Deposition of C-terminally truncated Aβ species Aβ37 and Aβ39 in Alzheimer’s disease and transgenic mouse models
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Deposition of C-terminally truncated Aβ species Aβ37 and Aβ39 in Alzheimer’s disease and transgenic mouse models
Authors
Keywords
Alzheimer, C-terminal truncation, Amyloid precursor protein, Transgenic mice, Aβ37, Aβ39, Immunohistochemistry, Mass spectrometry
Journal
Acta Neuropathologica Communications
Volume 4, Issue 1, Pages -
Publisher
Springer Nature
Online
2016-03-08
DOI
10.1186/s40478-016-0294-7
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- C-Terminal Fragment, Aβ32–37, Analogues Protect Against Aβ Aggregation-Induced Toxicity
- (2016) Sunil Bansal et al. ACS Chemical Neuroscience
- Tau pathogenesis is promoted by Aβ1-42 but not Aβ1-40
- (2014) Xiaoyan Hu et al. Molecular Neurodegeneration
- Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site
- (2014) Wen Chen et al. Nature Communications
- Analysis of Amino-Terminal Variants of Amyloid-β Peptides by Capillary Isoelectric Focusing Immunoassay
- (2013) Ute Haußmann et al. ANALYTICAL CHEMISTRY
- γ-Secretase inhibitors and modulators
- (2013) Todd E. Golde et al. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
- γ-Secretase Associated with Lipid Rafts
- (2013) Nobutaka Matsumura et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Characterization of Intermediate Steps in Amyloid Beta (Aβ) Production under Near-native Conditions
- (2013) Fredrik Olsson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Autosomal-dominant Alzheimer's disease mutations at the same codon of amyloid precursor protein differentially alter Aβ production
- (2013) Marc Suárez-Calvet et al. JOURNAL OF NEUROCHEMISTRY
- The Genetics of Alzheimer Disease
- (2013) R. E. Tanzi Cold Spring Harbor Perspectives in Medicine
- Trafficking and Proteolytic Processing of APP
- (2013) C. Haass et al. Cold Spring Harbor Perspectives in Medicine
- The Arctic AβPP mutation leads to Alzheimer’s disease pathology with highly variable topographic deposition of differentially truncated Aβ
- (2013) Hannu Kalimo et al. Acta Neuropathologica Communications
- APP mutations in the Aβ coding region are associated with abundant cerebral deposition of Aβ38
- (2012) Maria Luisa Moro et al. ACTA NEUROPATHOLOGICA
- A comparative analysis of the aggregation behavior of amyloid-β peptide variants
- (2012) Annelies Vandersteen et al. FEBS LETTERS
- Overlapping profiles of Abeta peptides in the Alzheimer's disease and pathological aging brains
- (2012) Brenda D Moore et al. Alzheimers Research & Therapy
- Amyloid Precursor Protein Processing and Alzheimer's Disease
- (2011) Richard J. O'Brien et al. Annual Review of Neuroscience
- Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer’s disease
- (2010) Erik Portelius et al. ACTA NEUROPATHOLOGICA
- Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio
- (2010) Inna Kuperstein et al. EMBO JOURNAL
- Distinct cerebrospinal fluid amyloid β peptide signatures in sporadic and PSEN1 A431E-associated familial Alzheimer's disease
- (2010) Erik Portelius et al. Molecular Neurodegeneration
- Clinical, Neuropathologic, and Biochemical Profile of the Amyloid Precursor Protein I716F Mutation
- (2009) Cristina Guardia-Laguarta et al. JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY
- Mutations in amyloid precursor protein affect its interactions with presenilin/γ-secretase
- (2009) Lauren Herl et al. MOLECULAR AND CELLULAR NEUROSCIENCE
- Independent Generation of Aβ42 and Aβ38 Peptide Species by γ-Secretase
- (2008) Eva Czirr et al. JOURNAL OF BIOLOGICAL CHEMISTRY
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started