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BMC Neuroscience|April 30, 2011
Regional and developmental brain expression patterns of SNAP25 splice variantsGerald R Prescott, Luke H Chamberlain
Journal of Neurochemistry|June 11, 2009
Palmitoylation of the synaptic vesicle fusion machineryGerald R Prescott, Oforiwa A Gorleku, Jennifer Greaves, et al.
Molecular Membrane Biology|December 31, 2008
The fat controller: roles of palmitoylation in intracellular protein trafficking and targeting to membrane microdomains (Review)Jennifer Greaves, Gerald R Prescott, Oforiwa A Gorleku, et al.
Biochemical Society Transactions|January 16, 2010
Regulation of SNAP-25 trafficking and function by palmitoylationJennifer Greaves, Gerald R Prescott, Oforiwa A Gorleku, et al.
Biochemical and Biophysical Research Communications|October 28, 2008
Phosphorylation of cysteine string protein on Serine 10 triggers 14-3-3 protein bindingGerald R Prescott, Rosalind E Jenkins, Ciara M Walsh, et al.
Structure (London, England : 1993)|July 26, 2016
Phosphorylation of Cysteine String Protein Triggers a Major Conformational SwitchPryank Patel, Gerald R Prescott, Robert D Burgoyne, et al.
The Journal of Biological Chemistry|September 20, 2011
Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signalsOforiwa A Gorleku, Anna-Marie Barns, Gerald R Prescott, et al.
Molecular Biology of the Cell|January 23, 2009
The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferasesJennifer Greaves, Gerald R Prescott, Yuko Fukata, et al.
The Journal of Biological Chemistry|October 26, 2005
Protein kinase B/Akt is a novel cysteine string protein kinase that regulates exocytosis release kinetics and quantal sizeGareth J O Evans, Jeff W Barclay, Gerald R Prescott, et al.
Plos One|March 30, 2011
Structure-function study of mammalian Munc18-1 and C. elegans UNC-18 implicates domain 3b in the regulation of exocytosisMargaret E Graham, Gerald R Prescott, James R Johnson, et al.
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