Evidence map›Paper›PMID 33849365›Full record

ReviewExpert review of proteomics2021

Proteomic characterization of the human lens and Cataractogenesis.

Lee S Cantrell, Kevin L Schey

Open access · greenAbstract readReview
In one paragraph

Review in Expert review of proteomics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Biomedical optics express · 2022
    Article
  10. 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.

Lee S CantrellDepartment of Biochemistry, Vanderbilt University, Nashville, TN, United States.ORCID 0000-0001-9845-4163
Kevin L ScheyDepartment of Biochemistry, Vanderbilt University, Nashville, TN, United States.
Vanderbilt University · US

Funding

Shop Module CoreP30EY008126 · NEI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI David J. Calkins · 1989 to 2026
$19.6M
THE ROLE OF LENS MIP IN AGING AND CATARACTOGENESISR01EY013462 · NEI · VANDERBILT UNIVERSITY · PI Kevin L Schey · 2001 to 2026
$8.2M
Chemistry-Biology Interface Training GrantT32GM065086 · NIGMS · VANDERBILT UNIVERSITY · PI BACHMANN, BRIAN O, SULIKOWSKI, GARY ALLEN · 2002 to 2022
$7.0M
Mechanisms of Protein Aging in Normal and Cataractous LensesR01EY024258 · NEI · VANDERBILT UNIVERSITY · PI SCHEY, KEVIN L · 2014 to 2022
$2.6M
Corneal Innervation and Epithelial Cell MigrationR01EY013463 · NEI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLARLUND, JES K · 2003 to 2007
$1.9M
NEI NIH HHS P30 EY008126NEI NIH HHS R01 EY013462NEI NIH HHS R01 EY013463NEI NIH HHS R01 EY024258NIGMS NIH HHS T32 GM065086
6 · The paper itself

Abstract

introductionThe goal of this review is to highlight the triumphs and frontiers in measurement of the lens proteome as it relates to onset of age-related nuclear cataract. As global life expectancy increases, so too does the frequency of age-related nuclear cataracts. Molecular therapeutics do not exist for delay or relief of cataract onset in humans. Since lens fiber cells are incapable of protein synthesis after initial maturation, age-related changes in proteome composition and post-translational modification accumulation can be measured with various techniques. Several of these modifications have been associated with cataract onset. AREAS COVERED: We discuss the impact of long-lived proteins on the lens proteome and lens homeostasis as well as proteomic techniques that may be used to measure proteomes at various levels of proteomic specificity and spatial resolution. EXPERT OPINION: There is clear evidence that several proteome modifications are correlated with cataract formation. Past studies should be enhanced with cutting-edge, spatially resolved mass spectrometry techniques to enhance the specificity and sensitivity of modification detection as it relates to cataract formation.

Indexed as

CataractLens, CrystallineHumansMass SpectrometryProteomeProteomicsProteomeagingcataractLenslong-lived proteinsmass spectrometryspatial proteomics

Identifiers

PMID33849365
PMCPMC9227965
OpenAlexW3154467204

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.