Evidence map›Paper›PMID 1474606›Full record

ArticleJournal of molecular evolution1992

Phylogeny of the alpha-crystallin-related heat-shock proteins.

N Plesofsky-Vig, J Vig, R Brambl

Abstract read
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In one paragraph

Article in Journal of molecular evolution, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
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  3. Ethylene andFrontiers in plant science · 2020
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  16. Chloroplast small heat shock proteins: evidence for atypical evolution of an organelle-localized protein.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
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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

3 authors at 1 institution in 1 country.

N Plesofsky-VigDepartment of Plant Biology, University of Minnesota, St. Paul 55108.
J Vig
R Brambl
University of Minnesota · US

Funding

MOLECULAR BIOLOGY OF MITOCHONDRIA IN NEUROSPORA CRASSAR01GM019398 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BRAMBL, ROBERT M · 1985 to 1998
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NIGMS NIH HHS GM-19398
6 · The paper itself

Abstract

Phylogenetic relationships were examined among 35 alpha-crystallin-related heat-shock proteins from animals, plants, and fungi. Approximately one-third of the aligned amino acids in these proteins were conserved in 74% of the proteins, and three blocks of consensus sequence were identified. Relationships were established by maximum parsimony and distance matrix analyses of the aligned amino acid sequences. The inferred phylogeny trees show the plant proteins clearly divided into three major groups that are unrelated to taxonomy: the chloroplast-localized proteins and two groups that originate from a common ancestral plant protein. The animal proteins, in contrast, branch in accordance with taxonomy, the only clear exception being the alpha-crystallin subgrouping of vertebrates. This analysis indicates that the small heat-shock proteins of animals have diverged more widely than have the plant proteins, one group of which is especially stable.

Indexed as

PhylogenyAmino Acid SequenceAnimalsCrystallinsFungiHeat-Shock ProteinsHumansMolecular Sequence DataPlantsSequence AlignmentCrystallinsHeat-Shock Proteins

Identifiers

PMID1474606
OpenAlexW2046063607

What OpenQuestion holds

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Registered trials

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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.