Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Rebecca S. Woodruff"'
Autor:
Mao-fu Sun, Ivan Ivanov, Rebecca S. Woodruff, David Gailani, Bruce A. Sullenger, Ingrid M. Verhamme
Publikováno v:
Thrombosis research. 156
Background The plasma protease factor XIa (FXIa) has become a target of interest for therapeutics designed to prevent or treat thrombotic disorders. Methods We used a solution-based, directed evolution approach called systematic evolution of ligands
Publikováno v:
Journal of Thrombosis and Thrombolysis. 32:9-20
Understanding inherent differences between thrombosis and hemostasis in the vascular system are critical to developing safe and effective anticoagulants. To this end, constituents of the contact activated and intrinsic pathway of coagulation appear t
As a novel class of therapeutics, aptamers, or nucleic acid ligands, have garnered clinical interest because of the ease of isolating a highly specific aptamer against a wide range of targets, their chemical flexibility and synthesis, and their inher
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78b0215173bebc5b3130a62269fac7de
https://europepmc.org/articles/PMC5304947/
https://europepmc.org/articles/PMC5304947/
Publikováno v:
Journal of thrombosis and haemostasis : JTH. 11(7)
Summary Background Exposure of the plasma protein factor XII (FXII) to an anionic surface generates activated FXII that not only triggers the intrinsic pathway of blood coagulation through the activation of FXI but also mediates various vascular resp
Publikováno v:
Archivum immunologiae et therapiae experimentalis. 61(4)
Aptamers are short, single-stranded oligonucleotides that are isolated through a process termed systematic evolution of ligands by exponential enrichment. With the advent of cell-based selection technology, aptamers can be selected to bind protein ta
Potent Anticoagulant Aptamer Directed against Factor IXa Blocks Macromolecular Substrate Interaction
An aptamer targeting factor IXa has been evaluated in animal models and several clinical studies as a potential antithombotic therapy. We elucidate the molecular mechanism by which this aptamer acts as an anticoagulant. The aptamer binds tightly to f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d2b2010b7b727ef2dd6467740f6dc78
Autor:
Bruce A. Sullenger, Shahid M Nimjee, Rebecca S. Woodruff, Kristin M. Bompiani, Richard C. Becker
Publikováno v:
Current pharmaceutical biotechnology. 13(10)
Aptamers, or nucleic acid ligands, have gained clinical interest over the past 20 years due to their unique characteristics, which are a combination of the best facets of small molecules and antibodies. The high binding affinity and specificity of ap