Evidence map›Paper›PMID 27992995›Full record

ArticleBiochemistry2016

Calcium Binding Dramatically Stabilizes an Ancestral Crystallin Fold in Tunicate βγ-Crystallin.

Natalia Kozlyuk, Suvrajit Sengupta, Jan C Bierma, Rachel W Martin

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
  5. Manipulating polydispersity of lens β-crystallins using divalent cations demonstrates evidence of calcium regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Protein refractive index increment is determined by conformation as well as composition.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    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

4 authors at 1 institution in 1 country.

Natalia KozlyukDepartment of Chemistry, University of California , Irvine, California 92697-2025, United States.
Suvrajit SenguptaDepartment of Chemistry, University of California , Irvine, California 92697-2025, United States.ORCID http://orcid.org/0000-0002-9665-0088
Jan C BiermaDepartment of Molecular Biology and Biochemistry, University of California , Irvine, California 92697-3900, United States.
Rachel W MartinDepartment of Chemistry, University of California , Irvine, California 92697-2025, United States.ORCID http://orcid.org/0000-0001-9996-7411
University of California, Irvine · US

Funding

Solid-state NMR methods for investigating native and aggregated eye lens proteinsR01EY021514 · NEI · UNIVERSITY OF CALIFORNIA-IRVINE · PI MARTIN, RACHEL WAGNER · 2011 to 2022
$2.8M
NEI NIH HHS R01 EY021514
6 · The paper itself

Abstract

The tunicate (Ciona intestinalis) βγ-crystallin represents an intermediate case between the calcium-binding proteins ancestral to the vertebrate βγ-crystallin fold and the vertebrate structural crystallins. Unlike the structural βγ-crystallins in the vertebrate eye lens, this βγ-crystallin strongly binds Ca

Indexed as

Amino Acid SequenceAnimalsbeta-CrystallinsBinding SitesCalciumCiona intestinalisCircular DichroismEvolution, Moleculargamma-CrystallinsHumansLens, CrystallineModels, MolecularProtein ConformationSequence Homology, Amino AcidSpectrometry, Fluorescencebeta-CrystallinsCalciumgamma-Crystallins

Identifiers

PMID27992995
PMCPMC6936725
OpenAlexW2558115269

What OpenQuestion holds

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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.