J. Fadeeva

发表

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

W. K. Cullen, R. Anwyl, M. Rowan, 2002, Nature.

gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins.

D. Selkoe, D. Walsh, J. Fadeeva, 2003, Biochemistry.

The role of cell-derived oligomers of Abeta in Alzheimer's disease and avenues for therapeutic intervention.

M. Rowan, D. Selkoe, K. Ashe, 2005, Biochemical Society transactions.

Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition.

M. Rowan, D. Selkoe, D. Walsh, 2002, Biochemical Society transactions.

Soluble Arctic amyloid β protein inhibits hippocampal long‐term potentiation in vivo

W. K. Cullen, R. Anwyl, M. Rowan, 2004, The European journal of neuroscience.

γ-secretase processing of APLP1 leads to the production of a p3-like peptide that does not aggregate and is not toxic to neurons

D. Selkoe, D. Walsh, J. Fadeeva, 2009, Brain Research.

Amyloid-β oligomers: their production, toxicity and therapeutic inhibition

Michael J. Rowan, Dominic M. Walsh, M. Rowan, 2001 .

Certain Inhibitors of Synthetic Amyloid β-Peptide (Aβ) Fibrillogenesis Block Oligomerization of Natural Aβ and Thereby Rescue Long-Term Potentiation

Dominic M. Walsh, D. Selkoe, D. Walsh, 2005, The Journal of Neuroscience.

Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation.

D. Selkoe, D. Walsh, J. Fadeeva, 2005, The Journal of neuroscience : the official journal of the Society for Neuroscience.

The APP family of proteins: similarities and differences.

D. Selkoe, D. Walsh, J. Fadeeva, 2007, Biochemical Society transactions.

β‐Secretase cleavage is not required for generation of the intracellular C‐terminal domain of the amyloid precursor family of proteins

D. Selkoe, D. Walsh, J. Fadeeva, 2010, The FEBS journal.