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Mendeley readers
| Chapter title |
In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles
|
|---|---|
| Chapter number | 18 |
| Book title |
Protein Amyloid Aggregation
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-2978-8_18 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-2977-1, 978-1-4939-2978-8
|
| Authors |
Ping Cao, Daniel P. Raleigh |
| Abstract |
The process of amyloid formation is cytotoxic and contributes to a wide range of human diseases, but the mechanisms of amyloid-induced cytotoxicity are not well understood. It has been proposed that amyloidogenic peptides exert their toxic effects by damaging membranes. Membrane disruption is clearly not the only mechanism of toxicity, but the literature suggests that loss of membrane integrity may be a contributing factor. In this chapter we describe the measurement of in vitro membrane leakage induced by amyloidogenic proteins via the use of model vesicles. We use islet amyloid polypeptide (IAPP, amylin) as an example, but the methods are general. |
Mendeley readers
The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 3 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 2 | 67% |
| Student > Bachelor | 1 | 33% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 1 | 33% |
| Agricultural and Biological Sciences | 1 | 33% |
| Chemistry | 1 | 33% |