Evidence map›Paper›PMID 36291719›Full record

ArticleBiomolecules2022

The Effect of Positive Charge Distribution on the Cryoprotective Activity of Dehydrins.

Margaret A Smith, Steffen P Graether

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
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

2 authors at 1 institution in 1 country.

Margaret A SmithDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada.
Steffen P GraetherDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada.ORCID 0000-0002-2356-3936
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dehydrins are intrinsically disordered proteins expressed ubiquitously throughout the plant kingdom in response to desiccation. Dehydrins have been found to have a cryoprotective effect on lactate dehydrogenase (LDH) in vitro, which is in large part influenced by their hydrodynamic radius rather than the order of the amino acids within the sequence (alternatively, this may be a sequence specific effect). However, it seems that a different mechanism may underpin the cryoprotection that they confer to the cold-labile yeast frataxin homolog-1 (Yfh1). Circular dichroism spectroscopy (CD) was used to assess the degree of helicity of Yfh1 at 1 °C, both alone and in the presence of several dehydrin constructs. Three constructs were compared to the wild type: YSK

Indexed as

Intrinsically Disordered ProteinsAmino AcidsArginineCryoprotective AgentsL-Lactate DehydrogenaseLysinePlant ProteinsAmino AcidsArginineCryoprotective AgentsIntrinsically Disordered ProteinsL-Lactate DehydrogenaseLysinePlant Proteinschargecircular dichroismcryoprotectiondehydrinsintrinsically disordered proteinslactate dehydrogenasesequence orderyeast frataxin homolog 1

Identifiers

PMID36291719
PMCPMC9599493
OpenAlexW4306836449

What OpenQuestion holds

Textmetadata
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.