Evidence map›Paper›PMID 15722445›Full record

ArticleProtein science : a publication of the Protein Society2005

Insights into the domains required for dimerization and assembly of human alphaB crystallin.

Joy G Ghosh, John I Clark

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  3. Review
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  9. Effect of Structural Changes Induced by Deletion ofInternational journal of molecular sciences · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. A novel dominant D109ABBA clinical · 2017
    Article
  14. Article
  15. Functional sequences in human alphaB crystallin.Biochimica et biophysica acta · 2016
    Review
  16. Review
  17. Review
  18. Article
  19. Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    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

2 authors at 1 institution in 1 country.

Joy G GhoshDepartment of Biological Structure and Design, HSB G514, Box 357420, University of Washington, Seattle, WA 98195-7420, USA.
John I Clark
University of Washington · US

Funding

DEVELOPMENT AND MAINTENANCE OF TRANSPARENCY IN LENSESR01EY004542 · NEI · UNIVERSITY OF WASHINGTON · PI CLARK, JOHN IRWIN · 1985 to 2013
$7.1M
NEI NIH HHS EY04542NEI NIH HHS R01 EY004542
6 · The paper itself

Abstract

Protein pin array technology was used to identify subunit-subunit interaction sites in the small heat shock protein (sHSP) alphaB crystallin. Subunit-subunit interaction sites were defined as consensus sequences that interacted with both human alphaA crystallin and alphaB crystallin. The human alphaB crystallin protein pin array consisted of contiguous and overlapping peptides, eight amino acids in length, immobilized on pins that were in a 96-well ELISA plate format. The interaction of alphaB crystallin peptides with physiological partner proteins, alphaA crystallin and alphaB crystallin, was detected using antibodies and recorded using spectrophotometric absorbance. Five peptide sequences including 37LFPTSTSLSPFYLRPPSF54 in the N terminus, 75FSVNLDVK82)(beta3), 131LTITSSLS138 (beta8) and 141GVLTVNGP148 (beta9) that form beta strands in the conserved alpha crystallin core domain, and 155PERTIPITREEK166 in the C-terminal extension were identified as subunit-subunit interaction sites in human alphaB crystallin using the novel protein pin array assay. The subunit-subunit interaction sites were mapped to a three-dimensional (3D) homology model of wild-type human alphaB crystallin that was based on the crystal structure of wheat sHSP16.9 and Methanococcus jannaschi sHSP16.5 (Mj sHSP16.5). The subunit-subunit interaction sites identified and mapped onto the homology model were solvent-exposed and had variable secondary structures ranging from beta strands to random coils and short alpha helices. The subunit-subunit interaction sites formed a pattern of hydrophobic patches on the 3D surface of human alphaB crystallin.

Indexed as

alpha-Crystallin B ChainAmino Acid SequenceBradyrhizobiumDimerizationEnzyme-Linked Immunosorbent AssayHumansMolecular Sequence DataProtein Array AnalysisProtein Structure, TertiarySequence Alignmentalpha-Crystallin B Chain

Identifiers

PMID15722445
PMCPMC2279284
OpenAlexW2086026114

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.