- SAA2
Serum amyloid A2, also known as SAA2, is a human
gene . [cite web | title = Entrez Gene: SAA2 Serum amyloid A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6289| accessdate = ]PBB_Summary
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summary_text =References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Betts JC, Edbrooke MR, Thakker RV, Woo P |title=The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells. |journal=Scand. J. Immunol. |volume=34 |issue= 4 |pages= 471–82 |year= 1991 |pmid= 1656519 |doi=
*cite journal | author=Zimlichman S, Danon A, Nathan I, "et al." |title=Serum amyloid A, an acute phase protein, inhibits platelet activation. |journal=J. Lab. Clin. Med. |volume=116 |issue= 2 |pages= 180–6 |year= 1990 |pmid= 1697614 |doi=
*cite journal | author=Steinkasserer A, Weiss EH, Schwaeble W, Linke RP |title=Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis. |journal=Biochem. J. |volume=268 |issue= 1 |pages= 187–93 |year= 1990 |pmid= 1971508 |doi=
*cite journal | author=Woo P, Sipe J, Dinarello CA, Colten HR |title=Structure of a human serum amyloid A gene and modulation of its expression in transfected L cells. |journal=J. Biol. Chem. |volume=262 |issue= 32 |pages= 15790–5 |year= 1987 |pmid= 2890635 |doi=
*cite journal | author=Kluve-Beckerman B, Dwulet FE, Benson MD |title=Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person. |journal=J. Clin. Invest. |volume=82 |issue= 5 |pages= 1670–5 |year= 1988 |pmid= 3183061 |doi=
*cite journal | author=Kluve-Beckerman B, Long GL, Benson MD |title=DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA). |journal=Biochem. Genet. |volume=24 |issue= 11-12 |pages= 795–803 |year= 1987 |pmid= 3800865 |doi=
*cite journal | author=Meek RL, Hoffman JS, Benditt EP |title=Amyloidogenesis. One serum amyloid A isotype is selectively removed from the circulation. |journal=J. Exp. Med. |volume=163 |issue= 3 |pages= 499–510 |year= 1986 |pmid= 3950541 |doi=
*cite journal | author=Badolato R, Wang JM, Murphy WJ, "et al." |title=Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. |journal=J. Exp. Med. |volume=180 |issue= 1 |pages= 203–9 |year= 1994 |pmid= 7516407 |doi=
*cite journal | author=Badolato R, Johnston JA, Wang JM, "et al." |title=Serum amyloid A induces calcium mobilization and chemotaxis of human monocytes by activating a pertussis toxin-sensitive signaling pathway. |journal=J. Immunol. |volume=155 |issue= 8 |pages= 4004–10 |year= 1995 |pmid= 7561109 |doi=
*cite journal | author=Xu L, Badolato R, Murphy WJ, "et al." |title=A novel biologic function of serum amyloid A. Induction of T lymphocyte migration and adhesion. |journal=J. Immunol. |volume=155 |issue= 3 |pages= 1184–90 |year= 1995 |pmid= 7636186 |doi=
*cite journal | author=Steel DM, Sellar GC, Uhlar CM, "et al." |title=A constitutively expressed serum amyloid A protein gene (SAA4) is closely linked to, and shares structural similarities with, an acute-phase serum amyloid A protein gene (SAA2). |journal=Genomics |volume=16 |issue= 2 |pages= 447–54 |year= 1993 |pmid= 7686132 |doi= 10.1006/geno.1993.1209
*cite journal | author=Liepnieks JJ, Kluve-Beckerman B, Benson MD |title=Characterization of amyloid A protein in human secondary amyloidosis: the predominant deposition of serum amyloid A1. |journal=Biochim. Biophys. Acta |volume=1270 |issue= 1 |pages= 81–6 |year= 1995 |pmid= 7827140 |doi=
*cite journal | author=Arai K, Miura K, Baba S, Shirasawa H |title=Transformation from SAA2-fibrils to AA-fibrils in amyloid fibrillogenesis: in vivo observations in murine spleen using anti-SAA and anti-AA antibodies. |journal=J. Pathol. |volume=173 |issue= 2 |pages= 127–34 |year= 1994 |pmid= 8089807 |doi= 10.1002/path.1711730209
*cite journal | author=Meek RL, Urieli-Shoval S, Benditt EP |title=Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: implications for serum amyloid A function. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 3186–90 |year= 1994 |pmid= 8159722 |doi=
*cite journal | author=Sellar GC, Jordan SA, Bickmore WA, "et al." |title=The human serum amyloid A protein (SAA) superfamily gene cluster: mapping to chromosome 11p15.1 by physical and genetic linkage analysis. |journal=Genomics |volume=19 |issue= 2 |pages= 221–7 |year= 1994 |pmid= 8188252 |doi= 10.1006/geno.1994.1051
*cite journal | author=Ducret A, Bruun CF, Bures EJ, "et al." |title=Characterization of human serum amyloid A protein isoforms separated by two-dimensional electrophoresis by liquid chromatography/electrospray ionization tandem mass spectrometry. |journal=Electrophoresis |volume=17 |issue= 5 |pages= 866–76 |year= 1996 |pmid= 8783012 |doi= 10.1002/elps.1150170508
*cite journal | author=Ancsin JB, Kisilevsky R |title=Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 406–13 |year= 1997 |pmid= 8995276 |doi=
*cite journal | author=Hershkoviz R, Preciado-Patt L, Lider O, "et al." |title=Extracellular matrix-anchored serum amyloid A preferentially induces mast cell adhesion. |journal=Am. J. Physiol. |volume=273 |issue= 1 Pt 1 |pages= C179–87 |year= 1997 |pmid= 9252455 |doi=
*cite journal | author=Migita K, Kawabe Y, Tominaga M, "et al." |title=Serum amyloid A protein induces production of matrix metalloproteinases by human synovial fibroblasts. |journal=Lab. Invest. |volume=78 |issue= 5 |pages= 535–9 |year= 1998 |pmid= 9605178 |doi=
*cite journal | author=Urieli-Shoval S, Cohen P, Eisenberg S, Matzner Y |title=Widespread expression of serum amyloid A in histologically normal human tissues. Predominant localization to the epithelium. |journal=J. Histochem. Cytochem. |volume=46 |issue= 12 |pages= 1377–84 |year= 1999 |pmid= 9815279 |doi=PBB_Controls
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