메뉴 건너뛰기




Volumn 6, Issue 2, 2015, Pages 306-315

Hyperspectral imaging signatures detect amyloidopathy in alzheimers mouse retina well before onset of cognitive decline

Author keywords

advanced glycation end products; Alzheimers disease; Hyperspectral imaging (HSI); methylglyoxal; amyloid peptide

Indexed keywords

NOOTROPIC AGENT; PSI GLUTATHIONE; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); AMYLOID PRECURSOR PROTEIN; APP PROTEIN, HUMAN; PEPTIDE FRAGMENT; PRESENILIN 1; PSEN1 PROTEIN, HUMAN;

EID: 84923253222     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn500242z     Document Type: Article
Times cited : (88)

References (42)
  • 1
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • Herczenik, E. and Gebbink, M. F. (2008) Molecular and cellular aspects of protein misfolding and disease FASEB J. 22, 2115-2133
    • (2008) FASEB J. , vol.22 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.2
  • 2
    • 28544437885 scopus 로고    scopus 로고
    • Quality control of protein folding in extracellular space
    • Yerbury, J. J., Stewart, E. M., Wyatt, A. R., and Wilson, M. R. (2005) Quality control of protein folding in extracellular space EMBO Rep. 6, 1131-1136
    • (2005) EMBO Rep. , vol.6 , pp. 1131-1136
    • Yerbury, J.J.1    Stewart, E.M.2    Wyatt, A.R.3    Wilson, M.R.4
  • 5
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J. (2003) Folding proteins in fatal ways Nature 426, 900-904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 6
    • 84876945450 scopus 로고    scopus 로고
    • The cell biology of prion-like spread of protein aggregates: Mechanisms and implication in neurodegeneration
    • Costanzo, M. and Zurzolo, C. (2013) The cell biology of prion-like spread of protein aggregates: Mechanisms and implication in neurodegeneration Biochem. J. 452, 1-17
    • (2013) Biochem. J. , vol.452 , pp. 1-17
    • Costanzo, M.1    Zurzolo, C.2
  • 7
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimers and Parkinsons diseases
    • Selkoe, D. J. (2004) Cell biology of protein misfolding: The examples of Alzheimers and Parkinsons diseases Nat. Cell Biol. 6, 1054-1061
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 9
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers-A novel pathway of amyloid formation
    • Modler, A. J., Gast, K., Lutsch, G., and Damaschun, G. (2003) Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation J. Mol. Biol. 325, 135-148
    • (2003) J. Mol. Biol. , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 10
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate J. Biol. Chem. 272, 22364-22372
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 12
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid beta-protein assembly and Alzheimers disease
    • Roychaudhuri, R., Yang, M., Hoshi, M. M., and Teplow, D. B. (2009) Amyloid beta-protein assembly and Alzheimers disease J. Biol. Chem. 284, 4749-4753
    • (2009) J. Biol. Chem. , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 13
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimers disease: Current status
    • Kagan, B. L., Hirakura, Y., Azimov, R., Azimova, R., and Lin, M. C. (2002) The channel hypothesis of Alzheimers disease: current status Peptides 23, 1311-1315
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.C.5
  • 14
    • 77956269194 scopus 로고    scopus 로고
    • Hollow core of Alzheimers Aβ42 amyloid observed by cryoEM is relevant at physiological pH
    • Miller, Y., Ma, B., Tsai, C. J., and Nussinov, R. (2010) Hollow core of Alzheimers Aβ42 amyloid observed by cryoEM is relevant at physiological pH Proc. Natl. Acad. Sci. U. S. A. 107, 14128-14133
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 14128-14133
    • Miller, Y.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 15
    • 84897082403 scopus 로고    scopus 로고
    • Soluble beta-amyloid peptides, but not insoluble fibrils, have specific effect on neuronal microRNA expression
    • Li, J. J., Dolios, G., Wang, R., and Liao, F. F. (2014) Soluble beta-amyloid peptides, but not insoluble fibrils, have specific effect on neuronal microRNA expression PLoS One 9 e90770
    • (2014) PLoS One , vol.9 , pp. 90770
    • Li, J.J.1    Dolios, G.2    Wang, R.3    Liao, F.F.4
  • 16
    • 77955367175 scopus 로고    scopus 로고
    • Involvement of beta-amyloid in the etiology of Alzheimers disease
    • Tomiyama, T. (2010) Involvement of beta-amyloid in the etiology of Alzheimers disease Brain Nerve 62, 691-699
    • (2010) Brain Nerve , vol.62 , pp. 691-699
    • Tomiyama, T.1
  • 19
    • 76649138290 scopus 로고    scopus 로고
    • Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status
    • Groenning, M. (2010) Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status J. Chem. Biol. 3, 1-18
    • (2010) J. Chem. Biol. , vol.3 , pp. 1-18
    • Groenning, M.1
  • 20
    • 77958062569 scopus 로고    scopus 로고
    • Label-free high-throughput screening assay for inhibitors of Alzheimers amyloid-beta peptide aggregation based on MALDI MS
    • Zovo, K., Helk, E., Karafin, A., Tougu, V., and Palumaa, P. (2010) Label-free high-throughput screening assay for inhibitors of Alzheimers amyloid-beta peptide aggregation based on MALDI MS Anal. Chem. 82, 8558-8565
    • (2010) Anal. Chem. , vol.82 , pp. 8558-8565
    • Zovo, K.1    Helk, E.2    Karafin, A.3    Tougu, V.4    Palumaa, P.5
  • 21
    • 84869016210 scopus 로고    scopus 로고
    • A novel inhibitor of amyloid β (Aβ) peptide aggregation: From high throughput screening to efficacy in an animal model of Alzheimers disease
    • McKoy, A. F., Chen, J., Schupbach, T., and Hecht, M. H. (2012) A novel inhibitor of amyloid β (Aβ) peptide aggregation: from high throughput screening to efficacy in an animal model of Alzheimers disease J. Biol. Chem. 287, 38992-39000
    • (2012) J. Biol. Chem. , vol.287 , pp. 38992-39000
    • McKoy, A.F.1    Chen, J.2    Schupbach, T.3    Hecht, M.H.4
  • 23
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V., and Lee, J. M. (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide Proc. Natl. Acad. Sci. U. S. A. 106, 20324-20329
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 24
    • 84871749175 scopus 로고    scopus 로고
    • Differential Regulation of Amyloid-β Endocytic Trafficking and Lysosomal Degradation by Apolipoprotein e Isoforms
    • Li, J., Kanekiyo, T., Shinohara, M., Zhang, Y., LaDu, M. J., Xu, H., and Bu, G. (2012) Differential Regulation of Amyloid-β Endocytic Trafficking and Lysosomal Degradation by Apolipoprotein E Isoforms J. Biol. Chem. 287, 44593-44601
    • (2012) J. Biol. Chem. , vol.287 , pp. 44593-44601
    • Li, J.1    Kanekiyo, T.2    Shinohara, M.3    Zhang, Y.4    Ladu, M.J.5    Xu, H.6    Bu, G.7
  • 25
    • 0345929645 scopus 로고
    • Absorption of Scattered Light in Colloidal Systems of Aggregated Particles
    • Quinten, M. and Stier, J. (1995) Absorption of Scattered Light in Colloidal Systems of Aggregated Particles Colloid Polym. Sci. 273, 233-241
    • (1995) Colloid Polym. Sci. , vol.273 , pp. 233-241
    • Quinten, M.1    Stier, J.2
  • 26
    • 80053335788 scopus 로고    scopus 로고
    • Optical Trapping for the Characterization of Amyloid-Beta Aggregation Kinetics
    • Veloso, A. J., Yoshikawa, H., Cheng, X. R., Tamiya, E., and Kerman, K. (2011) Optical Trapping for the Characterization of Amyloid-Beta Aggregation Kinetics Analyst 136, 4164-4167
    • (2011) Analyst , vol.136 , pp. 4164-4167
    • Veloso, A.J.1    Yoshikawa, H.2    Cheng, X.R.3    Tamiya, E.4    Kerman, K.5
  • 29
    • 77957142844 scopus 로고    scopus 로고
    • Vitamin C and urea inhibit the formation of advanced glycation end products in vitro
    • Subratty, A. H., Aukburally, N., Jowaheer, V., and Joonus, N. (2010) Vitamin C and urea inhibit the formation of advanced glycation end products in vitro Nutr. Food Sci. 40, 456-465
    • (2010) Nutr. Food Sci. , vol.40 , pp. 456-465
    • Subratty, A.H.1    Aukburally, N.2    Jowaheer, V.3    Joonus, N.4
  • 31
    • 78650832181 scopus 로고    scopus 로고
    • Identification of amyloid plaques in retinas from Alzheimers patients and noninvasive in vivo optical imaging of retinal plaques in a mouse model
    • Koronyo-Hamaoui, M., Koronyo, Y., Ljubimov, A. V., Miller, C. A., Ko, M. K., Black, K. L., Schwartz, M., and Farkas, D. L. (2011) Identification of amyloid plaques in retinas from Alzheimers patients and noninvasive in vivo optical imaging of retinal plaques in a mouse model Neuroimage 54, S204-S217
    • (2011) Neuroimage , vol.54 , pp. 204-S217
    • Koronyo-Hamaoui, M.1    Koronyo, Y.2    Ljubimov, A.V.3    Miller, C.A.4    Ko, M.K.5    Black, K.L.6    Schwartz, M.7    Farkas, D.L.8
  • 33
  • 34
    • 34249298364 scopus 로고    scopus 로고
    • Abnormal retinal thickness in patients with mild cognitive impairment and Alzheimers disease
    • Paquet, C., Boissonnot, M., Roger, F., Dighiero, P., Gil, R., and Hugon, J. (2007) Abnormal retinal thickness in patients with mild cognitive impairment and Alzheimers disease Neurosci. Lett. 420, 97-99
    • (2007) Neurosci. Lett. , vol.420 , pp. 97-99
    • Paquet, C.1    Boissonnot, M.2    Roger, F.3    Dighiero, P.4    Gil, R.5    Hugon, J.6
  • 37
    • 84874074927 scopus 로고    scopus 로고
    • Restoration of glyoxalase enzyme activity precludes cognitive dysfunction in a mouse model of Alzheimers disease
    • More, S. S., Vartak, A. P., and Vince, R. (2013) Restoration of glyoxalase enzyme activity precludes cognitive dysfunction in a mouse model of Alzheimers disease ACS Chem. Neurosci. 4, 330-338
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 330-338
    • More, S.S.1    Vartak, A.P.2    Vince, R.3
  • 38
    • 0021173996 scopus 로고
    • Developments of a water-maze procedure for studying spatial learning in the rat
    • Morris, R. (1984) Developments of a water-maze procedure for studying spatial learning in the rat J. Neurosci. Methods 11, 47-60
    • (1984) J. Neurosci. Methods , vol.11 , pp. 47-60
    • Morris, R.1
  • 40
    • 15944378854 scopus 로고    scopus 로고
    • An analysis of spectral metrics for hyperspectral image processing
    • IEEE International, Piscataway, NJ
    • Robila, S. A. (2004) An analysis of spectral metrics for hyperspectral image processing. Geoscience and Remote Sensing Symposium, IGARSS 04. Proceedings. 2004, Vol. 5, pp 3233 - 3236, IEEE International, Piscataway, NJ.
    • (2004) Geoscience and Remote Sensing Symposium, IGARSS 04. Proceedings. 2004 , vol.5 , pp. 3233-3236
    • Robila, S.A.1
  • 41
    • 84873107891 scopus 로고    scopus 로고
    • Evaluation of similarity measure methods for hyperspectral remote sensing data
    • IEEE International, Piscataway, NJ
    • Zhang, J., Zhu, W., Wang, L., and Jiang, N. (2012) Evaluation of similarity measure methods for hyperspectral remote sensing data. Geoscience and Remote Sensing Symposium (IGARSS), 2012, pp 4138 - 4141, IEEE International, Piscataway, NJ.
    • (2012) Geoscience and Remote Sensing Symposium (IGARSS), 2012 , pp. 4138-4141
    • Zhang, J.1    Zhu, W.2    Wang, L.3    Jiang, N.4
  • 42
    • 77955860340 scopus 로고    scopus 로고
    • Inducible gene targeting in the neonatal vasculature and analysis of retinal angiogenesis in mice
    • Pitulescu, M. E., Schmidt, I., Benedito, R., and Adams, R. H. (2010) Inducible gene targeting in the neonatal vasculature and analysis of retinal angiogenesis in mice Nat. Protoc. 5, 1518-1534
    • (2010) Nat. Protoc. , vol.5 , pp. 1518-1534
    • Pitulescu, M.E.1    Schmidt, I.2    Benedito, R.3    Adams, R.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.