| 释义 |
- References
- Further reading
{{Underlinked|date=May 2016}}{{Infobox_gene}}Dipeptidyl peptidase 9 is an enzyme that in humans is encoded by the DPP9 gene.[1]This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. The protein has been shown to have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Although the activity of this protein is similar to that of dipeptidyl peptidase 4 (DPP4), it does not appear to be membrane bound. In general, dipeptidyl peptidases appear to be involved in the regulation of the activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. Several transcript variants of this gene have been described but not fully characterized.[1] References1. ^1 {{cite web | title = Entrez Gene: DPP9 dipeptidyl-peptidase 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=91039| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal | vauthors=Olsen C, Wagtmann N |title=Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV |journal=Gene |volume=299 |issue= 1–2 |pages= 185–93 |year= 2003 |pmid= 12459266 |doi=10.1016/S0378-1119(02)01059-4 }}
- {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |display-authors=etal}}
- {{cite journal | vauthors=Ajami K, Abbott CA, Obradovic M |title=Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family |journal=Biochemistry |volume=42 |issue= 3 |pages= 694–701 |year= 2003 |pmid= 12534281 |doi= 10.1021/bi026846s |display-authors=etal}}
- {{cite journal | vauthors=Qi SY, Riviere PJ, Trojnar J |title=Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases |journal=Biochem. J. |volume=373 |issue= Pt 1 |pages= 179–89 |year= 2003 |pmid= 12662155 |doi= 10.1042/BJ20021914 | pmc=1223468 |display-authors=etal}}
- {{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |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 |display-authors=etal}}
- {{cite journal | vauthors=Ajami K, Abbott CA, McCaughan GW, Gorrell MD |title=Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity |journal=Biochim. Biophys. Acta |volume=1679 |issue= 1 |pages= 18–28 |year= 2004 |pmid= 15245913 |doi= 10.1016/j.bbaexp.2004.03.010 }}
- {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |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.2596504 | pmc=528928 |display-authors=etal}}
- {{cite journal | vauthors=Ogasawara W, Tanaka C, Suzuki M |title=Isoforms of dipeptidyl aminopeptidase IV from Pseudomonas sp. WO24: role of the signal sequence and overexpression in Escherichia coli |journal=Protein Expr. Purif. |volume=41 |issue= 2 |pages= 241–51 |year= 2005 |pmid= 15866709 |doi= 10.1016/j.pep.2004.10.027 |display-authors=etal}}
- {{cite journal | vauthors=Bjelke JR, Christensen J, Nielsen PF |title=Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV |journal=Biochem. J. |volume=396 |issue= 2 |pages= 391–9 |year= 2006 |pmid= 16475979 |doi= 10.1042/BJ20060079 | pmc=1462722 |display-authors=etal}}
- {{cite journal | vauthors=Yu DM, Wang XM, Ajami K |title=DP8 and DP9 have extra-enzymatic roles in cell adhesion, migration and apoptosis |journal=Adv. Exp. Med. Biol. |volume=575 |issue= |pages= 63–72 |year= 2006 |pmid= 16700509 |doi=10.1007/0-387-32824-6_7 | series=Advances in Experimental Medicine and Biology | isbn=978-0-387-29058-4 |display-authors=etal}}
- {{cite journal | vauthors=Yu DM, Wang XM, McCaughan GW, Gorrell MD |title=Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis |journal=FEBS J. |volume=273 |issue= 11 |pages= 2447–60 |year= 2006 |pmid= 16704418 |doi= 10.1111/j.1742-4658.2006.05253.x }}
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