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

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

Antioxidants & redox signaling - 10 May 2017

Strader Michael Brad, Alayash Abdu I

Abstract excerpt

SIGNIFICANCE: Worldwide demand has driven the development of hemoglobin (Hb)-based oxygen carriers (HBOCs) as potential acellular oxygen therapeutics. HBOCs have the potential to provide an oxygen bridge to patients and minimize current problems associated with supply and storage of donated blood. However, to date, safety and efficacy issues have hampered the approval of viable HBOCs in the United States. These...

Read the complete abstract on PubMed

Topics

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

Share to Genetic Variation
Share to Hemoglobins
Share to Mass Spectrometry

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

Share to Oxidation-Reduction

Share to Oxygen

Source

Open in PubMed Open full text

Identifiers

PMID: 27626360
DOI: 10.1089/ars.2016.6805
PMCID: PMC5421604

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

Exploring Oxidative Reactions in Hemoglobin Variants Using Mass Spectrometry: Lessons for Engineering Oxidatively Stable Oxygen Therapeutics.PMID 27626360Read ↗

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

Genetic architecture of the red blood cell proteome in genetically diverse mice reveals central role of hemoglobin beta cysteine redox status in maintaining circulating glutathione poolsSemantic proximity Read ↗

Hemoglobin Variants as Targets for Stabilizing DrugsSemantic proximity Read ↗

Haptoglobin: From hemoglobin scavenging to human health.Semantic proximity Read ↗

Structural characterization of hemoglobin variants using capillary electrophoresis and fast atom bombardment mass spectrometry.Semantic proximity Read ↗

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

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

Ferroptosis regulates hemolysis in stored murine and human red blood cellsSemantic proximity Read ↗

Hemoglobin C is prone to oxidative denaturation, resulting in red blood cell membrane damage in HbSC diseaseSemantic proximity Read ↗

A wealth of genotype-specific proteoforms fine-tunes hemoglobin scavenging by haptoglobin.Semantic proximity Read ↗

Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design.Semantic proximity Read ↗

Identification of hemoglobin variants by top-down mass spectrometry using selected diagnostic product ions.Semantic proximity Read ↗

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