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Plant dehydrins — Tissue location, structure and function

Overview of attention for article published in Cellular & Molecular Biology Letters, January 2006
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About this Attention Score

  • Good Attention Score compared to outputs of the same age (66th percentile)

Mentioned by

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1 Wikipedia page

Citations

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284 Dimensions

Readers on

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163 Mendeley
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Title
Plant dehydrins — Tissue location, structure and function
Published in
Cellular & Molecular Biology Letters, January 2006
DOI 10.2478/s11658-006-0044-0
Pubmed ID
Authors

Tadeusz Rorat

Abstract

Dehydrins (DHNs) are part of a large group of highly hydrophilic proteins known as LEA (Late Embryogenesis Abundant). They were originally identified as group II of the LEA proteins. The distinctive feature of all DHNs is a conserved, lysine-rich 15-amino acid domain, EKKGIMDKIKEKLPG, named the K-segment. It is usually present near the C-terminus. Other typical dehydrin features are: a track of Ser residues (the S-segment); a consensus motif, T/VDEYGNP (the Y-segment), located near the N-terminus; and less conserved regions, usually rich in polar amino acids (the Phi-segments). They do not display a well-defined secondary structure. The number and order of the Y-, S-and K-segments define different DHN sub-classes: Y(n)SK(n), Y(n)Kn, SK(n), K(n) and K(n)S. Dehydrins are distributed in a wide range of organisms including the higher plants, algae, yeast and cyanobacteria. They accumulate late in embryogenesis, and in nearly all the vegetative tissues during normal growth conditions and in response to stress leading to cellular dehydration (e.g. drought, low temperature and salinity). DHNs are localized in different cell compartments, such as the cytosol, nucleus, mitochondria, vacuole, and the vicinity of the plasma membrane; however, they are primarily localized to the cytoplasm and nucleus. The precise function of dehydrins has not been established yet, but in vitro experiments revealed that some DHNs (YSK(n)-type) bind to lipid vesicles that contain acidic phospholipids, and others (K(n)S) were shown to bind metals and have the ability to scavenge hydroxyl radicals [Asghar, R. et al. Protoplasma 177 (1994) 87-94], protect lipid membranes against peroxidation or display cryoprotective activity towards freezing-sensitive enzymes. The SK(n)-and K-type seem to be directly involved in cold acclimation processes. The main question arising from the in vitro findings is whether each DHN structural type could possess a specific function and tissue distribution. Much recent in vitro data clearly indicates that dehydrins belonging to different subclasses exhibit distinct functions.

Mendeley readers

The data shown below were compiled from readership statistics for 163 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 2 1%
Portugal 1 <1%
Germany 1 <1%
Chile 1 <1%
Paraguay 1 <1%
Bangladesh 1 <1%
Spain 1 <1%
United Kingdom 1 <1%
Japan 1 <1%
Other 1 <1%
Unknown 152 93%

Demographic breakdown

Readers by professional status Count As %
Student > Master 34 21%
Researcher 30 18%
Student > Ph. D. Student 26 16%
Student > Bachelor 19 12%
Student > Postgraduate 15 9%
Other 21 13%
Unknown 18 11%
Readers by discipline Count As %
Agricultural and Biological Sciences 111 68%
Biochemistry, Genetics and Molecular Biology 20 12%
Psychology 2 1%
Environmental Science 2 1%
Chemistry 2 1%
Other 2 1%
Unknown 24 15%

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 07 December 2012.
All research outputs
#2,644,228
of 9,789,451 outputs
Outputs from Cellular & Molecular Biology Letters
#13
of 77 outputs
Outputs of similar age
#75,647
of 253,031 outputs
Outputs of similar age from Cellular & Molecular Biology Letters
#2
of 4 outputs
Altmetric has tracked 9,789,451 research outputs across all sources so far. This one has received more attention than most of these and is in the 57th percentile.
So far Altmetric has tracked 77 research outputs from this source. They receive a mean Attention Score of 2.1. This one has done particularly well, scoring higher than 99% 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 253,031 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 66% of its contemporaries.
We're also able to compare this research output to 4 others from the same source and published within six weeks on either side of this one. This one has scored higher than 2 of them.