Zobrazeno 1 - 10
of 182
pro vyhledávání: '"Anthony P. Corfield"'
Autor:
Taewoo Chun, Jacob Pattem, Richard B. Gillis, Vlad T. Dinu, Gleb E. Yakubov, Anthony P. Corfield, Stephen E. Harding
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-9 (2023)
Abstract Glycopeptide antibiotics are regularly used in ophthalmology to treat infections of Gram-positive bacteria. Aggregative interactions of antibiotics with mucins however can lead to long exposure and increases the risk of resistant species. Th
Externí odkaz:
https://doaj.org/article/0f617717d6274b9ca9f42fc027375cfd
Autor:
Taewoo Chun, Jacob Pattem, Richard B. Gillis, Vlad T. Dinu, Gleb E. Yakubov, Anthony P. Corfield, Stephen E. Harding
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-11 (2023)
Abstract The natural glycopeptide antibiotic teicoplanin is used for the treatment of serious Gram-positive related bacterial infections and can be administered intravenously, intramuscularly, topically (ocular infections), or orally. It has also bee
Externí odkaz:
https://doaj.org/article/2a94ba0eb66d44028f5eed0cdaadcc3e
Autor:
Anthony P. Corfield
Publikováno v:
Microorganisms, Vol 6, Iss 3, p 78 (2018)
Glycoproteins are major players in the mucus protective barrier in the gastrointestinal and other mucosal surfaces. In particular the mucus glycoproteins, or mucins, are responsible for the protective gel barrier. They are characterized by their high
Externí odkaz:
https://doaj.org/article/6446d27cbdeb4fdc8efd57e5d5f2a0a9
Autor:
Jürgen Kopitz, Herbert Kaltner, Anthony P. Corfield, Hans-Joachim Gabius, José Abad-Rodríguez
Publikováno v:
Biochemical Journal. 476:2623-2655
Ubiquitous occurrence in Nature, abundant presence at strategically important places such as the cell surface and dynamic shifts in their profile by diverse molecular switches qualifies the glycans to serve as versatile biochemical signals. However,
Autor:
Anthony P. Corfield
Publikováno v:
Histochemistry and Cell Biology
Proteins undergo co- and posttranslational modifications, and their glycosylation is the most frequent and structurally variegated type. Histochemically, the detection of glycan presence has first been performed by stains. The availability of carbohy
Publikováno v:
Soft Matter. 9:1740-1743
In this highlight, we discuss the multifaceted biology of mucins, where molecular architecture meets function, and especially the collective properties of mucin networks and gels that select adherent bacteria and restrict penetration.
Autor:
Anthony P. Corfield, Barbara Mulloy
Publikováno v:
Biochemical Society Transactions. 38:1329-1332
The glycans (carbonhydrates) form a diverse group of biomolecules which play active parts in most physiological processes. The field of structural glycobiology concerns the structures of the glycans themselves, the proteins which interact with them a
Autor:
Anthony P. Corfield, Stefan Müller, Udo Roth, Katja Engelmann, Stephan Baldus, Tilo Schwientek, Julia Hommer, Franz-Georg Hanisch, Christos Paraskeva, Hanieh Razawi, Georgios Patsos
Publikováno v:
PROTEOMICS. 10:194-202
This is the first differential expression proteomics study on a human syngeneic cellular in vitro progression model of the colorectal adenoma-to-carcinoma sequence, the anchorage-dependent non-tumorigenic adenoma derived cell line AA/C1 and the deriv
Autor:
Georgios Patsos, Anthony P. Corfield
Publikováno v:
bchm. 390:581-590
The human gastrointestinal barrier comprises several layers which enable protection against the external environment. The mucosal epithelium, lamina propria, glycocalyx and secreted mucus each make a contribution to barrier protection. Glycocalyx and
Autor:
Catherine Robbe-Masselot, Andreas Klein, Christos Paraskeva, David Masselot, Rosemary Greenwood, M. Graessmann, Anthony P. Corfield, Jean Claude Michalski, Raul San Martin, Virginie Hebbe-Viton, Timothy Gallagher, Georgios Patsos
Publikováno v:
Glycobiology. 19:382-398
Our studies provide direct evidence that O-glycosylation pathways play a role in the regulation of cell growth through apoptosis and proliferation pathways. A series of small molecular weight analogs of the GalNAc-alpha-1-O-serine/threonine structure