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Mendeley readers
Attention Score in Context
| Title |
Single amino acids in the carboxyl terminal domain of aquaporin-1 contribute to cGMP-dependent ion channel activation
|
|---|---|
| Published in |
BMC Physiology, October 2003
|
| DOI | 10.1186/1472-6793-3-12 |
| Pubmed ID | |
| Authors |
Daniela Boassa, Andrea J Yool |
| Abstract |
Aquaporin-1 (AQP1) functions as an osmotic water channel and a gated cation channel. Activation of the AQP1 ion conductance by intracellular cGMP was hypothesized to involve the carboxyl (C-) terminus, based on amino acid sequence alignments with cyclic-nucleotide-gated channels and cGMP-selective phosphodiesterases. Voltage clamp analyses of human AQP1 channels expressed in Xenopus oocytes demonstrated that the nitric oxide donor, sodium nitroprusside (SNP; 3-14 mM) activated the ionic conductance response in a dose-dependent manner. Block of soluble guanylate cyclase prevented the response. Enzyme immunoassays confirmed a linear dose-dependent relationship between SNP and the resulting intracellular cGMP levels (up to 1700 fmol cGMP /oocyte at 14 mM SNP). Results here are the first to show that the efficacy of ion channel activation is decreased by mutations of AQP1 at conserved residues in the C-terminal domain (aspartate D237 and lysine K243). These data support the idea that the limited amino acid sequence similarities found between three diverse classes of cGMP-binding proteins are significant to the function of AQP1 as a cGMP-gated ion channel, and provide direct evidence for the involvement of the AQP1 C-terminal domain in cGMP-mediated ion channel activation. |
Mendeley readers
The data shown below were compiled from readership statistics for 10 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Sweden | 1 | 10% |
| Argentina | 1 | 10% |
| Unknown | 8 | 80% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 6 | 60% |
| Student > Ph. D. Student | 4 | 40% |
| Student > Bachelor | 2 | 20% |
| Professor | 2 | 20% |
| Student > Doctoral Student | 1 | 10% |
| Other | 4 | 40% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 9 | 90% |
| Biochemistry, Genetics and Molecular Biology | 3 | 30% |
| Neuroscience | 2 | 20% |
| Medicine and Dentistry | 2 | 20% |
| Pharmacology, Toxicology and Pharmaceutical Science | 1 | 10% |
| Other | 1 | 10% |
Attention Score in Context
This research output has an Altmetric Attention Score of 3. 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 13 April 2020.
All research outputs
#8,535,684
of 25,374,917 outputs
Outputs from BMC Physiology
#32
of 88 outputs
Outputs of similar age
#19,934
of 56,877 outputs
Outputs of similar age from BMC Physiology
#1
of 1 outputs
Altmetric has tracked 25,374,917 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 88 research outputs from this source. They typically receive more attention than average, with a mean Attention Score of 7.8. This one has gotten more attention than average, scoring higher than 50% 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 56,877 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 11th percentile – i.e., 11% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 1 others from the same source and published within six weeks on either side of this one. This one has scored higher than all of them