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Volumn 51, Issue 21, 2008, Pages 2003-2010

Potential Role of the Ubiquitin-Proteasome System in Atherosclerosis. Aspects of a Protein Quality Disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CHAPERONE; PROTEASOME; UBIQUITIN;

EID: 43549098451     PISSN: 07351097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jacc.2008.02.047     Document Type: Review
Times cited : (56)

References (50)
  • 1
    • 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 (2006) 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 2
    • 34248379575 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in protein regulation
    • Herrmann J., Lerman L.O., and Lerman A. Ubiquitin and ubiquitin-like proteins in protein regulation. Circ Res 100 (2007) 1276-1291
    • (2007) Circ Res , vol.100 , pp. 1276-1291
    • Herrmann, J.1    Lerman, L.O.2    Lerman, A.3
  • 3
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: folding, refolding, and degrading proteins
    • Wickner S., Maurizi M.R., and Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286 (1999) 1888-1893
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 4
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8 (2007) 519-529
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 5
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales S., McDonald K.L., and Walter P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol 4 (2006) e423
    • (2006) PLoS Biol , vol.4
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 6
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell R.W., and Lomas D.A. Conformational disease. Lancet 350 (1997) 134-138
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 7
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor J.P., Hardy J., and Fischbeck K.H. Toxic proteins in neurodegenerative disease. Science 296 (2002) 1991-1995
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 8
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat Med 10 Suppl (2004) S10-S17
    • (2004) Nat Med , vol.10 , Issue.SUPPL
    • Ross, C.A.1    Poirier, M.A.2
  • 9
    • 7044238416 scopus 로고    scopus 로고
    • Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs
    • Forman M.S., Trojanowski J.Q., and Lee V.M. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat Med 10 (2004) 1055-1063
    • (2004) Nat Med , vol.10 , pp. 1055-1063
    • Forman, M.S.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 10
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., and 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
  • 11
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla F.M., Green K.N., and Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 8 (2007) 499-509
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 12
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M., Giannoni E., Chiti F., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3
  • 13
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • Stocker R., and Keaney Jr. J.F. Role of oxidative modifications in atherosclerosis. Physiol Rev 84 (2004) 1381-1478
    • (2004) Physiol Rev , vol.84 , pp. 1381-1478
    • Stocker, R.1    Keaney Jr., J.F.2
  • 14
    • 0027755138 scopus 로고
    • Immunology of atherosclerosis. Demonstration of heat shock protein 60 expression and T lymphocytes bearing alpha/beta or gamma/delta receptor in human atherosclerotic lesions
    • Kleindienst R., Xu Q., Willeit J., Waldenberger F.R., Weimann S., and Wick G. Immunology of atherosclerosis. Demonstration of heat shock protein 60 expression and T lymphocytes bearing alpha/beta or gamma/delta receptor in human atherosclerotic lesions. Am J Pathol 142 (1993) 1927-1937
    • (1993) Am J Pathol , vol.142 , pp. 1927-1937
    • Kleindienst, R.1    Xu, Q.2    Willeit, J.3    Waldenberger, F.R.4    Weimann, S.5    Wick, G.6
  • 15
    • 0025125876 scopus 로고
    • Immunohistochemical localization of heat shock protein-70 in normal-appearing and atherosclerotic specimens of human arteries
    • Berberian P.A., Myers W., Tytell M., Challa V., and Bond M.G. Immunohistochemical localization of heat shock protein-70 in normal-appearing and atherosclerotic specimens of human arteries. Am J Pathol 136 (1990) 71-80
    • (1990) Am J Pathol , vol.136 , pp. 71-80
    • Berberian, P.A.1    Myers, W.2    Tytell, M.3    Challa, V.4    Bond, M.G.5
  • 16
    • 0035570685 scopus 로고    scopus 로고
    • Temporal expression of heat shock proteins 60 and 70 at lesion-prone sites during atherogenesis in ApoE-deficient mice
    • Kanwar R.K., Kanwar J.R., Wang D., Ormrod D.J., and Krissansen G.W. Temporal expression of heat shock proteins 60 and 70 at lesion-prone sites during atherogenesis in ApoE-deficient mice. Arterioscler Thromb Vasc Biol 21 (2001) 1991-1997
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 1991-1997
    • Kanwar, R.K.1    Kanwar, J.R.2    Wang, D.3    Ormrod, D.J.4    Krissansen, G.W.5
  • 17
    • 0037021520 scopus 로고    scopus 로고
    • Increased ubiquitin immunoreactivity in unstable atherosclerotic plaques associated with acute coronary syndromes
    • Herrmann J., Edwards W.D., Holmes Jr. D.R., et al. Increased ubiquitin immunoreactivity in unstable atherosclerotic plaques associated with acute coronary syndromes. J Am Coll Cardiol 40 (2002) 1919-1927
    • (2002) J Am Coll Cardiol , vol.40 , pp. 1919-1927
    • Herrmann, J.1    Edwards, W.D.2    Holmes Jr., D.R.3
  • 18
    • 33744978316 scopus 로고    scopus 로고
    • Increased activity of the ubiquitin-proteasome system in patients with symptomatic carotid disease is associated with enhanced inflammation and may destabilize the atherosclerotic plaque: effects of rosiglitazone treatment
    • Marfella R., D'Amico M., Di Filippo C., et al. Increased activity of the ubiquitin-proteasome system in patients with symptomatic carotid disease is associated with enhanced inflammation and may destabilize the atherosclerotic plaque: effects of rosiglitazone treatment. J Am Coll Cardiol 47 (2006) 2444-2455
    • (2006) J Am Coll Cardiol , vol.47 , pp. 2444-2455
    • Marfella, R.1    D'Amico, M.2    Di Filippo, C.3
  • 19
    • 33747405122 scopus 로고    scopus 로고
    • Dysregulation of the ubiquitin-proteasome system in human carotid atherosclerosis
    • Versari D., Herrmann J., Gossl M., et al. Dysregulation of the ubiquitin-proteasome system in human carotid atherosclerosis. Arterioscler Thromb Vasc Biol 26 (2006) 2132-2139
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 2132-2139
    • Versari, D.1    Herrmann, J.2    Gossl, M.3
  • 20
    • 0141818108 scopus 로고    scopus 로고
    • Oxidative stress-related increase in ubiquitination in early coronary atherogenesis
    • Herrmann J., Gulati R., Napoli C., et al. Oxidative stress-related increase in ubiquitination in early coronary atherogenesis. FASEB J 17 (2003) 1730-1732
    • (2003) FASEB J , vol.17 , pp. 1730-1732
    • Herrmann, J.1    Gulati, R.2    Napoli, C.3
  • 21
    • 33750043779 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system: a new avenue for atherosclerosis
    • Tan C., Li Y., Tan X., Pan H., and Huang W. Inhibition of the ubiquitin-proteasome system: a new avenue for atherosclerosis. Clin Chem Lab Med 44 (2006) 1218-1225
    • (2006) Clin Chem Lab Med , vol.44 , pp. 1218-1225
    • Tan, C.1    Li, Y.2    Tan, X.3    Pan, H.4    Huang, W.5
  • 22
    • 37349073383 scopus 로고    scopus 로고
    • Chronic proteasome inhibition contributes to coronary atherosclerosis
    • Herrmann J., Saguner A.M., Versari D., et al. Chronic proteasome inhibition contributes to coronary atherosclerosis. Circ Res 101 (2007) 865-874
    • (2007) Circ Res , vol.101 , pp. 865-874
    • Herrmann, J.1    Saguner, A.M.2    Versari, D.3
  • 23
    • 34548134851 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of guanosine 5′-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus
    • Xu J., Wu Y., Song P., Zhang M., Wang S., and Zou M.H. Proteasome-dependent degradation of guanosine 5′-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus. Circulation 116 (2007) 944-953
    • (2007) Circulation , vol.116 , pp. 944-953
    • Xu, J.1    Wu, Y.2    Song, P.3    Zhang, M.4    Wang, S.5    Zou, M.H.6
  • 24
    • 17144419252 scopus 로고    scopus 로고
    • Activation of the unfolded protein response occurs at all stages of atherosclerotic lesion development in apolipoprotein E-deficient mice
    • Zhou J., Lhotak S., Hilditch B.A., and Austin R.C. Activation of the unfolded protein response occurs at all stages of atherosclerotic lesion development in apolipoprotein E-deficient mice. Circulation 111 (2005) 1814-1821
    • (2005) Circulation , vol.111 , pp. 1814-1821
    • Zhou, J.1    Lhotak, S.2    Hilditch, B.A.3    Austin, R.C.4
  • 25
    • 0042972934 scopus 로고    scopus 로고
    • The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages
    • Feng B., Yao P.M., Li Y., et al. The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages. Nat Cell Biol 5 (2003) 781-792
    • (2003) Nat Cell Biol , vol.5 , pp. 781-792
    • Feng, B.1    Yao, P.M.2    Li, Y.3
  • 26
    • 33644790277 scopus 로고    scopus 로고
    • Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: implications in atherogenesis
    • Dickhout J.G., Hossain G.S., Pozza L.M., Zhou J., Lhotak S., and Austin R.C. Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: implications in atherogenesis. Arterioscler Thromb Vasc Biol 25 (2005) 2623-2629
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 2623-2629
    • Dickhout, J.G.1    Hossain, G.S.2    Pozza, L.M.3    Zhou, J.4    Lhotak, S.5    Austin, R.C.6
  • 27
    • 33750221963 scopus 로고    scopus 로고
    • The unfolded protein response is an important regulator of inflammatory genes in endothelial cells
    • Gargalovic P.S., Gharavi N.M., Clark M.J., et al. The unfolded protein response is an important regulator of inflammatory genes in endothelial cells. Arterioscler Thromb Vasc Biol 26 (2006) 2490-2496
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 2490-2496
    • Gargalovic, P.S.1    Gharavi, N.M.2    Clark, M.J.3
  • 28
    • 34247213490 scopus 로고    scopus 로고
    • Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation
    • Horke S., Witte I., Wilgenbus P., Kruger M., Strand D., and Forstermann U. Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation. Circulation 115 (2007) 2055-2064
    • (2007) Circulation , vol.115 , pp. 2055-2064
    • Horke, S.1    Witte, I.2    Wilgenbus, P.3    Kruger, M.4    Strand, D.5    Forstermann, U.6
  • 29
    • 0028942292 scopus 로고
    • Differential distribution of 70-kD heat shock protein in atherosclerosis. Its potential role in arterial SMC survival
    • Johnson A.D., Berberian P.A., Tytell M., and Bond M.G. Differential distribution of 70-kD heat shock protein in atherosclerosis. Its potential role in arterial SMC survival. Arterioscler Thromb Vasc Biol 15 (1995) 27-36
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 27-36
    • Johnson, A.D.1    Berberian, P.A.2    Tytell, M.3    Bond, M.G.4
  • 30
    • 0037192316 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway as a new target for the prevention of restenosis
    • Meiners S., Laule M., Rother W., et al. Ubiquitin-proteasome pathway as a new target for the prevention of restenosis. Circulation 105 (2002) 483-489
    • (2002) Circulation , vol.105 , pp. 483-489
    • Meiners, S.1    Laule, M.2    Rother, W.3
  • 31
    • 10744223540 scopus 로고    scopus 로고
    • Long-term up-regulation of eNOS and improvement of endothelial function by inhibition of the ubiquitin-proteasome pathway
    • Stangl V., Lorenz M., Meiners S., et al. Long-term up-regulation of eNOS and improvement of endothelial function by inhibition of the ubiquitin-proteasome pathway. Faseb J 18 (2004) 272-279
    • (2004) Faseb J , vol.18 , pp. 272-279
    • Stangl, V.1    Lorenz, M.2    Meiners, S.3
  • 32
    • 0034010468 scopus 로고    scopus 로고
    • Oxidized LDLs alter the activity of the ubiquitin-proteasome pathway: potential role in oxidized LDL-induced apoptosis
    • Vieira O., Escargueil-Blanc I., Jurgens G., et al. Oxidized LDLs alter the activity of the ubiquitin-proteasome pathway: potential role in oxidized LDL-induced apoptosis. FASEB J 14 (2000) 532-542
    • (2000) FASEB J , vol.14 , pp. 532-542
    • Vieira, O.1    Escargueil-Blanc, I.2    Jurgens, G.3
  • 33
    • 0034746557 scopus 로고    scopus 로고
    • Apolipoprotein A-1-derived amyloid in atherosclerotic plaques of the human aorta
    • Mucchiano G.I., Haggqvist B., Sletten K., and Westermark P. Apolipoprotein A-1-derived amyloid in atherosclerotic plaques of the human aorta. J Pathol 193 (2001) 270-275
    • (2001) J Pathol , vol.193 , pp. 270-275
    • Mucchiano, G.I.1    Haggqvist, B.2    Sletten, K.3    Westermark, P.4
  • 34
    • 33646544769 scopus 로고    scopus 로고
    • Prevalence and pathology of amyloid in atherosclerotic arteries
    • Rocken C., Tautenhahn J., Buhling F., et al. Prevalence and pathology of amyloid in atherosclerotic arteries. Arterioscler Thromb Vasc Biol 26 (2006) 676-677
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 676-677
    • Rocken, C.1    Tautenhahn, J.2    Buhling, F.3
  • 36
    • 21744451038 scopus 로고    scopus 로고
    • Oxidation of low-density lipoproteins induces amyloid-like structures that are recognized by macrophages
    • Stewart C.R., Tseng A.A., Mok Y.F., et al. Oxidation of low-density lipoproteins induces amyloid-like structures that are recognized by macrophages. Biochemistry 44 (2005) 9108-9116
    • (2005) Biochemistry , vol.44 , pp. 9108-9116
    • Stewart, C.R.1    Tseng, A.A.2    Mok, Y.F.3
  • 37
    • 33748519935 scopus 로고    scopus 로고
    • Untangling the role of amyloid in atherosclerosis
    • Howlett G.J., and Moore K.J. Untangling the role of amyloid in atherosclerosis. Curr Opin Lipidol 17 (2006) 541-547
    • (2006) Curr Opin Lipidol , vol.17 , pp. 541-547
    • Howlett, G.J.1    Moore, K.J.2
  • 38
    • 1642264113 scopus 로고    scopus 로고
    • Fibrillar amyloid protein present in atheroma activates CD36 signal transduction
    • Medeiros L.A., Khan T., El Khoury J.B., et al. Fibrillar amyloid protein present in atheroma activates CD36 signal transduction. J Biol Chem 279 (2004) 10643-10648
    • (2004) J Biol Chem , vol.279 , pp. 10643-10648
    • Medeiros, L.A.1    Khan, T.2    El Khoury, J.B.3
  • 39
    • 0141457931 scopus 로고    scopus 로고
    • Age-dependent cerebrovascular abnormalities and blood flow disturbances in APP23 mice modeling Alzheimer's disease
    • Beckmann N., Schuler A., Mueggler T., et al. Age-dependent cerebrovascular abnormalities and blood flow disturbances in APP23 mice modeling Alzheimer's disease. J Neurosci 23 (2003) 8453-8459
    • (2003) J Neurosci , vol.23 , pp. 8453-8459
    • Beckmann, N.1    Schuler, A.2    Mueggler, T.3
  • 40
    • 31844456345 scopus 로고    scopus 로고
    • Bosentan preserves endothelial function in mice overexpressing APP
    • Elesber A.A., Bonetti P.O., Woodrum J.E., et al. Bosentan preserves endothelial function in mice overexpressing APP. Neurobiol Aging 27 (2006) 446-450
    • (2006) Neurobiol Aging , vol.27 , pp. 446-450
    • Elesber, A.A.1    Bonetti, P.O.2    Woodrum, J.E.3
  • 41
    • 0032573452 scopus 로고    scopus 로고
    • Soluble Alzheimers beta-amyloid constricts the cerebral vasculature in vivo
    • Suo Z., Humphrey J., Kundtz A., et al. Soluble Alzheimers beta-amyloid constricts the cerebral vasculature in vivo. Neurosci Lett 257 (1998) 77-80
    • (1998) Neurosci Lett , vol.257 , pp. 77-80
    • Suo, Z.1    Humphrey, J.2    Kundtz, A.3
  • 42
    • 9144223132 scopus 로고    scopus 로고
    • Mechanisms of soluble beta-amyloid impairment of endothelial function
    • Gentile M.T., Vecchione C., Maffei A., et al. Mechanisms of soluble beta-amyloid impairment of endothelial function. J Biol Chem 279 (2004) 48135-48142
    • (2004) J Biol Chem , vol.279 , pp. 48135-48142
    • Gentile, M.T.1    Vecchione, C.2    Maffei, A.3
  • 43
    • 0030991218 scopus 로고    scopus 로고
    • Cerebrovascular endothelial dysfunction mediated by beta-amyloid
    • Thomas T., McLendon C., Sutton E.T., and Thomas G. Cerebrovascular endothelial dysfunction mediated by beta-amyloid. Neuroreport 8 (1997) 1387-1391
    • (1997) Neuroreport , vol.8 , pp. 1387-1391
    • Thomas, T.1    McLendon, C.2    Sutton, E.T.3    Thomas, G.4
  • 44
    • 0031179444 scopus 로고    scopus 로고
    • In vivo vascular damage, leukocyte activation and inflammatory response induced by beta-amyloid
    • Thomas T., Sutton E.T., Bryant M.W., and Rhodin J.A. In vivo vascular damage, leukocyte activation and inflammatory response induced by beta-amyloid. J Submicrosc Cytol Pathol 29 (1997) 293-304
    • (1997) J Submicrosc Cytol Pathol , vol.29 , pp. 293-304
    • Thomas, T.1    Sutton, E.T.2    Bryant, M.W.3    Rhodin, J.A.4
  • 45
    • 0141566766 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathies: a pathologic, biochemical, and genetic view
    • Revesz T., Ghiso J., Lashley T., et al. Cerebral amyloid angiopathies: a pathologic, biochemical, and genetic view. J Neuropathol Exp Neurol 62 (2003) 885-898
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 885-898
    • Revesz, T.1    Ghiso, J.2    Lashley, T.3
  • 46
    • 0345275964 scopus 로고    scopus 로고
    • Association of aortic atherosclerosis with cerebral beta-amyloidosis and learning deficits in a mouse model of Alzheimer's disease
    • Li L., Cao D., Garber D.W., Kim H., and Fukuchi K. Association of aortic atherosclerosis with cerebral beta-amyloidosis and learning deficits in a mouse model of Alzheimer's disease. Am J Pathol 163 (2003) 2155-2164
    • (2003) Am J Pathol , vol.163 , pp. 2155-2164
    • Li, L.1    Cao, D.2    Garber, D.W.3    Kim, H.4    Fukuchi, K.5
  • 47
    • 33845638625 scopus 로고    scopus 로고
    • Heart failure and protein quality control
    • Wang X., and Robbins J. Heart failure and protein quality control. Circ Res 99 (2006) 1315-1328
    • (2006) Circ Res , vol.99 , pp. 1315-1328
    • Wang, X.1    Robbins, J.2
  • 48
    • 34147131267 scopus 로고    scopus 로고
    • The bitter end: the ubiquitin-proteasome system and cardiac dysfunction
    • Patterson C., Ike C., Willis P.Wt., Stouffer G.A., and Willis M.S. The bitter end: the ubiquitin-proteasome system and cardiac dysfunction. Circulation 115 (2007) 1456-1463
    • (2007) Circulation , vol.115 , pp. 1456-1463
    • Patterson, C.1    Ike, C.2    Willis, P.Wt.3    Stouffer, G.A.4    Willis, M.S.5
  • 49
    • 33745910558 scopus 로고    scopus 로고
    • Prion-induced amyloid heart disease with high blood infectivity in transgenic mice
    • Trifilo M.J., Yajima T., Gu Y., et al. Prion-induced amyloid heart disease with high blood infectivity in transgenic mice. Science 313 (2006) 94-97
    • (2006) Science , vol.313 , pp. 94-97
    • Trifilo, M.J.1    Yajima, T.2    Gu, Y.3
  • 50
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Chesebro B., Trifilo M., Race R., et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308 (2005) 1435-1439
    • (2005) Science , vol.308 , pp. 1435-1439
    • Chesebro, B.1    Trifilo, M.2    Race, R.3


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