File:Fnmol-13-592644-g002 (1).jpg
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[edit]DescriptionFnmol-13-592644-g002 (1).jpg |
English: FIGURE 2. Mechanisms-driving TTR amyloidogenesis and different therapeutic targets for the treatment of ATTR amyloidosis. Tetramer destabilization is widely accepted as a rate-limiting step for the development of amyloid fibrils. However, TTR proteolysis has been increasingly suggested as an alternative mechanism contributing to amyloid formation. Several pharmacological agents have been implicated in the treatment of ATTR amyloidosis, from inhibitors of TTR synthesis, tetramer stabilizers, inhibitors of amyloid formation and even disruptors of formed fibrils. The modulation of TTR proteolysis may also be helpful for the treatment of ATTR amyloidosis. Despite the protease responsible for this process has not yet been identified, its specific cleavage patterns suggest that it could be a trypsin-like serine protease. Accordingly, pharmacological molecules targeting lysine residues, as well as physiological serine protease inhibitors may be act as modulators of TTR proteolysis, consequently inhibiting amyloid formation. |
Date | |
Source | https://www.frontiersin.org/articles/10.3389/fnmol.2020.592644/full |
Author | Filipa Bezerra,Maria João Saraiva,Maria Rosário Almeida |
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current | 16:41, 23 March 2024 | 1,084 × 718 (331 KB) | Ozzie10aaaa (talk | contribs) | Uploaded a work by Filipa Bezerra,Maria João Saraiva,Maria Rosário Almeida from https://www.frontiersin.org/articles/10.3389/fnmol.2020.592644/full with UploadWizard |
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Width | 1,280 px |
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Height | 720 px |
Compression scheme | LZW |
Pixel composition | RGB |
Orientation | Normal |
Number of components | 4 |
Horizontal resolution | 72 dpi |
Vertical resolution | 72 dpi |
Data arrangement | chunky format |
Software used | Adobe Photoshop CS6 (Windows) |
File change date and time | 14:50, 6 December 2020 |
Color space | Uncalibrated |
Date and time of digitizing | 18:38, 22 November 2020 |
Date metadata was last modified | 20:20, 6 December 2020 |
Unique ID of original document | xmp.did:6858d6a6-9a38-d646-8c1f-8a6b9d88ef26 |