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Mendeley readers
Attention Score in Context
| Title |
Vacuolar processing enzyme in plant programmed cell death
|
|---|---|
| Published in |
Frontiers in Plant Science, April 2015
|
| DOI | 10.3389/fpls.2015.00234 |
| Pubmed ID | |
| Authors |
Noriyuki Hatsugai, Kenji Yamada, Shino Goto-Yamada, Ikuko Hara-Nishimura |
| Abstract |
Vacuolar processing enzyme (VPE) is a cysteine proteinase originally identified as the proteinase responsible for the maturation and activation of vacuolar proteins in plants, and it is known to be an ortholog of animal asparaginyl endopeptidase (AEP/VPE/legumain). VPE has been shown to exhibit enzymatic properties similar to that of caspase 1, which is a cysteine protease that mediates the programmed cell death (PCD) pathway in animals. Although there is limited sequence identity between VPE and caspase 1, their predicted three-dimensional structures revealed that the essential amino-acid residues for these enzymes form similar pockets for the substrate peptide YVAD. In contrast to the cytosolic localization of caspases, VPE is localized in vacuoles. VPE provokes vacuolar rupture, initiating the proteolytic cascade leading to PCD in the plant immune response. It has become apparent that the VPE-dependent PCD pathway is involved not only in the immune response, but also in the responses to a variety of stress inducers and in the development of various tissues. This review summarizes the current knowledge on the contribution of VPE to plant PCD and its role in vacuole-mediated cell death, and it also compares VPE with the animal cell death executor caspase 1. |
Mendeley readers
The data shown below were compiled from readership statistics for 204 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Germany | 1 | <1% |
| Brazil | 1 | <1% |
| Unknown | 202 | 99% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 57 | 28% |
| Researcher | 34 | 17% |
| Student > Master | 26 | 13% |
| Student > Bachelor | 24 | 12% |
| Student > Doctoral Student | 14 | 7% |
| Other | 18 | 9% |
| Unknown | 31 | 15% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 104 | 51% |
| Biochemistry, Genetics and Molecular Biology | 47 | 23% |
| Immunology and Microbiology | 3 | 1% |
| Chemistry | 2 | <1% |
| Business, Management and Accounting | 1 | <1% |
| Other | 5 | 2% |
| Unknown | 42 | 21% |
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 11 March 2021.
All research outputs
#7,540,398
of 23,003,906 outputs
Outputs from Frontiers in Plant Science
#4,868
of 20,501 outputs
Outputs of similar age
#91,290
of 265,322 outputs
Outputs of similar age from Frontiers in Plant Science
#59
of 267 outputs
Altmetric has tracked 23,003,906 research outputs across all sources so far. This one is in the 44th percentile – i.e., 44% of other outputs scored the same or lower than it.
So far Altmetric has tracked 20,501 research outputs from this source. They receive a mean Attention Score of 4.0. This one has done well, scoring higher than 75% 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 265,322 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 55% of its contemporaries.
We're also able to compare this research output to 267 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 77% of its contemporaries.