메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; BETA 2 MICROGLOBULIN; C REACTIVE PROTEIN; CALCIUM; GLUTATHIONE TRANSFERASE; SERUM AMYLOID P;

EID: 84977262514     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep29077     Document Type: Article
Times cited : (22)

References (56)
  • 1
    • 84895513254 scopus 로고    scopus 로고
    • Pentraxins: Structure, function, and role in inflammation
    • Du Clos, T. W. Pentraxins: structure, function, and role in inflammation. ISRN Inflamm. 2013, 379040(2013).
    • (2013) ISRN Inflamm. , vol.2013 , pp. 379040
    • Du Clos, T.W.1
  • 2
    • 0000186474 scopus 로고    scopus 로고
    • Amyloid P component. A critical review
    • Pepys, M. B. et al. Amyloid P component. A critical review. Amyloid 4, 274-295 (1997).
    • (1997) Amyloid , vol.4 , pp. 274-295
    • Pepys, M.B.1
  • 3
    • 0042744797 scopus 로고    scopus 로고
    • C-reactive protein: A critical update
    • Pepys, M. B. & Hirschfield, G. M. C-reactive protein: a critical update. J. Clin. Invest. 111, 1805-1812 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 1805-1812
    • Pepys, M.B.1    Hirschfield, G.M.2
  • 4
    • 0018101816 scopus 로고
    • Comparative clinical study of protein SAP (amyloid P component) and C-reactive protein in serum
    • Pepys, M. B. et al. Comparative clinical study of protein SAP (amyloid P component) and C-reactive protein in serum. Clin. Exp. Immunol. 32, 119-124 (1978).
    • (1978) Clin. Exp. Immunol. , vol.32 , pp. 119-124
    • Pepys, M.B.1
  • 5
    • 33751243644 scopus 로고    scopus 로고
    • Individuals homozygous for the age-related macular degeneration risk-conferring variant of complement factor H have elevated levels of CRP in the choroid
    • Johnson, P. T. et al. Individuals homozygous for the age-related macular degeneration risk-conferring variant of complement factor H have elevated levels of CRP in the choroid. Proc. Natl. Acad. Sci. USA 103, 17456-17461 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17456-17461
    • Johnson, P.T.1
  • 6
    • 0000205893 scopus 로고
    • Studies of acute phase protein. I. An immunohistochemical method for the localization of Cx-reactive protein in rabbits. Association with necrosis in local inflammatory lesions
    • Kushner, I. & Kaplan, M. H. Studies of acute phase protein. I. An immunohistochemical method for the localization of Cx-reactive protein in rabbits. Association with necrosis in local inflammatory lesions. J. Exp. Med. 114, 961-974 (1961).
    • (1961) J. Exp. Med. , vol.114 , pp. 961-974
    • Kushner, I.1    Kaplan, M.H.2
  • 7
    • 84903759929 scopus 로고    scopus 로고
    • Dissociation of pentameric to monomeric C-reactive protein localizes and aggravates inflammation: In vivo proof of a powerful proinflammatory mechanism and a new anti-inflammatory strategy
    • Thiele, J. R. et al. Dissociation of pentameric to monomeric C-reactive protein localizes and aggravates inflammation: in vivo proof of a powerful proinflammatory mechanism and a new anti-inflammatory strategy. Circulation 130, 35-50 (2014).
    • (2014) Circulation , vol.130 , pp. 35-50
    • Thiele, J.R.1
  • 8
    • 78149242569 scopus 로고    scopus 로고
    • Identification of acidic pH-dependent ligands of pentameric C-reactive protein
    • Hammond, D. J. Jr. et al. Identification of acidic pH-dependent ligands of pentameric C-reactive protein. J. Biol. Chem. 285, 36235-36244 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 36235-36244
    • Hammond, D.J.1
  • 9
    • 84863044357 scopus 로고    scopus 로고
    • Exposing a hidden functional site of C-reactive protein by site-directed mutagenesis
    • Singh, S. K. et al. Exposing a hidden functional site of C-reactive protein by site-directed mutagenesis. J. Biol. Chem. 287, 3550-3558 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 3550-3558
    • Singh, S.K.1
  • 10
    • 0014994384 scopus 로고
    • Changes in the interstitial pH of dog myocardium in response to local ischemia, hypoxia, hyper-and hypocapnia, measured continuously by means of glass microelectrodes
    • Gebert, G., Benzing, H. & Strohm, M. Changes in the interstitial pH of dog myocardium in response to local ischemia, hypoxia, hyper-and hypocapnia, measured continuously by means of glass microelectrodes. Pflügers Arch. 329, 72-81 (1971).
    • (1971) Pflügers Arch. , vol.329 , pp. 72-81
    • Gebert, G.1    Benzing, H.2    Strohm, M.3
  • 11
    • 84921920048 scopus 로고    scopus 로고
    • Acidification of the intimal fluid: The perfect storm for atherogenesis
    • Öörni, K. et al. Acidification of the intimal fluid: the perfect storm for atherogenesis. J. Lipid. Res. 56, 203-214 (2015).
    • (2015) J. Lipid. Res. , vol.56 , pp. 203-214
    • Öörni, K.1
  • 12
    • 84877705901 scopus 로고    scopus 로고
    • Extracellular acidosis is a novel danger signal alerting innate immunity via the NLRP3 inflammasome
    • Rajamäki, K. et al. Extracellular acidosis is a novel danger signal alerting innate immunity via the NLRP3 inflammasome. J. Biol. Chem. 288, 13410-13419 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 13410-13419
    • Rajamäki, K.1
  • 13
    • 0031017154 scopus 로고    scopus 로고
    • C-reactive protein-like immunoreactivity in the neurofibrillary tangles of Alzheimer's disease
    • Duong, T., Nikolaeva, M. & Acton, P. J. C-reactive protein-like immunoreactivity in the neurofibrillary tangles of Alzheimer's disease. Brain Res. 749, 152-156 (1997).
    • (1997) Brain Res , vol.749 , pp. 152-156
    • Duong, T.1    Nikolaeva, M.2    Acton, P.J.3
  • 14
    • 0027938567 scopus 로고
    • Demonstration of CRP immunoreactivity in brains of Alzheimer's disease: Immunohistochemical study using formic acid pretreatment of tissue sections
    • Iwamoto, N., Nishiyama, E., Ohwada, J. & Arai, H. Demonstration of CRP immunoreactivity in brains of Alzheimer's disease: immunohistochemical study using formic acid pretreatment of tissue sections. Neurosci. Lett. 177, 23-26 (1994).
    • (1994) Neurosci. Lett. , vol.177 , pp. 23-26
    • Iwamoto, N.1    Nishiyama, E.2    Ohwada, J.3    Arai, H.4
  • 15
    • 0035696284 scopus 로고    scopus 로고
    • The pentraxins: Possible role in Alzheimer's disease and other innate inflammatory diseases
    • McGeer, E. G., Yasojima, K., Schwab, C. & McGeer, P. L. The pentraxins: possible role in Alzheimer's disease and other innate inflammatory diseases. Neurobiol. Aging 22, 843-848 (2001).
    • (2001) Neurobiol. Aging , vol.22 , pp. 843-848
    • McGeer, E.G.1    Yasojima, K.2    Schwab, C.3    McGeer, P.L.4
  • 16
    • 0030757182 scopus 로고    scopus 로고
    • Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
    • Botto, M. et al. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nat. Med. 3, 855-859 (1997).
    • (1997) Nat. Med. , vol.3 , pp. 855-859
    • Botto, M.1
  • 17
    • 84860117142 scopus 로고    scopus 로고
    • Serum amyloid P component accelerates the formation and enhances the stability of amyloid fibrils in a physiologically significant under-saturated solution of amyloid-β 42
    • Mold, M., Shrive, A. K. & Exley, C. Serum amyloid P component accelerates the formation and enhances the stability of amyloid fibrils in a physiologically significant under-saturated solution of amyloid-β 42. J. Alzheimers Dis. 29, 875-881 (2012).
    • (2012) J. Alzheimers Dis. , vol.29 , pp. 875-881
    • Mold, M.1    Shrive, A.K.2    Exley, C.3
  • 18
    • 33144471714 scopus 로고    scopus 로고
    • A systematic study of the effect of physiological factors on β 2-microglobulin amyloid formation at neutral pH
    • Myers, S. L. et al. A systematic study of the effect of physiological factors on β 2-microglobulin amyloid formation at neutral pH. Biochemistry 45, 2311-2321 (2006).
    • (2006) Biochemistry , vol.45 , pp. 2311-2321
    • Myers, S.L.1
  • 19
    • 0029010736 scopus 로고
    • Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis
    • Tennent, G. A., Lovat, L. B. & Pepys, M. B. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc. Natl. Acad. Sci. USA 92, 4299-4303 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4299-4303
    • Tennent, G.A.1    Lovat, L.B.2    Pepys, M.B.3
  • 20
    • 0030702134 scopus 로고    scopus 로고
    • Serum amyloid P component enhances induction of murine amyloidosis
    • Togashi, S. et al. Serum amyloid P component enhances induction of murine amyloidosis. Lab. Invest. 77, 525-531 (1997).
    • (1997) Lab. Invest. , vol.77 , pp. 525-531
    • Togashi, S.1
  • 21
    • 0034202740 scopus 로고    scopus 로고
    • Human serum amyloid P component is a single uncomplexed pentamer in whole serum
    • Hutchinson, W. L., Hohenester, E. & Pepys, M. B. Human serum amyloid P component is a single uncomplexed pentamer in whole serum. Mol. Med. 6, 482-493 (2000).
    • (2000) Mol. Med. , vol.6 , pp. 482-493
    • Hutchinson, W.L.1    Hohenester, E.2    Pepys, M.B.3
  • 23
    • 84873493924 scopus 로고    scopus 로고
    • Inhibition of TTR aggregation-induced cell death A new role for serum amyloid P component
    • Andersson, K., Pokrzywa, M., Dacklin, I. & Lundgren, E. Inhibition of TTR aggregation-induced cell death. A new role for serum amyloid P component. PLoS One 8, e55766 (2013).
    • (2013) PLoS One , vol.8 , pp. e55766
    • Andersson, K.1    Pokrzywa, M.2    Dacklin, I.3    Lundgren, E.4
  • 24
    • 0034640346 scopus 로고    scopus 로고
    • Molecular chaperone properties of serum amyloid P component
    • Coker, A. R., Purvis, A., Baker, D., Pepys, M. B. & Wood, S. P. Molecular chaperone properties of serum amyloid P component. FEBS Lett. 473, 199-202 (2000).
    • (2000) FEBS Lett. , vol.473 , pp. 199-202
    • Coker, A.R.1    Purvis, A.2    Baker, D.3    Pepys, M.B.4    Wood, S.P.5
  • 26
  • 28
    • 79953208604 scopus 로고    scopus 로고
    • Inhibition of β 2-microglobulin amyloid fibril formation by α 2-macroglobulin
    • Ozawa, D. et al. Inhibition of β 2-microglobulin amyloid fibril formation by α 2-macroglobulin. J. Biol. Chem. 286, 9668-9676 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 9668-9676
    • Ozawa, D.1
  • 29
    • 84862198496 scopus 로고    scopus 로고
    • Hereditary systemic amyloidosis due to Asp76Asn variant β 2-microglobulin
    • Valleix, S. et al. Hereditary systemic amyloidosis due to Asp76Asn variant β 2-microglobulin. N. Engl. J. Med. 366, 2276-2283 (2012).
    • (2012) N. Engl. J. Med. , vol.366 , pp. 2276-2283
    • Valleix, S.1
  • 32
    • 0031587295 scopus 로고    scopus 로고
    • Pentameric and decameric structures in solution of serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses
    • Ashton, A. W., Boehm, M. K., Gallimore, J. R., Pepys, M. B. & Perkins, S. J. Pentameric and decameric structures in solution of serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses. J. Mol. Biol. 272, 408-422 (1997).
    • (1997) J. Mol. Biol. , vol.272 , pp. 408-422
    • Ashton, A.W.1    Boehm, M.K.2    Gallimore, J.R.3    Pepys, M.B.4    Perkins, S.J.5
  • 33
    • 33748767364 scopus 로고    scopus 로고
    • Acceleration of amyloid β-peptide aggregation by physiological concentrations of calcium
    • Isaacs, A. M., Senn, D. B., Yuan, M., Shine, J. P. & Yankner, B. A. Acceleration of amyloid β-peptide aggregation by physiological concentrations of calcium. J. Biol. Chem. 281, 27916-27923 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 27916-27923
    • Isaacs, A.M.1    Senn, D.B.2    Yuan, M.3    Shine, J.P.4    Yankner, B.A.5
  • 34
    • 84873020544 scopus 로고    scopus 로고
    • Ca2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner
    • Brännström, K., Ohman, A., Lindhagen-Persson, M. & Olofsson, A. Ca2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner. Biochem. J. 450, 189-197 (2013).
    • (2013) Biochem. J. , vol.450 , pp. 189-197
    • Brännström, K.1    Ohman, A.2    Lindhagen-Persson, M.3    Olofsson, A.4
  • 36
    • 74349084862 scopus 로고    scopus 로고
    • Chaperone-like activity of the acute-phase component human serum alpha 1-acid glycoprotein: Inhibition of thermal-and chemical-induced aggregation of various proteins
    • Zsila, F. Chaperone-like activity of the acute-phase component human serum alpha 1-acid glycoprotein: inhibition of thermal-and chemical-induced aggregation of various proteins. Bioorg. Med. Chem. Lett. 20, 1205-1209 (2010).
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 1205-1209
    • Zsila, F.1
  • 37
    • 34547823043 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
    • Yerbury, J. J. et al. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 21, 2312-2322 (2007).
    • (2007) FASEB J. , vol.21 , pp. 2312-2322
    • Yerbury, J.J.1
  • 38
    • 63249134826 scopus 로고    scopus 로고
    • α2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species
    • Yerbury, J. J., Kumita, J. R., Meehan, S., Dobson, C. M. & Wilson, M. R. α2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. J. Biol. Chem. 284, 4246-4254 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4246-4254
    • Yerbury, J.J.1    Kumita, J.R.2    Meehan, S.3    Dobson, C.M.4    Wilson, M.R.5
  • 39
    • 84865957943 scopus 로고    scopus 로고
    • Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation
    • Yoshimura, Y. et al. Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation. Proc. Natl. Acad. Sci. USA 109, 14446-14451 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 14446-14451
    • Yoshimura, Y.1
  • 40
    • 34247364018 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species
    • Kumita, J. R. et al. The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species. J. Mol. Biol. 369, 157-167 (2007).
    • (2007) J. Mol. Biol. , vol.369 , pp. 157-167
    • Kumita, J.R.1
  • 41
    • 84855450514 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β (1-40) peptide
    • Narayan, P. et al. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β (1-40) peptide. Nat. Struct. Mol. Biol. 19, 79-83 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.19 , pp. 79-83
    • Narayan, P.1
  • 42
    • 84901052763 scopus 로고    scopus 로고
    • Hypochlorite-induced structural modifications enhance the chaperone activity of human α 2-macroglobulin
    • Wyatt, A. R. et al. Hypochlorite-induced structural modifications enhance the chaperone activity of human α 2-macroglobulin. Proc. Natl. Acad. Sci. USA 111, E2081-E2090 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E2081-E2090
    • Wyatt, A.R.1
  • 43
    • 0037066773 scopus 로고    scopus 로고
    • Distinct binding sites in the structure of α 2-macroglobulin mediate the interaction with β-amyloid peptide and growth factors
    • Mettenburg, J. M., Webb, D. J. & Gonias, S. L. Distinct binding sites in the structure of α 2-macroglobulin mediate the interaction with β-amyloid peptide and growth factors. J. Biol. Chem. 277, 13338-13345 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 13338-13345
    • Mettenburg, J.M.1    Webb, D.J.2    Gonias, S.L.3
  • 44
    • 1642528843 scopus 로고    scopus 로고
    • Small heat-shock proteins and clusterin: Intra-and extracellular molecular chaperones with a common mechanism of action and function?
    • Carver, J. A., Rekas, A., Thorn, D. C. & Wilson, M. R. Small heat-shock proteins and clusterin: intra-and extracellular molecular chaperones with a common mechanism of action and function? IUBMB Life 55, 661-668 (2003).
    • (2003) IUBMB Life , vol.55 , pp. 661-668
    • Carver, J.A.1    Rekas, A.2    Thorn, D.C.3    Wilson, M.R.4
  • 45
    • 84861850079 scopus 로고    scopus 로고
    • Global analysis of chaperone effects using a reconstituted cell-free translation system
    • Niwa, T., Kanamori, T., Ueda, T. & Taguchi, H. Global analysis of chaperone effects using a reconstituted cell-free translation system. Proc. Natl. Acad. Sci. USA 109, 8937-8942 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8937-8942
    • Niwa, T.1    Kanamori, T.2    Ueda, T.3    Taguchi, H.4
  • 47
    • 0036678856 scopus 로고    scopus 로고
    • Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease
    • DeMattos, R. B. et al. Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 99, 10843-10848 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10843-10848
    • DeMattos, R.B.1
  • 48
    • 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. et al. 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).
    • (2007) J. Cereb. Blood Flow Metab. , vol.27 , pp. 909-918
    • Bell, R.D.1
  • 49
    • 84923444904 scopus 로고    scopus 로고
    • Innate immunity in Alzheimer's disease
    • Heneka, M. T., Golenbock, D. T. & Latz, E. Innate immunity in Alzheimer's disease. Nat. Immunol. 16, 229-236 (2015).
    • (2015) Nat. Immunol. , vol.16 , pp. 229-236
    • Heneka, M.T.1    Golenbock, D.T.2    Latz, E.3
  • 50
    • 79955156438 scopus 로고    scopus 로고
    • Disease-associated amyloid and misfolded protein aggregates activate the inflammasome
    • Masters, S. L. & O'Neill, L. A. Disease-associated amyloid and misfolded protein aggregates activate the inflammasome. Trends Mol. Med. 17, 276-282 (2011).
    • (2011) Trends Mol. Med. , vol.17 , pp. 276-282
    • Masters, S.L.1    O'Neill, L.A.2
  • 51
    • 2942627626 scopus 로고    scopus 로고
    • Hydrophobicity: An ancient damage-associated molecular pattern that initiates innate immune responses
    • Seong, S. Y. & Matzinger, P. Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses. Nat. Rev. Immunol. 4, 469-478 (2004).
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 469-478
    • Seong, S.Y.1    Matzinger, P.2
  • 52
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • Pepys, M. B. et al. Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 417, 254-259 (2002).
    • (2002) Nature , vol.417 , pp. 254-259
    • Pepys, M.B.1
  • 53
    • 74849100946 scopus 로고    scopus 로고
    • Lack of effect of a single injection of human C-reactive protein on murine lupus or nephrotoxic nephritis
    • Carlucci, F., Cook, H. T., Garg, A., Pepys, M. B. & Botto, M. Lack of effect of a single injection of human C-reactive protein on murine lupus or nephrotoxic nephritis. Arthritis Rheum 62, 245-249 (2010).
    • (2010) Arthritis Rheum , vol.62 , pp. 245-249
    • Carlucci, F.1    Cook, H.T.2    Garg, A.3    Pepys, M.B.4    Botto, M.5
  • 54
    • 0025752708 scopus 로고
    • Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis
    • Hawkins, P. N., Tennent, G. A., Woo, P. & Pepys, M. B. Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis. Clin. Exp. Immunol. 84, 308-316 (1991).
    • (1991) Clin. Exp. Immunol. , vol.84 , pp. 308-316
    • Hawkins, P.N.1    Tennent, G.A.2    Woo, P.3    Pepys, M.B.4
  • 55
    • 0017811737 scopus 로고
    • One step preparation of both human C-reactive protein and CIt
    • Pontet, M., Engler, R. & Jayle, M. F. One step preparation of both human C-reactive protein and CIt. FEBS Lett. 88, 172-175 (1978).
    • (1978) FEBS Lett. , vol.88 , pp. 172-175
    • Pontet, M.1    Engler, R.2    Jayle, M.F.3
  • 56
    • 0344875516 scopus 로고    scopus 로고
    • Amyloid fibril formation in the context of full-length protein: Effects of proline mutations on the amyloid fibril formation of β 2-microglobulin
    • Chiba, T. et al. Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of β 2-microglobulin. J. Biol. Chem. 278, 47016-47024 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 47016-47024
    • Chiba, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.