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Mendeley readers
Attention Score in Context
| Title |
Alternative salt bridge formation in Aβ—a hallmark of early-onset Alzheimer's disease?
|
|---|---|
| Published in |
Frontiers in Molecular Biosciences, April 2015
|
| DOI | 10.3389/fmolb.2015.00014 |
| Pubmed ID | |
| Authors |
Maarten Schledorn, Beat H. Meier, Anja Böckmann |
| Abstract |
Recently the 3D structure of the Osaka mutant form (E22Δ) of Amyloid-β1-40 has been determined. We here compare the NMR chemical-shift with the published shifts of a brain-seeded form of wild-type Aβ and suggest that the determined mutant fold is accessible to the wild-type protein as well, with small conformational adaptations which accommodate the E22 residue missing in the Osaka mutant. In addition, we illustrate how other mutants could also conform to this model. The stabilization of the N-terminal part of the protein via an intermolecular salt bridge to Lys28 may represent a common structural motif for the mutants which are related to early-onset Alzheimer disease. This feature might connect to the observed increased toxicity of the mutant forms compared to wild-type Aβ1-40, where the salt bridge involving Lys28 is intramolecular. |
X Demographics
The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Switzerland | 1 | 100% |
Demographic breakdown
| Type | Count | As % |
|---|---|---|
| Scientists | 1 | 100% |
Mendeley readers
The data shown below were compiled from readership statistics for 21 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 1 | 5% |
| India | 1 | 5% |
| Unknown | 19 | 90% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 5 | 24% |
| Researcher | 5 | 24% |
| Student > Doctoral Student | 2 | 10% |
| Student > Bachelor | 2 | 10% |
| Other | 2 | 10% |
| Other | 5 | 24% |
| Readers by discipline | Count | As % |
|---|---|---|
| Chemistry | 6 | 29% |
| Biochemistry, Genetics and Molecular Biology | 5 | 24% |
| Chemical Engineering | 2 | 10% |
| Medicine and Dentistry | 2 | 10% |
| Agricultural and Biological Sciences | 2 | 10% |
| Other | 4 | 19% |
Attention Score in Context
This research output has an Altmetric Attention Score of 10. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 26 May 2015.
All research outputs
#3,118,499
of 22,800,560 outputs
Outputs from Frontiers in Molecular Biosciences
#235
of 3,765 outputs
Outputs of similar age
#42,406
of 264,516 outputs
Outputs of similar age from Frontiers in Molecular Biosciences
#4
of 21 outputs
Altmetric has tracked 22,800,560 research outputs across all sources so far. Compared to these this one has done well and is in the 86th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 3,765 research outputs from this source. They receive a mean Attention Score of 3.3. This one has done particularly well, scoring higher than 93% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 264,516 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 83% of its contemporaries.
We're also able to compare this research output to 21 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 80% of its contemporaries.