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Volumn 382, Issue 2, 2008, Pages 147-149

Modification of amyloid-β(1-40) by a protease inhibitor creates risk of error in mass spectrometric quantitation of amyloid-β(1-42)

Author keywords

[No Author keywords available]

Indexed keywords

DRUG PRODUCTS; FLUORINE COMPOUNDS; GLYCOPROTEINS; MAMMALS; MASS SPECTROMETRY;

EID: 52049124015     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.07.033     Document Type: Article
Times cited : (5)

References (5)
  • 1
    • 18244389436 scopus 로고    scopus 로고
    • The role of cerebral amyloid β accumulation in common forms of Alzheimer disease
    • Gandy S. The role of cerebral amyloid β accumulation in common forms of Alzheimer disease. J. Clin. Invest. 115 (2005) 1121-1129
    • (2005) J. Clin. Invest. , vol.115 , pp. 1121-1129
    • Gandy, S.1
  • 2
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid β protein in cultured cell media. Detection and quantification of amyloid β protein and variants by immunoprecipitation-mass spectrometry
    • Wang R., Sweeney D., Gandy S.E., and Sisodia S.S. The profile of soluble amyloid β protein in cultured cell media. Detection and quantification of amyloid β protein and variants by immunoprecipitation-mass spectrometry. J. Biol. Chem. 271 (1996) 31894-31902
    • (1996) J. Biol. Chem. , vol.271 , pp. 31894-31902
    • Wang, R.1    Sweeney, D.2    Gandy, S.E.3    Sisodia, S.S.4
  • 3
    • 33847105164 scopus 로고    scopus 로고
    • Dominance of amyloid precursor protein sequence over host cell secretases in determining β-amyloid profiles studies of interspecies variation and drug action by internally standardized immunoprecipitation/mass spectrometry
    • Du P., Wood K.M., Rosner M.H., Cunningham D., Tate B., and Geoghegan K.F. Dominance of amyloid precursor protein sequence over host cell secretases in determining β-amyloid profiles studies of interspecies variation and drug action by internally standardized immunoprecipitation/mass spectrometry. J. Pharmacol. Exp. Ther. 320 (2007) 1144-1152
    • (2007) J. Pharmacol. Exp. Ther. , vol.320 , pp. 1144-1152
    • Du, P.1    Wood, K.M.2    Rosner, M.H.3    Cunningham, D.4    Tate, B.5    Geoghegan, K.F.6
  • 4
    • 52049114529 scopus 로고
    • Frequent undesired covalent modification of proteins by the protease inhibitor 4-(2-aminoethyl)-benzenesulfonylfluoride (AEBSF, Pefabloc)
    • Bourell J.H., Stults J.T., Gonzalez T., Pearce K., and Vandlen R.L. Frequent undesired covalent modification of proteins by the protease inhibitor 4-(2-aminoethyl)-benzenesulfonylfluoride (AEBSF, Pefabloc). Protein Sci. 4 Suppl. 2 (1995) 148
    • (1995) Protein Sci. , vol.4 , Issue.SUPPL. 2 , pp. 148
    • Bourell, J.H.1    Stults, J.T.2    Gonzalez, T.3    Pearce, K.4    Vandlen, R.L.5
  • 5
    • 38749146267 scopus 로고    scopus 로고
    • Qualitative and quantitative characterization of the amyloid β peptide (Aβ) population in biological matrices using an immunoprecipitation-LC/MS assay
    • Ford M.J., Cantone J.L., Polson C., Toyn J.H., Meredith J.E., and Drexler D.M. Qualitative and quantitative characterization of the amyloid β peptide (Aβ) population in biological matrices using an immunoprecipitation-LC/MS assay. J. Neurosci. Methods 168 (2008) 465-474
    • (2008) J. Neurosci. Methods , vol.168 , pp. 465-474
    • Ford, M.J.1    Cantone, J.L.2    Polson, C.3    Toyn, J.H.4    Meredith, J.E.5    Drexler, D.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.