Literature for peptidase C13.005: glycosylphosphatidylinositol:protein transamidase
(Topics flags: M Mutation, K Knockout, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)
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Sah,S.K., Shefali,S., Yadav,A., Som,P. and Komath,S.S.
The caspase-like Gpi8 subunit of Candida albicans GPI transamidase is a metal-dependent endopeptidase
Biochem Biophys Res Commun PubMed Europe PubMed DOI -
Bundy,M.G., Kosentka,P.Z., Willet,A.H., Zhang,L., Miller,E. and Shpak,E.D.
A mutation in the catalytic subunit of the glycosylphosphatidylinositol transamidase disrupts growth, fertility, and stomata formation
Plant Physiol171, 974-985. PubMed Europe PubMed DOI M -
Riezman,H. and Conzelmann,A.
Glycosylphosphatidylinositol: protein transamidase
[ISSN:978-0-12-407743-0]3, 2320-2323. DOI -
Riezman,H. and Conzelmann,A.
Glycosylphosphatidylinositol:protein transamidase
[ISSN:0-12-079610-4]2, 1313-1317. V -
[YEAR:28-3-2000]Meyer,U., Benghezal,M., Imhof,I. and Conzelmann,A.
Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins
Biochemistry39, 3461-3471. PubMed Europe PubMed DOI -
Ohishi,K., Inoue,N., Maeda,Y., Takeda,J., Riezman,H. and Kinoshita,T.
Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins
Mol Biol Cell11, 1523-1533. PubMed Europe PubMed -
[YEAR:11-11-1997]Yu,J., Nagarajan,S., Knez,J.J., Udenfriend,S., Chen,R. and Medof,M.E.
The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase
Proc Natl Acad Sci U S A94, 12580-12585. PubMed Europe PubMed DOI -
Chen,R., Udenfriend,S., Prince,G.M., Maxwell,S.E., Ramalingam,S., Gerber,L.D., Knez,J. and Medof,M.E.
A defect in glycosylphosphatidylinositol (GPI) transamidase activity in mutant K cells is responsible for their inability to display GPI surface proteins
Proc Natl Acad Sci U S A93, 2280-2284. PubMed Europe PubMed DOI K
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