Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Nikola Kitic"'
Publikováno v:
Molecules, Vol 26, Iss 18, p 5512 (2021)
Glycosaminoglycans are a class of linear, highly negatively charged, O-linked polysaccharides that are involved in many (patho)physiological processes. In vitro experimental investigations of such processes typically involve porcine-derived heparan s
Externí odkaz:
https://doaj.org/article/809b0e8692c44d40bdff426d00ce1907
Publikováno v:
Seminars in Thrombosis and Hemostasis. 47:316-332
Heparan sulfate proteoglycans (HSPGs) occur in almost every tissue of the human body and consist of a protein core, with covalently attached glycosaminoglycan polysaccharide chains. These glycosaminoglycans are characterized by their polyanionic natu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ebd4afbe0b7c33647556ccd6e4360ba
https://doi.org/10.1055/s-0041-1725067
https://doi.org/10.1055/s-0041-1725067
Publikováno v:
Molecules
Volume 26
Issue 18
Molecules, Vol 26, Iss 5512, p 5512 (2021)
Volume 26
Issue 18
Molecules, Vol 26, Iss 5512, p 5512 (2021)
Glycosaminoglycans are a class of linear, highly negatively charged, O-linked polysaccharides that are involved in many (patho)physiological processes. In vitro experimental investigations of such processes typically involve porcine-derived heparan s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b0380da96b71a1317b6055ba11e1aa
http://europepmc.org/articles/PMC8469465
http://europepmc.org/articles/PMC8469465
Autor:
Nikola Kitic, Andreas J. Kungl, Christina Zankl, Sophie Winkler, Akos Heinemann, Roland Weis, Aid Atlic, Tiziana Adage, Elisabeth Strutzmann, Tanja Gerlza, Kerstin Knebl, Viktoria Konya
Publikováno v:
Protein Engineering Design and Selection. 28:231-240
Chemokines like CCL2 mediate leukocyte migration to inflammatory sites by binding to G-protein coupled receptors on the target cell as well as to glycosaminoglycans (GAGs) on the endothelium of the inflamed tissue. We have recently shown that the dom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7039f19662bca2490b30fc9b5940776f
https://doi.org/10.1093/protein/gzv025
https://doi.org/10.1093/protein/gzv025
Publikováno v:
Methods in enzymology. 570
Interactions between chemokines and glycosaminoglycans (GAGs) are crucial for the physiological and pathophysiological activities of chemokines. GAGs are therefore commonly designated as chemokine coreceptors which are deeply involved in the chemokin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::75c195a6d7312582fc3302f98c56f973
https://pubmed.ncbi.nlm.nih.gov/26921960
https://pubmed.ncbi.nlm.nih.gov/26921960
Interactions between chemokines and glycosaminoglycans (GAGs) are crucial for the physiological and pathophysiological activities of chemokines. GAGs are therefore commonly designated as chemokine coreceptors which are deeply involved in the chemokin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f8ce9431da09112f52664190ebce75f
https://doi.org/10.1016/bs.mie.2015.09.018
https://doi.org/10.1016/bs.mie.2015.09.018
Autor:
Nele Berghmans, Mauro M. Teixeira, Jo Van Damme, Rik Janssens, Paul Proost, Isabelle Ronsse, Daiane Boff, Andreas J. Kungl, Flávio A. Amaral, Anneleen Mortier, Vincent Vanheule, Nikola Kitic
The ELR(-)CXC chemokine CXCL9 is characterized by a long, highly positively charged COOH-terminal region, absent in most other chemokines. Several natural leukocyte- and fibroblast-derived COOH-terminally truncated CXCL9 forms missing up to 30 amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0568b015b729c5775941c15f02846344
https://biblio.vub.ac.be/vubir/the-positively-charged-coohterminal-glycosaminoglycanbinding-cxcl974103-peptide-inhibits-cxcl8induced-neutrophil-extravasation-and-monosodium-urate-crystalinduced-gout-in-mice(1429c173-3fcc-42c4-9300-e7644e9e5137).html
https://biblio.vub.ac.be/vubir/the-positively-charged-coohterminal-glycosaminoglycanbinding-cxcl974103-peptide-inhibits-cxcl8induced-neutrophil-extravasation-and-monosodium-urate-crystalinduced-gout-in-mice(1429c173-3fcc-42c4-9300-e7644e9e5137).html