Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Redox report : communications in free radical research - 1 Dec 2020

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

Abstract excerpt

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 (H2O2) in α subunit mutations in βE6 V (at both the putative and lateral contact regions) that included (1) αH20Q/βE6 V; (2) αH50Q/βE6 V; (3) αH20Q/H50Q/βE6 V;...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cysteine
Share to Heme
Share to Hemoglobin, Sickle

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrogen Peroxide

Share to Isoelectric Focusing

Share to Mass Spectrometry

Share to Protein Stability

Share to Protein Subunits

Source

Open in PubMed Open full text

Identifiers

PMID: 33059548
DOI: 10.1080/13510002.2020.1834250
PMCID: PMC7594797

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of α subunit substitutions on the oxidation of βCys93 and the stability of sickle cell hemoglobin.PMID 33059548Read ↗

Oxidative stress in β-thalassaemia and sickle cell diseaseSemantic proximity Read ↗

Isolated Hb Providence β82Asn and β82Asp fractions are more stable than native HbA(0) under oxidative stress conditions.Semantic proximity Read ↗

The βLys66Tyr Variant of Human Hemoglobin as a Component of a Blood Substitute.Semantic proximity Read ↗

Exploring Oxidative Reactions in Hemoglobin Variants Using Mass Spectrometry: Lessons for Engineering Oxidatively Stable Oxygen Therapeutics.Semantic proximity Read ↗

Novel Redox Active Tyrosine Mutations Enhance the Regeneration of Functional Oxyhemoglobin from Methemoglobin: Implications for Design of Blood Substitutes.Semantic proximity Read ↗

Structural and functional studies indicating altered redox properties of hemoglobin E: implications for production of bioactive nitric oxide.Semantic proximity Read ↗

Hemoglobin Variants as Targets for Stabilizing DrugsSemantic proximity Read ↗

Molecular mechanism of myoglobin autoxidation: insights from computer simulations.Semantic proximity Read ↗

Structure of fully liganded Hb ζ2β2s trapped in a tense conformation.Semantic proximity Read ↗

Role of alpha-hemoglobin-stabilizing protein in normal erythropoiesis and beta-thalassemia.Semantic proximity Read ↗

Base editing HbS to HbG-Makassar improves hemoglobin function supporting its use in sickle cell disease.Semantic proximity Read ↗

VZHE-039, a novel antisickling agent that prevents erythrocyte sickling under both hypoxic and anoxic conditionsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.