Anna Taylor
Postdoctoral Fellow
I received my PhD from the University of Texas Southwestern Medical Center in Dallas, TX. My dissertation work focused on uncovering the mechanisms of potential therapies for Niemann Pick Type C Disease, a rare neurodegenerative disease which mainly affects children. While studying Niemann Pick disease, it became apparent to me that the processes for demyelination and ultimately neuronal degeneration have not been fully ascertained.  Therefore for my postdoctoral studies in the Bhat Lab, I will be taking advantage of spatio-temporally controlled knock out mouse models to determine when the loss of proteins critical to the organization of nodal and paranodal domains in myelinated axons leads to neurodegeneration. In addition, I will be developing Tet-on mice to ask if axonal domain organization can be rescued by reestablishing axo-glial junctional complexes. These studies could potentially lead to novel therapies to restore nerve conduction and neuronal function, which would be also applicable to many neurodegenerative diseases.


Taylor AM, Shi Q, Bhat MA (2018) Simultaneous Ablation of Neuronal Neurofascin and Ankyrin G in Young and Adult Mice Reveals Age-Dependent Increase in Nodal Stability in Myelinated Axons and Differential Effects on the Lifespan. eNeuro DOI:

Shi Q, Saifetiarova J, Taylor AM, Bhat MA (2018) mTORC1 Activation by Loss of Tsc1 in Myelinating Glia Causes Downregulation of Quaking and Neurofascin 155 Leading to Paranodal Domain Disorganization. Front. Cell. Neurosci. doi: 10.3389/fncel.2018.00201

Saifetiarova, J., Liu, X., Taylor, A.M., Li, J. and Bhat, M.A. (2017). Axonal Domain Disorganization in Caspr1 and Caspr2 Mutant Myelinated Axons Affects Neuromuscular Junction Integrity Leading to Muscle Atrophy. J. Neurosci. Res. 95, 1373-1390.

Saifetiarova, J., Taylor, A.M., and Bhat, M.A. (2017) Early and Late Loss of the Cytoskeletal Scaffolding Protein, Ankyrin G Reveals its Role in Maturation and Maintenance of Nodes of Ranvier in Myelinated Axons. J Neurosci. 2661-16.2017 

Taylor, A.M., Saifetyarova, J., and Bhat, M.A. (2017) Postnatal Loss of Neuronal and Glial Neurofascins Differentially Affects Node of Ranvier Maintenance and Myelinated Axon Function.  Front. Cell. Neurosci. 11:11. doi: 10.3389/fncel.2017.00011 

Jones, R. D., A.M. Taylor, E. Tong, and J. J. Repa. 2013. Carboxylesterases are uniquely expressed among tissues and regulated by nuclear hormone receptors in the mouse. Drug Metab. Dispos. 41(1):40-9. PMID: 23011759

Taylor, A.M, B. Liu, Y. Mari, B. Liu, and J.J. Repa. 2012. Cyclodextrin mediates rapid changes in lipid balance in Npc1-/- mice without carrying cholesterol through the bloodstream. J. Lipid Res. 53(11):2331-42. PMID: 22892156

Ramirez, C.M., B. Liu, A. Aqul, A.M. Taylor, J. J. Repa, S. D. Turley and J. M. Dietschy. 2011. Quantitative role of LAL, NPC2, and NPC1 in lysosomal cholesterol processing defined by genetic and pharmacological manipulations. J. Lipid Res. 52(4):688-98. PMID: 21289032

Ramirez, C. M., B. Liu, A.M. Taylor, J. J. Repa, D. K. Burns, A. G. Weinberg, S. D. Turley and J. M. Dietschy. 2010. Weekly cyclodextrin administration normalizes cholesterol metabolism in nearly every organ of the Niemann-Pick Type C1 mouse and markedly prolongs life. Pediatr. Res. 68: 309-15. PMID: 20581737

Liu, B., C. M. Ramirez, A.M. Miller*, J. J. Repa, S. D. Turley and J. M. Dietschy. 2010. Cyclodextrin reverses the transport defect in the NPC1 mouse at any age and in nearly every organ leading to excretion of sequestered cholesterol as bile acid. J. Lipid Res. 51:933-944. PMID: 19965601

Liu, B., S. D. Turley, D. K. Burns, A.M. Miller*, J. J. Repa and J. M. Dietschy. 2009. Reversal of defective lysosomal transport in NPC disease ameliorates the liver dysfunction and neurodegeneration in npc1-/- mouse. Proc. Natl. Acad. Sci. USA 106: 2377-2382. PMID: 19171898

Miller, A.M.*, C. Crumbley, and K. Prüfer. 2009. N-terminal nuclear localization sequences of liver X receptors alpha and beta bind to importin alpha and are essential for both nuclear import and transactivating functions. Int. J. Biochem. Cell Biol. 41: 834-843. PMID: 18773967