T. Garver

The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation.

V. Bennett, S. Tuvia, T. Garver, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Reduction of calcineurin activity in brain by antisense oligonucleotides leads to persistent phosphorylation of tau protein at Thr181 and Thr231.

M. Billingsley, R. Kincaid, T. Garver, 1999, Molecular pharmacology.

Microtubule assembly competence analysis of freshly‐biopsied human tau, dephosphorylated tau, and Alzheimer tau

M. Billingsley, R. Lehman, T. Garver, 1996, Journal of neuroscience research.

τ Phosphorylation in Human, Primate, and Rat Brain: Evidence that a Pool of τ Is Highly Phosphorylated In Vivo and Is Rapidly Dephosphorylated In Vitro

J. Trojanowski, M. Billingsley, R. Lehman, 1994, Journal of neurochemistry.

Tyrosine Phosphorylation at a Site Highly Conserved in the L1 Family of Cell Adhesion Molecules Abolishes Ankyrin Binding and Increases Lateral Mobility of Neurofascin

V. Bennett, S. Tuvia, Q. Ren, 1997, The Journal of cell biology.

Tau phosphorylation in brain slices: pharmacological evidence for convergent effects of protein phosphatases on tau and mitogen-activated protein kinase.

M. Billingsley, G. Oyler, R. Lehman, 1995, Molecular pharmacology.