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Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins

Overview of attention for article published in Journal of Molecular Evolution, February 1990
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20 Mendeley
Title
Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins
Published in
Journal of Molecular Evolution, February 1990
DOI 10.1007/bf02099940
Pubmed ID
Authors

Graeme Wistow

Abstract

A search of sequence databases shows that spherulin 3a, an encystment-specific protein of Physarum polycephalum, is probably structurally related to the beta- and gamma-crystallins, vertebrate ocular lens proteins, and to Protein S, a sporulation-specific protein of Myxococcus xanthus. The beta- and gamma-crystallins have two similar domains thought to have arisen by two successive gene duplication and fusion events. Molecular modeling confirms that spherulin 3a has all the characteristics required to adopt the tertiary structure of a single gamma-crystallin domain. The structure of spherulin 3a thus illustrates an earlier stage in the evolution of this protein superfamily. The relationship of beta- and gamma-crystallins to spherulin 3a and Protein S suggests that the lens proteins were derived from an ancestor with a role in stress-response, perhaps a response to osmotic stress.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 20 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 20 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 5 25%
Student > Master 3 15%
Student > Ph. D. Student 2 10%
Student > Bachelor 2 10%
Professor > Associate Professor 2 10%
Other 2 10%
Unknown 4 20%
Readers by discipline Count As %
Agricultural and Biological Sciences 8 40%
Biochemistry, Genetics and Molecular Biology 5 25%
Chemistry 3 15%
Unknown 4 20%
Attention Score in Context

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 12 April 2014.
All research outputs
#7,451,942
of 22,782,096 outputs
Outputs from Journal of Molecular Evolution
#450
of 1,438 outputs
Outputs of similar age
#11,500
of 57,953 outputs
Outputs of similar age from Journal of Molecular Evolution
#3
of 7 outputs
Altmetric has tracked 22,782,096 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 1,438 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.2. This one is in the 29th percentile – i.e., 29% of its peers scored the same or lower than it.
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 57,953 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 21st percentile – i.e., 21% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 7 others from the same source and published within six weeks on either side of this one. This one has scored higher than 4 of them.