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pro vyhledávání: '"Stephen, Verespy"'
Autor:
Rami A. Al-Horani, Rio S. Boothello, Stephen Verespy, Rajesh Karuturi, Umesh R. Desai, Daniel K. Afosah
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 28:1101-1105
Despite the development of promising direct oral anticoagulants, which are all orthosteric inhibitors, a sizable number of patients suffer from bleeding complications. We have hypothesized that allosterism based on the heparin-binding exosites presen
Publikováno v:
Faraday Discuss
Faraday discussions, vol 219, iss 0
Faraday discussions, vol 219, iss 0
In the mucosal epithelium, the cellular glycocalyx can project tens to hundreds of nanometers into the extracellular space, erecting a physical barrier that provides protective functions, mediates the exchange of nutrients and regulates cellular inte
Publikováno v:
Bioconjugate chemistry, vol 30, iss 3
Heparan sulfate glycosaminoglycans (HS GAGs) attached to proteoglycans harbor high affinity binding sites for various growth factors (GFs) and direct their organization and activity across the cell-matrix interface. Here, we describe a mild and effic
Publikováno v:
Current protocols in chemical biology. 10(2)
This article describes a protocol for remodeling cells with synthetic glycoprotein and glycolipid mimetics that are functionalized with lipid anchors, allowing for cell surface display of specific glycan structures in predefined nanoscale arrangement
Publikováno v:
ChemInform. 47
In nearly all cases of biological activity of sulfated GAGs, the sulfate group(s) are critical for interacting with target proteins. A growing paradigm is that appropriate small, sulfated, nonsaccharide GAG mimetics can be designed to either mimic or
Publikováno v:
Scientific Reports
Allosteric partial inhibition of soluble, monomeric proteases can offer major regulatory advantages, but remains a concept on paper to date; although it has been routinely documented for receptors and oligomeric proteins. Thrombin, a key protease of
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1229
In nearly all cases of biological activity of sulfated GAGs, the sulfate group(s) are critical for interacting with target proteins. A growing paradigm is that appropriate small, sulfated, nonsaccharide GAG mimetics can be designed to either mimic or
Publikováno v:
Methods in Molecular Biology ISBN: 9781493917136
In nearly all cases of biological activity of sulfated GAGs, the sulfate group(s) are critical for interacting with target proteins. A growing paradigm is that appropriate small, sulfated, nonsaccharide GAG mimetics can be designed to either mimic or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90d64fa0f6bb45fe8d1818af329abe01
https://doi.org/10.1007/978-1-4939-1714-3_7
https://doi.org/10.1007/978-1-4939-1714-3_7