The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes
Published 2014 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes
Authors
Keywords
Tau, Annular protofibrils, Oligomers, Tauopathies
Journal
Acta Neuropathologica Communications
Volume 2, Issue 1, Pages -
Publisher
Springer Nature
Online
2014-05-29
DOI
10.1186/2051-5960-2-56
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Evidence that Non-Fibrillar Tau Causes Pathology Linked to Neurodegeneration and Behavioral Impairments
- (2017) Kurt R. Brunden et al. JOURNAL OF ALZHEIMERS DISEASE
- Identification of oligomers at early stages of tau aggregation in Alzheimer's disease
- (2012) Cristian A. Lasagna-Reeves et al. FASEB JOURNAL
- Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability
- (2012) Katharina Flach et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Synergistic Interactions between Repeats in Tau Protein and Aβ Amyloids May Be Responsible for Accelerated Aggregation via Polymorphic States
- (2011) Yifat Miller et al. BIOCHEMISTRY
- Astrocytes contain amyloid-β annular protofibrils in Alzheimer's disease brains
- (2011) Cristian A. Lasagna-Reeves et al. FEBS LETTERS
- Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain
- (2011) Cristian A. Lasagna-Reeves et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
- (2011) Cristian A Lasagna-Reeves et al. Molecular Neurodegeneration
- Dynamic association of tau with neuronal membranes is regulated by phosphorylation
- (2011) Amy M. Pooler et al. NEUROBIOLOGY OF AGING
- Functional implications of the association of tau with the plasma membrane
- (2010) Amy M. Pooler et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Preparation and Characterization of Neurotoxic Tau Oligomers
- (2010) Cristian A. Lasagna-Reeves et al. BIOCHEMISTRY
- Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
- (2010) Lars M. Ittner et al. CELL
- N-terminal Domain of Myelin Basic Protein Inhibits Amyloid β-Protein Fibril Assembly
- (2010) Mei-Chen Liao et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Direct Transfer of α-Synuclein from Neuron to Astroglia Causes Inflammatory Responses in Synucleinopathies
- (2010) He-Jin Lee et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Truncated -amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome
- (2010) H. Jang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Mechanisms of tau-induced neurodegeneration
- (2009) Khalid Iqbal et al. ACTA NEUROPATHOLOGICA
- Myelin Basic Protein Binds to and Inhibits the Fibrillar Assembly of Aβ42 in Vitro
- (2009) Michael D. Hoos et al. BIOCHEMISTRY
- Degradation of Amyloid β Protein by Purified Myelin Basic Protein
- (2009) Mei-Chen Liao et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Age-Dependent Impairment of Cognitive and Synaptic Function in the htau Mouse Model of Tau Pathology
- (2009) M. Polydoro et al. JOURNAL OF NEUROSCIENCE
- Mechanism of Tau-Induced Neurodegeneration in Alzheimer Disease and Related Tauopathies
- (2008) Alejandra del Alonso et al. Current Alzheimer Research
- Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer
- (2008) Rakez Kayed et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane
- (2008) M. F. M. Engel et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Find the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
SearchAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started