J. I. Baños-Sanz

Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with a singular inositide binding site for axial 2-OH recognition

Beatriz González, Maider Villate, C. Brearley, 2010, Proceedings of the National Academy of Sciences.

A new calmodulin-binding motif for inositol 1,4,5-trisphosphate 3-kinase regulation.

B. González, A. Round, B. Monterroso, 2014, The Biochemical journal.

Conformational Changes in Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase upon Substrate Binding

C. Brearley, B. González, J. Sanz-Aparicio, 2012, The Journal of Biological Chemistry.

Crystallization and preliminary X-ray diffraction analysis of inositol 1,3,4,5,6-pentakisphosphate kinase from Arabidopsis thaliana.

C. Brearley, B. González, J. Sanz-Aparicio, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystal structure and functional insights into uracil-DNA glycosylase inhibition by phage ϕ29 DNA mimic protein p56

B. González, G. Serrano-Heras, M. Salas, 2013, Nucleic acids research.

Expression, purification, crystallization and preliminary X-ray diffraction analysis of the apo form of InsP5 2-K from Arabidopsis thaliana.

C. Brearley, B. González, J. Sanz-Aparicio, 2012, Acta crystallographica. Section F, Structural biology and crystallization communications.

Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with a singular inositide binding site for axial 2-OH recognition

C. Brearley, B. González, J. Sanz-Aparicio, 2010, Proceedings of the National Academy of Sciences.