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145 related items for PubMed ID: 9603949
1. Coagulation factor XIIIa undergoes a conformational change evoked by glutamine substrate. Studies on kinetics of inhibition and binding of XIIIA by a cross-reacting antifibrinogen antibody. Mitkevich OV, Shainoff JR, DiBello PM, Yee VC, Teller DC, Smejkal GB, Bishop PD, Kolotushkina IS, Fickenscher K, Samokhin GP. J Biol Chem; 1998 Jun 05; 273(23):14387-91. PubMed ID: 9603949 [Abstract] [Full Text] [Related]
2. Contact with the N termini in the central E domain enhances the reactivities of the distal D domains of fibrin to factor XIIIa. Samokhin GP, Lorand L. J Biol Chem; 1995 Sep 15; 270(37):21827-32. PubMed ID: 7665605 [Abstract] [Full Text] [Related]
3. Gly-Pro-Arg-Pro modifies the glutamine residues in the alpha- and gamma-chains of fibrinogen: inhibition of transglutaminase cross-linking. Achyuthan KE, Dobson JV, Greenberg CS. Biochim Biophys Acta; 1986 Aug 15; 872(3):261-8. PubMed ID: 2873839 [Abstract] [Full Text] [Related]