메뉴 건너뛰기




Volumn 53, Issue 1, 2006, Pages 87-91

Congo red interaction with α-proteins

Author keywords

Congo red; Dye binding; Native proteins; Oligomerization

Indexed keywords


EID: 33645227600     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2006_3366     Document Type: Article
Times cited : (29)

References (27)
  • 1
    • 3543145525 scopus 로고    scopus 로고
    • Determination of the dissociation constant and stoichiometry of a complex of the protein Interferon α-2b with Cibacron Blue F3G-A
    • Bumeliene Zh, Sereikaite J, Bumelis V-A, Smimovas V, Gedminiene G, Braziunaite L, Bajorunaite E (2003) Determination of the dissociation constant and stoichiometry of a complex of the protein Interferon α-2b with Cibacron Blue F3G-A. J Anal Chem 58: 1038-1041.
    • (2003) J Anal Chem , vol.58 , pp. 1038-1041
    • Bumeliene, Zh.1    Sereikaite, J.2    Bumelis, V.-A.3    Smimovas, V.4    Gedminiene, G.5    Braziunaite, L.6    Bajorunaite, E.7
  • 2
    • 1542301571 scopus 로고    scopus 로고
    • Diseases of protein conformation: What do in vitro experiments tell us about in vivo diseases
    • Buxbaum JN (2003) Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases. Trends Biochem Sci 28: 585-592.
    • (2003) Trends Biochem Sci , vol.28 , pp. 585-592
    • Buxbaum, J.N.1
  • 5
    • 0001016442 scopus 로고
    • Triazines from formaldehyde and nitriles
    • Gresham TL, Steadman TR (1949) Triazines from formaldehyde and nitriles. J Am Chem Soc 71: 1872-1873.
    • (1949) J Am Chem Soc , vol.71 , pp. 1872-1873
    • Gresham, T.L.1    Steadman, T.R.2
  • 6
    • 19944406829 scopus 로고    scopus 로고
    • Template-directed self-assembly and growth of insulin amyloid fibrils
    • Ha C, Park CB (2005) Template-directed self-assembly and growth of insulin amyloid fibrils. Biotechnol Bioeng 90: 848-855.
    • (2005) Biotechnol Bioeng , vol.90 , pp. 848-855
    • Ha, C.1    Park, C.B.2
  • 8
    • 0037178811 scopus 로고    scopus 로고
    • Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein
    • Kim YS, Randolph TW, Stevens FJ, Carpenter JF (2002) Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. J Biol Chem 277: 27240-27246.
    • (2002) J Biol Chem , vol.277 , pp. 27240-27246
    • Kim, Y.S.1    Randolph, T.W.2    Stevens, F.J.3    Carpenter, J.F.4
  • 9
    • 0038532258 scopus 로고    scopus 로고
    • Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation
    • Kim YS, Randolph TW, Manning MC, Stevens FJ, Carpenter JF (2003) Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J Biol Chem 278: 10842-10850.
    • (2003) J Biol Chem , vol.278 , pp. 10842-10850
    • Kim, Y.S.1    Randolph, T.W.2    Manning, M.C.3    Stevens, F.J.4    Carpenter, J.F.5
  • 10
    • 0024363054 scopus 로고
    • Two simple methods for quantifying low-affinity dye-substrate binding
    • Klunk WE, Pettegrew JW, Abraham DJ (1989) Two simple methods for quantifying low-affinity dye-substrate binding. J Histochem Cytochem 37: 1293-1297.
    • (1989) J Histochem Cytochem , vol.37 , pp. 1293-1297
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 11
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid β-peptide (Aβ) aggregation using the Congo red-Aβ (CR-Aβ) spectrophotometric assay
    • Klunk WE, Jacob RF, Mason RP (1999) Quantifying amyloid β-peptide (Aβ) aggregation using the Congo red-Aβ (CR-Aβ) spectrophotometric assay. Anal Biochem 266: 66-76.
    • (1999) Anal Biochem , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 12
    • 0037032413 scopus 로고    scopus 로고
    • Amyloid formation of native folded protein induced by peptide-based graft copolymer
    • Koga T, Taguchi K, Kogiso M, Kobuke Y, Kinoshita T, Higuchi M (2002) Amyloid formation of native folded protein induced by peptide-based graft copolymer. FEBS Lett 531: 137-140.
    • (2002) FEBS Lett , vol.531 , pp. 137-140
    • Koga, T.1    Taguchi, K.2    Kogiso, M.3    Kobuke, Y.4    Kinoshita, T.5    Higuchi, M.6
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0034826292 scopus 로고    scopus 로고
    • Self-oligomerization and protein aggregation of α-synuclein in the presence of Coomassie Brilliant Blue
    • Lee D, Lee EK, Lee JH, Chang CS, Paik SR (2001) Self-oligomerization and protein aggregation of α-synuclein in the presence of Coomassie Brilliant Blue. Eur J Biochem 268: 295-301.
    • (2001) Eur J Biochem , vol.268 , pp. 295-301
    • Lee, D.1    Lee, E.K.2    Lee, J.H.3    Chang, C.S.4    Paik, S.R.5
  • 17
    • 0342547156 scopus 로고    scopus 로고
    • Analysis of protein aggregates by combination of cross-linking reactions and chromatographic separations
    • Loster K, Josic D (1997) Analysis of protein aggregates by combination of cross-linking reactions and chromatographic separations. J Chromatogr B 699: 439-461.
    • (1997) J Chromatogr B , vol.699 , pp. 439-461
    • Loster, K.1    Josic, D.2
  • 18
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson M (2004) Techniques to study amyloid fibril formation in vitro. Methods 34: 151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.1
  • 21
  • 22
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado M, Merkel JS, Regan L (2000) A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc Natl Acad Sci 97: 8979-8984.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 23
    • 32544445162 scopus 로고    scopus 로고
    • Examination of dye-protein interaction by gel-permeation chromatography
    • Sereikaite J, Bumelis VA (2006) Examination of dye-protein interaction by gel-permeation chromatography. Biomed Chromatogr 20: 195-199.
    • (2006) Biomed Chromatogr , vol.20 , pp. 195-199
    • Sereikaite, J.1    Bumelis, V.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.