Evidence map›Paper›PMID 25346739›Full record

ArticleFrontiers in plant science2014

A dehydrin-dehydrin interaction: the case of SK3 from Opuntia streptacantha.

Itzell E Hernández-Sánchez, David M Martynowicz, Aida A Rodríguez-Hernández, Maria B Pérez-Morales, Steffen P Graether, Juan F Jiménez-Bremont

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.1field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 48 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Itzell E Hernández-SánchezLaboratorio de Estudios Moleculares de Respuesta a Estrés en Plantas, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica AC Tangamanga, México.
David M MartynowiczDepartment of Molecular and Cellular Biology, University of Guelph Guelph, ON, Canada.
Aida A Rodríguez-HernándezLaboratorio de Estudios Moleculares de Respuesta a Estrés en Plantas, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica AC Tangamanga, México.
Maria B Pérez-MoralesLaboratorio de Estudios Moleculares de Respuesta a Estrés en Plantas, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica AC Tangamanga, México.
Steffen P GraetherDepartment of Molecular and Cellular Biology, University of Guelph Guelph, ON, Canada.
Juan F Jiménez-BremontLaboratorio de Estudios Moleculares de Respuesta a Estrés en Plantas, División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica AC Tangamanga, México.
Institute for Scientific and Technological Research · MXUniversity of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dehydrins belongs to a large group of highly hydrophilic proteins known as Late Embryogenesis Abundant (LEA) proteins. It is well known that dehydrins are intrinsically disordered plant proteins that accumulate during the late stages of embryogenesis and in response to abiotic stresses; however, the molecular mechanisms by which their functions are carried out are still unclear. We have previously reported that transgenic Arabidopsis plants overexpressing an Opuntia streptacantha SK3 dehydrin (OpsDHN1) show enhanced tolerance to freezing stress. Herein, we show using a split-ubiquitin yeast two-hybrid system that OpsDHN1 dimerizes. We found that the deletion of regions containing K-segments and the histidine-rich region in the OpsDHN1 protein affects dimer formation. Not surprisingly, in silico protein sequence analysis suggests that OpsDHN1 is an intrinsically disordered protein, an observation that was confirmed by circular dichroism and gel filtration of the recombinantly expressed protein. The addition of zinc triggered the association of recombinantly expressed OpsDHN1 protein, likely through its histidine-rich motif. These data brings new insights about the molecular mechanism of the OpsDHN1 SK3-dehydrin.

Indexed as

histidine-rich regionhomodimerintrinsically disordered proteinsK-segmentsSK3-dehydrinyeast two-hybrid

Identifiers

PMID25346739
PMCPMC4193212
OpenAlexW2042364739

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.