Patton E. Garay
Allergan
24 Papers
271 Citations
Patton E. Garay is an academic researcher from Allergan. The author has contributed to research in topics: Cancer & Blood vessel. The author has an hindex of 11, co-authored 24 publications.
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Papers
Plasma membrane localization signals in the light chain of botulinum neurotoxin.
Ester Fernandez-Salas,Lance E. Steward,Helen Ho,Patton E. Garay,Sarah W. Sun,Marcella A. Gilmore,Joseph V. Ordas,Joanne Wang,Joseph Francis,K. Roger Aoki +9 more
TL;DR: Using confocal microscopy and site-specific mutagenesis, this paper determined that the protease domain of BoNT/A light chain localizes in a punctate manner to the plasma membrane, colocalizing with the cleaved product, SNAP25197.
148
Identification of Fibroblast Growth Factor Receptor 3 (FGFR3) as a Protein Receptor for Botulinum Neurotoxin Serotype A (BoNT/A)
Birgitte P.S. Jacky,Patton E. Garay,Jérôme Dupuy,Jeremy B. Nelson,Brian B. Cai,Yanira Molina,Joanne Wang,Lance E. Steward,Ron S. Broide,Joseph Francis,K. Roger Aoki,Raymond C. Stevens,Ester Fernandez-Salas +12 more
TL;DR: Findings show that FGFR3 plays a pivotal role in the specific uptake of BoNT/A across the cell membrane being part of a larger receptor complex involving ganglioside- and protein-protein interactions.
Patent
Immuno-Based Botulinum Toxin Serotype A Activity Assays
Ester Fernandez-Salas,Joanne Wang,Patton E. Garay,Lina S. Wong,D. Dianne Hodges,Kei Roger Aoki +5 more
- 13 Mar 2009
TL;DR: In this paper, a method of detecting anti-BoNT/A neutralizing antibodies was proposed, which was directed to a method to detect anti-rabidus neutralization.
62
Is the light chain subcellular localization an important factor in botulinum toxin duration of action
TL;DR: Data from animal and cell culture models suggests that the long‐lasting duration of inhibition of neurotransmitter release induced by BoNT/A maybe due to the persistence of the endopeptidase activity of the light chain (LC/A) in cells, interactions of the cleaved substrates, and the response of the nerve to the temporary disruption of communication with its target tissue.
54
Recruitment of septin cytoskeletal proteins by botulinum toxin A protease determines its remarkable stability.
Olga Vagin,Elmira Tokhtaeva,Patton E. Garay,Puneet Souda,Sara Bassilian,Julian P. Whitelegge,Ramilla Lewis,George Sachs,Larry A. Wheeler,Roger K. Aoki,Ester Fernandez-Salas +10 more
TL;DR: The dileucine-mediated LCA–septin co-clustering is crucial for the long-lasting stabilization of LCA-related proteolytic and presumably neuroparalytic activity.