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090			_aB-10054
245	1	0	_aIn silicio Identification of Glycosyl-Phosphatidylinositol-Anchored Plasma-Membrane and Cell Wall Proteins of Saccharomyces cerevisiae
490	0		_vYeast, 13(15), p.1477-1489, 1998
520	3		_aUse of the Von Heijne algorithm allowed the identification of 686 open reading frames (ORFs)in the genome of Saccharomyces cerevisiae that encode proteins with a potential N-terminal signal sequence for entering the secretory pathway. On further analysis, 51 of these proteins contain a potential glycosyl-phosphatidylinositol (GPI)- attachment signal. Seven additional ORFs were found to belong to this group. Upon examination of the possible GPI-attachment sites, it was found that in yeast the most probable amino acids for GPI-attachment are asparagine and glycine. In yeast, GPI-proteins are found at the cell surface, either attached to the plasma-membrane or as an intrinsic part of the cell wall. It was noted that plasma-membrane GPI-proteins possess a dibasic residue motif just before their predicted GPI-attachment site. Based on this, and on homologies between proteins, families of plasma-membrane and cell wall proteins were assigned, revealing 20 potential plasma-membrane and 38 potential cell wall proteins. For members of three plasma-membrane protein families, a function has been described. On the other hand, most of the cell wall proteins seem to be structural components of the wall, responsive to different growth conditions. The GPI-attachment site of yeast slightly differs from mammalian cells. This might be of use in the development of anti-fungal drugs.
650	1	4	_aGPI-ANCHOR
650	1	4	_aGPI-ATTACHMENT SITE
650	1	4	_aYEAST
650	1	4	_aASCOMYCETES
650	1	4	_aFUNGI
700	1	2	_aHeleen, L.
700	1	2	_aCaro, P.
700	1	2	_aTettelin, H.
700	1	2	_aVossen, J.H.
700	1	2	_aRam, A.F.J.
700	1	2	_aVan Den Ende, H.
700	1	2	_aKlis, F.M.
856	4	0	_uhttps://drive.google.com/file/d/1bN_kIqGQD5IKExYa7C1iSOxMAvg7W4UN/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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