Evidence map›Paper›PMID 21280121›Full record

ArticleProtein science : a publication of the Protein Society2011

Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.

Wietske Lambert, Philip J B Koeck, Emma Ahrman, Pasi Purhonen, Kimberley Cheng, Dominika Elmlund, Hans Hebert, Cecilia Emanuelsson

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. TheFrontiers in plant science · 2020
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
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

8 authors at 2 institutions in 1 country.

Wietske LambertDepartment of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Sweden. wietske.lambert@biochemistry.lu.se
Philip J B Koeck
Emma Ahrman
Pasi Purhonen
Kimberley Cheng
Dominika Elmlund
Hans Hebert
Cecilia Emanuelsson
Karolinska Institutet · SELund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Unfolding proteins are prevented from irreversible aggregation by small heat shock proteins (sHsps) through interactions that depend on a dynamic equilibrium between sHsp subunits and sHsp oligomers. A chloroplast-localized sHsp, Hsp21, provides protection to client proteins to increase plant stress resistance. Structural information is lacking concerning the oligomeric conformation of this sHsp. We here present a structure model of Arabidopsis thaliana Hsp21, obtained by homology modeling, single-particle electron microscopy, and lysine-specific chemical crosslinking. The model shows that the Hsp21 subunits are arranged in two hexameric discs, similar to a cytosolic plant sHsp homolog that has been structurally determined after crystallization. However, the two hexameric discs of Hsp21 are rotated by 25° in relation to each other, suggesting a role for global dynamics in dodecamer function.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChloroplastsCross-Linking ReagentsCytosolHeat-Shock ProteinsImage Processing, Computer-AssistedLysineMicroscopy, ElectronModels, MolecularMolecular Sequence DataProtein ConformationProtein MultimerizationProtein SubunitsSequence AlignmentArabidopsis ProteinsCross-Linking ReagentsHeat-Shock ProteinsHSP21 protein, ArabidopsisLysineProtein Subunits

Identifiers

PMID21280121
PMCPMC3048414
OpenAlexW2170273405

What OpenQuestion holds

Textmetadata
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.