Introduction of α-hydroxymethyamino acid residues in substrate specificity P1 position of trypsin inhibitor SFTI-1 from sunflower seeds retains its activity-Reference-Cited by-同舟云学术

Introduction of α-hydroxymethyamino acid residues in substrate specificity P1 position of trypsin inhibitor SFTI-1 from sunflower seeds retains its activity

Published:2006-02 Issue:3 Volume:340 Page:823-828
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Zabłotna Ewa,Kret Agnieszka,Jaśkiewicz Anna,Olma Aleksandra,Leplawy Mirosław T.,Rolka Krzysztof

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference25 articles.

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2. A new family of beta-hairpin mimetics based on a trypsin inhibitor from sunflower seeds;Descours;Chem. BioChem.,2002

3. Design, synthesis and analysis of novel bicyclic and bifunctional protease inhibitors;Jaulent;Protein Eng.,2004

4. Chemical synthesis and kinetic study of the smallest naturally occurring trypsin inhibitor SFTI-1 isolated from sunflower seeds and its analogues;Zabłotna;Biochem. Biophys. Res. Commun.,2002

5. Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1;Korsinczky;Biochemistry,2005

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