M. Citron

发表

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

G. Schellenberg, J. Hardy, M. Viitanen, 1996, Nature Medicine.

The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway

D. Selkoe, L. Lannfelt, C. Lemere, 1995, Nature Medicine.

Excessive production of amyloid beta-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation.

B. Winblad, D. Selkoe, D. Teplow, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production.

D. Selkoe, C. Vigo‐Pelfrey, M. Citron, 1992, Nature.

Enhanced Production and Oligomerization of the 42-residue Amyloid β-Protein by Chinese Hamster Ovary Cells Stably Expressing Mutant Presenilins*

D. Selkoe, D. Teplow, D. Kholodenko, 1997, The Journal of Biological Chemistry.

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice

Weiming Xia, Paul Fraser, J. Rommens, 1997, Nature Medicine.

Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease.

J. Hardy, M. Viitanen, D. Selkoe, 1996, Nature medicine.

A Substrate-Based Difluoro Ketone Selectively Inhibits Alzheimer's γ-Secretase Activity

D. Selkoe, M. Wolfe, M. Citron, 1998 .

Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

D. Selkoe, C. Vigo‐Pelfrey, M. Citron, 1992, Nature.

Activation of protein kinase C inhibits cellular production of the amyloid beta-protein.

J. Growdon, D. Selkoe, R. Wurtman, 1993, The Journal of biological chemistry.

Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.

M. Citron, H. Loetscher, C. Haass, 1999, Biochemistry.

Proteolytic processing of the Alzheimer disease-associated presenilin-1 generates an in vivo substrate for protein kinase C.

D. Selkoe, P. George-Hyslop, G. Multhaup, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The Proteolytic Fragments of the Alzheimer’s Disease-associated Presenilin-1 Form Heterodimers and Occur as a 100–150-kDa Molecular Mass Complex*

D. Selkoe, K. Beyreuther, M. Citron, 1998, The Journal of Biological Chemistry.

Presenilin Proteins Undergo Heterogeneous Endoproteolysis between Thr291and Ala299and Occur as Stable N- and C-Terminal Fragments in Normal and Alzheimer Brain Tissue

R. Sherrington, D. Selkoe, P. Fraser, 1997, Neurobiology of Disease.

Generation of amyloid β protein from its precursor is sequence specific

D. Selkoe, D. Teplow, M. Citron, 1995, Neuron.

The Vacuolar H-ATPase Inhibitor Bafilomycin A1 Differentially Affects Proteolytic Processing of Mutant and Wild-type -Amyloid Precursor Protein (*)

D. Selkoe, D. Teplow, M. Citron, 1995, The Journal of Biological Chemistry.

beta-Amyloid, protein processing and Alzheimer's disease.

D. Selkoe, D. Teplow, M. Citron, 1995, Arzneimittel-Forschung.

A Loss of Function Mutation of Presenilin-2 Interferes with Amyloid β-Peptide Production and Notch Signaling*

S. Lincoln, J. Hardy, T. Iwatsubo, 1999, The Journal of Biological Chemistry.

The Role of APP Processing and Trafficking Pathways in the Formation of Amyloid β‐Protein a

D. Selkoe, D. Teplow, M. Citron, 1996 .

Inhibition of Amyloid β-Protein Production in Neural Cells by the Serine Protease Inhibitor AEBSF

D. Selkoe, D. Teplow, M. Citron, 1996, Neuron.

Expression of Alzheimer’s Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation*

P. Kloetzel, D. Selkoe, M. Citron, 1998, The Journal of Biological Chemistry.

Evidence that the 42- and 40-amino acid forms of amyloid beta protein are generated from the beta-amyloid precursor protein by different protease activities.

D. Selkoe, M. Citron, P. Seubert, 1996, Proceedings of the National Academy of Sciences of the United States of America.