Evidence map›Paper›PMID 28234481›Full record

ArticleJournal of proteome research2017

Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.

Yana A Lyon, Georgette M Sabbah, Ryan R Julian

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2017. 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, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Unusually Rapid Isomerization of Aspartic Acid in Tau.bioRxiv : the preprint server for biology · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. A Novel Mutation inOphthalmology science · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. 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 1 institution in 1 country.

Yana A LyonDepartment of Chemistry, University of California , Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
Georgette M SabbahDepartment of Chemistry, University of California , Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
Ryan R JulianDepartment of Chemistry, University of California , Riverside, 501 Big Springs Road, Riverside, California 92521, United States.ORCID 0000-0003-1580-8355
University of California, Riverside · US

Funding

Identification of peptide epimers in crystallin proteinsR01GM107099 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI JULIAN, RYAN ROY · 2014 to 2017
$1.1M
NIGMS NIH HHS R01 GM107099
6 · The paper itself

Abstract

The eye lens crystallins represent an ideal target for studying the effects of aging on protein structure. Herein we examine separately the water-soluble (WS) and water-insoluble (WI) crystallin fractions and identify sites of isomerization and epimerization. Both collision-induced dissociation and radical-directed dissociation are needed for detection of these non-mass-shifting post-translational modifications. Isomerization levels differ significantly between the WS and the WI fractions from sheep, pig, and cow eye lenses. Residues that are most susceptible to isomerization are identified site-specifically and are found to reside in structurally disordered regions. However, isomerization in structured domains, although less common, often yields more dramatic effects on solubility. Numerous isomerization hotspots were also identified and occur in regions with aspartic acid and serine repeats. For example,

Indexed as

Protein ConformationAgingAmino Acid SequenceAnimalsCataractCattleCrystallinsHumansLens, CrystallineProtein Processing, Post-TranslationalSheepSolubilitySwineCrystallinsepimerizationisomerizationlong-lived proteinsphotodissociation

Identifiers

PMID28234481
PMCPMC5387677
OpenAlexW2590978276

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.