Evidence map›Paper›PMID 35163513›Full record

ArticleInternational journal of molecular sciences2022

Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations.

Shu-Shun Hsueh, S-S Steven Wang, Shu-Han Chen, Chia-Lin Wang, W Josephine Wu, Ta-Hsien Lin

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Shu-Shun HsuehDepartment of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
S-S Steven WangDepartment of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
Shu-Han ChenDepartment of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
Chia-Lin WangLaboratory of Nuclear Magnetic Resonance, Medical Research Department, Taipei Veterans General Hospital, Taipei 11217, Taiwan.
W Josephine WuDepartment of Optometry, Yuanpei University of Medical Technology, Hsinchu City 30015, Taiwan.
Ta-Hsien LinLaboratory of Nuclear Magnetic Resonance, Medical Research Department, Taipei Veterans General Hospital, Taipei 11217, Taiwan.

Funding

Ministry of Science and Technology MOST
6 · The paper itself

Abstract

Human γD-crystallin (HGDC) is an abundant lens protein residing in the nucleus of the human lens. Aggregation of this and other structural proteins within the lens leads to the development of cataract. Much has been explored on the stability and aggregation of HGDC and where detailed investigation at the atomic resolution was needed, the X-ray structure was used as an initial starting conformer for molecular modeling. In this study, we implemented NMR-solution HGDC structures as starting conformers for molecular dynamics simulations to provide the missing pieces of the puzzle on the very early stages of HGDC unfolding leading up to the domain swap theories proposed by past studies. The high-resolution details of the conformational dynamics also revealed additional insights to possible early intervention for cataractogenesis.

Indexed as

gamma-CrystallinsHumansMagnetic Resonance SpectroscopyModels, MolecularMolecular Dynamics SimulationProtein ConformationProtein UnfoldingCRYGD protein, humangamma-Crystallinsaggregationcataracthuman γD-crystallinmolecular dynamics simulationsNMR spectroscopystabilityunfolding

Identifiers

PMID35163513
PMCPMC8836049

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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.