Evidence map›Paper›PMID 33059548›Full record

ArticleRedox report : communications in free radical research2020

Effects of α subunit substitutions on the oxidation of βCys93 and the stability of sickle cell hemoglobin.

Wayne Hicks, Fantao Meng, Tigist Kassa, Abdu I Alayash

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox report : communications in free radical research, 2020. 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
–field-weighted citation impact, top 86% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

4 authors at 1 institution in 1 country.

Wayne HicksLaboratory of Biochemistry and Vascular Biology, Center for Biologics Evaluation and Research, Food and Drug Administration (FDA), Silver Spring, Maryland, USA.
Fantao MengHemoglobin Oxygen Therapeutics, Souderton, Pennsylvania, USA.
Tigist KassaLaboratory of Biochemistry and Vascular Biology, Center for Biologics Evaluation and Research, Food and Drug Administration (FDA), Silver Spring, Maryland, USA.
Abdu I AlayashLaboratory of Biochemistry and Vascular Biology, Center for Biologics Evaluation and Research, Food and Drug Administration (FDA), Silver Spring, Maryland, USA.
Center for Biologics Evaluation and Research · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The β subunit substitutions, F41Y and K82D, in sickle cell hemoglobin (Hb) (βE6 V) provides significant resistance to oxidative stress by shielding βCys93 from the oxidizing ferryl heme. We evaluated the oxidative resistance of βCys93 to hydrogen peroxide (H

Indexed as

Amino Acid SubstitutionChromatography, High Pressure LiquidChromatography, Reverse-PhaseCysteineHemeHemoglobin, SickleHumansHydrogen PeroxideIsoelectric FocusingMass SpectrometryMutationOxidation-ReductionOxidative StressProtein StabilityProtein SubunitsCysteineHemeHemoglobin, SickleHydrogen PeroxideProtein SubunitsoxidationSickle cell hemoglobin mutantsβCys93

Identifiers

PMID33059548
PMCPMC7594797
OpenAlexW3093274414

What OpenQuestion holds

Textmetadata
LicenceCC0
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.