dominant spinal muscular atrophy is caused by mutations in bicd2, an important golgin protein
Clicks: 252
ID: 160487
2015
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This
article has not been analysed, so there is no overall score —
reader engagement is measured and shown alongside.
Reader Engagement
Steady Performance
30.0
/100
252 views
31 readers
AI Quality Assessment
Not analyzed
Readership in this journal
SteadyRanked #235 of 403 articles by views in Journal of enzyme inhibition and medicinal chemistry
Most read
Least read
Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 403 in total.
Mint this article as an NFT
Not yet mintedCreate a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.
5
SUSD
one-off · no wallet required
Abstract
Spinal muscular atrophies (SMAs) are characterized by degeneration of spinal motor neurons and muscle weakness. Autosomal recessive SMA is the most common form and is caused by homozygous deletions/mutations of the SMN1 gene. However, families with dominant inherited SMA have been reported, for most of them the causal gene remains unknown. Recently, we and others have identified heterozygous mutations in BICD2 as causative for autosomal dominant SMA, lower extremity-predominant, 2 (SMALED2). BICD2 encodes the Bicaudal D2 protein, which is considered to be a golgin, due to its coiled-coil structure and interaction with the small GTPase RAB6A located at the Golgi apparatus. Golgins are resident proteins in the Golgi apparatus and form a matrix that helps to maintain the structure of this organelle. Golgins are also involved in the regulation of vesicle transport. In vitro overexpression experiments and studies of fibroblast cell lines derived from patients, showed fragmentation of the Golgi apparatus. In the current review, we will discuss possible causes for this disruption and the consequences at cellular level, with a view to better understand the pathomechanism of this disease.
| Reference Key |
ewirth2015frontiersdominant
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | ;Brunhilde eWirth;Brunhilde eWirth;Brunhilde eWirth;Lilian A. Martinez-Carrera;Lilian A. Martinez-Carrera;Lilian A. Martinez-Carrera |
| Journal | Journal of enzyme inhibition and medicinal chemistry |
| Year | 2015 |
| DOI |
10.3389/fnins.2015.00401
|
| URL | |
| Keywords |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.