Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology

By Hai Lin, R. Bhatia, R. Lal. 2001

667 citations recorded by the source corpus.

Subfields: Molecular Biology, Nutrition and Dietetics, Physiology

View Paper: https://www.semanticscholar.org/paper/d0f227bbcec819ee22b49b5348370b86de748255

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. M. Duchen
2. A. Abramov
3. E. Masliah
4. Leslie A. Crews
5. R. Balaban
6. B. Glancy

In Nutrition and Dietetics

1. M. Duchen
2. A. Abramov

In Physiology

1. M. Duchen
2. A. Abramov
3. K. Viola
4. P. Velasco
5. E. Masliah
6. P. Lacor
7. W. Klein
8. Leslie A. Crews

Citations in the corpus

• Aβ Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease (2007, background): “Prevention of drebrin loss by memantine Although evidence from model membranes (Lin et al., 2001) suggests that ADDLs ostensibly might exert synaptotoxicity by creating annular pores within plasma membranes, the specificity of binding to particular synaptic spines has been suggested to support a rec”
• β-Amyloid Peptides Induce Mitochondrial Dysfunction and Oxidative Stress in Astrocytes and Death of Neurons through Activation of NADPH Oxidase (2004, background): “We wondered whether they might be induced by transient opening of the mitochondrial permeability transition pore (MPTP) or whetherA might be internalized and form a pore directly in the mitochondrial inner membrane, as it does in the plasma membrane ( Lin et al., 2001; Abramov et al., 2003).”
• Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain. (2002, background): “These findings lend strong support to the hypothesis that the peptide neurotoxicity is due to a membrane-poration process [10,11].”
• Molecular mechanisms of neurodegeneration in Alzheimer's disease. (2010, background): “A number of possibilities are under investigation, including the formation of porelike structures with channel activity (93-96); alterations in glutamate receptors and excitotoxicity (97-101); circuitry hyper-excitability (102); mitochondrial dysfunction (103, 104); lysosomal failure (105) and alter”