Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem. - Wikidata - awgldk - TriplyDB

Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem.

Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem.

http://www.wikidata.org/entity/Q46523648

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Oxidative stress in β-thalassaemia and sickle cell disease Ineffective erythropoiesis in β -thalassemia Development of recombinant hemoglobin-based oxygen carriers Structural Characterization of Ferric Hemoglobins from Three Antarctic Fish Species of the Suborder Notothenioidei Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins A cis-Proline in -Hemoglobin Stabilizing Protein Directs the Structural Reorganization of -Hemoglobin The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly.Alpha-hemoglobin stabilizing protein (AHSP), a kinetic scheme of the action of a human mutant, AHSPV56G Morphological and flow-cytometric analysis of haemin-induced human neutrophil activation: implications for transfusion-related acute lung injury Reversible hexacoordination of alpha-hemoglobin-stabilizing protein (AHSP)/alpha-hemoglobin Versus pressure. Evidence for protection of the alpha-chains by their chaperone.2D DIGE based proteomics study of erythrocyte cytosol in sickle cell disease: altered proteostasis and oxidative stress.Description of two new alpha variants: Hb Canuts [alpha85(F6)Asp-->His (alpha1)] and Hb Ambroise Pare [alpha117(GH5)Phe-->Ile (alpha2)]; two new beta variants: Hb Beaujolais [beta84(EF8)Thr-->Asn] and Hb Monplaisir [beta147 (Tyr-Lys-Leu-Ala-Phe-Phe-α-Thalassemia associated with hb instability: a tale of two features. the case of Hb Rogliano or α1 Cod 108(G15)Thr→Asn and Hb Policoro or α2 Cod 124(H7)Ser→Pro AHSP (α-haemoglobin-stabilizing protein) stabilizes apo-α-haemoglobin in a partially folded state Blood substitutes: why haven't we been more successful?An erythroid chaperone that facilitates folding of alpha-globin subunits for hemoglobin synthesis Kinetics of α-globin binding to α-hemoglobin stabilizing protein (AHSP) indicate preferential stabilization of hemichrome folding intermediate.Insights into hemoglobin assembly through in vivo mutagenesis of α-hemoglobin stabilizing protein 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.Proximal influences in two-on-two globins: effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobin An iron responsive element-like stem-loop regulates alpha-hemoglobin-stabilizing protein mRNA.α-Hemoglobin-stabilizing protein (AHSP) perturbs the proximal heme pocket of oxy-α-hemoglobin and weakens the iron-oxygen bond.Chaperoning erythropoiesis.Unraveling the Specific Ischemic Core and Penumbra Transcriptome in the Permanent Middle Cerebral Artery Occlusion Mouse Model Brain Treated with the Neuropeptide PACAP38.Unstable and thalassemic alpha chain hemoglobin variants: a cause of Hb H disease and thalassemia intermedia.Analysis of human alpha globin gene mutations that impair binding to the alpha hemoglobin stabilizing protein Occurrence and formation of endogenous histidine hexa-coordination in cold-adapted hemoglobins.Faithful chaperones.Reactivity of the human hemoglobin "dark side".Genomic organisation and regulation of murine alpha haemoglobin stabilising protein by erythroid Kruppel-like factor.Mutation near the binding interfaces at α-hemoglobin stabilizing protein is highly pathogenic.Alpha-hemoglobin-stabilizing protein: an erythroid molecular chaperone.AHSP: a novel hemoglobin helper.Redox reactions of hemoglobin: mechanisms of toxicity and control.UBE2O is a quality control factor for orphans of multiprotein complexes.The effect of histone deacetylase inhibitors on AHSP expression.Hsp90 chaperones hemoglobin maturation in erythroid and nonerythroid cells.A twins heritability study on alpha hemoglobin stabilizing protein (AHSP) expression variability.Activation of STAT3 stimulates AHSP expression in K562 cells.

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P2860

Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem.

http://www.wikidata.org/entity/Q46523648

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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name

Structure of oxidized alpha-ha ...... protective mechanism for haem.

@en

Structure of oxidized alpha-ha ...... protective mechanism for haem.

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type

label

Structure of oxidized alpha-ha ...... protective mechanism for haem.

@en

Structure of oxidized alpha-ha ...... protective mechanism for haem.

@nl

prefLabel

Structure of oxidized alpha-ha ...... protective mechanism for haem.

@en

Structure of oxidized alpha-ha ...... protective mechanism for haem.

@nl

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Structure of oxidized alpha-ha ...... protective mechanism for haem.

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P2093

Liang Feng

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

Lichuan Gu

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

Suiping Zhou

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

Yigong Shi

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P2860

A vertebrate globin expressed in the brain

An abundant erythroid protein that stabilizes free alpha-haemoglobin

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

Structural basis of human cytoglobin for ligand binding

Loss of alpha-hemoglobin-stabilizing protein impairs erythropoiesis and exacerbates beta-thalassemia

NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.

Correlated phasing of multiple isomorphous replacement data.

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697-701

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scholarly article

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10.1038/NATURE03609

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7042

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435

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Mitchell J Weiss

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2005-06-01T00:00:00Z

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1001089455

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15931225

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