Investigating fibrillar aggregates of tau protein by atomic force microscopy
Methods in Molecular Biology, ISSN: 1064-3745, Vol: 849, Page: 169-183
2012
- 8Citations
- 29Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations8
- Citation Indexes8
- CrossRef5
- Captures29
- Readers29
- 29
Book Chapter Description
Atomic force microscopy (AFM) has been used in numerous studies to visualize and analyze the structure and conformation of biological samples, from single molecules to biopolymers to cells. The possibility to analyze native samples without fixation, staining and in physiological buffer conditions, combined with the sub-nanometer resolution, makes AFM a versatile tool for the analysis of protein aggregation and amyloid structures. Here, we describe the application of AFM to study fibrillar Tau protein aggregates. © 2012 Springer Science+Business Media, LLC.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84864624676&origin=inward; http://dx.doi.org/10.1007/978-1-61779-551-0_12; http://www.ncbi.nlm.nih.gov/pubmed/22528090; http://link.springer.com/10.1007/978-1-61779-551-0_12; https://dx.doi.org/10.1007/978-1-61779-551-0_12; https://link.springer.com/protocol/10.1007/978-1-61779-551-0_12; http://www.springerlink.com/index/10.1007/978-1-61779-551-0_12; http://www.springerlink.com/index/pdf/10.1007/978-1-61779-551-0_12
Springer Science and Business Media LLC
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