Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes. - Wikidata - wikimedia - TriplyDB

Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes.

Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes.

http://www.wikidata.org/entity/Q30486705

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Transformative Innovations in Reproductive, Maternal, Newborn, and Child Health over the Next 20 Years.Development of recombinant hemoglobin-based oxygen carriers Oxidized Hemoglobin Is an Endogenous Proinflammatory Agonist That Targets Vascular Endothelial Cells Haptoglobin, hemopexin, and related defense pathways-basic science, clinical perspectives, and drug development Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure.Molecular modeling of the human hemoglobin-haptoglobin complex sheds light on the protective mechanisms of haptoglobin.Dissection of the radical reactions linked to fetal hemoglobin reveals enhanced pseudoperoxidase activity.Comparative In Vivo Effects of Hemoglobin-Based Oxygen Carriers (HBOC) with Varying Prooxidant and Physiological Reactivity Sickle Cell Hemoglobin in the Ferryl State Promotes βCys-93 Oxidation and Mitochondrial Dysfunction in Epithelial Lung Cells (E10)α-Hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of α-subunits of human HbA with hydrogen peroxide Oxidative instability of hemoglobin E (β26 Glu→Lys) is increased in the presence of free α subunits and reversed by α-hemoglobin stabilizing protein (AHSP): Relevance to HbE/β-thalassemia.Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine β145 Post-translational transformation of methionine to aspartate is catalyzed by heme iron and driven by peroxide: a novel subunit-specific mechanism in hemoglobin Transcriptional Suppression of Renal Antioxidant Enzyme Systems in Guinea Pigs Exposed to Polymerized Cell-Free Hemoglobin.Antioxidant functions for the hemoglobin β93 cysteine residue in erythrocytes and in the vascular compartment in vivo.Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design.Understanding and applying tyrosine biochemical diversity.Oxidative pathways in the sickle cell and beyond.Towards hemerythrin-based blood substitutes: comparative performance to hemoglobin on human leukocytes and umbilical vein endothelial cells.A new polyethyleneglycol-derivatized hemoglobin derivative with decreased oxygen affinity and limited toxicity.Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin.Red cells, hemoglobin, heme, iron, and atherogenesis.Fetal hemoglobin is much less prone to DNA cleavage compared to the adult protein.Redox reactivity in propolis: direct detection of free radicals in basic medium and interaction with hemoglobin.Hemoglobin-albumin cross-linking with disuccinimidyl suberate (DSS) and/or glutaraldehyde for blood substitutes.Effects of quercetin on hemoglobin-dependent redox reactions: relationship to iron-overload rat liver injury.Mechanisms involved in hemoglobin-mediated oxidation of lipids in washed fish muscle and inhibitory effects of phospholipase A2.2017 Military Supplement: Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.The βLys66Tyr Variant of Human Hemoglobin as a Component of a Blood Substitute.Mechanisms of Toxicity and Modulation of Hemoglobin-Based Oxygen Carriers (HBOCs).Engineering oxidative stability in human hemoglobin based on the Hb providence (βK82D) mutation and genetic cross-linking.Characterization of Protein-Protein Interactions in Recombinant Hemoglobin Producing Escherichia coli Cells Using Molecularly Imprinted Polymers.A superoxide dismutase-human hemoglobin fusion protein showing enhanced antioxidative properties.Copolymerization of recombinant Phascolopsis gouldii hemerythrin with human serum albumin for use in blood substitutes.The Penultimate Tyrosine Residues are Critical for the Genotoxic Effect of Human Hemoglobin.Academia-Industry Collaboration in Blood Substitute Development: Issues, Case Histories and a Proposal Possibilities of Using Fetal Hemoglobin as a Platform for Producing Hemoglobin-Based Oxygen Carriers (HBOCs).Site-directed mutagenesis of cysteine residues alters oxidative stability of fetal hemoglobin

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P2860

Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes.

http://www.wikidata.org/entity/Q30486705

description

2008 nî lūn-bûn

@nan

2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Tyrosine residues as redox cof ...... ng nontoxic blood substitutes.

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Tyrosine residues as redox cof ...... ng nontoxic blood substitutes.

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Tyrosine residues as redox cof ...... ng nontoxic blood substitutes.

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Tyrosine residues as redox cof ...... ng nontoxic blood substitutes.

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Tyrosine residues as redox cof ...... ng nontoxic blood substitutes.

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Journal of Biological Chemistry

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Tyrosine residues as redox cof ...... ing nontoxic blood substitutes

@en

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Leif Bülow

http://www.w3.org/2001/XMLSchema#string

Marie Grey

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Michael T Wilson

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P2860

Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: a meta-analysis

A role for the myoglobin redox cycle in the induction of endothelial cell apoptosis.

A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure.

Redox equilibria of liganded forms of methemoglobin

Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease States.

Current status of oxygen carriers ('blood substitutes'): 2006.

First-generation blood substitutes: what have we learned? Biochemical and physiological perspectives.

Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase.

Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide.

Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin.

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30780-30787

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10.1074/JBC.M804709200

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45

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283

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Chris E. Cooper

Dimitri A Svistunenko

Brandon J Reeder

Radu Silaghi-Dumitrescu

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2008-08-26T00:00:00Z

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18728007

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2662160

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