Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 7

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  protein glycosylation
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
1

The participation of ribosomes in protein glycosylation. Interaction of the ribosome-UDP-N-acetyl-glucosamine complex with dolichol phosphate

100%
Paszkiewicz-Gadek A., Porowska H., Galasinski W.
Acta Biochimica Polonica
|
1992
|
tom 39
|
nr 3
UDP-N-acetylglucosaminc can be bound by pure ribosomes. The part of N-acetylglucosamine-1-P can be transferred from the complex ribosome-UDP-N-acetylglucosamine onto dolichol phosphate. Evidence Is presented that N-acetylglucosamine bound to dolichol phosphate can be transferred to the nascent peptide synthesized on the ribosomc.
2

Studies on oligosaccharyl transferase in yeast

75%
Lennarz W. J.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 4
673-677
 In yeast, OT consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. All yeast OT subunits have been cloned and sequenced (Kelleher et al., 1992; 2003; Kelleher & Gilmore, 1997; Kumar et al., 1994; 1995; Breuer & Bause, 1995) and the structure of one of them, Ost4p, has been solved by NMR (Zubkov et al., 2004). Very recently, the preliminary crystal structure of the lumenal domain of an archaeal Stt3p homolog has been reported (Mayumi et al., 2007). Homologs of all OT subunits have been identified in higher eukaryotic organisms (Kelleher et al., 1992; 2003; Kumar et al., 1994; Kelleher & Gilmore, 1997).
3

Carbohydrate moiety of immunoglobulins in health and pathology

75%
Krotkiewski H.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 2
Most of glycoproteins described so far, including immunoglobulins, are glycosylated during post-translational modifications of protein molecules. Current knowledge of the structure of sugar chains in immunoglobulin molecules and their biological role in health and pathology is reviewed.
4

Glycosylation of proteins in healthy and pathological human renal tissues

63%
Borzym-Kluczyk M., Radziejewska I., Darewicz B.
Folia Histochemica et Cytobiologica
|
2012
|
tom 50
|
nr 4
5

Glycosylation defects corrected by the changes in GDPmannose level

63%
Kruszewska J., Janik A., Lenart U., Palamarczyk G.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 2
GDPMan is a key substrate in glycoprotein formation. This is especially true for lower eukaryotes where, in addition to the involvement in N-glycan biosynthesis and GPI-anchor formation, GDPMan takes part in the process which is unique for yeast and fungi i.e. O-mannosylation. Several lines of evidence have been presented that the level of GDPMan affects the process occurring in the Golgi compartment i.e. the elongation of outer mannose chain of glycoproteins in Saccharomyces cerevisiae. Results from our laboratory indicate that the availability of GDPMan affects also the early steps of glycoprotein formation ascribed to the endoplasmic reticulum, i.e. assembly of the dolichol-linked oligosaccharide as well as mannosyl-phosphodolichol (MPD) formation. The biochemical basis of carbohydrate deficient glycoprotein syndrome, a severe neurological disorder related to the GDPMan deficiency, is also discussed.
6

Disruption of Trichoderma reesei gene encoding protein O-mannosyl-transferase I results in a decrease of the enzyme activity and alteration of cell wall composition

51%
Gorka-Niec W., Pniewski M., Kania A., Perlinska-Lenart U., Palamarczyk G., Kruszewska J. S.
Acta Biochimica Polonica
|
2008
|
tom 55
|
nr 2
251-259
In fungi transfer of the first mannosyl residue to proteins during their O-glycosylation is catalyzed by protein O-mannosyltransferases encoded by pmt genes. Disruption of the pmt1gene in Trichodermacaused a significant decrease in the total activity of protein O-mannosyltransferases. Moreover, disruption of the pmt1gene also led to osmotic sensitivity of the strain, indicating an essential role of the PMTI protein activity for cell wall synthesis. At the same time, the strain was defective in septa formation, producing only half the number of septa per unit length of hypha compared with the wild type. Disruption of the pmt1gene decreased protein secretion but had no effect on glycosylation of secreted proteins, which suggests that PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins.
7

Modulators of protein glycosylation and secretion change the pattern of wall [glyco]proteins and affect the functioning of plant cell walls

51%
Luczak M., Bugajewska A., Wojtaszek P.
Biological Letters
|
2005
|
tom 42
|
nr 2 Spec.Vol.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.