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Characterization of interaction between blood coagulation factor VIII and LRP1 suggests dynamic binding by alternating complex contacts.
Chun H, Kurasawa JH, Olivares P, Marakasova ES, Shestopal SA, Hassink GU, Karnaukhova E, Migliorini M, Obi JO, Smith AK, Wintrode PL, Durai P, Park K, Deredge D, Strickland DK, Sarafanov AG. Chun H, et al. Among authors: sarafanov ag. J Thromb Haemost. 2022 Oct;20(10):2255-2269. doi: 10.1111/jth.15817. Epub 2022 Aug 4. J Thromb Haemost. 2022. PMID: 35810466 Free PMC article.
Interaction of coagulation factor VIII with members of the low-density lipoprotein receptor family follows common mechanism and involves consensus residues within the A2 binding site 484-509.
Ananyeva NM, Makogonenko YM, Sarafanov AG, Pechik IV, Gorlatova N, Radtke KP, Shima M, Saenko EL. Ananyeva NM, et al. Among authors: sarafanov ag. Blood Coagul Fibrinolysis. 2008 Sep;19(6):543-55. doi: 10.1097/MBC.0b013e3283068859. Blood Coagul Fibrinolysis. 2008. PMID: 18685438
Hysteresis-like binding of coagulation factors X/Xa to procoagulant activated platelets and phospholipids results from multistep association and membrane-dependent multimerization.
Podoplelova NA, Sveshnikova AN, Kurasawa JH, Sarafanov AG, Chambost H, Vasil'ev SA, Demina IA, Ataullakhanov FI, Alessi MC, Panteleev MA. Podoplelova NA, et al. Among authors: sarafanov ag. Biochim Biophys Acta. 2016 Jun;1858(6):1216-27. doi: 10.1016/j.bbamem.2016.02.008. Epub 2016 Feb 10. Biochim Biophys Acta. 2016. PMID: 26874201 Free article. Review.
36 results