ALG8

Asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase), also known as ALG8, is a human gene.cite web | title = Entrez Gene: ALG8 asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79053| 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 second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation of proteins. Mutations in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ih). Alternatively spliced transcript variants encoding different isoforms have been identified.cite web | title = Entrez Gene: ALG8 asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79053| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Jaeken J |title=Congenital disorders of glycosylation (CDG): update and new developments. |journal=J. Inherit. Metab. Dis. |volume=27 |issue= 3 |pages= 423–6 |year= 2005 |pmid= 15272470 |doi=
*cite journal | author=Jaeken J, Carchon H |title=Congenital disorders of glycosylation: a booming chapter of pediatrics. |journal=Curr. Opin. Pediatr. |volume=16 |issue= 4 |pages= 434–9 |year= 2004 |pmid= 15273506 |doi=
*cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, "et al." |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3–174 |year= 1995 |pmid= 7566098 |doi=
*cite journal | author=Stanchi F, Bertocco E, Toppo S, "et al." |title=Characterization of 16 novel human genes showing high similarity to yeast sequences. |journal=Yeast |volume=18 |issue= 1 |pages= 69–80 |year= 2001 |pmid= 11124703 |doi= 10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H |doilabel=10.1002/1097-0061(200101)18:169::AID-YEA6473.0.CO;2-H
*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=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=Chantret I, Dancourt J, Dupré T, "et al." |title=A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9962–71 |year= 2003 |pmid= 12480927 |doi= 10.1074/jbc.M211950200
*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=Schollen E, Frank CG, Keldermans L, "et al." |title=Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency). |journal=J. Med. Genet. |volume=41 |issue= 7 |pages= 550–6 |year= 2004 |pmid= 15235028 |doi=
*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=Otsuki T, Ota T, Nishikawa T, "et al." |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117
*cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, "et al." |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406

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