Nalazite se na CroRIS probnoj okolini. Ovdje evidentirani podaci neće biti pohranjeni u Informacijskom sustavu znanosti RH. Ako je ovo greška, CroRIS produkcijskoj okolini moguće je pristupi putem poveznice www.croris.hr
izvor podataka: crosbi

Alternative glycosylation modulates function of IgG and other proteins - Implications on evolution and disease (CROSBI ID 188521)

Prilog u časopisu | pregledni rad (znanstveni) | međunarodna recenzija

Gornik, Olga ; Pavić, Tamara ; Lauc, Gordan Alternative glycosylation modulates function of IgG and other proteins - Implications on evolution and disease // Biochimica et biophysica acta. G, General subjects, 1820 (2012), 9; 1318-1326. doi: 10.1016/j.bbagen.2011.12.004

Podaci o odgovornosti

Gornik, Olga ; Pavić, Tamara ; Lauc, Gordan

engleski

Alternative glycosylation modulates function of IgG and other proteins - Implications on evolution and disease

Nearly all membrane and secreted proteins, as well as numerous intracellular proteins are glycosylated. However, contrary to proteins which are defined by their individual genetic templates, glycans are encoded in a complex dynamic network of hundreds of genes which participate in the complex biosynthetic pathway of protein glycosylation. This review summarizes present knowledge about the importance of alternative glycosylation of IgG and other proteins. Numerous proteins depend on correct glycosylation for proper function. Very good example for this is the alternative glycosylation of IgG whose effector functions can be completely changed by the addition or removal of a single monosaccharide residue from its glycans. The change in the structure of a protein requires mutations in DNA and subsequent selection in the next generation, while even slight alterations in activity or intracellular localization of one or more biosynthetic enzymes are sufficient for the creation of novel glycan structures, which can then perform new functions. Glycome composition varies significantly between individuals, which makes them slightly or even significantly different in their ability to execute specific molecular pathways with numerous implications for development and progression of various diseases. This article is part of a Special Issue entitled Glycoproteomics.

protein glycosylation ; glycome ; glycoprotein ; glycan ; evolution ; disease

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

Podaci o izdanju

1820 (9)

2012.

1318-1326

objavljeno

0304-4165

10.1016/j.bbagen.2011.12.004

Povezanost rada

Biologija, Temeljne medicinske znanosti

Poveznice
Indeksiranost