Evidence map›Paper›PMID 22210597›Full record

ArticlePlanta2012

Evolution and functional diversification of the small heat shock protein/α-crystallin family in higher plants.

Hernán Gabriel Bondino, Estela Marta Valle, Arjen Ten Have

Abstract read
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In one paragraph

Article in Planta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

42 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
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  12. A genome forHorticulture research · 2022
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  13. Review
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  19. Pumpkin (Frontiers in genetics · 2021
    Article
  20. 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

3 authors at 2 institutions in 1 country.

Hernán Gabriel BondinoFacultad de Ciencias Exactas y Naturales, Instituto de Investigaciones Biológicas-IIB-CONICET-UNMdP, Universidad Nacional de Mar del Plata, CC 1245, 7600 Mar del Plata, Argentina.
Estela Marta Valle
Arjen Ten Have
Consejo Nacional de Investigaciones Científicas y Técnicas · ARNational University of Mar del Plata · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small heat shock proteins (sHSPs) are chaperones that play an important role in stress tolerance. They consist of an alpha-crystallin domain (ACD) flanked by N- and C-terminal regions. However, not all proteins that contain an ACD, hereafter referred to as ACD proteins, are sHSPs because certain ACD proteins are known to have different functions. Furthermore, since not all ACD proteins have been identified yet, current classifications are incomplete. A total of 17 complete plant proteomes were screened for the presence of ACD proteins by HMMER profiling and the identified ACD protein sequences were classified by maximum likelihood phylogeny. Differences among and within groups were analysed, and levels of functional constraint were determined. There are 29 different classes of ACD proteins, eight of which contain classical sHSPs and five likely chaperones. The other classes contain proteins with uncharacterised or poorly characterised functions. N- and C-terminal sequences are conserved within the phylogenetic classes. Phylogenetics suggests a single duplication of the CI sHSP ancestor that occurred prior to the speciation of mono- and dicotyledons. This was followed by a number of more recent duplications that resulted in the presence of many paralogues. The results suggest that N- and C-terminal sequences of sHSPs play a role in class-specific functionality and that non-sHSP ACD proteins have conserved but unexplored functions, which are mainly determined by subsequences other than that of the ACD.

Indexed as

Evolution, MolecularMultigene Familyalpha-CrystallinsAmino Acid SequenceAnimalsCluster AnalysisConserved SequenceCytosolHeat-Shock Proteins, SmallHumansPhylogenyPlantsProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRatsalpha-CrystallinsHeat-Shock Proteins, Small

Identifiers

PMID22210597
OpenAlexW2068158573

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.