P. Foran

发表

Botulinum A Like Type B and Tetanus Toxins Fulfils Criteria for Being a Zinc‐Dependent Protease

C. Montecucco, J. Dolly, A. Ashton, 1993, Journal of neurochemistry.

A single mutation in the recombinant light chain of tetanus toxin abolishes its proteolytic activity and removes the toxicity seen after reconstitution with native heavy chain.

N. Fairweather, G. Dougan, J. Dolly, 1994, Biochemistry.

Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments.

J. Dolly, C. Shone, P. Foran, 1994, Biochemistry.

Protein Kinase B Stimulates the Translocation of GLUT4 but Not GLUT1 or Transferrin Receptors in 3T3-L1 Adipocytes by a Pathway Involving SNAP-23, Synaptobrevin-2, and/or Cellubrevin*

J. Tavaré, L. Fletcher, J. Dolly, 1999, The Journal of Biological Chemistry.

Rescue of Exocytosis in Botulinum Toxin A-poisoned Chromaffin Cells by Expression of Cleavage-resistant SNAP-25

J. Dolly, G. Lawrence, P. Foran, 1999, The Journal of Biological Chemistry.

Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release.

J. Dolly, G. Lawrence, C. Shone, 1996, Biochemistry.

The janus faces of botulinum neurotoxin: Sensational medicine and deadly biological weapon

F. Meunier, S. Osborne, P. Wen, 2007, Journal of neuroscience research.

Getting muscles moving again after botulinum toxin: novel therapeutic challenges.

B. Davletov, F. Meunier, P. Foran, 2003, Trends in molecular medicine.

Tetanus toxin and botulinum toxins type A and B inhibit glutamate, gamma-aminobutyric acid, aspartate, and met-enkephalin release from synaptosomes. Clues to the locus of action.

M. Verhage, D. Nicholls, J. Dolly, 1992, The Journal of biological chemistry.

Probing the process of transmitter release with botulinum and tetanus neurotoxins

J. Dolly, G. Lawrence, A. Ashton, 1994 .

Botulinum neurotoxin B inhibits insulin-stimulated glucose uptake into 3T3-L1 adipocytes and cleaves cellubrevin unlike type A toxin which failed to proteolyze the SNAP-23 present.

J. Dolly, C. Shone, J. Melling, 1997, Biochemistry.

Importance of two adjacent C-terminal sequences of SNAP-25 in exocytosis from intact and permeabilized chromaffin cells revealed by inhibition with botulinum neurotoxins A and E.

J. Dolly, G. Lawrence, B. Dasgupta, 1997, Biochemistry.

Insights into a basis for incomplete inhibition by botulinum toxin A of Ca2+-evoked exocytosis from permeabilised chromaffin cells.

G. Lawrence, P. Foran, J. Oliver Dolly, 2002, Toxicology.

Evaluation of the Therapeutic Usefulness of Botulinum Neurotoxin B, C1, E, and F Compared with the Long Lasting Type A

Leonard A. Smith, J. Dolly, G. Lawrence, 2003, The Journal of Biological Chemistry.

Recombinant Forms of Tetanus Toxin Engineered for Examining and Exploiting Neuronal Trafficking Pathways*

P. Foran, N. Mohammed, Y. Li, 2001, The Journal of Biological Chemistry.

Distinct exocytotic responses of intact and permeabilised chromaffin cells after cleavage of the 25-kDa synaptosomal-associated protein (SNAP-25) or synaptobrevin by botulinum toxin A or B.

P Foran, J. Dolly, G. Lawrence, 1996, European journal of biochemistry.

Blockade by botulinum neurotoxin B of catecholamine release from adrenochromaffin cells correlates with its cleavage of synaptobrevin and a homologue present on the granules.

J. Dolly, G. Lawrence, P. Foran, 1995, Biochemistry.

Glial heterogeneity in expression of the inwardly rectifying K+ channel, Kir4.1, in adult rat CNS

S Poopalasundaram, O. Shamotienko, V. Gallo, 2000, Glia.

A novel polyclonal antibody specific for the Nav1.5 voltage-gated Na+ channel ‘neonatal’ splice form

G. Wilkin, M. Djamgoz, S. P. Fraser, 2005, Journal of Neuroscience Methods.

PROTEIN KINASE B STIMULATES TRANSLOCATION OF GLUT4 BUT NOT GLUT1 OR TRANSFERRIN RECEPTORS: THE INVOLVEMENT OF SNAP-23 AND CELLUBREVIN

J. Tavaré, J. Dolly, P. Oatey, 1999 .