Evidence map›Paper›PMID 34332989›Full record

ReviewExperimental eye research2021

Redox chemistry of lens crystallins: A system of cysteines.

Eugene Serebryany, David C Thorn, Liliana Quintanar

Open access · greenAbstract readReview
In one paragraph

Review in Experimental eye research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

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  15. Mutations of CX46/CX50 and Cataract Development.Frontiers in molecular biosciences · 2022
    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 at 2 institutions in 2 countries.

Eugene SerebryanyDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA. Electronic address: evgeny_serebryany@fas.harvard.edu.
David C ThornDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.
Liliana QuintanarDepartment of Chemistry, Centro de Investigación y de Estudios Avanzados (Cinvestav), Mexico City, Mexico.
Harvard University · USCentro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional · MX

Funding

Structure and Interactions of Conformational Intermediates in gamma-D Crystallin Aggregation, and Their Targeting for Cataract PreventionR01EY030444 · NEI · HARVARD UNIVERSITY · PI SHAKHNOVICH, EUGENE I · 2020 to 2024
$2.1M
NEI NIH HHS R01 EY030444
6 · The paper itself

Abstract

The nuclear region of the lens is metabolically quiescent, but it is far from inert chemically. Without cellular renewal and with decades of environmental exposures, the lens proteome, lipidome, and metabolome change. The lens crystallins have evolved exquisite mechanisms for resisting, slowing, adapting to, and perhaps even harnessing the effects of these cumulative chemical modifications to minimize the amount of light-scattering aggregation in the lens over a lifetime. Redox chemistry is a major factor in these damages and mitigating adaptations, and as such, it is likely to be a key component of any successful therapeutic strategy for preserving or rescuing lens transparency, and perhaps flexibility, during aging. Protein redox chemistry is typically mediated by Cys residues. This review will therefore focus primarily on the Cys-rich γ-crystallins of the human lens, taking care to extend these findings to the β- and α-crystallins where pertinent.

Indexed as

AgingCysteineDisulfidesgamma-CrystallinsGlutathioneGlutathione DisulfideHumansLens, CrystallineOxidation-ReductionSulfhydryl CompoundsCysteineDisulfidesgamma-CrystallinsGlutathioneGlutathione DisulfideSulfhydryl CompoundsCataractCrystallinsDisulfide exchangeLens biochemistryProtein aggregation

Identifiers

PMID34332989
PMCPMC8511183
OpenAlexW3192704338

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.