Zobrazeno 1 - 10
of 10
pro vyhledávání: '"David Stenitzer"'
Publikováno v:
Biomolecules, Vol 12, Iss 11, p 1578 (2022)
β-Galactosidases (β-Gal, EC 3.2.1.23) catalyze the cleavage of terminal non-reducing β-D-galactose residues or transglycosylation reactions yielding galacto-oligosaccharides. In this study, we present the isolation and characterization of a β-gal
Externí odkaz:
https://doaj.org/article/3dc8ff07f7544fe8a46ba17ca87d8294
Autor:
Réka Mócsai, Kathrin Göritzer, David Stenitzer, Daniel Maresch, Richard Strasser, Friedrich Altmann
Publikováno v:
Frontiers in Plant Science, Vol 12 (2021)
Plant glycoproteins display a characteristic type of O-glycosylation where short arabinans or larger arabinogalactans are linked to hydroxyproline. The conversion of proline to 4-hydroxyproline is accomplished by prolyl-hydroxylases (P4Hs). Eleven pu
Externí odkaz:
https://doaj.org/article/0031287fcb2e4bda88a116b6d98c57f0
Autor:
David Stenitzer, Réka Mócsai, Harald Zechmeister, Ralf Reski, Eva L. Decker, Friedrich Altmann
Publikováno v:
Biomolecules, Vol 12, Iss 1, p 136 (2022)
In the animal kingdom, a stunning variety of N-glycan structures have emerged with phylogenetic specificities of various kinds. In the plant kingdom, however, N-glycosylation appears to be strictly conservative and uniform. From mosses to all kinds o
Externí odkaz:
https://doaj.org/article/5f881efe07da4b7486afe29cb4c060ca
Autor:
David Stenitzer, Friedrich Altmann
Publikováno v:
Bryophytes-The State of Knowledge in a Changing World
Bryophytes-The State of Knowledge in a Changing World ISBN: 9781803569383
Bryophytes-The State of Knowledge in a Changing World ISBN: 9781803569383
Glycosylation substantially contributes to the physicochemical properties of proteins, and hence also cell walls. Moreover, they are key factors for the recognition of free or cell-bound glycoproteins by internal and external interaction partners. Gr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2eb811c20067ec0d73a69122b198fbb7
https://mts.intechopen.com/articles/show/title/protein-glycosylation-in-bryophytes-differs-subtly-from-that-in-vascular-plants
https://mts.intechopen.com/articles/show/title/protein-glycosylation-in-bryophytes-differs-subtly-from-that-in-vascular-plants
Autor:
Clemens Grünwald-Gruber, Martin Pabst, Johannes Helm, Johannes Führer, Jonathan Urteil, Daniel Maresch, David Stenitzer, Friedrich Altmann, Andreas Thader, Laura Neumann
Publikováno v:
Analytical Chemistry. 93:15175-15182
The importance of protein glycosylation in the biomedical field requires methods that not only quantitate structures by their monosaccharide composition, but also resolve and identify the many isomers expressed by mammalian cells. The art of unambigu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87123374a7ee1250b73a37d1ef449f54
https://doi.org/10.1021/acs.analchem.1c03793
https://doi.org/10.1021/acs.analchem.1c03793
Publikováno v:
Biomolecules; Volume 12; Issue 11; Pages: 1578
β-Galactosidases (β-Gal, EC 3.2.1.23) catalyze the cleavage of terminal non-reducing β-D-galactose residues or transglycosylation reactions yielding galacto-oligosaccharides. In this study, we present the isolation and characterization of a β-gal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b7119a0f3009d1f92749038df7b5b3d
https://pubmed.ncbi.nlm.nih.gov/36358928
https://pubmed.ncbi.nlm.nih.gov/36358928
Autor:
Eva Decker, Harald Zechmeister, David Stenitzer, Friedrich Altmann, Ralf Reski, Réka Tünde Mócsai
Publikováno v:
Biomolecules
Biomolecules; Volume 12; Issue 1; Pages: 136
Biomolecules, Vol 12, Iss 136, p 136 (2022)
Biomolecules; Volume 12; Issue 1; Pages: 136
Biomolecules, Vol 12, Iss 136, p 136 (2022)
In the animal kingdom, a stunning variety of N-glycan structures has emerged with phylogenetic specificities of various kinds. In the plant kingdom, however, N-glycosylation appears as strictly conservative and uniform. From mosses to all kinds of gy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de3c5c3c48b832deb20a4c7beabd64a1
http://europepmc.org/articles/PMC8773788
http://europepmc.org/articles/PMC8773788
Autor:
Johannes, Helm, Clemens, Grünwald-Gruber, Andreas, Thader, Jonathan, Urteil, Johannes, Führer, David, Stenitzer, Daniel, Maresch, Laura, Neumann, Martin, Pabst, Friedrich, Altmann
Publikováno v:
Analytical Chemistry
The importance of protein glycosylation in the biomedical field requires methods that not only quantitate structures by their monosaccharide composition, but also resolve and identify the many isomers expressed by mammalian cells. The art of unambigu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::30bc1b40f5c4d22d8c5b14cb9de8910e
https://pubmed.ncbi.nlm.nih.gov/34723506
https://pubmed.ncbi.nlm.nih.gov/34723506
Time grid-based isomer specific N-glycan analysis and detection of bi-secting Lewis X in human brain
Autor:
Laura Neumann, Friedrich Altmann, Clemens Gruber, Daniel Maresch, Johannes Helm, Andreas Thader, Jonathan Urteil, Martin Pabst, Johannes Führer, David Stenitzer
The importance of protein glycosylation in the biomedical field demands for methods capable of resolving and identifying isomeric structures of N-glycans. However, the unambiguous identification of isomeric structures from complex mixtures is current
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7aded263b3cce682740860d76238e188
https://doi.org/10.1101/2021.04.14.439640
https://doi.org/10.1101/2021.04.14.439640
Autor:
Réka, Mócsai, Kathrin, Göritzer, David, Stenitzer, Daniel, Maresch, Richard, Strasser, Friedrich, Altmann
Publikováno v:
Frontiers in Plant Science
Plant glycoproteins display a characteristic type of O-glycosylation where short arabinans or larger arabinogalactans are linked to hydroxyproline. The conversion of proline to 4-hydroxyproline is accomplished by prolyl-hydroxylases (P4Hs). Eleven pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::10e8fbcdac070c1fb79894e69ada3bc1
https://pubmed.ncbi.nlm.nih.gov/33737944
https://pubmed.ncbi.nlm.nih.gov/33737944