characterization-glycoproteins-with-immunoglobulin-fold-x-ray

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Glycoproteins on the surface of cells play critical roles in cellular function, including signalling, adhesion and transport. On leukocytes, several of ...

The Hospital for Sick Children Research Institute

EspP (E. coli secreted serine protease, large plasmid encoded) is an extracellular serine protease produced by enterohemorrhagic E. coli (EHEC) O157:H7, a causative agent of diarrhea-associated Hemolytic Uremic Syndrome (D+HUS). The mechanism by which EHEC induces D+HUS has not been fully elucidated.

EspP, an Extracellular Serine Protease from Enterohemorrhagic E. coli, Reduces Coagulation Factor Activities, Reduces Clot Strength, and Promotes Clot Lysis.

Indira Akula

Program in Molecular Medicine

The Hospital for Sick Children Research Institute

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Indira Akula

.css-o250i3{font-size:18px;font-family:Open Sans,sans-serif;line-height:21.6px;}Program in Molecular Medicine

The Hospital for Sick Children Research Institute

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Program in Molecular Medicine