- AOAH
Acyloxyacyl hydrolase (neutrophil), also known as AOAH, is a human
gene .cite web | title = Entrez Gene: AOAH acyloxyacyl hydrolase (neutrophil)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=313| accessdate = ]PBB_Summary
section_title =
summary_text = Acyloxyacyl hydrolase (AOAH) is a 2-subunit lipase which selectively hydrolyzes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial endotoxins. AOAH may modulate host inflammatory responses to gram-negative bacterial invasion. The 2 subunits are encoded by a single mRNA.cite web | title = Entrez Gene: AOAH acyloxyacyl hydrolase (neutrophil)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=313| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Hagen FS, Grant FJ, Kuijper JL, "et al." |title=Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides. |journal=Biochemistry |volume=30 |issue= 34 |pages= 8415–23 |year= 1991 |pmid= 1883828 |doi=
*cite journal | author=McDermott CM, Cullor JS, Fenwick BW |title=Intracellular and extracellular enzymatic deacylation of bacterial endotoxin during localized inflammation induced by Escherichia coli. |journal=Infect. Immun. |volume=59 |issue= 2 |pages= 478–85 |year= 1991 |pmid= 1987068 |doi=
*cite journal | author=Whitmore TE, Mathewes SL, O'Hara PJ, Durnam DM |title=Chromosomal localization of the acyloxyacyl hydrolase (AOAH) gene to 7p14-p12 using fluorescence in situ hybridization. |journal=Genomics |volume=21 |issue= 2 |pages= 457–8 |year= 1994 |pmid= 8088847 |doi= 10.1006/geno.1994.1298
*cite journal | author=Staab JF, Ginkel DL, Rosenberg GB, Munford RS |title=A saposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase. |journal=J. Biol. Chem. |volume=269 |issue= 38 |pages= 23736–42 |year= 1994 |pmid= 8089145 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Coulthard MG, Swindle J, Munford RS, "et al." |title=Adenovirus-mediated transfer of a gene encoding acyloxyacyl hydrolase (AOAH) into mice increases tissue and plasma AOAH activity. |journal=Infect. Immun. |volume=64 |issue= 5 |pages= 1510–5 |year= 1996 |pmid= 8613354 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes
Wikimedia Foundation. 2010.
