Evidence map›Paper›PMID 38600176›Full record

ArticleCommunications chemistry2024

An ultraviolet-driven rescue pathway for oxidative stress to eye lens protein human gamma-D crystallin.

Jake A Hill, Yvonne Nyathi, Sam Horrell, David von Stetten, Danny Axford, Robin L Owen, Godfrey S Beddard, Arwen R Pearson, Helen M Ginn, Briony A Yorke

Abstract read
In one paragraph

Article in Communications chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

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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

10 authors.

Jake A HillSchool of Chemistry and Biosciences, University of Bradford, Richmond Road, Bradford, BD7 1DP, United Kingdom.ORCID http://orcid.org/0000-0002-9984-3387
Yvonne NyathiFaculty of Biological Sciences, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, United Kingdom.
Sam HorrellDiamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, OX11 0DE, United Kingdom.ORCID http://orcid.org/0000-0001-6355-8640
David von StettenEuropean Molecular Biology Laboratory, Notkestraße 85, 22607, Hamburg, Germany.ORCID http://orcid.org/0000-0001-7906-9788
Danny AxfordDiamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, OX11 0DE, United Kingdom.ORCID http://orcid.org/0000-0001-7694-8525
Robin L OwenDiamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, OX11 0DE, United Kingdom.ORCID http://orcid.org/0000-0002-2104-7057
Godfrey S BeddardSchool of Chemistry, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, United Kingdom.
Arwen R PearsonHARBOR, Institute for Nanostructure and Solid State Physics, Hamburg, 22761, Germany.ORCID http://orcid.org/0000-0001-8499-7490
Helen M GinnHARBOR, Institute for Nanostructure and Solid State Physics, Hamburg, 22761, Germany. crystallin@hginn.co.uk.ORCID http://orcid.org/0000-0002-7894-4939
Briony A YorkeSchool of Chemistry, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, United Kingdom. b.a.yorke@leeds.ac.uk.ORCID http://orcid.org/0000-0002-1868-8435

Funding

Academy of Medical Sciences SBF006044
6 · The paper itself

Abstract

Human gamma-D crystallin (HGD) is a major constituent of the eye lens. Aggregation of HGD contributes to cataract formation, the leading cause of blindness worldwide. It is unique in its longevity, maintaining its folded and soluble state for 50-60 years. One outstanding question is the structural basis of this longevity despite oxidative aging and environmental stressors including ultraviolet radiation (UV). Here we present crystallographic structures evidencing a UV-induced crystallin redox switch mechanism. The room-temperature serial synchrotron crystallographic (SSX) structure of freshly prepared crystallin mutant (R36S) shows no post-translational modifications. After aging for nine months in the absence of light, a thiol-adduct (dithiothreitol) modifying surface cysteines is observed by low-dose SSX. This is shown to be UV-labile in an acutely light-exposed structure. This suggests a mechanism by which a major source of crystallin damage, UV, may also act as a rescuing factor in a finely balanced redox system.

Identifiers

PMID38600176
PMCPMC11006947

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LicenceCC BY
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Registered trials

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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.