-
1
-
-
84895513254
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
22
-
-
0028802246
-
Inhibition of Alzheimer β-peptide fibril formation by serum amyloid P component
-
Janciauskiene, S., García de Frutos, P., Carlemalm, E., Dahlbäck, B. & Eriksson, S. Inhibition of Alzheimer β-peptide fibril formation by serum amyloid P component. J. Biol. Chem. 270, 26041-26044 (1995).
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 26041-26044
-
-
Janciauskiene, S.1
García De Frutos, P.2
Carlemalm, E.3
Dahlbäck, B.4
Eriksson, S.5
-
23
-
-
84873493924
-
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
-
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
-
25
-
-
84874463886
-
Extracellular chaperones
-
Dabbs, R. A., Wyatt, A. R., Yerbury, J. J., Ecroyd, H. & Wilson, M. R. Extracellular chaperones. Top Curr. Chem. 328, 241-268 (2013).
-
(2013)
Top Curr. Chem.
, vol.328
, pp. 241-268
-
-
Dabbs, R.A.1
Wyatt, A.R.2
Yerbury, J.J.3
Ecroyd, H.4
Wilson, M.R.5
-
26
-
-
84863986350
-
Roles of extracellular chaperones in amyloidosis
-
Wyatt, A. R., Yerbury, J. J., Dabbs, R. A. & Wilson, M. R. Roles of extracellular chaperones in amyloidosis. J. Mol. Biol. 421, 499-516. (2012).
-
(2012)
J. Mol. Biol.
, vol.421
, pp. 499-516
-
-
Wyatt, A.R.1
Yerbury, J.J.2
Dabbs, R.A.3
Wilson, M.R.4
-
27
-
-
84878916720
-
Extracellular chaperones and proteostasis
-
Wyatt, A. R., Yerbury, J. J., Ecroyd, H. & Wilson, M. R. Extracellular chaperones and proteostasis. Annu. Rev. Biochem. 82, 295-322 (2013).
-
(2013)
Annu. Rev. Biochem.
, vol.82
, pp. 295-322
-
-
Wyatt, A.R.1
Yerbury, J.J.2
Ecroyd, H.3
Wilson, M.R.4
-
28
-
-
79953208604
-
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
-
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
-
30
-
-
84977270308
-
The crystal structure of the calcium-free Serum Amyloid P-component decamer
-
[Hazenberg, B. P. & Bijzet, J. (ed.)] (Groningen, The Netherlands)
-
Coker, A. R. et al. The crystal structure of the calcium-free Serum Amyloid P-component decamer. The Proceedings of the XIIIth International Symposium on Amyloidosis "From Misfolded Proteins to Well-Designed Treatment" [Hazenberg, B. P. & Bijzet, J. (ed.)] [64-66] (Groningen, The Netherlands, 2013).
-
(2013)
The Proceedings of the XIIIth International Symposium on Amyloidosis "from Misfolded Proteins to Well-Designed Treatment"
, pp. 64-66
-
-
Coker, A.R.1
-
31
-
-
0020085635
-
Calcium-dependent aggregation of human serum amyloid P component
-
Baltz, M. L., De Beer, F. C., Feinstein, A. & Pepys, M. B. Calcium-dependent aggregation of human serum amyloid P component. Biochim. Biophys. Acta 701, 229-236 (1982).
-
(1982)
Biochim. Biophys. Acta
, vol.701
, pp. 229-236
-
-
Baltz, M.L.1
De Beer, F.C.2
Feinstein, A.3
Pepys, M.B.4
-
32
-
-
0031587295
-
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
-
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
-
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
-
35
-
-
0034684197
-
Alpha-1-acid glycoprotein
-
Fournier, T., Medjoubi-N, N. & Porquet, D. Alpha-1-acid glycoprotein. Biochim. Biophys. Acta 1482, 157-171 (2000).
-
(2000)
Biochim. Biophys. Acta
, vol.1482
, pp. 157-171
-
-
Fournier, T.1
Medjoubi-N, N.2
Porquet, D.3
-
36
-
-
74349084862
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
46
-
-
84954405061
-
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
-
Stull, F., Koldewey, P., Humes, J. R., Radford, S. E. & Bardwell, J. C. Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nat. Struct. Mol. Biol. 23, 53-58 (2016).
-
(2016)
Nat. Struct. Mol. Biol.
, vol.23
, pp. 53-58
-
-
Stull, F.1
Koldewey, P.2
Humes, J.R.3
Radford, S.E.4
Bardwell, J.C.5
-
47
-
-
0036678856
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
|