HTRA1

HtrA serine peptidase 1, also known as HTRA1, is a human gene.cite web | title = Entrez Gene: HTRA1 HtrA serine peptidase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5654| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a member of the trypsin family of serine proteases. This protein is a secreted enzyme that is proposed to regulate the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. It has also been suggested to be a regulator of cell growth.cite web | title = Entrez Gene: HTRA1 HtrA serine peptidase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5654| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Zurawa-Janicka D, Narkiewicz J, Lipińska B |title= [Characterization of the HtrA family of proteins] |journal=Postepy Biochem. |volume=53 |issue= 1 |pages= 27–36 |year= 2007 |pmid= 17718385 |doi=
*cite journal | author=Andersson B, Wentland MA, Ricafrente JY, "et al." |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138
*cite journal | author=Zumbrunn J, Trueb B |title=Primary structure of a putative serine protease specific for IGF-binding proteins. |journal=FEBS Lett. |volume=398 |issue= 2-3 |pages= 187–92 |year= 1997 |pmid= 8977104 |doi=
*cite journal | author=Yu W, Andersson B, Worley KC, "et al." |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=
*cite journal | author=Zumbrunn J, Trueb B |title=Localization of the gene for a serine protease with IGF-binding domain (PRSS11) to human chromosome 10q25.3-q26.2. |journal=Genomics |volume=45 |issue= 2 |pages= 461–2 |year= 1998 |pmid= 9344681 |doi= 10.1006/geno.1997.4953
*cite journal | author=Hu SI, Carozza M, Klein M, "et al." |title=Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage. |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34406–12 |year= 1999 |pmid= 9852107 |doi=
*cite journal | author=Baldi A, De Luca A, Morini M, "et al." |title=The HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cells. |journal=Oncogene |volume=21 |issue= 43 |pages= 6684–8 |year= 2002 |pmid= 12242667 |doi= 10.1038/sj.onc.1205911
*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=Nie GY, Hampton A, Li Y, "et al." |title=Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2. |journal=Biochem. J. |volume=371 |issue= Pt 1 |pages= 39–48 |year= 2003 |pmid= 12513693 |doi= 10.1042/BJ20021569
*cite journal | author=De Luca A, De Falco M, Severino A, "et al." |title=Distribution of the serine protease HtrA1 in normal human tissues. |journal=J. Histochem. Cytochem. |volume=51 |issue= 10 |pages= 1279–84 |year= 2003 |pmid= 14500695 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Chien J, Staub J, Hu SI, "et al." |title=A candidate tumor suppressor HtrA1 is downregulated in ovarian cancer. |journal=Oncogene |volume=23 |issue= 8 |pages= 1636–44 |year= 2004 |pmid= 14716297 |doi= 10.1038/sj.onc.1207271
*cite journal | author=Oka C, Tsujimoto R, Kajikawa M, "et al." |title=HtrA1 serine protease inhibits signaling mediated by Tgfbeta family proteins. |journal=Development |volume=131 |issue= 5 |pages= 1041–53 |year= 2004 |pmid= 14973287 |doi= 10.1242/dev.00999
*cite journal | author=Colland F, Jacq X, Trouplin V, "et al." |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104
*cite journal | author=Grau S, Baldi A, Bussani R, "et al." |title=Implications of the serine protease HtrA1 in amyloid precursor protein processing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 17 |pages= 6021–6 |year= 2005 |pmid= 15855271 |doi= 10.1073/pnas.0501823102
*cite journal | author=Ozturk A, Desai PP, Minster RL, "et al." |title=Three SNPs in the GSTO1, GSTO2 and PRSS11 genes on chromosome 10 are not associated with age-at-onset of Alzheimer's disease. |journal=Neurobiol. Aging |volume=26 |issue= 8 |pages= 1161–5 |year= 2005 |pmid= 15917099 |doi= 10.1016/j.neurobiolaging.2004.11.001
*cite journal | author=Grau S, Richards PJ, Kerr B, "et al." |title=The role of human HtrA1 in arthritic disease. |journal=J. Biol. Chem. |volume=281 |issue= 10 |pages= 6124–9 |year= 2006 |pmid= 16377621 |doi= 10.1074/jbc.M500361200
*cite journal | author=Bowden MA, Di Nezza-Cossens LA, Jobling T, "et al." |title=Serine proteases HTRA1 and HTRA3 are down-regulated with increasing grades of human endometrial cancer. |journal=Gynecol. Oncol. |volume=103 |issue= 1 |pages= 253–60 |year= 2006 |pmid= 16650464 |doi= 10.1016/j.ygyno.2006.03.006
*cite journal | author=Chien J, Aletti G, Baldi A, "et al." |title=Serine protease HtrA1 modulates chemotherapy-induced cytotoxicity. |journal=J. Clin. Invest. |volume=116 |issue= 7 |pages= 1994–2004 |year= 2006 |pmid= 16767218 |doi= 10.1172/JCI27698
*cite journal | author=Dewan A, Liu M, Hartman S, "et al." |title=HTRA1 promoter polymorphism in wet age-related macular degeneration. |journal=Science |volume=314 |issue= 5801 |pages= 989–92 |year= 2006 |pmid= 17053108 |doi= 10.1126/science.1133807

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