1998
DOI: 10.1016/s0142-9612(98)00086-6
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Selective plasminogen binding: Cysteinyl–lysine–dextran protein interactions

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Cited by 7 publications
(2 citation statements)
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“…As indicated above, it is known that plasminogen and t-PA bind specically to the surface of brin via carboxy-terminal lysine residues in which the carboxyl and 3-amino groups are free (referred to as "3-lysines"). 125,[207][208][209] Therefore, it is expected that an 3-lysine-enriched surface could provide a substrate for the capture of plasminogen and t-PA from blood; the interaction of these two molecules should then lead to plasmin formation and thus to brinolysis. 44,210 This concept was rst introduced by Brash and coworkers.…”
Section: Thrombomodulin-protein Cmentioning
confidence: 99%
“…As indicated above, it is known that plasminogen and t-PA bind specically to the surface of brin via carboxy-terminal lysine residues in which the carboxyl and 3-amino groups are free (referred to as "3-lysines"). 125,[207][208][209] Therefore, it is expected that an 3-lysine-enriched surface could provide a substrate for the capture of plasminogen and t-PA from blood; the interaction of these two molecules should then lead to plasmin formation and thus to brinolysis. 44,210 This concept was rst introduced by Brash and coworkers.…”
Section: Thrombomodulin-protein Cmentioning
confidence: 99%
“…Recently,4, 5 a thromboresistant material obtained by photochemical attachment polyacrylamide bearing α‐aminocoupled lysine to polyurethane has been reported. A material based on dextran with covalently attached dipeptide l ‐cysteinyl‐ l ‐lysine was also prepared 6…”
Section: Introductionmentioning
confidence: 99%