Disease protein muscles out of the nucleus

Using an array of analytical methods - including an antibody to specifically detect amyloid-like material, and high-resolution microscopy and X-ray diffraction techniques to enable examination of the myo-granule's structure - the authors demonstrated that TDP-43 myo-granules have amyloid-like p...

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Bibliographic Details
Published in:Nature (London) 2018-11, Vol.563 (7732), p.1-2
Main Authors: Becker, Lindsay A, Gitler, Aaron D
Format: Article
Language:English
Subjects:
Aggregates
Amyloid
Amyotrophic lateral sclerosis
Disease
Dismantling
Granular materials
Granule cells
Medical research
Muscles
Neurodegeneration
Physiology
Proteins
Robinson, J
Stem cells
Weightlifting
X-ray diffraction
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Summary:Using an array of analytical methods - including an antibody to specifically detect amyloid-like material, and high-resolution microscopy and X-ray diffraction techniques to enable examination of the myo-granule's structure - the authors demonstrated that TDP-43 myo-granules have amyloid-like properties. Unlike myo-granules, most TDP-43 disease aggregates seem to have an amorphous structure, although some do have amyloid-like characteristics9. [...]the disease aggregates seem to be irreversible, whereas myo-granules disassemble as muscle cells mature. Because of this, myogranules could provide an opportunity to investigate how strongly bound aggregate structures are disassembled.
ISSN:0028-0836
1476-4687
DOI:10.1038/d41586-018-07141-2