C1 Inhibitor Serpin Domain Structure Reveals the Likely Mechanism of Heparin Potentiation and Conformational Disease
Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use
A Glycosyltransferase Inhibitor from a Molecular Fragment Library Simultaneously Interferes with Metal Ion and Substrate Binding
C1 Inhibitor Serpin Domain Structure Reveals the Likely Mechanism of Heparin Potentiation and Conformational Disease
Calgary Herald from Calgary, Alberta, Canada on February 22, 1918 · 2
TheFabs
A Glycosyltransferase Inhibitor from a Molecular Fragment Library Simultaneously Interferes with Metal Ion and Substrate Binding
Characterization of the DNA Binding Domain of StbA, A Key Protein of A New Type of DNA Segregation System
Structure of a Therapeutic Full
A Glycosyltransferase Inhibitor from a Molecular Fragment Library Simultaneously Interferes with Metal Ion and Substrate Binding
Characterization of the DNA Binding Domain of StbA, A Key Protein of A New Type of DNA Segregation System
Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use
C1 Inhibitor Serpin Domain Structure Reveals the Likely Mechanism of Heparin Potentiation and Conformational Disease
Structural and biological insights into Klebsiella pneumoniae surface polysaccharide degradation by a bacteriophage K1 lyase: implications for clinical use
