A. Powe

发表

Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease.

Gregory A Petsko, Dagmar Ringe, R. L. Lieberman, 2006, Nature chemical biology.

Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders.

J. Flanagan, Gary Lee, A. Powe, 2011, Assay and drug development technologies.

The iminosugar isofagomine increases the activity of N370S mutant acid β-glucosidase in Gaucher fibroblasts by several mechanisms

S. Chung, S. Kornfeld, B. Wustman, 2006, Proceedings of the National Academy of Sciences.

CFTR misfolds during native-centric simulations due to entropic penalties of native state formation

V. Pande, G. McGaughey, A. Powe, 2018, bioRxiv.

The pharmacological chaperone isofagomine increases the activity of the Gaucher disease L444P mutant form of β‐glucosidase

D. Lockhart, R. Schiffmann, Y. Lun, 2010, The FEBS journal.

The Pharmacological Chaperone AT2220 Increases the Specific Activity and Lysosomal Delivery of Mutant Acid Alpha-Glucosidase, and Promotes Glycogen Reduction in a Transgenic Mouse Model of Pompe Disease

D. Lockhart, Y. Lun, B. Wustman, 2014, PloS one.

In vivo functional analysis of Drosophila Gap1: involvement of Ca2+ and IP4 regulation

U. Gaul, J. Carlson, T. Cutforth, 1999, Mechanisms of Development.

Quantitative analysis of ATP-dependent gating of CFTR.

G. Nagel, A. Powe, T. Hwang, 2002, Methods in molecular medicine.

Mutation of Walker‐A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide‐binding domains

A. Powe, T. Hwang, L. Al-Nakkash, 2002, The Journal of physiology.