Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Roger K. Aoki"'
Autor:
Larry A. Wheeler, George Sachs, Elmira Tokhtaeva, Roger K. Aoki, Patton E. Garay, Ramilla Lewis, Puneet Souda, Ester Fernandez-Salas, Olga Vagin, Julian P. Whitelegge, Sara Bassilian
Publikováno v:
Journal of Cell Science.
Proteolytic cleavage of synaptosomal-associated protein 25 by the light chain of Botulinum neurotoxin type A (LCA), resulting in a blockade of neurotransmitter release, persists for several months in motor neurons. The L428A/L429A mutation in LCA is
Autor:
Yan Li, Godfrey Lisk, Patrick G. Foran, Oliver Dolly, Roger K. Aoki, Chan-Ka-Ning Chan-Kwo-Chion, Nadiem Mohammed, Gary W. Lawrence
Publikováno v:
Journal of Biological Chemistry. 276:31394-31401
Tetanus toxin is a fascinating, multifunctional protein that binds to peripheral neurons, undergoes retrograde transport and trans-synaptic transfer to central inhibitory neurons where it blocks transmitter release, thereby, causing spastic paralysis
Autor:
Martin K. Childers, Greg Petroski, Roger K. Aoki, Laura Otaviani, Daniel J. Bogan, Joe N. Kornegay
Publikováno v:
Muscle & Nerve. 21:653-655
Tarsal joint forces were measured in dogs over 70 days following botulinum toxin type A (BTX-A) injections. Three dogs were injected at motor end-plates located by electromyography (EMG), while 3 dogs were similarly injected, but without EMG guidance
Publikováno v:
Journal of biochemistry. 125(6)
Tetanus toxin, composed of a disulphide-linked heavy (HC) and light (LC) chain, preferentially blocks the release of inhibitory neurotransmitters in the spinal cord by Zn2+-dependent proteolytic cleavage of synaptobrevin. This intoxication involves b
Publikováno v:
Biochemistry. 34(46)
Botulinum neurotoxin type A (BoNT/A) selectively and irreversibly inhibits acetylcholine release from peripheral nerve endings. While the toxin's heavy (H) chain contributes to neuronal binding and internalization, its light (L) chain is a Zn(2+)-dep
Autor:
Roger K. Aoki, Dudley J. Williams, Nicholas G. James, Marcella A. Gilmore, Lance E. Steward, David M. Jameson, Justin A. Ross
Publikováno v:
Biophysical Journal. 98:584a
The assay is based on depolarization due to Forster Resonance Energy Transfer (FRET) between Blue Fluorescent Protein (BFP) and Green Fluorescent Protein (GFP) moieties linked by a peptide containing residues 134-206 of SNAP-25, the protein substrate