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

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

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

http://www.wikidata.org/entity/Q28510933

about

Hepcidin as a therapeutic tool to limit iron overload and improve anemia in β-thalassemic mice Suppression of Fas-FasL coexpression by erythropoietin mediates erythroblast expansion during the erythropoietic stress response in vivo A global role for EKLF in definitive and primitive erythropoiesis Oxidative stress in β-thalassaemia and sickle cell disease Ineffective erythropoiesis in β -thalassemia A cis-Proline in -Hemoglobin Stabilizing Protein Directs the Structural Reorganization of -Hemoglobin Iron-heme-Bach1 axis is involved in erythroblast adaptation to iron deficiency.The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly.Prion Protein-Hemin Interaction Upregulates Hemoglobin Synthesis: Implications for Cerebral Hemorrhage and Sporadic Creutzfeldt-Jakob Disease Differential regulation of redox proteins and chaperones in HbEβ-thalassemia erythrocyte proteome.Protein quality control during erythropoiesis and hemoglobin synthesis FOXO3-mTOR metabolic cooperation in the regulation of erythroid cell maturation and homeostasis.Role of α-globin H helix in the building of tetrameric human hemoglobin: interaction with α-hemoglobin stabilizing protein (AHSP) and heme molecule Role of alpha-hemoglobin-stabilizing protein in normal erythropoiesis and beta-thalassemia.Alterations in expression and chromatin configuration of the alpha hemoglobin-stabilizing protein gene in erythroid Kruppel-like factor-deficient mice.A synthetic model of human beta-thalassemia erythropoiesis using CD34+ cells from healthy adult donors.Phosphoproteomic analysis of apoptotic hematopoietic stem cells from hemoglobin E/β-thalassemia.AHSP (α-haemoglobin-stabilizing protein) stabilizes apo-α-haemoglobin in a partially folded state Disruption of erythroid K-Cl cotransporters alters erythrocyte volume and partially rescues erythrocyte dehydration in SAD mice.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 Assembly of recently translated full-length and C-terminal truncated human gamma-globin chains with a pool of alpha-globin chains to form Hb F in a cell-free system Integrated protein quality-control pathways regulate free α-globin in murine β-thalassemia.AHSP and beta-thalassemia: a possible genetic modifier.α-Hemoglobin-stabilizing protein is a sensitive and specific marker of erythroid precursors.Designer blood: creating hematopoietic lineages from embryonic stem cells.Late stage erythroid precursor production is impaired in mice with chronic inflammation Pathophysiology and Clinical Manifestations of the β-Thalassemias.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.Macrophages support pathological erythropoiesis in polycythemia vera and β-thalassemia Analysis of alpha hemoglobin stabilizing protein overexpression in murine β-thalassemia Decreased differentiation of erythroid cells exacerbates ineffective erythropoiesis in beta-thalassemia An RNAi therapeutic targeting Tmprss6 decreases iron overload in Hfe(-/-) mice and ameliorates anemia and iron overload in murine β-thalassemia intermedia.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.Analysis of human alpha globin gene mutations that impair binding to the alpha hemoglobin stabilizing protein

P2860

5258bca75cd3d39a0427873634b81612d6d0617f e181c3a6dc4e09a2a0add8eda60b4c4cec71dfb3

P248

Q24633423-0524C8CE-B5DB-4419-9BAC-B5DDA12BF5D2 Q24685620-C20C303A-629B-4596-A050-D65B2B3EDCE1 Q24685702-61D06F95-3BB9-43D9-B678-B51EA9802A18 Q26797178-912F5567-2130-4FD6-8B8A-0E29BEC8781B Q26830255-B32201B7-97C1-495B-9FD0-5C7845D5D0F7 Q27657179-258F3FD8-128E-46BD-835E-4D154BB0942E Q33573747-E7447E97-897B-4B90-B8AA-C6CBFC2FB7A1 Q33649910-5F431DB4-5A70-4ACD-BC29-4C4BB659482B Q33712255-959D641E-926B-4A98-AF3D-80D8560ADA88 Q33764494-46546050-D3EA-4A09-80A1-6B567D726A94 Q34060218-5D38155B-2837-42B2-8668-4BDA5BD8F5C3 Q34362420-2AAC3CDC-FAB1-4723-A599-A3953EBE7BA2 Q34450297-1E72AEF6-72A5-4C4F-8B3F-54F62F9D6F08 Q34474592-4C584B2C-BB54-46EE-B914-EDBD9BFAB172 Q34717967-1AD49025-67A9-4B9E-96C9-C1C3116E6D28 Q34827231-60D52BC4-DBCB-4086-BEF6-82DE6D10461F Q35124711-DDF74CC3-EE66-45D5-9363-0924673F83C1 Q35258752-C1A5BA22-49BB-4F00-A137-82AE99B046F1 Q35785736-7542850C-C663-45C6-B1C2-4E67D7F83F8F Q35865381-E26F0F81-2380-4B3B-A2BF-87EEEFF432F7 Q35879569-10DAB8CA-3AA0-46EE-98A4-CC560D8B4319 Q35879658-846A546C-C0D8-4A89-BF83-C68A443A5C45 Q35995025-81F2D783-A9A9-4C3F-9273-08833C34A46B Q36015022-5267E76A-6814-4604-937D-83CF44163060 Q36194560-250D96C0-CC40-41D1-AE5E-8EDF86F05F57 Q36242687-3A84F436-57D0-43B9-B96E-18F44B8122A4 Q36299248-48667E1D-7639-4BF7-91FC-2E31BED530EA Q36366570-E7A34F11-0E1B-4F49-A699-619A10CCCB61 Q36526536-6519639D-707E-4E04-8C33-5A91B212B1E6 Q36596310-654DFFAE-779A-4ED7-8756-4A2399A28C32 Q36719908-4164FC53-7BE5-429B-8515-56AF4450E9B3 Q36745518-B5FE64C9-7068-4ACD-B00F-A28452291162 Q36784224-3755709D-E7AB-4175-A603-0990012154CC Q36787514-935F2447-3C40-44A5-BFEA-39754D76CCF3 Q36849024-0BEFB710-91A4-4E6C-94F8-6993FA997A44 Q36914433-A0A8E1CA-4601-4C32-BC0E-A7EF33E9F3AA Q37000641-9601C3CD-E0F6-4AD0-B34A-80F74C6B4D90 Q37119895-DA14E0DB-6B34-4D7C-A884-6D6C28FAD276 Q37200799-A563B194-9BED-4848-8874-77FC081CB6A4 Q37237484-ED869E67-6FDA-4380-8155-84349D3F25C4

P2860

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

http://www.wikidata.org/entity/Q28510933

description

2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 2004

@ast

im November 2004 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2004/11/01)

@sk

vědecký článek publikovaný v roce 2004

@cs

wetenschappelijk artikel (gepubliceerd op 2004/11/01)

@nl

наукова стаття, опублікована в листопаді 2004

@uk

مقالة علمية (نشرت في نوفمبر 2004)

@ar

name

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@ast

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@en

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@nl

type

label

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@ast

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@en

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@nl

prefLabel

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@ast

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@en

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@nl

P1433

Q28510933-EBE264DA-6EA1-4E5A-BB84-B978BA418465

P1476

Q28510933-E4DDFC5C-7396-46E2-98D9-8585FA6A9C39

P2093

Q28510933-3DEA7244-FF4F-47F3-AD55-E8FA92DA652F

Q28510933-4EE96681-2947-4724-88D5-3A1067E35C76

Q28510933-68B0AB49-B095-4CAB-91C3-3A9DECA646D5

Q28510933-81720C00-4490-4F85-92F0-9F0472D9ADBA

Q28510933-938982F5-5282-4FBD-B6EF-C6EA103F59DD

Q28510933-A98E9D97-DBA0-4D79-AFF0-AB3F8D7B9B8D

Q28510933-B3FE4BCE-4763-4B28-B004-DD7447E8FEF9

Q28510933-B781402A-37EC-488D-AF6F-7FA33A745C60

Q28510933-C1C9377A-7FDF-45C2-8250-F70937501A3A

Q28510933-C57FD2F6-F070-4BDE-9C82-7EC6BD531786

P2860

Q28510933-0BD49C10-AEDF-4028-B0F9-6EFA3BDA8C86

Q28510933-13C070E4-3135-479E-955A-E15924D0105A

Q28510933-1D5DD35F-A47B-4451-A1A8-1B7A176AC0A2

Q28510933-1DB1C726-C6AE-4477-8F28-9960069F0F1A

Q28510933-29B5A78F-48FA-4E4E-8F52-2982F05F49E6

Q28510933-2F12BD43-626B-4035-8470-FB690FC1A6BF

Q28510933-3A176C3D-8CCF-45FF-8ACF-7D6660AD3CA6

Q28510933-44278A28-FAC6-4286-8F2C-85C0BA9058FC

Q28510933-45AFEA01-31C2-4F5E-A134-6379BE9B6DBA

Q28510933-47447CC0-597A-4409-B7B5-A28F75E8CCE7

P304

Q28510933-2AD89479-5631-448A-8327-A84A792900A9

P31

Q28510933-6CF1000C-0A97-4977-8569-1AF6D1D28D57

P356

Q28510933-906317D5-B44B-414C-987E-82DF6202B1EE

P407

Q28510933-1EA561F4-8787-4BF1-BBBD-57C9310AD06A

P433

Q28510933-432496AF-76DA-4692-97F8-4DD86BA240DC

P478

Q28510933-137CC6DF-58F3-458E-9E20-6428CAE24A4E

P577

Q28510933-28BC84B7-0A43-4904-AE7E-43C73A37243A

P698

Q28510933-748FF4D4-C5A3-414F-87EA-2E351187E7C8

P921

Q28510933-C33AD70C-B2BC-4924-A3AB-67558932136A

P932

Q28510933-C4303BE3-75FE-4B32-8CA1-391BC3E32110

P356

P1433

Journal of Clinical Investigation

P1476

Loss of alpha-hemoglobin-stabi ...... d exacerbates beta-thalassemia

@en

P2093

Andrew J. Gow

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

Anne M. Katein

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

Anthony J. Kihm

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

Calvert S. Louden

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

David A. Gell

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

Joel P. Mackay

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

Kazuhiko Adachi

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

Linda Foster-Brown

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

Mitchell J. Weiss

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

Suiping Zhou

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

P2860

An abundant erythroid protein that stabilizes free alpha-haemoglobin

Heme positively regulates the expression of beta-globin at the locus control region via the transcriptional factor Bach1 in erythroid cells

Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency

A mouse model for beta 0-thalassemia

Posttranslational quality control: folding, refolding, and degrading proteins.

Effect of excess alpha-hemoglobin chains on cellular and membrane oxidation in model beta-thalassemic erythrocytes

Ineffective erythropoiesis in Stat5a(-/-)5b(-/-) mice due to decreased survival of early erythroblasts.

Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein.

Phenotype-genotype relationships in monogenic disease: lessons from the thalassaemias.

Hemoglobin synthesis in beta-thalassemia: the properties of the free alpha-chains.

P304

1457–1466

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

P31

scholarly article

P356

10.1172/JCI21982

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

P407

P433

10

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

P478

114

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

P577

2004-11-01T00:00:00Z

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

P698

15545996

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

P921

Eukaryotic translation initiation factor 2-alpha kinase 2

P932

525742

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