Evidence map›Paper›PMID 19296714›Full record

ArticleBiochemistry2009

Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens.

Kelly A Barton, Cheng-Da Hsu, J Mark Petrash

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Through theGenes · 2024
    Review
  3. Article
  4. Examining Galectin Gene Regulation by Reporter Assays.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  5. Article
  6. Article
  7. How galectins have become multifunctional proteins.Histology and histopathology · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Vascular dysfunction precedes hypertension associated with a blood pressure locus on rat chromosome 12.American journal of physiology. Heart and circulatory physiology · 2014
    Article
  12. Matricellular proteins in the trabecular meshwork: review and update.Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics · 2014
    Review
  13. Article
  14. Article
  15. Article
  16. Novel roles for α-crystallins in retinal function and disease.Progress in retinal and eye research · 2012
    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

3 authors.

Kelly A BartonDepartment of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Cheng-Da Hsu
J Mark Petrash

Funding

WASHINGTON UNIVERSITY CENTER VISION RESEARCHP30EY002687 · NEI · WASHINGTON UNIVERSITY · PI Philip Andrew Ruzycki · 1985 to 2026
$18.4M
MOLECULAR BIOLOGY OF ALDOSE REDUCTASE AND CATARACTR01EY005856 · NEI · WASHINGTON UNIVERSITY · PI PETRASH, JONATHAN MARK · 1988 to 2014
$6.8M
Research Training Program in the Vision SciencesT32EY013360 · NEI · WASHINGTON UNIVERSITY · PI SHIMING CHEN, Daniel Kerschensteiner · 2000 to 2026
$5.6M
Molecular Interactions of Crystallins in the EyeR01EY013897 · NEI · WASHINGTON UNIVERSITY · PI PETRASH, JONATHAN MARK · 2002 to 2005
$1.4M
NEI NIH HHS P30 EY002687NEI NIH HHS P30EY02687NEI NIH HHS R01 EY005856NEI NIH HHS R01 EY013897NEI NIH HHS R01EY05856NEI NIH HHS R01EY13897NEI NIH HHS T32 EY013360NEI NIH HHS T32EY013360
6 · The paper itself

Abstract

As a member of the small heat shock protein superfamily, alpha-crystallin has a chaperone-like ability to recognize and bind denatured or unfolded proteins and prevent their aggregation. Recent studies suggest that alpha-crystallin may also interact with a variety of proteins under native conditions in vitro. To identify potential binding partners for alpha-crystallin in the intact ocular lens, we conducted cross-linking studies in transgenic mouse lenses designed for overexpression of His-tagged human alphaA-crystallin. Interacting proteins were copurified with the epitope-tagged crystallin complexes and were identified by tandem mass spectrometry. This approach identified GRIFIN (galectin-related interfiber protein) as a novel binding partner. Consistent with results from cross-linking, GRIFIN subunits copurified with alpha-crystallin complexes during size exclusion chromatography of nontransgenic mouse lens extracts prepared without chemical cross-linking. Equilibrium binding to GRIFIN was studied using native alpha-crystallin isolated from calf lenses as well as oligomeric complexes reconstituted from recombinant alphaA- and alphaB-crystallin subunits. Calf lens alpha-crystallin binds GRIFIN with relatively high affinity (K(d) = 6.5 +/- 0.8 microM) at a stoichiometry of 0.25 +/- 0.01 GRIFIN monomer/alpha-crystallin subunit. The binding interaction between alpha-crystallin and GRIFIN is enhanced up to 5-fold in the presence of 3 mM ATP. These binding data support the hypothesis that GRIFIN is a novel binding partner of alpha-crystallin in the lens.

Indexed as

alpha-CrystallinsAmino Acid SequenceAnimalsBase SequenceBlotting, WesternCattleChromatography, AffinityChromatography, GelDNA PrimersElectrophoresis, Polyacrylamide GelHumansLens, CrystallineMiceMice, TransgenicMolecular Sequence DataProtein Bindingalpha-CrystallinsDNA Primers

Identifiers

PMID19296714
PMCPMC3615986
OpenAlexW2035856080

What OpenQuestion holds

Textmetadata
LicenceTDM
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.