- ALG6
Asparagine-linked glycosylation 6 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase), also known as ALG6, is a human
gene .cite web | title = Entrez Gene: ALG6 asparagine-linked glycosylation 6 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29929| accessdate = ]PBB_Summary
section_title =
summary_text = This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type Ic.cite web | title = Entrez Gene: ALG6 asparagine-linked glycosylation 6 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29929| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Burda P, Borsig L, de Rijk-van Andel J, "et al." |title=A novel carbohydrate-deficient glycoprotein syndrome characterized by a deficiency in glucosylation of the dolichol-linked oligosaccharide. |journal=J. Clin. Invest. |volume=102 |issue= 4 |pages= 647–52 |year= 1998 |pmid= 9710431 |doi=
*cite journal | author=Körner C, Knauer R, Holzbach U, "et al." |title=Carbohydrate-deficient glycoprotein syndrome type V: deficiency of dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 22 |pages= 13200–5 |year= 1998 |pmid= 9789065 |doi=
*cite journal | author=Imbach T, Burda P, Kuhnert P, "et al." |title=A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 12 |pages= 6982–7 |year= 1999 |pmid= 10359825 |doi=
*cite journal | author=Imbach T, Grünewald S, Schenk B, "et al." |title=Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic. |journal=Hum. Genet. |volume=106 |issue= 5 |pages= 538–45 |year= 2000 |pmid= 10914684 |doi=
*cite journal | author=Westphal V, Schottstädt C, Marquardt T, Freeze HH |title=Analysis of multiple mutations in the hALG6 gene in a patient with congenital disorder of glycosylation Ic. |journal=Mol. Genet. Metab. |volume=70 |issue= 3 |pages= 219–23 |year= 2000 |pmid= 10924277 |doi= 10.1006/mgme.2000.3017
*cite journal | author=Westphal V, Murch S, Kim S, "et al." |title=Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation. |journal=Am. J. Pathol. |volume=157 |issue= 6 |pages= 1917–25 |year= 2001 |pmid= 11106564 |doi=
*cite journal | author=de Lonlay P, Seta N, Barrot S, "et al." |title=A broad spectrum of clinical presentations in congenital disorders of glycosylation I: a series of 26 cases. |journal=J. Med. Genet. |volume=38 |issue= 1 |pages= 14–9 |year= 2001 |pmid= 11134235 |doi=
*cite journal | author=Vuillaumier-Barrot S, Le Bizec C, Durand G, Seta N |title=The T911C (F304S) substitution in the human ALG6 gene is a common polymorphism and not a causal mutation of CDG-Ic. |journal=J. Hum. Genet. |volume=46 |issue= 9 |pages= 547–8 |year= 2001 |pmid= 11558905 |doi=
*cite journal | author=Westphal V, Kjaergaard S, Schollen E, "et al." |title=A frequent mild mutation in ALG6 may exacerbate the clinical severity of patients with congenital disorder of glycosylation Ia (CDG-Ia) caused by phosphomannomutase deficiency. |journal=Hum. Mol. Genet. |volume=11 |issue= 5 |pages= 599–604 |year= 2002 |pmid= 11875054 |doi=
*cite journal | author=Oriol R, Martinez-Duncker I, Chantret I, "et al." |title=Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate. |journal=Mol. Biol. Evol. |volume=19 |issue= 9 |pages= 1451–63 |year= 2003 |pmid= 12200473 |doi=
*cite journal | author=Schollen E, Martens K, Geuzens E, Matthijs G |title=DHPLC analysis as a platform for molecular diagnosis of congenital disorders of glycosylation (CDG). |journal=Eur. J. Hum. Genet. |volume=10 |issue= 10 |pages= 643–8 |year= 2003 |pmid= 12357336 |doi= 10.1038/sj.ejhg.5200858
*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=Imabayashi H, Mori T, Gojo S, "et al." |title=Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis. |journal=Exp. Cell Res. |volume=288 |issue= 1 |pages= 35–50 |year= 2003 |pmid= 12878157 |doi=
*cite journal | author=Westphal V, Xiao M, Kwok PY, Freeze HH |title=Identification of a frequent variant in ALG6, the cause of Congenital Disorder of Glycosylation-Ic. |journal=Hum. Mutat. |volume=22 |issue= 5 |pages= 420–1 |year= 2004 |pmid= 14517965 |doi= 10.1002/humu.9195
*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=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.2596504
*cite journal | author=Eklund EA, Sun L, Yang SP, "et al." |title=Congenital disorder of glycosylation Ic due to a de novo deletion and an hALG-6 mutation. |journal=Biochem. Biophys. Res. Commun. |volume=339 |issue= 3 |pages= 755–60 |year= 2006 |pmid= 16321363 |doi= 10.1016/j.bbrc.2005.11.073
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727PBB_Controls
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