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Volumn 99, Issue , 2017, Pages 477-482

Vitamin B12 offers neuronal cell protection by inhibiting Aβ-42 amyloid fibrillation

Author keywords

Amyloids; Cytotoxicity; Neurodegenation; Protein aggregation

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; CYANOCOBALAMIN; THIOFLAVINE; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

EID: 85014811900     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2017.03.001     Document Type: Article
Times cited : (100)

References (41)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • [1] Hardy, J., Selkoe, D.J., The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002), 353–356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 84867477898 scopus 로고    scopus 로고
    • The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization
    • [2] Hamley, I.W., The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization. Chem. Rev. 112 (2012), 5147–5192.
    • (2012) Chem. Rev. , vol.112 , pp. 5147-5192
    • Hamley, I.W.1
  • 5
    • 70349923038 scopus 로고    scopus 로고
    • Alzheimer's disease: from pathology to therapeutic approaches
    • [5] Jakob-Roetne, R., Jacobsen, H., Alzheimer's disease: from pathology to therapeutic approaches. Angew. Chem. Int. Ed. 48 (2009), 3030–3059.
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 3030-3059
    • Jakob-Roetne, R.1    Jacobsen, H.2
  • 6
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
    • [6] Selkoe, D.J., The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8 (1998), 447–453.
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 9
    • 84858984601 scopus 로고    scopus 로고
    • Unraveling the early events of amyloid β protein (Aβ) aggregation: techniques for the determination of Aβ aggregate size
    • [9] Pryor, N.E., Moss, M.A., Hestekin, C.N., Unraveling the early events of amyloid β protein (Aβ) aggregation: techniques for the determination of Aβ aggregate size. Int. J. Mol. Sci. 13 (2012), 3038–3072.
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 3038-3072
    • Pryor, N.E.1    Moss, M.A.2    Hestekin, C.N.3
  • 10
    • 77950941375 scopus 로고    scopus 로고
    • Amyloid- β fibrillogenesis: structural insight and therapeutic intervention
    • [10] DaSilva, K.A., Shaw, J.E., McLaurin, J., Amyloid- β fibrillogenesis: structural insight and therapeutic intervention. Exp. Neurol. 223 (2010), 311–321.
    • (2010) Exp. Neurol. , vol.223 , pp. 311-321
    • DaSilva, K.A.1    Shaw, J.E.2    McLaurin, J.3
  • 12
  • 14
    • 1642549173 scopus 로고
    • Molecular volumes and the Stokes-Einstein equation
    • [14] Edward, J.T., Molecular volumes and the Stokes-Einstein equation. J. Chem. Educ., 47, 1970, 261.
    • (1970) J. Chem. Educ. , vol.47 , pp. 261
    • Edward, J.T.1
  • 16
    • 85014852236 scopus 로고    scopus 로고
    • Stain: An Easier and More Sensitive Method for Amyloid Detection, Amyloid and Related Disorders
    • Springer 2015
    • [16] Picken, M.M., Herrera, G.A., Thioflavin, T., Stain: An Easier and More Sensitive Method for Amyloid Detection, Amyloid and Related Disorders. 2017, Springer, 2015, 225–227.
    • (2017) , pp. 225-227
    • Picken, M.M.1    Herrera, G.A.2    Thioflavin, T.3
  • 19
    • 84964222453 scopus 로고    scopus 로고
    • Effect of surfactants on Ra-sHSPI-A small heat shock protein from the cattle tick Rhipicephalus annulatus
    • [19] Siddiqi, M.K., Shahein, Y.E., Hussein, N., Khan, R.H., Effect of surfactants on Ra-sHSPI-A small heat shock protein from the cattle tick Rhipicephalus annulatus. J. Mol. Struct. 1119 (2016), 12–17.
    • (2016) J. Mol. Struct. , vol.1119 , pp. 12-17
    • Siddiqi, M.K.1    Shahein, Y.E.2    Hussein, N.3    Khan, R.H.4
  • 20
    • 36849078628 scopus 로고    scopus 로고
    • Insight into the kinetic of amyloid beta (amyloid beta- 42) peptide self-aggregation: elucidation of inhibitors mechanism of action
    • [20] Bartolini, M., Bertucci, C., Bolognesi, M.L., Cavalli, A., Melchiorre, C., Andrisano, V., Insight into the kinetic of amyloid beta (amyloid beta- 42) peptide self-aggregation: elucidation of inhibitors mechanism of action. Chembiochem 8 (2007), 2152–2161.
    • (2007) Chembiochem , vol.8 , pp. 2152-2161
    • Bartolini, M.1    Bertucci, C.2    Bolognesi, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 21
    • 84905708160 scopus 로고    scopus 로고
    • Gallic acid, one of the components in many plant tissues, is a potential inhibitor for insulin amyloid fibril formation
    • [21] Jayamani, J., Shanmugam, G., Gallic acid, one of the components in many plant tissues, is a potential inhibitor for insulin amyloid fibril formation. Eur. J. Med. Chem. 85 (2014), 352–358.
    • (2014) Eur. J. Med. Chem. , vol.85 , pp. 352-358
    • Jayamani, J.1    Shanmugam, G.2
  • 22
    • 84966312394 scopus 로고    scopus 로고
    • Familial mutations in fibrinogen Aα(FGA) chain identified in renal amyloidosis increase in vitro amyloidogenicity of FGA fragment
    • [22] Sivalingam, V., Patel, B.K., Familial mutations in fibrinogen Aα(FGA) chain identified in renal amyloidosis increase in vitro amyloidogenicity of FGA fragment. Biochimie 127 (2016), 44–49.
    • (2016) Biochimie , vol.127 , pp. 44-49
    • Sivalingam, V.1    Patel, B.K.2
  • 23
    • 1842790837 scopus 로고    scopus 로고
    • Aggregation of the acylphosphatase from sulfolobus solfataricus THE FOLDED AND PARTIALLY UNFOLDED STATES CAN BOTH BE PRECURSORS FOR AMYLOID FORMATION
    • [23] Plakoutsi, G., Taddei, N., Stefani, M., Chiti, F., Aggregation of the acylphosphatase from sulfolobus solfataricus THE FOLDED AND PARTIALLY UNFOLDED STATES CAN BOTH BE PRECURSORS FOR AMYLOID FORMATION. J. Biol. Chem. 279 (2004), 14111–14119.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14111-14119
    • Plakoutsi, G.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 25
    • 84984680182 scopus 로고    scopus 로고
    • Bis (indolyl) phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme
    • [25] Ramshini, H., Mannini, B., Khodayari, K., Ebrahim-Habibi, A., Moghaddasi, A.S., Tayebee, R., Chiti, F., Bis (indolyl) phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme. Eur. J. Med. Chem. 124 (2016), 361–371.
    • (2016) Eur. J. Med. Chem. , vol.124 , pp. 361-371
    • Ramshini, H.1    Mannini, B.2    Khodayari, K.3    Ebrahim-Habibi, A.4    Moghaddasi, A.S.5    Tayebee, R.6    Chiti, F.7
  • 26
    • 34548847733 scopus 로고    scopus 로고
    • U sing circular dichroism spectra to estimate protein secondary structure
    • [26] Greenfield, N.J., U sing circular dichroism spectra to estimate protein secondary structure. Nat. Protoc. 1 (2006), 2876–2890.
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 27
    • 0003786121 scopus 로고    scopus 로고
    • Circular Dichroism and the Conformational Analysis of Biomolecules
    • Springer Science & Business Media
    • [27] Fasman, G.D., Circular Dichroism and the Conformational Analysis of Biomolecules. 2013, Springer Science & Business Media.
    • (2013)
    • Fasman, G.D.1
  • 28
    • 84942871083 scopus 로고    scopus 로고
    • Unraveling comparative anti-Amyloidogenic behavior of pyrazinamide and D-cycloserine: a mechanistic biophysical insight
    • [28] Chaturvedi, S.K., Zaidi, N., Alam, P., Khan, J.M., Qadeer, A., Siddique, I.A., Asmat, S., Zaidi, Y., Khan, R.H., Unraveling comparative anti-Amyloidogenic behavior of pyrazinamide and D-cycloserine: a mechanistic biophysical insight. PLoS One, 10, 2015, e0136528.
    • (2015) PLoS One , vol.10 , pp. e0136528
    • Chaturvedi, S.K.1    Zaidi, N.2    Alam, P.3    Khan, J.M.4    Qadeer, A.5    Siddique, I.A.6    Asmat, S.7    Zaidi, Y.8    Khan, R.H.9
  • 31
    • 84907942353 scopus 로고    scopus 로고
    • Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule
    • [31] Rosen, L.E., Connell, K.B., Marqusee, S., Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule. Proc. Natl. Acad. Sci. 111 (2014), 14746–14751.
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , pp. 14746-14751
    • Rosen, L.E.1    Connell, K.B.2    Marqusee, S.3
  • 32
    • 84982189648 scopus 로고    scopus 로고
    • Anti-amyloidogenic behavior and interaction of diallylsulfide with human serum albumin
    • [32] Siddiqi, M.K., Alam, P., Chaturvedi, S.K., Khan, R.H., Anti-amyloidogenic behavior and interaction of diallylsulfide with human serum albumin. Int. J. Biol. Macromol. 92 (2016), 1220–1228.
    • (2016) Int. J. Biol. Macromol. , vol.92 , pp. 1220-1228
    • Siddiqi, M.K.1    Alam, P.2    Chaturvedi, S.K.3    Khan, R.H.4
  • 33
    • 84966700844 scopus 로고    scopus 로고
    • Binding of janus kinase inhibitor tofacitinib with human serum albumin: multi-technique approach
    • [33] Abdelhameed, A.S., Alam, P., Khan, R.H., Binding of janus kinase inhibitor tofacitinib with human serum albumin: multi-technique approach. J. Biomol. Struct. Dyn. 34 (2017), 2037–2044.
    • (2017) J. Biomol. Struct. Dyn. , vol.34 , pp. 2037-2044
    • Abdelhameed, A.S.1    Alam, P.2    Khan, R.H.3
  • 35
    • 0344490335 scopus 로고    scopus 로고
    • Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition
    • [35] Scheibel, T., Parthasarathy, R., Sawicki, G., Lin, X.-M., Jaeger, H., Lindquist, S.L., Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. Proc. Natl. Acad. Sci. 100 (2003), 4527–4532.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 4527-4532
    • Scheibel, T.1    Parthasarathy, R.2    Sawicki, G.3    Lin, X.-M.4    Jaeger, H.5    Lindquist, S.L.6
  • 36
    • 85018192829 scopus 로고    scopus 로고
    • Inhibition and degradation of amyloid beta (amyloid beta- 40) fibrillation by designed small pep-tide: a combined spectroscopy, microscopy and cell toxicity study
    • [36] Ghosh, A., Pradhan, N., Bera, S., Datta, A., Krishnamoorthy, J., Jana, N.R., Bhunia, A., Inhibition and degradation of amyloid beta (amyloid beta- 40) fibrillation by designed small pep-tide: a combined spectroscopy, microscopy and cell toxicity study. ACS Chem. Neurosci., 2017, 10.1021/acschemneuro.6b00349.
    • (2017) ACS Chem. Neurosci.
    • Ghosh, A.1    Pradhan, N.2    Bera, S.3    Datta, A.4    Krishnamoorthy, J.5    Jana, N.R.6    Bhunia, A.7
  • 37
    • 84955565065 scopus 로고    scopus 로고
    • Curcumin attenuates amyloid-β aggregate toxicity and modulates amyloid-β aggregation pathway
    • [37] Thapa, A., Jett, S.D., Chi, E.Y., Curcumin attenuates amyloid-β aggregate toxicity and modulates amyloid-β aggregation pathway. ACS Chem. Neurosci. 7 (2015), 56–68.
    • (2015) ACS Chem. Neurosci. , vol.7 , pp. 56-68
    • Thapa, A.1    Jett, S.D.2    Chi, E.Y.3
  • 38
    • 70350348150 scopus 로고    scopus 로고
    • Inhibition of beta amyloid beta- 40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots
    • [38] Xiao, L., Zhao, D., Chan, W.-H., Choi, M.M.F., Li, H.-W., Inhibition of beta amyloid beta- 40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots. Biomaterials 31 (2010), 91–98.
    • (2010) Biomaterials , vol.31 , pp. 91-98
    • Xiao, L.1    Zhao, D.2    Chan, W.-H.3    Choi, M.M.F.4    Li, H.-W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.