Major acute-phase reactant synthesis during chronic inflammation in amyloid-susceptible and -resistant mouse strains

[1]  A. Whitehead,et al.  Molecular genetics of mouse serum amyloid P component (SAP): cloning and gene mapping , 2004, Immunogenetics.

[2]  J. Lélias,et al.  Mouse C-reactive protein. Generation of cDNA clones, structural analysis, and induction of mRNA during inflammation. , 1990, The Biochemical journal.

[3]  F. Gervais,et al.  apo‐SAA1/apo‐SAA2 Isotype Ratios during Casein‐ and Amyloid‐Enhancing‐Factor‐Induced Secondary Amyloidosis in A/J and C57BL/6J Mice , 1990, Scandinavian journal of immunology.

[4]  J. Sipe,et al.  Direct binding enzyme-linked immunosorbent assay (ELISA) for serum amyloid A (SAA). , 1989, Journal of immunological methods.

[5]  G. Coetzee,et al.  Human serum amyloid A protein. The assignment of the six major isoforms to three published gene sequences and evidence for two genetic loci. , 1989, The Journal of biological chemistry.

[6]  A. Whitehead,et al.  Acute phase induction of mouse serum amyloid P component. Correlation with other parameters of inflammation. , 1989, Journal of immunology.

[7]  I. Nakanishi,et al.  The role of fibronectin in the development of experimental amyloidosis. Evidence of immunohistochemical codistribution and binding property with serum amyloid protein A. , 1989, The American journal of pathology.

[8]  M. Pepys,et al.  Specific localization and imaging of amyloid deposits in vivo using 123I-labeled serum amyloid P component , 1988, The Journal of experimental medicine.

[9]  G. Coetzee,et al.  Identification of three isoform patterns of human serum amyloid A protein. , 1988, The Biochemical journal.

[10]  H. Moses,et al.  Induction of fibronectin gene transcription and mRNA is a primary response to growth-factor stimulation of AKR-2B cells. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[11]  Z. Ali-Khan,et al.  Alveolar hydatid cyst induced amyloid enhancing factor (AEF): physicochemical properties and abolition of AEF activity by serine protease inhibitors. , 1988, British journal of experimental pathology.

[12]  I. Nakanishi,et al.  Specific Deposition of Serum Amyloid A Protein 2 in the Mouse , 1987, Scandinavian journal of immunology.

[13]  R. Mortensen,et al.  Binding specificity of mouse serum amyloid P-component for fibronectin. , 1986, Immunological investigations.

[14]  M. Pepys,et al.  Circulating serum amyloid P component is the precursor of amyloid P component in tissue amyloid deposits. , 1986, Clinical and experimental immunology.

[15]  M. Pepys,et al.  Is the serum amyloid A protein in acute phase plasma high density lipoprotein the precursor of AA amyloid fibrils? , 1986, Clinical and experimental immunology.

[16]  R. Meek,et al.  Amyloid A gene family expression in different mouse tissues , 1986, The Journal of experimental medicine.

[17]  D. Potter,et al.  Structure of the murine serum amyloid A gene family. Gene conversion. , 1986, The Journal of biological chemistry.

[18]  S. Migita,et al.  Diverse gene expression for isotypes of murine serum amyloid A protein during acute phase reaction. , 1986, Science.

[19]  R. Meek,et al.  Amyloidogenesis. One serum amyloid A isotype is selectively removed from the circulation , 1986, The Journal of experimental medicine.

[20]  H. Colten,et al.  Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA. , 1985, Biochemistry.

[21]  G. Marhaug,et al.  Transformation of Amyloid Precursor SAA to Protein AA and Incorporation in Amyloid Fibrils in Vivo , 1985, Scandinavian journal of immunology.

[22]  K. Beisel,et al.  Acute-phase reactants of mice. II. Strain dependence of serum amyloid P-component (SAP) levels and response to inflammation. , 1983, Journal of immunology.

[23]  R. Kisilevsky,et al.  Kinetics of amyloid deposition. I. The effects of amyloid-enhancing factor and splenectomy. , 1983, Laboratory investigation; a journal of technical methods and pathology.

[24]  I. Kushner THE PHENOMENON OF THE ACUTE PHASE RESPONSE * , 1982, Annals of the New York Academy of Sciences.

[25]  A. Feinstein,et al.  Fibronectin and C4-binding protein are selectively bound by aggregated amyloid P component , 1981, The Journal of experimental medicine.

[26]  C. Auffray,et al.  Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. , 2005, European journal of biochemistry.

[27]  M. Pepys,et al.  Differences in the acute phase responses of serum amyloid P-component (SAP) and C3 to injections of casein or bovine serum albumin in amyloid-susceptible and -resistant mouse strains. , 1980, Clinical and experimental immunology.

[28]  M. Skinner,et al.  Binding of serum amyloid P-component (SAP) by amyloid fibrils. , 1979, Clinical and experimental immunology.

[29]  E. Cathcart,et al.  Amyloid resistance in A/J mice is determined by a single gene , 1979, Nature.

[30]  M. Pepys,et al.  Serum amyloid P-component is an acute-phase reactant in the mouse , 1979, Nature.

[31]  Kenneth M. Yamada,et al.  Fibronectins—adhesive glycoproteins of cell surface and blood , 1978, Nature.

[32]  J. Sipe,et al.  Biochemical evidence for the biphasic development of experimental amyloidosis. , 1978, Laboratory investigation; a journal of technical methods and pathology.

[33]  N. Eriksen,et al.  Amyloid protein SAA is associated with high density lipoprotein from human serum. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[34]  H. Gewurz,et al.  Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins). , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[35]  G. Glenner,et al.  Amyloid fibril protein AA: purification and properties of the antigenically related serum component as determined by solid phase radioimmunoassay. , 1976, Journal of immunology.

[36]  Axelsen Nh,et al.  Reversed rocket immunoelectrophoresis. , 1973 .

[37]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[38]  D. Janigan,et al.  Experimental amyloidosis. Role of antigenicity and rapid induction. , 1966, The American journal of pathology.

[39]  H. Puchtler,et al.  ON THE BINDING OF CONGO RED BY AMYLOID , 1962 .

[40]  A. Cohen,et al.  Electron Microscopic Observations on a Fibrous Component in Amyloid of Diverse Origins , 1959, Nature.