| Range |
40 - 200 nm
|
| Organism |
Unspecified |
| Reference |
Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6689 left columnPubMed ID24901537
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| Primary Source |
[786] Fauerbach JA et al., Supramolecular non-amyloid intermediates in the early stages of α-synuclein aggregation. Biophys J. 2012 Mar 7 102(5):1127-36. doi: 10.1016/j.bpj.2012.01.051 [787] Roberti MJ et al., Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy. Biophys J. 2012 Apr 4 102(7):1598-607. doi: 10.1016/j.bpj.2012.03.010 [788] Roberti MJ, Jovin TM, Jares-Erijman E. Confocal fluorescence anisotropy and FRAP imaging of α-synuclein amyloid aggregates in living cells. PLoS One. 2011 6(8):e23338. doi: 10.1371/journal.pone.0023338PubMed ID22404935, 22500760, 21858077
|
| Method |
Primary source [786] abstract: "The sequence of structural transformations between metastable intermediates were captured and characterized by atomic force microscopy guided by a fluorescent probe sensitive to preamyloid species…[and] Cryo-electron tomography." Primary source [787] abstract: "The morphological features of α-synuclein (AS) amyloid aggregation in vitro and in cells were elucidated at the nanoscale by far-field subdiffraction fluorescence localization microscopy. Labeling AS with rhodamine spiroamide probes allowed [investigators] to image AS fibrillar structures by fluorescence stochastic nanoscopy with an enhanced resolution at least 10-fold higher than that achieved with conventional, diffraction-limited techniques. The implementation of dual-color detection, combined with atomic force microscopy, revealed the propagation of individual fibrils in vitro…[and] cryo-electron tomography." Primary source [788] abstract: "[Investigators] assessed the intracellular association states of the Parkinson's disease related protein α-synuclein (AS) in living cells by transfection with a functional recombinant mutant protein (AS-C4) bearing a tetracysteine tag binding the fluorogenic biarsenical ligands FlAsH and ReAsH, The aggregation states of AS-C4 were assessed by in situ microscopy of molecular translational mobility with FRAP (fluorescence recovery after photobleaching) and of local molecular density with confocal fluorescence anisotropy (CFA)…The combined strategy (FRAP+CFA) provides a highly sensitive means for elucidating both the dynamics and structural features of protein aggregates and other intracellular complexes in living cells, and can be extended to other amyloid systems and to drug screening protocols." |
| Comments |
P.6689 left column: "A detailed investigation of these cellular α-synuclein aggregates revealed that they contained diameters ranging from 40 to 200 nm, resembling those of large prefibrillar species observed in vitro (Figure 9B) (primary sources)." |
| Entered by |
Uri M |
| ID |
116357 |