Evidence map›Paper›PMID 32619897›Full record

ArticleJournal of inorganic biochemistry2020

Protein dynamics of [Cu-Zn] superoxide dismutase (SOD1): How protein motions at the global and local levels impact the reactivity of SOD1.

Eamonn F Healy, Rafael Flores, Vincent M Lynch, Santiago Toledo

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PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

4 authors.

Eamonn F HealyDepartment of Chemistry, St. Edward's University, Austin, TX 78704, USA. Electronic address: healy@stedwards.edu.
Rafael FloresDepartment of Chemistry, St. Edward's University, Austin, TX 78704, USA.
Vincent M LynchDepartment of Chemistry, The University of Texas at Austin, Austin, TX 78712, USA.
Santiago ToledoDepartment of Chemistry, St. Edward's University, Austin, TX 78704, USA.

Funding

A Biomimetic Approach to Elucidating the Role in Disease of the Oxygenase Enzyme Acireductone Dioxygenase (ARD)SC2GM130438 · NIGMS · ST. EDWARD'S UNIVERSITY · PI TOLEDO CARRION, SANTIAGO ANDRES · 2020 to 2022
$331k
NIGMS NIH HHS SC2 GM130438
6 · The paper itself

Abstract

This work explores the pivotal role that protein mobility plays in facilitating the catalytic activity of Copper-Zinc superoxide dismutase (SOD1). Through both localized active site distortions and correlated domain movement, these motions enable the enzyme to adopt the conformations necessary to achieve both substrate delivery and efficient catalytic transformation. Structural and computational studies of a biomimetic model complex are used to probe the localized interactions between substrate and secondary sphere residues that play a role in guiding substrate to the active site, as well as facilitating the conformational changes necessary for substrate turnover. Normal mode analysis (NMA) of SOD1 demonstrates how collective domain motion influences key residues of the electrostatic loop (ESL), guiding substrate to the active site and facilitating the delivery of the conserved water network necessary for proton transfer.

Indexed as

AnimalsBiocatalysisCatalytic DomainCattleCoordination ComplexesCopperDensity Functional TheoryHumansLigandsModels, ChemicalModels, MolecularProtein BindingSuperoxide Dismutase-1Coordination ComplexesCopperLigandsSOD1 protein, humanSuperoxide Dismutase-1Biomimetic modelNormal mode analysisProtein motionSOD1Superoxide dusmutase

Identifiers

PMID32619897
PMCPMC7586375

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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.