Glycoproteins found on the membrane or surface of cells
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Glycoproteins -- Pathophysiology -- Congresses : Advanced glycation end-products in nephrology / Meeting on Advanced Glycosylation End Products in Nephrology: Much More Than Diabetic Nephrology, January 14, 2000, Padua, Italy ; volume editors, Angela D'Angelo, Silvana Favaro, Giovanni Gambaro
N-Glycosidases that remove adenines from RIBOSOMAL RNA, depurinating the conserved alpha-sarcin loop of 28S RIBOSOMAL RNA. They often consist of a toxic A subunit and a binding lectin B subunit. They may be considered as PROTEIN SYNTHESIS INHIBITORS. They are found in many PLANTS and have cytotoxic and antiviral activity
Enzymes that catalyze the transfer of glycosyl groups to an acceptor. Most often another carbohydrate molecule acts as an acceptor, but inorganic phosphate can also act as an acceptor, such as in the case of PHOSPHORYLASES. Some of the enzymes in this group also catalyze hydrolysis, which can be regarded as transfer of a glycosyl group from the donor to water. Subclasses include the HEXOSYLTRANSFERASES; PENTOSYLTRANSFERASES; SIALYLTRANSFERASES; and those transferring other glycosyl groups. EC 2.4
Glycosides -- Congresses : Advances in plant glycosides, chemistry and biology : proceedings of the International Symposium on Plant Glycosides, August 12-15, 1997 Kunming, China / edited by Chong-Ren Yang and Osamu Tanaka
Glycosides -- Physiological effect -- Congresses : Advances in plant glycosides, chemistry and biology : proceedings of the International Symposium on Plant Glycosides, August 12-15, 1997 Kunming, China / edited by Chong-Ren Yang and Osamu Tanaka
N-Glycosidases that remove adenines from RIBOSOMAL RNA, depurinating the conserved alpha-sarcin loop of 28S RIBOSOMAL RNA. They often consist of a toxic A subunit and a binding lectin B subunit. They may be considered as PROTEIN SYNTHESIS INHIBITORS. They are found in many PLANTS and have cytotoxic and antiviral activity
A class of fibrous proteins or scleroproteins that represents the principal constituent of EPIDERMIS; HAIR; NAILS; horny tissues, and the organic matrix of tooth ENAMEL. Two major conformational groups have been characterized, alpha-keratin, whose peptide backbone forms a coiled-coil alpha helical structure consisting of TYPE I KERATIN and a TYPE II KERATIN, and beta-keratin, whose backbone forms a zigzag or pleated sheet structure. alpha-Keratins have been classified into at least 20 subtypes. In addition multiple isoforms of subtypes have been found which may be due to GENE DUPLICATION
