메뉴 건너뛰기




Volumn 10, Issue 3, 2015, Pages 766-774

Binding of human proteins to amyloid-β protofibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; APOLIPOPROTEIN E; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; PLASMA PROTEIN; PROTEIN AGGREGATE; PROTEIN BINDING; PROTEIN CEREBROSPINAL FLUID LEVEL; RECOMBINANT PROTEIN;

EID: 84925355903     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb5008663     Document Type: Article
Times cited : (25)

References (44)
  • 1
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A. and Higgins, G. A. (1992) Alzheimer's disease: the amyloid cascade hypothesis Science 256, 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 2
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - A decade of discovery
    • Walsh, D. M. and Selkoe, D. J. (2007) Aβ oligomers-a decade of discovery J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 7
    • 35349010059 scopus 로고    scopus 로고
    • The nanoparticle-protein complex as a biological entity; A complex fluids and surface science challenge for the 21st century
    • Lynch, I., Cedervall, T., Lundqvist, M., Cabaleiro-Lago, C., Linse, S., and Dawson, K. A. (2007) The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century Adv. Colloid Interface Sci. 134-135, 167-174
    • (2007) Adv. Colloid Interface Sci. , vol.134-135 , pp. 167-174
    • Lynch, I.1    Cedervall, T.2    Lundqvist, M.3    Cabaleiro-Lago, C.4    Linse, S.5    Dawson, K.A.6
  • 9
    • 84879773805 scopus 로고    scopus 로고
    • Amyloid-β protofibrils: Size, morphology and synaptotoxicity of an engineered mimic
    • Dubnovitsky, A., Sandberg, A., Rahman, M. M., Benilova, I., Lendel, C., and Hard, T. (2013) Amyloid-β protofibrils: size, morphology and synaptotoxicity of an engineered mimic PLoS One 8, e66101
    • (2013) PLoS One , vol.8 , pp. 66101
    • Dubnovitsky, A.1    Sandberg, A.2    Rahman, M.M.3    Benilova, I.4    Lendel, C.5    Hard, T.6
  • 11
    • 0036269973 scopus 로고    scopus 로고
    • Proteomics of the eukaryotic transcription machinery: Identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry
    • Sanders, S. L., Jennings, J., Canutescu, A., Link, A. J., and Weil, P. A. (2002) Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry Mol. Cell. Biol. 22, 4723-4738
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4723-4738
    • Sanders, S.L.1    Jennings, J.2    Canutescu, A.3    Link, A.J.4    Weil, P.A.5
  • 12
    • 77949423619 scopus 로고    scopus 로고
    • Cerebrospinal fluid and plasma biomarkers in Alzheimer disease
    • Blennow, K., Hampel, H., Weiner, M., and Zetterberg, H. (2010) Cerebrospinal fluid and plasma biomarkers in Alzheimer disease Nat. Rev. Neurol. 6, 131-144
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 131-144
    • Blennow, K.1    Hampel, H.2    Weiner, M.3    Zetterberg, H.4
  • 13
    • 84864602596 scopus 로고    scopus 로고
    • Search for amyloid-binding proteins by affinity chromatography
    • Calero, M., Rostagno, A., and Ghiso, J. (2012) Search for amyloid-binding proteins by affinity chromatography Methods Mol. Biol. 849, 213-223
    • (2012) Methods Mol. Biol. , vol.849 , pp. 213-223
    • Calero, M.1    Rostagno, A.2    Ghiso, J.3
  • 14
    • 0030592330 scopus 로고    scopus 로고
    • Alpha 1-antichymotrypsin interaction with Aβ(1-42) does not inhibit fibril formation but attenuates the peptide toxicity
    • Aksenov, M. Y., Aksenova, M. V., Carney, J. M., and Butterfield, D. A. (1996) Alpha 1-antichymotrypsin interaction with Aβ(1-42) does not inhibit fibril formation but attenuates the peptide toxicity Neurosci. Lett. 217, 117-120
    • (1996) Neurosci. Lett. , vol.217 , pp. 117-120
    • Aksenov, M.Y.1    Aksenova, M.V.2    Carney, J.M.3    Butterfield, D.A.4
  • 15
    • 0035163413 scopus 로고    scopus 로고
    • ApoE protects cortical neurones against neurotoxicity induced by the non-fibrillar C-terminal domain of the amyloid-β peptide
    • Drouet, B., Fifre, A., Pincon-Raymond, M., Vandekerckhove, J., Rosseneu, M., Gueant, J. L., Chambaz, J., and Pillot, T. (2001) ApoE protects cortical neurones against neurotoxicity induced by the non-fibrillar C-terminal domain of the amyloid-β peptide J. Neurochem. 76, 117-127
    • (2001) J. Neurochem. , vol.76 , pp. 117-127
    • Drouet, B.1    Fifre, A.2    Pincon-Raymond, M.3    Vandekerckhove, J.4    Rosseneu, M.5    Gueant, J.L.6    Chambaz, J.7    Pillot, T.8
  • 17
    • 38049107388 scopus 로고    scopus 로고
    • Complement component C1q inhibits β-amyloid- and serum amyloid P-induced neurotoxicity via caspase- and calpain-independent mechanisms
    • Pisalyaput, K. and Tenner, A. J. (2008) Complement component C1q inhibits β-amyloid- and serum amyloid P-induced neurotoxicity via caspase- and calpain-independent mechanisms J. Neurochem. 104, 696-707
    • (2008) J. Neurochem. , vol.104 , pp. 696-707
    • Pisalyaput, K.1    Tenner, A.J.2
  • 18
    • 34547823043 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
    • Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., and Wilson, M. R. (2007) The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures FASEB J. 21, 2312-2322
    • (2007) FASEB J. , vol.21 , pp. 2312-2322
    • Yerbury, J.J.1    Poon, S.2    Meehan, S.3    Thompson, B.4    Kumita, J.R.5    Dobson, C.M.6    Wilson, M.R.7
  • 19
    • 79955663093 scopus 로고    scopus 로고
    • High ability of apolipoprotein E4 to stabilize amyloid-β peptide oligomers, the pathological entities responsible for Alzheimer's disease
    • Cerf, E., Gustot, A., Goormaghtigh, E., Ruysschaert, J. M., and Raussens, V. (2011) High ability of apolipoprotein E4 to stabilize amyloid-β peptide oligomers, the pathological entities responsible for Alzheimer's disease FASEB J. 25, 1585-1595
    • (2011) FASEB J. , vol.25 , pp. 1585-1595
    • Cerf, E.1    Gustot, A.2    Goormaghtigh, E.3    Ruysschaert, J.M.4    Raussens, V.5
  • 21
    • 34247506244 scopus 로고    scopus 로고
    • Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins e and J in the mouse central nervous system
    • Bell, R. D., Sagare, A. P., Friedman, A. E., Bedi, G. S., Holtzman, D. M., Deane, R., and Zlokovic, B. V. (2007) Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins E and J in the mouse central nervous system J. Cereb. Blood Flow Metab. 27, 909-918
    • (2007) J. Cereb. Blood Flow Metab. , vol.27 , pp. 909-918
    • Bell, R.D.1    Sagare, A.P.2    Friedman, A.E.3    Bedi, G.S.4    Holtzman, D.M.5    Deane, R.6    Zlokovic, B.V.7
  • 22
    • 79955051063 scopus 로고    scopus 로고
    • Linking lipids to Alzheimer's disease: Cholesterol and beyond
    • Di Paolo, G. and Kim, T. W. (2011) Linking lipids to Alzheimer's disease: cholesterol and beyond Nat. Rev. Neurosci. 12, 284-296
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 284-296
    • Di Paolo, G.1    Kim, T.W.2
  • 27
    • 0019993831 scopus 로고
    • Immunoglobulins and complement factors in senile plaques. An immunoperoxidase study
    • Eikelenboom, P. and Stam, F. C. (1982) Immunoglobulins and complement factors in senile plaques. An immunoperoxidase study Acta Neuropathol. 57, 239-242
    • (1982) Acta Neuropathol. , vol.57 , pp. 239-242
    • Eikelenboom, P.1    Stam, F.C.2
  • 29
    • 49749220896 scopus 로고
    • Parahaemophilia; Haemorrhagic diathesis due to absence of a previously unknown clotting factor
    • Owren, P. A. (1947) Parahaemophilia; haemorrhagic diathesis due to absence of a previously unknown clotting factor Lancet 1, 446-448
    • (1947) Lancet , vol.1 , pp. 446-448
    • Owren, P.A.1
  • 33
    • 78649842470 scopus 로고    scopus 로고
    • The diverse functions of GAPDH: Views from different subcellular compartments
    • Tristan, C., Shahani, N., Sedlak, T. W., and Sawa, A. (2011) The diverse functions of GAPDH: views from different subcellular compartments Cell Signal 23, 317-323
    • (2011) Cell Signal , vol.23 , pp. 317-323
    • Tristan, C.1    Shahani, N.2    Sedlak, T.W.3    Sawa, A.4
  • 34
    • 13844318224 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases
    • Chuang, D. M., Hough, C., and Senatorov, V. V. (2005) Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases Annu. Rev. Pharmacol. Toxicol. 45, 269-290
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 269-290
    • Chuang, D.M.1    Hough, C.2    Senatorov, V.V.3
  • 35
    • 0034660602 scopus 로고    scopus 로고
    • Glutamine synthetase, hemoglobin alpha-chain, and macrophage migration inhibitory factor binding to amyloid β-protein: Their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation
    • Oyama, R., Yamamoto, H., and Titani, K. (2000) Glutamine synthetase, hemoglobin alpha-chain, and macrophage migration inhibitory factor binding to amyloid β-protein: their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation Biochim. Biophys. Acta 1479, 91-102
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 91-102
    • Oyama, R.1    Yamamoto, H.2    Titani, K.3
  • 36
    • 47249104380 scopus 로고    scopus 로고
    • Characterization of the interaction between Aβ1-42 and glyceraldehyde phosphodehydrogenase
    • Verdier, Y., Foldi, I., Sergeant, N., Fulop, L., Penke, Z., Janaky, T., Szucs, M., and Penke, B. (2008) Characterization of the interaction between Aβ1-42 and glyceraldehyde phosphodehydrogenase J. Pept Sci. 14, 755-762
    • (2008) J. Pept Sci. , vol.14 , pp. 755-762
    • Verdier, Y.1    Foldi, I.2    Sergeant, N.3    Fulop, L.4    Penke, Z.5    Janaky, T.6    Szucs, M.7    Penke, B.8
  • 37
    • 28744448949 scopus 로고    scopus 로고
    • Amyloid-β induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease
    • Cumming, R. C. and Schubert, D. (2005) Amyloid-β induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease FASEB J. 19, 2060-2062
    • (2005) FASEB J. , vol.19 , pp. 2060-2062
    • Cumming, R.C.1    Schubert, D.2
  • 38
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang, Q., Woltjer, R. L., Cimino, P. J., Pan, C., Montine, K. S., Zhang, J., and Montine, T. J. (2005) Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein FASEB J. 19, 869-871
    • (2005) FASEB J. , vol.19 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6    Montine, T.J.7
  • 39
    • 0035157875 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan expression in cerebrovascular amyloid beta deposits in Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis (Dutch) brains
    • van Horssen, J., Otte-Holler, I., David, G., Maat-Schieman, M. L., van den Heuvel, L. P., Wesseling, P., de Waal, R. M., and Verbeek, M. M. (2001) Heparan sulfate proteoglycan expression in cerebrovascular amyloid beta deposits in Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis (Dutch) brains Acta Neuropathol. 102, 604-614
    • (2001) Acta Neuropathol. , vol.102 , pp. 604-614
    • Van Horssen, J.1    Otte-Holler, I.2    David, G.3    Maat-Schieman, M.L.4    Van Den Heuvel, L.P.5    Wesseling, P.6    De Waal, R.M.7    Verbeek, M.M.8
  • 41
    • 84863987464 scopus 로고    scopus 로고
    • Inhibition of amyloid formation
    • Hard, T. and Lendel, C. (2012) Inhibition of amyloid formation J. Mol. Biol. 421, 441-465
    • (2012) J. Mol. Biol. , vol.421 , pp. 441-465
    • Hard, T.1    Lendel, C.2
  • 42
  • 43
    • 32544435900 scopus 로고    scopus 로고
    • Association between CSF biomarkers and incipient Alzheimer's disease in patients with mild cognitive impairment: A follow-up study
    • Hansson, O., Zetterberg, H., Buchhave, P., Londos, E., Blennow, K., and Minthon, L. (2006) Association between CSF biomarkers and incipient Alzheimer's disease in patients with mild cognitive impairment: a follow-up study Lancet Neurol. 5, 228-234
    • (2006) Lancet Neurol. , vol.5 , pp. 228-234
    • Hansson, O.1    Zetterberg, H.2    Buchhave, P.3    Londos, E.4    Blennow, K.5    Minthon, L.6
  • 44
    • 84856873078 scopus 로고    scopus 로고
    • Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly
    • Abelein, A., Bolognesi, B., Dobson, C. M., Graslund, A., and Lendel, C. (2012) Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly Biochemistry 51, 126-137
    • (2012) Biochemistry , vol.51 , pp. 126-137
    • Abelein, A.1    Bolognesi, B.2    Dobson, C.M.3    Graslund, A.4    Lendel, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.