메뉴 건너뛰기




Volumn 12, Issue 3, 2011, Pages 2019-2035

Amyloidogenic properties of a D/N mutated 12 amino acid fragment of the C-terminal domain of the cholesteryl-ester transfer protein (CETP)

Author keywords

helix and sheet secondary structures; Amyloids; CETP C terminal domain; Cholesteryl ester transfer protein (CETP); Peptide oligomers

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; CHOLESTEROL ESTER TRANSFER PROTEIN; REACTIVE OXYGEN METABOLITE; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); AMYLOID BETA-PROTEIN (25-35); PEPTIDE; PEPTIDE FRAGMENT;

EID: 79953299218     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12032019     Document Type: Article
Times cited : (17)

References (36)
  • 2
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson, J.F.; Theos, A.C.; Harper, D.C.; Tenza, D.; Raposo, G.; Marks, M.S. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell. Biol. 2003, 161, 521-533.
    • (2003) J. Cell. Biol , vol.161 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 3
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M. Protein folding and misfolding. Nature 2003, 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 5
    • 50849131197 scopus 로고    scopus 로고
    • Forces between hydrophilic surfaces adsorbed with apolipoprotein AII alpha helices
    • Ramos, S.; Campos-Terán, J.; Mas-Oliva, J.; Nylander, T.; Castillo, R. Forces between hydrophilic surfaces adsorbed with apolipoprotein AII alpha helices. Langmuir 2008, 24, 8568-8575.
    • (2008) Langmuir , vol.24 , pp. 8568-8575
    • Ramos, S.1    Campos-Terán, J.2    Mas-Oliva, J.3    Nylander, T.4    Castillo, R.5
  • 6
    • 36048938680 scopus 로고    scopus 로고
    • Lipid dependant disorder-to-order conformational transitions in apolipoprotein CI derived peptides
    • Mendoza-Espinosa, P.; Moreno, A.; Castillo, R.; Mas-Oliva, J. Lipid dependant disorder-to-order conformational transitions in apolipoprotein CI derived peptides. Biochem. Biophys. Res. Commun. 2008, 365, 8-15.
    • (2008) Biochem. Biophys. Res. Commun , vol.365 , pp. 8-15
    • Mendoza-Espinosa, P.1    Moreno, A.2    Castillo, R.3    Mas-Oliva, J.4
  • 7
    • 33646715318 scopus 로고    scopus 로고
    • Cholesteryl ester transfer protein (CETP) inhibition beyond raising high-density lipoprotein cholesterol levels: Pathways by which modulation of CETP activity may alter atherogenesis
    • Klerkx, A.H.; El Harchaoui, K.; van der Steeg, W.A.; Boekholdt, S.M.; Stroes, E.S.; Kastelein, J.J.; Kuivenhoven, J.A. Cholesteryl ester transfer protein (CETP) inhibition beyond raising high-density lipoprotein cholesterol levels: pathways by which modulation of CETP activity may alter atherogenesis. Arterioscler. Thromb. Vasc. Biol. 2006, 26, 706-715.
    • (2006) Arterioscler. Thromb. Vasc. Biol , vol.26 , pp. 706-715
    • Klerkx, A.H.1    El, H.K.2    van der, S.W.A.3    Boekholdt, S.M.4    Stroes, E.S.5    Kastelein, J.J.6    Kuivenhoven, J.A.7
  • 8
  • 9
    • 0027528310 scopus 로고
    • Point mutagenesis of carboxyl-terminal amino acids of cholesteryl ester transfer protein
    • Wang, S.; Wang, X.; Deng, L.; Rassart, E.; Milne, R.S.; Tall, A.R. Point mutagenesis of carboxyl-terminal amino acids of cholesteryl ester transfer protein. J. Biol. Chem. 1993, 66, 1955-1959.
    • (1993) J. Biol. Chem , vol.66 , pp. 1955-1959
    • Wang, S.1    Wang, X.2    Deng, L.3    Rassart, E.4    Milne, R.S.5    Tall, A.R.6
  • 10
    • 0028899709 scopus 로고
    • Defective binding of neutral lipids by a carboxyl-terminal deletion mutant of cholesteryl ester transfer protein. Evidence for a carboxyl-terminal cholesteryl ester binding site essential for neutral lipid transfer activity
    • Wang, S.; Kussie, P.; Deng, L.; Tall, A. Defective binding of neutral lipids by a carboxyl-terminal deletion mutant of cholesteryl ester transfer protein. Evidence for a carboxyl-terminal cholesteryl ester binding site essential for neutral lipid transfer activity. J. Biol. Chem. 1995, 270, 612-618.
    • (1995) J. Biol. Chem , vol.270 , pp. 612-618
    • Wang, S.1    Kussie, P.2    Deng, L.3    Tall, A.4
  • 13
    • 0037357794 scopus 로고    scopus 로고
    • Characterization of a naturally occurring new version of the cholesterol ester transfer protein (CETP) from small intestine
    • Alonso, A.L.; Zentella-Dehesa, A.; Mas-Oliva, J. Characterization of a naturally occurring new version of the cholesterol ester transfer protein (CETP) from small intestine. Mol. Cell. Biochem. 2003, 245, 173-182.
    • (2003) Mol. Cell. Biochem , vol.245 , pp. 173-182
    • Alonso, A.L.1    Zentella-Dehesa, A.2    Mas-Oliva, J.3
  • 15
    • 56349166514 scopus 로고    scopus 로고
    • Mechanisms of microglia accumulation in Alzheimer's disease: Therapeutic implications
    • El Khoury, J.; Luster, A.D. Mechanisms of microglia accumulation in Alzheimer's disease: therapeutic implications. Trends. Pharmacol. Sci. 2008, 29, 626-632.
    • (2008) Trends. Pharmacol. Sci , vol.29 , pp. 626-632
    • El, K.J.1    Luster, A.D.2
  • 16
    • 51149120624 scopus 로고    scopus 로고
    • Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice
    • Hickman, S.E.; Allison, E.K.; El Khoury, J. Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice. J. Neurosci. 2008, 28, 8354-8360.
    • (2008) J. Neurosci , vol.28 , pp. 8354-8360
    • Hickman, S.E.1    Allison, E.K.2    El, K.J.3
  • 18
    • 0033614679 scopus 로고    scopus 로고
    • Both oxidative stress-dependent and independent effects of amyloid beta protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction assay
    • Abe, K.; Saito, H. Both oxidative stress-dependent and independent effects of amyloid beta protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction assay. Brain Res. 1999, 830, 146-154.
    • (1999) Brain Res , vol.830 , pp. 146-154
    • Abe, K.1    Saito, H.2
  • 19
    • 0032573097 scopus 로고    scopus 로고
    • Amyloid beta peptide alters intracellular vesicle trafficking and cholesterol homeostasis
    • Liu, Y.; Peterson, D.A.; Schubert, D. Amyloid beta peptide alters intracellular vesicle trafficking and cholesterol homeostasis. Proc. Natl. Acad. Sci. USA 1998, 95, 13266-13271.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13266-13271
    • Liu, Y.1    Peterson, D.A.2    Schubert, D.3
  • 20
    • 0034598954 scopus 로고    scopus 로고
    • Nature disfavors sequences of alternating polar and non-polar amino acids: Implications for amyloidogenesis
    • Broome, B.M.; Hecht, M.H. Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis. J. Mol. Biol. 2000, 296, 961-968.
    • (2000) J. Mol. Biol , vol.296 , pp. 961-968
    • Broome, B.M.1    Hecht, M.H.2
  • 21
    • 0035055990 scopus 로고    scopus 로고
    • Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues
    • Schwartz, R.; Istrail, S.; King, J. Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues. Protein Sci. 2001, 10, 1023-1031.
    • (2001) Protein Sci , vol.10 , pp. 1023-1031
    • Schwartz, R.1    Istrail, S.2    King, J.3
  • 22
    • 0037059069 scopus 로고    scopus 로고
    • Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
    • Chiti, F.; Calamai, M.; Taddei, N.; Stefani, M.; Ramponi, G.; Dobson, C.M. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl. Acad. Sci. USA 2002, 99, 16419-16426.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16419-16426
    • Chiti, F.1    Calamai, M.2    Taddei, N.3    Stefani, M.4    Ramponi, G.5    Dobson, C.M.6
  • 24
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • Monsellier, E.; Chiti, F. Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep. 2007, 8, 737-742.
    • (2007) EMBO Rep , vol.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 25
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V.N. Natively unfolded proteins: A point where biology waits for physics. Protein Sci. 2002, 11, 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 26
    • 33749824175 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of amyloid fibril assembly
    • Wetzel, R. Kinetics and thermodynamics of amyloid fibril assembly. Acc. Chem. Res. 2006, 39, 671-679.
    • (2006) Acc. Chem. Res , vol.39 , pp. 671-679
    • Wetzel, R.1
  • 29
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic alpha-helices on membranes: Energetics of helix formation by melittin
    • Ladokhin, A.S.; White, S.H. Folding of amphipathic alpha-helices on membranes: energetics of helix formation by melittin. J. Mol. Biol. 1999, 285, 1363-1369.
    • (1999) J. Mol. Biol , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 30
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White, S.H.; Wimley, W.C. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta 1998, 1376, 339-352.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 31
    • 0038578753 scopus 로고    scopus 로고
    • Oxidative stress impairs endocytosis of the scavenger receptor class A
    • Aguilar-Gaytan, R.; Mas-Oliva, J. Oxidative stress impairs endocytosis of the scavenger receptor class A. Biochem. Biophys. Res. Commun. 2003, 305, 510-517.
    • (2003) Biochem. Biophys. Res. Commun , vol.305 , pp. 510-517
    • Aguilar-Gaytan, R.1    Mas-Oliva, J.2
  • 35
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay
    • Klunk, W.E.; Jacob, R.F.; Mason, R.P. Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay. Anal. Biochem. 1999, 266, 66-76.
    • (1999) Anal. Biochem , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.