Report for Vaux DJ

General

Full name : Vaux David JT

First name : David JT

Mail : Lincoln College, Turl St., Oxford, OXI 3DR

Zip Code :

City :

Country : United Kingdom

Email : david.vaux@lincoln.oxford.ac.uk

Phone : 44-1-865-279842

Fax : 44-1-865-279802

Website :

Directory :

References (10)

Title : In vivo localization of human acetylcholinesterase-derived species in a beta-sheet conformation at the core of senile plaques in Alzheimer's disease - Jean_2019_J.Biol.Chem_294_6253
Author(s) : Jean L , Brimijoin S , Vaux DJ
Ref : Journal of Biological Chemistry , 294 :6253 , 2019
Abstract : Jean_2019_J.Biol.Chem_294_6253
ESTHER : Jean_2019_J.Biol.Chem_294_6253
PubMedSearch : Jean_2019_J.Biol.Chem_294_6253
PubMedID: 30787102

Title : Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells - Davies_2012_J.Lipid.Res_53_2690
Author(s) : Davies BS , Goulbourne CN , Barnes RH, 2nd , Turlo KA , Gin P , Vaughan S , Vaux DJ , Bensadoun A , Beigneux AP , Fong LG , Young SG
Ref : J Lipid Res , 53 :2690 , 2012
Abstract : Davies_2012_J.Lipid.Res_53_2690
ESTHER : Davies_2012_J.Lipid.Res_53_2690
PubMedSearch : Davies_2012_J.Lipid.Res_53_2690
PubMedID: 23008484
Gene_locus related to this paper: human-LPL

Title : Structural elements regulating amyloidogenesis: a cholinesterase model system - Jean_2008_PLoS.One_3_e1834
Author(s) : Jean L , Lee CF , Shaw M , Vaux DJ
Ref : PLoS ONE , 3 :e1834 , 2008
Abstract : Jean_2008_PLoS.One_3_e1834
ESTHER : Jean_2008_PLoS.One_3_e1834
PubMedSearch : Jean_2008_PLoS.One_3_e1834
PubMedID: 18350169

Title : Heterologous amyloid seeding: revisiting the role of acetylcholinesterase in Alzheimer's disease - Jean_2007_PLoS.One_2_e652
Author(s) : Jean L , Thomas B , Tahiri-Alaoui A , Shaw M , Vaux DJ
Ref : PLoS ONE , 2 :e652 , 2007
Abstract : Jean_2007_PLoS.One_2_e652
ESTHER : Jean_2007_PLoS.One_2_e652
PubMedSearch : Jean_2007_PLoS.One_2_e652
PubMedID: 17653279

Title : Poster (75) A fragment of the AChE t-peptide forms amyloid fibrils: antibodies raised against the fibrillogenic fragment and the full-length t-peptide -
Author(s) : Cottingham MG , Hollinshead MS , Voskuil JL , Vaux DJ
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :360 , 2004
PubMedID:

Title : A fragment of the AChE T-peptide forms amyloid fibrils: Antibodies raised against the fibrillogenic fragment and the full-length T -peptide -
Author(s) : Cottingham MG , Hollinshead MS , Kirby B , Voskuil JL , Vaux DJ
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :109 , 2004
PubMedID:

Title : A peptide from the C-terminal oligomerization domain of human synaptic (T-form) acetylcholinesterase forms classical amyloid fibrils. -
Author(s) : Cottingham MG , Hollinshead MS , Vaux DJ
Ref : Cholinergic Mechanisms, CRC Press :535 , 2004
PubMedID:

Title : The intact human acetylcholinesterase C-terminal oligomerization domain is alpha-helical in situ and in isolation, but a shorter fragment forms beta-sheet-rich amyloid fibrils and protofibrillar oligomers - Cottingham_2003_Biochemistry_42_10863
Author(s) : Cottingham MG , Voskuil JL , Vaux DJ
Ref : Biochemistry , 42 :10863 , 2003
Abstract : Cottingham_2003_Biochemistry_42_10863
ESTHER : Cottingham_2003_Biochemistry_42_10863
PubMedSearch : Cottingham_2003_Biochemistry_42_10863
PubMedID: 12962511

Title : Amyloid Fibril Formation by a Synthetic Peptide from a Region of Human Acetylcholinesterase that Is Homologous to the Alzheimer's Amyloid-beta Peptide - Cottingham_2002_Biochemistry_41_13539
Author(s) : Cottingham MG , Hollinshead MS , Vaux DJ
Ref : Biochemistry , 41 :13539 , 2002
Abstract : Cottingham_2002_Biochemistry_41_13539
ESTHER : Cottingham_2002_Biochemistry_41_13539
PubMedSearch : Cottingham_2002_Biochemistry_41_13539
PubMedID: 12427014

Title : Parkinson's disease, Alzheimer's disease and motor neurone disease: identifying a common mechanism - Greenfield_2002_Neurosci_113_485
Author(s) : Greenfield SA , Vaux DJ
Ref : Neuroscience , 113 :485 , 2002
Abstract : Greenfield_2002_Neurosci_113_485
ESTHER : Greenfield_2002_Neurosci_113_485
PubMedSearch : Greenfield_2002_Neurosci_113_485
PubMedID: 12150769