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The surface-accessibility of wall-associated proteins, which serve as receptors for binding of plasminogen in C. neoformans, may change as cells age during culture, in vitro.
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Thus, in addition to a potential role as a contact site for plasminogen, the terminal lysine appears to exert a stabilizing function on the α-enolase structure that is important for binding of plasminogen via the IPM.
Thus, to examine a possible role for plasma membrane-associated proteins in the binding of plasminogen to C. neoformans, isolated cell wall fractions were further treated with 0.5% Triton-X-100, and the membrane pellets recovered from the detergent-soluble fractions tested for plasminogen labeling.
The experiments with S. oralis demonstrated that binding of plasminogen to the oral streptococci leads to its activation in a process that fully depends on plasminogen activators of the host, contrary to S. pyogenes and some of the Group C and G streptococcal species, which express their own bacterial plasminogen activator streptokinase [30], [31].
The specific binding of plasminogen, covalently bound to magnetic beads, to PrPSc aggregates in tissues from several species has been demonstrated [ 10, 12].
The lysine-dependent binding of plasminogen at 4°C to MDA-MB-231 cells was stable and resulted in an activation-susceptible conformation of plasminogen.
We report binding of plasminogen, tissue-type plasminogen activator (t-PA) and urinary-type plasminogen activator (u-PA) to intact SMCECM with concentrations of ligand yielding half-maximal binding (B50) of 34, 5 and 15 nM, respectively.
The binding of plasminogen to these receptors initiates inflammatory processes.
Mechanistically, fibrinolysis usually involves the binding of plasminogen to fibrin and conversion to plasmin (an active form of the plasminogen) by tissue-type plasminogen activator (tPA).
The apparently contradictory evidence might be explained by the different binding properties of plasminogen kringle domains to PrP in varying detergent conditions.
Both, chemical interactions, involved in the binding process of plasminogen to PrPSc, along with structural characteristics of the newly formed protein network, could have contributed to the positive velocity changes observed.
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