Distinguishing the specificities of closely related proteases. Role of P3 in substrate and inhibitor discrimination between tissue-type plasminogen activator and urokinase.

@article{Ke1997DistinguishingTS,
  title={Distinguishing the specificities of closely related proteases. Role of P3 in substrate and inhibitor discrimination between tissue-type plasminogen activator and urokinase.},
  author={S H Ke and Gary S Coombs and K Tachias and Marc Navre and David R. Corey and Edwin L. Madison},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 26},
  pages={16603-9}
}
Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design. We have addressed this issue for two intimately related serine proteases, tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA), by modifying the technique of substrate phage display to create substrate subtraction libraries. Characterization of individual members of the substrate subtraction library accomplished the rapid… CONTINUE READING

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We have addressed this issue for two intimately related serine proteases , tissue - type plasminogen activator ( t - PA ) and urokinase - type plasminogen activator ( u - PA ) , by modifying the technique of substrate phage display to create substrate subtraction libraries .
Role of P3 in substrate and inhibitor discrimination between tissue - type plasminogen activator and urokinase . Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design .
We have addressed this issue for two intimately related serine proteases , tissue - type plasminogen activator ( t - PA ) and urokinase - type plasminogen activator ( u - PA ) , by modifying the technique of substrate phage display to create substrate subtraction libraries .
Role of P3 in substrate and inhibitor discrimination between tissue - type plasminogen activator and urokinase . Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design .
We have addressed this issue for two intimately related serine proteases , tissue - type plasminogen activator ( t - PA ) and urokinase - type plasminogen activator ( u - PA ) , by modifying the technique of substrate phage display to create substrate subtraction libraries .
Role of P3 in substrate and inhibitor discrimination between tissue - type plasminogen activator and urokinase . Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design .
We have addressed this issue for two intimately related serine proteases , tissue - type plasminogen activator ( t - PA ) and urokinase - type plasminogen activator ( u - PA ) , by modifying the technique of substrate phage display to create substrate subtraction libraries .
Role of P3 in substrate and inhibitor discrimination between tissue - type plasminogen activator and urokinase . Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design .
We have addressed this issue for two intimately related serine proteases , tissue - type plasminogen activator ( t - PA ) and urokinase - type plasminogen activator ( u - PA ) , by modifying the technique of substrate phage display to create substrate subtraction libraries .
Role of P3 in substrate and inhibitor discrimination between tissue - type plasminogen activator and urokinase . Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design .
We have addressed this issue for two intimately related serine proteases , tissue - type plasminogen activator ( t - PA ) and urokinase - type plasminogen activator ( u - PA ) , by modifying the technique of substrate phage display to create substrate subtraction libraries .
Role of P3 in substrate and inhibitor discrimination between tissue - type plasminogen activator and urokinase . Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design .
We have addressed this issue for two intimately related serine proteases , tissue - type plasminogen activator ( t - PA ) and urokinase - type plasminogen activator ( u - PA ) , by modifying the technique of substrate phage display to create substrate subtraction libraries .
Role of P3 in substrate and inhibitor discrimination between tissue - type plasminogen activator and urokinase . Elucidating subtle specificity differences between closely related enzymes is a fundamental challenge for both enzymology and drug design .
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