메뉴 건너뛰기




Volumn 73, Issue 6, 2009, Pages 994-995

Anti-protein aggregation is a potential target for preventing delayed neuronal death after transient ischemia

Author keywords

[No Author keywords available]

Indexed keywords

4 PHENYLBUTYRIC ACID; AMINO ACID DERIVATIVE; BINDING PROTEIN; CHAPERONE; GELDANAMYCIN; GLYCINE ETHYL ESTER; POLYQ BINDING PEPTIDE; PROTEASOME; TREHALOSE; UNCLASSIFIED DRUG;

EID: 70449706439     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2008.10.041     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0037153037 scopus 로고    scopus 로고
    • Transient ischemic attack - proposal for a new definition
    • Albers G.W., Caplan L.R., Coull B., et al. Transient ischemic attack - proposal for a new definition. N Engl J Med 347 21 (2002) 1713-1716
    • (2002) N Engl J Med , vol.347 , Issue.21 , pp. 1713-1716
    • Albers, G.W.1    Caplan, L.R.2    Coull, B.3
  • 2
    • 0020051129 scopus 로고
    • Delayed neuronal death in the gerbil hippocampus following ischemia
    • Kirino T. Delayed neuronal death in the gerbil hippocampus following ischemia. Brain Res 239 1 (1982) 57-69
    • (1982) Brain Res , vol.239 , Issue.1 , pp. 57-69
    • Kirino, T.1
  • 3
    • 0034192398 scopus 로고    scopus 로고
    • Protein aggregation after transient cerebral ischemia
    • Hu B.R., Martone M.E., Jones Y.Z., and Liu C.L. Protein aggregation after transient cerebral ischemia. J Neurosci 20 9 (2000) 3191-3199
    • (2000) J Neurosci , vol.20 , Issue.9 , pp. 3191-3199
    • Hu, B.R.1    Martone, M.E.2    Jones, Y.Z.3    Liu, C.L.4
  • 4
    • 0034963383 scopus 로고    scopus 로고
    • Protein aggregation after focal brain ischemia and reperfusion
    • Hu B.R., Janelidze S., Ginsberg M.D., et al. Protein aggregation after focal brain ischemia and reperfusion. J Cereb Blood Flow Metab 21 7 (2001) 865-875
    • (2001) J Cereb Blood Flow Metab , vol.21 , Issue.7 , pp. 865-875
    • Hu, B.R.1    Janelidze, S.2    Ginsberg, M.D.3
  • 5
    • 2342597809 scopus 로고    scopus 로고
    • Chaperones, protein aggregation, and brain protection from hypoxic/ischemic injury
    • Giffard R.G., Xu L., and Zhao H. Chaperones, protein aggregation, and brain protection from hypoxic/ischemic injury. J Exp Biol 207 Pt 18 (2004) 3213-3220
    • (2004) J Exp Biol , vol.207 , Issue.PART 18 , pp. 3213-3220
    • Giffard, R.G.1    Xu, L.2    Zhao, H.3
  • 6
    • 36448993027 scopus 로고    scopus 로고
    • Protein aggregation and proteasome dysfunction after brain ischemia
    • Ge P., Luo Y., Liu C., et al. Protein aggregation and proteasome dysfunction after brain ischemia. Stroke 38 12 (2007) 3230-3236
    • (2007) Stroke , vol.38 , Issue.12 , pp. 3230-3236
    • Ge, P.1    Luo, Y.2    Liu, C.3
  • 7
    • 33344461775 scopus 로고    scopus 로고
    • Protein aggregation in the pathogenesis of familial and sporadic Parkinson's disease
    • McNaught K.S., and Olanow C.W. Protein aggregation in the pathogenesis of familial and sporadic Parkinson's disease. Neurobiol Aging 27 4 (2006) 530-545
    • (2006) Neurobiol Aging , vol.27 , Issue.4 , pp. 530-545
    • McNaught, K.S.1    Olanow, C.W.2
  • 8
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach N., Deechongkit S., Jiang X., et al. Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc Natl Acad Sci USA 101 9 (2004) 2817-2822
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.9 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3
  • 9
    • 26244434741 scopus 로고    scopus 로고
    • Towards a structural understanding of the fibrilization pathway in Machado-Joseph's disease: trapping early oligomers of non-expanded ataxin-3
    • Gales L., Cortes L., Almeida C., et al. Towards a structural understanding of the fibrilization pathway in Machado-Joseph's disease: trapping early oligomers of non-expanded ataxin-3. J Mol Biol 353 3 (2005) 642-654
    • (2005) J Mol Biol , vol.353 , Issue.3 , pp. 642-654
    • Gales, L.1    Cortes, L.2    Almeida, C.3
  • 10
    • 0026595567 scopus 로고
    • Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs
    • Burdick D., Soreghan B., Kwon M., et al. Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs. J Biol Chem 267 1 (1992) 546-554
    • (1992) J Biol Chem , vol.267 , Issue.1 , pp. 546-554
    • Burdick, D.1    Soreghan, B.2    Kwon, M.3
  • 11
    • 34447514202 scopus 로고    scopus 로고
    • Role of polyunsaturated fatty acids for misfolding protein aggregations: implication for neurodegenerative diseases
    • Kim Y.J., and Takahashi R. Role of polyunsaturated fatty acids for misfolding protein aggregations: implication for neurodegenerative diseases. Ann N Y Acad Sci 1086 11 (2006) 11-20
    • (2006) Ann N Y Acad Sci , vol.1086 , Issue.11 , pp. 11-20
    • Kim, Y.J.1    Takahashi, R.2
  • 12
    • 24944456875 scopus 로고    scopus 로고
    • Protein misfolding, aggregation, and degradation in disease
    • Gregersen N., Bolund L., and Bross P. Protein misfolding, aggregation, and degradation in disease. Mol Biotechnol 31 2 (2005) 141-150
    • (2005) Mol Biotechnol , vol.31 , Issue.2 , pp. 141-150
    • Gregersen, N.1    Bolund, L.2    Bross, P.3
  • 13
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M., and Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81 11 (2003) 678-699
    • (2003) J Mol Med , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 14
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 10 12 (2000) 524-530
    • (2000) Trends Cell Biol , vol.10 , Issue.12 , pp. 524-530
    • Kopito, R.R.1
  • 15
    • 0034963383 scopus 로고    scopus 로고
    • Protein aggregation after focal brain ischemia and reperfusion
    • Hu B.R., Janelidze S., Ginsberg M.D., et al. Protein aggregation after focal brain ischemia and reperfusion. J Cereb Blood Flow Metab 21 7 (2001) 865-875
    • (2001) J Cereb Blood Flow Metab , vol.21 , Issue.7 , pp. 865-875
    • Hu, B.R.1    Janelidze, S.2    Ginsberg, M.D.3
  • 16
    • 33645669213 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system
    • Nandi D., Tahiliani P., Kumar A., et al. The ubiquitin-proteasome system. J Biosci 31 1 (2006) 137-155
    • (2006) J Biosci , vol.31 , Issue.1 , pp. 137-155
    • Nandi, D.1    Tahiliani, P.2    Kumar, A.3
  • 17
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., Weissman J., and Horwich A. Molecular chaperones and protein quality control. Cell 125 3 (2006) 443-451
    • (2006) Cell , vol.125 , Issue.3 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 18
    • 33745167938 scopus 로고    scopus 로고
    • Protein-misfolding diseases and chaperone-based therapeutic approaches
    • Chaudhuri T.K., and Paul S. Protein-misfolding diseases and chaperone-based therapeutic approaches. FEBS J 273 7 (2006) 1331-1349
    • (2006) FEBS J , vol.273 , Issue.7 , pp. 1331-1349
    • Chaudhuri, T.K.1    Paul, S.2
  • 19
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • Liberek K., Lewandowska A., and Zietkiewicz S. Chaperones in control of protein disaggregation. EMBO J 27 2 (2008) 328-335
    • (2008) EMBO J , vol.27 , Issue.2 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 20
    • 45849094051 scopus 로고    scopus 로고
    • Emerging and potential therapies for Alzheimer's disease
    • Griffiths H.H., Morten I.J., and Hooper N.M. Emerging and potential therapies for Alzheimer's disease. Expert Opin Ther Targets 12 6 (2008) 693-704
    • (2008) Expert Opin Ther Targets , vol.12 , Issue.6 , pp. 693-704
    • Griffiths, H.H.1    Morten, I.J.2    Hooper, N.M.3
  • 21
    • 0037398420 scopus 로고    scopus 로고
    • Targeting aggregation in the development of therapeutics for the treatment of Huntington's disease and other polyglutamine repeat diseases
    • Steffan J.S., and Thompson L.M. Targeting aggregation in the development of therapeutics for the treatment of Huntington's disease and other polyglutamine repeat diseases. Expert Opin Ther Targets 7 2 (2003) 201-213
    • (2003) Expert Opin Ther Targets , vol.7 , Issue.2 , pp. 201-213
    • Steffan, J.S.1    Thompson, L.M.2
  • 22
    • 34948859111 scopus 로고    scopus 로고
    • Chemical chaperones reduce endoplasmic reticulum stress and prevent mutant HFE aggregate formation
    • de Almeida S.F., Picarote G., Fleming J.V., et al. Chemical chaperones reduce endoplasmic reticulum stress and prevent mutant HFE aggregate formation. J Biol Chem 282 38 (2007) 27905-27912
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 27905-27912
    • de Almeida, S.F.1    Picarote, G.2    Fleming, J.V.3
  • 23
    • 33646581674 scopus 로고    scopus 로고
    • Suppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stress
    • Kubota K., Niinuma Y., Kaneko M., et al. Suppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stress. J Neurochem 97 5 (2006) 1259-1268
    • (2006) J Neurochem , vol.97 , Issue.5 , pp. 1259-1268
    • Kubota, K.1    Niinuma, Y.2    Kaneko, M.3
  • 24
    • 29644437591 scopus 로고    scopus 로고
    • Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy
    • Davies J.E., Sarkar S., and Rubinsztein D.C. Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy. Hum Mol Genet 15 1 (2006) 23-31
    • (2006) Hum Mol Genet , vol.15 , Issue.1 , pp. 23-31
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 25
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • Arora A., Ha C., and Park C.B. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett 564 1 (2004) 121-125
    • (2004) FEBS Lett , vol.564 , Issue.1 , pp. 121-125
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 26
    • 1642633757 scopus 로고    scopus 로고
    • Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
    • Tanaka M., Machida Y., Niu S., et al. Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease. Nat Med 10 2 (2004) 148-154
    • (2004) Nat Med , vol.10 , Issue.2 , pp. 148-154
    • Tanaka, M.1    Machida, Y.2    Niu, S.3
  • 27
    • 70449732217 scopus 로고    scopus 로고
    • Delivery of the aggregate inhibitor peptide QBP1 into the mouse brain using PTDs and its therapeutic effect on polyglutamine disease mice
    • [Epub ahead of print]
    • Popiel H.A., Nagai Y., Fujikake N., et al. Delivery of the aggregate inhibitor peptide QBP1 into the mouse brain using PTDs and its therapeutic effect on polyglutamine disease mice. Neurosci Lett (2008) [Epub ahead of print]
    • (2008) Neurosci Lett
    • Popiel, H.A.1    Nagai, Y.2    Fujikake, N.3
  • 28
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen H.Y., He J.C., Wang Y., et al. Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J Biol Chem 280 48 (2005) 39962-39969
    • (2005) J Biol Chem , vol.280 , Issue.48 , pp. 39962-39969
    • Shen, H.Y.1    He, J.C.2    Wang, Y.3
  • 29
    • 42449098946 scopus 로고    scopus 로고
    • Effect of amino acids and amino acid derivatives on crystallization of hemoglobin and ribonuclease A
    • Ito L., Kobayashi T., Shiraki K., et al. Effect of amino acids and amino acid derivatives on crystallization of hemoglobin and ribonuclease A. J Synchrotron Radiat 15 Pt 3 (2008) 316-318
    • (2008) J Synchrotron Radiat , vol.15 , Issue.PART 3 , pp. 316-318
    • Ito, L.1    Kobayashi, T.2    Shiraki, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.