ArticleNuclear instruments & methods in physics research. Section A, Accelerators, spectrometers, detectors and associated equipment2011
X-ray diffraction from intact tau aggregates in human brain tissue.
Article in Nuclear instruments & methods in physics research. Section A, Accelerators, spectrometers, detectors and associated equipment, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
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- X-ray diffraction reveals alterations in mouse somatosensory cortex following sensory deprivation.Journal of neuroscience methods · 2025Article
- The Design of a Reflection Electron Energy Loss Spectrometer Attachment for Low Voltage Scanning Electron Microscopy.Materials (Basel, Switzerland) · 2021Article
- Inverse Transformation: Unleashing Spatially Heterogeneous Dynamics with an Alternative Approach to XPCS Data Analysis.Journal of applied crystallography · 2018Article
- Current advances in synchrotron radiation instrumentation for MX experiments.Archives of biochemistry and biophysics · 2016Review
- Development ofECS transactions · 2016Article
- X-ray micro-diffraction studies on biological samples at the BioCAT Beamline 18-ID at the Advanced Photon Source.Journal of synchrotron radiation · 2014Article
- A monochromatic, aberration-corrected, dual-beam low energy electron microscope.Ultramicroscopy · 2013Article
- Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
We describe an instrument to record x-ray diffraction patterns from diseased regions of human brain tissue by combining an in-line visible light fluorescence microscope with an x-ray diffraction microprobe. We use thiazine red fluorescence to specifically label and detect the filamentous tau protein pathology associated with Pick's disease, as several labs have done previously. We demonstrate that thiazine red-enhanced regions within the tissue show periodic structure in x-ray diffraction that is not observed in healthy tissue. One observed periodicity (4.2 Å) is characteristic of cross-beta sheet structure, consistent with previous results from powder diffraction studies performed on purified, dried tau protein.
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Registered trials
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