- ADAMTS3
ADAM metallopeptidase with thrombospondin type 1 motif, 3, also known as ADAMTS3, is a human
gene .cite web | title = Entrez Gene: ADAMTS3 ADAM metallopeptidase with thrombospondin type 1 motif, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9508| accessdate = ]PBB_Summary
section_title =
summary_text = This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene is the major procollagen II N-propeptidase. A deficiency of this protein may be responsible for dermatosparaxis, a genetic defect of connective tissues.cite web | title = Entrez Gene: ADAMTS3 ADAM metallopeptidase with thrombospondin type 1 motif, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9508| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Tang BL, Hong W |title=ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats. |journal=FEBS Lett. |volume=445 |issue= 2-3 |pages= 223–5 |year= 1999 |pmid= 10094461 |doi=
*cite journal | author=Tang BL |title=ADAMTS: a novel family of extracellular matrix proteases. |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 1 |pages= 33–44 |year= 2001 |pmid= 11167130 |doi=
*cite journal | author=Martel-Pelletier J, Welsch DJ, Pelletier JP |title=Metalloproteases and inhibitors in arthritic diseases. |journal=Best practice & research. Clinical rheumatology |volume=15 |issue= 5 |pages= 805–29 |year= 2002 |pmid= 11812023 |doi= 10.1053/berh.2001.0195
*cite journal | author=Hirohata S |title= [ADAMTS family--new extracellular matrix degrading enzyme] |journal=Seikagaku |volume=73 |issue= 11 |pages= 1333–7 |year= 2002 |pmid= 11831030 |doi=
*cite journal | author=Nagase T, Ishikawa K, Nakajima D, "et al." |title=Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=4 |issue= 2 |pages= 141–50 |year= 1997 |pmid= 9205841 |doi=
*cite journal | author=Hurskainen TL, Hirohata S, Seldin MF, Apte SS |title=ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25555–63 |year= 1999 |pmid= 10464288 |doi=
*cite journal | author=Fernandes RJ, Hirohata S, Engle JM, "et al." |title=Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. |journal=J. Biol. Chem. |volume=276 |issue= 34 |pages= 31502–9 |year= 2001 |pmid= 11408482 |doi= 10.1074/jbc.M103466200
*cite journal | author=Colige A, Vandenberghe I, Thiry M, "et al." |title=Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3. |journal=J. Biol. Chem. |volume=277 |issue= 8 |pages= 5756–66 |year= 2002 |pmid= 11741898 |doi= 10.1074/jbc.M105601200
*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.242603899PBB_Controls
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