- COL25A1
Collagen, type XXV, alpha 1, also known as COL25A1, is a human
gene .cite web | title = Entrez Gene: COL25A1 collagen, type XXV, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84570| accessdate = ]PBB_Summary
section_title =
summary_text = COL25A1 is a brain-specific membrane-bound collagen. Proteolytic processing releases CLAC, a soluble form of COL25A1 containing the extracellular collagen domains that associates with senile plaques in Alzheimer disease (AD; MIM 104300) brains (Osada et al., 2005). [supplied by OMIM] cite web | title = Entrez Gene: COL25A1 collagen, type XXV, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84570| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Kakuyama H, Söderberg L, Horigome K, "et al." |title=CLAC binds to aggregated Abeta and Abeta fragments, and attenuates fibril elongation. |journal=Biochemistry |volume=44 |issue= 47 |pages= 15602-9 |year= 2006 |pmid= 16300410 |doi= 10.1021/bi051263e
*cite journal | author=Söderberg L, Dahlqvist C, Kakuyama H, "et al." |title=Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. |journal=FEBS J. |volume=272 |issue= 9 |pages= 2231-6 |year= 2005 |pmid= 15853808 |doi= 10.1111/j.1742-4658.2005.04647.x
*cite journal | author=Osada Y, Hashimoto T, Nishimura A, "et al." |title=CLAC binds to amyloid beta peptides through the positively charged amino acid cluster within the collagenous domain 1 and inhibits formation of amyloid fibrils. |journal=J. Biol. Chem. |volume=280 |issue= 9 |pages= 8596-605 |year= 2005 |pmid= 15615705 |doi= 10.1074/jbc.M413340200
*cite journal | author=Söderberg L, Kakuyama H, Möller A, "et al." |title=Characterization of the Alzheimer's disease-associated CLAC protein and identification of an amyloid beta-peptide-binding site. |journal=J. Biol. Chem. |volume=280 |issue= 2 |pages= 1007-15 |year= 2005 |pmid= 15522881 |doi= 10.1074/jbc.M403628200
*cite journal | author=Kowa H, Sakakura T, Matsuura Y, "et al." |title=Mostly separate distributions of CLAC- versus Abeta40- or thioflavin S-reactivities in senile plaques reveal two distinct subpopulations of beta-amyloid deposits. |journal=Am. J. Pathol. |volume=165 |issue= 1 |pages= 273-81 |year= 2004 |pmid= 15215182 |doi=
*cite journal | author=Söderberg L, Zhukareva V, Bogdanovic N, "et al." |title=Molecular identification of AMY, an Alzheimer disease amyloid-associated protein. |journal=J. Neuropathol. Exp. Neurol. |volume=62 |issue= 11 |pages= 1108-17 |year= 2004 |pmid= 14656069 |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=Hashimoto T, Wakabayashi T, Watanabe A, "et al." |title=CLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXV. |journal=EMBO J. |volume=21 |issue= 7 |pages= 1524-34 |year= 2002 |pmid= 11927537 |doi= 10.1093/emboj/21.7.1524PBB_Controls
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