Jingjing Xu

This study investigates the magnetic properties of CRY4a in Japanese quail, showing similarities to robin CRY4a, suggesting quail as a potential model for studying magnetoreception in migratory birds.

The paper investigates whether ErCRY4a binds 8-HDF or MTHF and finds no evidence of binding, suggesting it may function with only FAD as a cofactor.

This paper shows that a charge-reversal mutation at position 356 in European robin Cry4a protein eliminates FAD binding, indicating electrostatic interactions are critical for FAD binding in this protein.

The paper investigates whether ErCry4b in European robins can function as a radical pair magnetic sensor, finding it lacks FAD binding and is not expressed at detectable levels.