Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Klara J. Belzar"'
Autor:
Ian Keyzor, Simon Shohet, Jeff Castelli, Sheela Sitaraman, Biliana Veleva-Rotse, Jill M. Weimer, Brian Fox, Tobias Willer, Steve Tuske, Louise Crathorne, Klara J. Belzar
Publikováno v:
Biomolecules, Vol 13, Iss 8, p 1227 (2023)
The treatment landscape for lysosomal storage disorders (LSDs) is rapidly evolving. An increase in the number of preclinical and clinical studies in the last decade has demonstrated that pharmacological chaperones are a feasible alternative to enzyme
Externí odkaz:
https://doaj.org/article/77e7ce7c2b764f51880d261188c06a9c
Publikováno v:
Journal of Molecular Biology. 386:1278-1289
Summary Antithrombin (AT) is the most important inhibitor of coagulation proteases. Its activity is stimulated by glycosaminoglycans, such as heparin, through allosteric and template mechanisms. AT utilises an induced-fit mechanism to bind with high
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea0057ecea66c338d08d19eb6cdbfa50
https://doi.org/10.1016/j.jmb.2009.01.028
https://doi.org/10.1016/j.jmb.2009.01.028
Publikováno v:
Journal of Biological Chemistry. 277:8551-8558
Antithrombin requires allosteric activation by heparin for efficient inhibition of its target protease, factor Xa. A pentasaccharide sequence found in heparin activates antithrombin by inducing conformational changes that affect the reactive center o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6eda5725ed8741d5b21c7bd67af48f1a
https://doi.org/10.1074/jbc.m110807200
https://doi.org/10.1074/jbc.m110807200
Autor:
James A. Huntington, Peter G.W. Gettins, Klara J. Belzar, Airlie J. McCoy, Robin W. Carrell, Xue Y. Pei
Publikováno v:
Journal of Biological Chemistry. 275:15377-15383
Antithrombin is unique among the serpins in that it circulates in a native conformation that is kinetically inactive toward its target proteinase, factor Xa. Activation occurs upon binding of a specific pentasaccharide sequence found in heparin that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b337fef876e49950fc14cf1d81e6c500
https://doi.org/10.1074/jbc.275.20.15377
https://doi.org/10.1074/jbc.275.20.15377
Publikováno v:
Journal of Biological Chemistry. 275:8733-8741
Antithrombin requires heparin for efficient inhibition of the final two proteinases of the blood coagulation cascade, factor Xa and thrombin. Antithrombin binds heparin via a specific pentasaccharide domain in a two-step mechanism whereby initial wea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ef4391be3e469fe4ba059e1a39fab2c
https://doi.org/10.1074/jbc.275.12.8733
https://doi.org/10.1074/jbc.275.12.8733
Publikováno v:
Blood Coagulation & Fibrinolysis. 10:540
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40a3b0ca943fb6c29632d2c64daa3939
https://doi.org/10.1097/00001721-199912000-00034
https://doi.org/10.1097/00001721-199912000-00034