Mol. Pharmacol. , vol.65 , pp. 655-664
    • Burcham, P.C.1    Fontaine, F.R.2    Kaminskas, L.M.3    Petersen, D.R.4    Pyke, S.M.5
  • 30
    • 4243084363 scopus 로고    scopus 로고
    • Strong protein adduct trapping accompanies abolition of acrolein-mediated hepatotoxicity by hydralazine in mice
    • Kaminskas, L. M., Pyke, S. M., and Burcham, P. C. (2004) Strong protein adduct trapping accompanies abolition of acrolein-mediated hepatotoxicity by hydralazine in mice J. Pharmacol. Exp. Ther. 310, 1003-1010
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 1003-1010
    • Kaminskas, L.M.1    Pyke, S.M.2    Burcham, P.C.3
  • 31
    • 33644845649 scopus 로고    scopus 로고
    • Hydralazine inhibits rapid acrolein-induced protein oligomerization: Role of aldehyde scavenging and adduct trapping in cross-link blocking and cytoprotection
    • Burcham, P. C. and Pyke, S. M. (2006) Hydralazine inhibits rapid acrolein-induced protein oligomerization: Role of aldehyde scavenging and adduct trapping in cross-link blocking and cytoprotection Mol. Pharmacol. 69, 1056-1065
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1056-1065
    • Burcham, P.C.1    Pyke, S.M.2
  • 33
    • 33947715680 scopus 로고    scopus 로고
    • Michael addition of acrolein to lysinyl and N-terminal residues of a model peptide: Targets for cytoprotective hydrazino drugs
    • Kaminskas, L. M., Pyke, S. M., and Burcham, P. C. (2007) Michael addition of acrolein to lysinyl and N-terminal residues of a model peptide: Targets for cytoprotective hydrazino drugs Rapid Commun. Mass Spectrum 21, 1155-1164
    • (2007) Rapid Commun. Mass Spectrum , vol.21 , pp. 1155-1164
    • Kaminskas, L.M.1    Pyke, S.M.2    Burcham, P.C.3
  • 34
    • 42949163044 scopus 로고    scopus 로고
    • Carbonyl-scavenging drugs & protection against carbonyl stress-associated cell injury
    • Burcham, P. C., Kaminskas, L. M., Tan, D., and Pyke, S. M. (2008) Carbonyl-scavenging drugs & protection against carbonyl stress-associated cell injury Mini Rev. Med. Chem. 8, 319-330
    • (2008) Mini Rev. Med. Chem. , vol.8 , pp. 319-330
    • Burcham, P.C.1    Kaminskas, L.M.2    Tan, D.3    Pyke, S.M.4
  • 36
    • 0016743198 scopus 로고
    • Bioenergetics in clinical medicine. III. Inhibition of coenzyme Q10-enzymes by clinically used anti-hypertensive drugs
    • Kishi., H., Kishi, T., and Folkers, K. (1975) Bioenergetics in clinical medicine. III. Inhibition of coenzyme Q10-enzymes by clinically used anti-hypertensive drugs Res. Commun. Chem. Pathol. Pharmacol. 12, 533-540
    • (1975) Res. Commun. Chem. Pathol. Pharmacol. , vol.12 , pp. 533-540
    • Kishi, H.1    Kishi, T.2    Folkers, K.3
  • 37
    • 1542332649 scopus 로고    scopus 로고
    • Antioxidant activity and inhibitory effects of hydralazine on inducible NOS/COX-2 gene and protein expression in rat peritoneal macrophages
    • Leiro, J. M., Alvarez, E., Arranz, J. A., Cano, E., and Orallo, F. (2004) Antioxidant activity and inhibitory effects of hydralazine on inducible NOS/COX-2 gene and protein expression in rat peritoneal macrophages Int. Immunopharmacol. 4, 162-177
    • (2004) Int. Immunopharmacol. , vol.4 , pp. 162-177
    • Leiro, J.M.1    Alvarez, E.2    Arranz, J.A.3    Cano, E.4    Orallo, F.5
  • 39
    • 33745789386 scopus 로고    scopus 로고
    • Hydralazine rescues PC12 cells from acrolein-mediated death
    • Liu-Snyder, P., Borgens, R. B., and Shi, R. (2006) Hydralazine rescues PC12 cells from acrolein-mediated death J. Neurol. Res. 84, 219-227
    • (2006) J. Neurol. Res. , vol.84 , pp. 219-227
    • Liu-Snyder, P.1    Borgens, R.B.2    Shi, R.3
  • 40
    • 33645741763 scopus 로고    scopus 로고
    • Desensitization of platelet-derived growth factor receptor-β by oxidized lipids in vascular cells and atherosclerotic lesions: Prevention by aldehyde scavengers
    • Vindis, C., Escargueil-Blanc, I., Elbaz, M., Marcheix, B., Grazide, M. H., Uchida, K., Salvayre, R., and Negre-Salvayre, A. (2006) Desensitization of platelet-derived growth factor receptor-β by oxidized lipids in vascular cells and atherosclerotic lesions: Prevention by aldehyde scavengers Circ. Res. 98, 785-792
    • (2006) Circ. Res. , vol.98 , pp. 785-792
    • Vindis, C.1    Escargueil-Blanc, I.2    Elbaz, M.3    Marcheix, B.4    Grazide, M.H.5    Uchida, K.6    Salvayre, R.7    Negre-Salvayre, A.8
  • 41
    • 59049105100 scopus 로고    scopus 로고
    • Cytoprotective mechanisms of carbonyl scavenging drugs in isolated rat hepatocytes
    • Mehta, R., Wong, L., and O'Brien, P. J. (2009) Cytoprotective mechanisms of carbonyl scavenging drugs in isolated rat hepatocytes Chem.-Biol. Interact. 178, 317-323
    • (2009) Chem.-Biol. Interact. , vol.178 , pp. 317-323
    • Mehta, R.1    Wong, L.2    O'Brien, P.J.3
  • 42
    • 70450176923 scopus 로고    scopus 로고
    • Acrolein scavenging: A potential novel mechanism of attenuating oxidative stress following spinal cord injury
    • Hamann, K. and Shi, R. (2009) Acrolein scavenging: A potential novel mechanism of attenuating oxidative stress following spinal cord injury J. Neurochem. 111, 1348-1356
    • (2009) J. Neurochem. , vol.111 , pp. 1348-1356
    • Hamann, K.1    Shi, R.2
  • 43
    • 77249109368 scopus 로고    scopus 로고
    • Traditional reactive carbonyl scavengers do not prevent the carbonylation of brain proteins induced by acute glutathione depletion
    • Zheng, J. and Bizzozero, O. A. (2010) Traditional reactive carbonyl scavengers do not prevent the carbonylation of brain proteins induced by acute glutathione depletion Free Radical Res. 44, 258-266
    • (2010) Free Radical Res. , vol.44 , pp. 258-266
    • Zheng, J.1    Bizzozero, O.A.2
  • 44
    • 0019773573 scopus 로고
    • Hydralazine and related compounds: Chemistry, metabolism, and mode of action
    • Reece, P. (1981) Hydralazine and related compounds: Chemistry, metabolism, and mode of action Med. Res. Rev. 1, 73-96
    • (1981) Med. Res. Rev. , vol.1 , pp. 73-96
    • Reece, P.1
  • 49
    • 33747056003 scopus 로고    scopus 로고
    • A novel in vitro filter trap assay identifies tannic acid as an amyloid aggregation inducer for HET-s
    • Boye-Harnasch, M. and Cullin, C. (2006) A novel in vitro filter trap assay identifies tannic acid as an amyloid aggregation inducer for HET-s J. Biotechnol. 125, 222-230
    • (2006) J. Biotechnol. , vol.125 , pp. 222-230
    • Boye-Harnasch, M.1    Cullin, C.2
  • 50
    • 0032879437 scopus 로고    scopus 로고
    • Membrane filter assay for detection of amyloid-like polyglutamine- containing protein aggregates
    • Wanker, E. E., Scherzinger, E., Heiser, V., Sittler, A., Eickhoff, H., and Lehrach, H. (1999) Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates Methods Enzymol. 309, 375-386
    • (1999) Methods Enzymol. , vol.309 , pp. 375-386
    • Wanker, E.E.1    Scherzinger, E.2    Heiser, V.3    Sittler, A.4    Eickhoff, H.5    Lehrach, H.6
  • 51
    • 37549071037 scopus 로고    scopus 로고
    • Detection and quantification of tau aggregation using a membrane filter assay
    • Chang, E. and Kuret, J. (2008) Detection and quantification of tau aggregation using a membrane filter assay Anal. Biochem. 373, 330-336
    • (2008) Anal. Biochem. , vol.373 , pp. 330-336
    • Chang, E.1    Kuret, J.2
  • 52
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson, B. I., Murray, I. V. J., Trojanowski, J. Q., and Lee, V. M. Y. (2001) A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly J. Biol. Chem. 276, 2380-2386
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.J.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 54
    • 49649116929 scopus 로고    scopus 로고
    • Designed amyloid β peptide fibril-A tool for high-throughput screening of fibril inhibitors
    • Dolphin, G. T., Ouberai, M., Dumy, P., and Garcia, J. (2007) Designed amyloid β peptide fibril-A tool for high-throughput screening of fibril inhibitors ChemMedChem 2, 1613-1623
    • (2007) ChemMedChem , vol.2 , pp. 1613-1623
    • Dolphin, G.T.1    Ouberai, M.2    Dumy, P.3    Garcia, J.4
  • 55
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct J. Biol. Chem. 282, 10311-10324
    • (2007) J. Biol. Chem. , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 56
    • 0022272164 scopus 로고
    • Free radical-mediated activation of hydrazine derivatives
    • Kalyanaraman, B. and Sinha, B. K. (1985) Free radical-mediated activation of hydrazine derivatives Environ. Health Perspect. 64, 179-184
    • (1985) Environ. Health Perspect. , vol.64 , pp. 179-184
    • Kalyanaraman, B.1    Sinha, B.K.2
  • 57
    • 0030949577 scopus 로고    scopus 로고
    • Peroxidase substrates stimulate the oxidation of hydralazine to metabolites which cause single-strand breaks in DNA
    • Reilly, C. A. and Aust, S. D. (1997) Peroxidase substrates stimulate the oxidation of hydralazine to metabolites which cause single-strand breaks in DNA Chem. Res. Toxicol. 10, 328-334
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 328-334
    • Reilly, C.A.1    Aust, S.D.2
  • 59
    • 27944444088 scopus 로고    scopus 로고
    • Hydrazide derivatives produce active oxygen species as hydrazine
    • Timperio, A. M., Rinalducci, S., and Zolla, L. (2005) Hydrazide derivatives produce active oxygen species as hydrazine Bioorg. Chem. 33, 459-469
    • (2005) Bioorg. Chem. , vol.33 , pp. 459-469
    • Timperio, A.M.1    Rinalducci, S.2    Zolla, L.3
  • 61
    • 34548721060 scopus 로고    scopus 로고
    • Simvastatin reverses target organ damage and oxidative stress in angiotensin II hypertension: Comparison with apocynin, tempol, and hydralazine
    • Rugale, C. M., Delbosc, S. P., Mimran, A. M., and Jover, B. P. (2007) Simvastatin reverses target organ damage and oxidative stress in angiotensin II hypertension: Comparison with apocynin, tempol, and hydralazine J. Cardiovasc. Pharmacol. 50, 293-298
    • (2007) J. Cardiovasc. Pharmacol. , vol.50 , pp. 293-298
    • Rugale, C.M.1    Delbosc, S.P.2    Mimran, A.M.3    Jover, B.P.4
  • 63
    • 73849116449 scopus 로고    scopus 로고
    • Olmesartan reduces oxidative stress in the brain of stroke-prone spontaneously hypertensive rats assessed by an in vivo ESR method
    • Araki, S., Hirooka, Y., Kishi, T., Yasukawa, K., Utsumi, H., and Sunagawa, K. (2009) Olmesartan reduces oxidative stress in the brain of stroke-prone spontaneously hypertensive rats assessed by an in vivo ESR method Hypertens. Res. 32, 1091-1096
    • (2009) Hypertens. Res. , vol.32 , pp. 1091-1096
    • Araki, S.1    Hirooka, Y.2    Kishi, T.3    Yasukawa, K.4    Utsumi, H.5    Sunagawa, K.6
  • 65
    • 0037076539 scopus 로고    scopus 로고
    • Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
    • Nichols, M. R., Moss, M. A., Reed, D. K., Lin, W. L., Mukhopadhyay, R., Hoh, J. H., and Rosenberry, T. L. (2002) Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy Biochemistry 41, 6115-6127
    • (2002) Biochemistry , vol.41 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 66
    • 33644940173 scopus 로고    scopus 로고
    • Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
    • de Groot, N. S., Aviles, F. X., Vendrell, J., and Ventura, S. (2006) Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities FEBS J. 273, 658-668
    • (2006) FEBS J. , vol.273 , pp. 658-668
    • De Groot, N.S.1    Aviles, F.X.2    Vendrell, J.3    Ventura, S.4
  • 68
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova, A. T., Yau, W. M., and Tycko, R. (2005) Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils Biochemistry 45, 498-512
    • (2005) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 70
    • 33748689799 scopus 로고    scopus 로고
    • Simulations as analytical tools to understand protein aggregation and predict amyloid conformation
    • Ma, B. and Nussinov, R. (2006) Simulations as analytical tools to understand protein aggregation and predict amyloid conformation Curr. Opin. Chem. Biol. 10, 445-452
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 445-452
    • Ma, B.1    Nussinov, R.2
  • 71
    • 0035797795 scopus 로고    scopus 로고
    • Structural features of the A beta amyloid fibril elucidated by limited proteolysis
    • Kheterpal, I., Williams, A., Murphy, C., Bledsoe, B., and Wetzel, R. (2001) Structural features of the A beta amyloid fibril elucidated by limited proteolysis Biochemistry 40, 11757-11767
    • (2001) Biochemistry , vol.40 , pp. 11757-11767
    • Kheterpal, I.1    Williams, A.2    Murphy, C.3    Bledsoe, B.4    Wetzel, R.5
  • 72
    • 0032729982 scopus 로고    scopus 로고
    • Computationally derived structural models of the beta-amyloid found in Alzheimer's disease plaques and the interaction with possible aggregation inhibitors
    • George, A. R. and Howlett, D. R. (1999) Computationally derived structural models of the beta-amyloid found in Alzheimer's disease plaques and the interaction with possible aggregation inhibitors Biopolymers 50, 733-741
    • (1999) Biopolymers , vol.50 , pp. 733-741
    • George, A.R.1    Howlett, D.R.2
  • 74
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • Porat, Y., Abramowitz, A., and Gazit, E. (2006) Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism Chem. Biol. Drug Des. 67, 27-37
    • (2006) Chem. Biol. Drug Des. , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 75
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for pi-stacking in the self-assembly of amyloid fibrils
    • Gazit, E. (2002) A possible role for pi-stacking in the self-assembly of amyloid fibrils FASEB J. 16, 77-83
    • (2002) FASEB J. , vol.16 , pp. 77-83
    • Gazit, E.1
  • 77
    • 73549106551 scopus 로고    scopus 로고
    • Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid-β aggregation pathway
    • Hamaguchi, T., Ono, K., Murase, A., and Yamada, M. (2009) Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid-β aggregation pathway Am. J. Pathol. 175, 2557-2565
    • (2009) Am. J. Pathol. , vol.175 , pp. 2557-2565
    • Hamaguchi, T.1    Ono, K.2    Murase, A.3    Yamada, M.4
  • 80
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush, A. I. (2003) The metallobiology of Alzheimer's disease Trends Neurosci. 26, 207-214
    • (2003) Trends Neurosci. , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 81
    • 46749100924 scopus 로고    scopus 로고
    • Therapeutics for Alzheimer's disease based on the metal hypothesis
    • Bush, A. I. and Tanzi, R. E. (2008) Therapeutics for Alzheimer's disease based on the metal hypothesis Neurotherapeutics 5, 421-432
    • (2008) Neurotherapeutics , vol.5 , pp. 421-432
    • Bush, A.I.1    Tanzi, R.E.2
  • 82
    • 0027101939 scopus 로고
    • Antioxidant drug mechanisms: Transition metal-binding and vasodilation
    • Weglicki, W. B. and Mak, I. T. (1992) Antioxidant drug mechanisms: Transition metal-binding and vasodilation Mol. Cell. Biochem. 118, 105-111
    • (1992) Mol. Cell. Biochem. , vol.118 , pp. 105-111
    • Weglicki, W.B.1    Mak, I.T.2
  • 83
    • 0021323164 scopus 로고
    • Metal binding by pharmaceuticals. Part 4. A comparative investigation of the interaction of metal ions with hydralazine, prizidilol and related compounds
    • Al-Falahi, H., May, P. M., Roe, A. M., Slater, R. A., Trolt, W. J., and Williams, D. R. (1984) Metal binding by pharmaceuticals. Part 4. A comparative investigation of the interaction of metal ions with hydralazine, prizidilol and related compounds Agents Actions 14, 113-120
    • (1984) Agents Actions , vol.14 , pp. 113-120
    • Al-Falahi, H.1    May, P.M.2    Roe, A.M.3    Slater, R.A.4    Trolt, W.J.5    Williams, D.R.6
  • 84


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.