X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2). - Wikidata - awgldk - TriplyDB

X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).

X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).

http://www.wikidata.org/entity/Q36217252

about

SLC25 Family Member Genetic Interactions Identify a Role for HEM25 in Yeast Electron Transport Chain Stability.Identification of the Mitochondrial Heme Metabolism Complex.Whole blood gene expression and interleukin-6 levels.Role of heme in cardiovascular physiology and disease.Expression of murine 5-aminolevulinate synthase variants causes protoporphyrin IX accumulation and light-induced mammalian cell death X-linked macrocytic dyserythropoietic anemia in females with an ALAS2 mutation.Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.Murine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysis Molecular expression and characterization of erythroid-specific 5-aminolevulinate synthase gain-of-function mutations causing X-linked protoporphyria Loss-of-function ferrochelatase and gain-of-function erythroid-specific 5-aminolevulinate synthase mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of Sideroblastic anemia: functional study of two novel missense mutations in ALAS2 Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities Iron regulatory protein-1 protects against mitoferrin-1-deficient porphyria.Intron 1 GATA site enhances ALAS2 expression indispensably during erythroid differentiation.The GABA transaminase, ABAT, is essential for mitochondrial nucleoside metabolism.Structure of GTP-specific succinyl-CoA synthetase in complex with CoA Upregulated heme biosynthesis, an exploitable vulnerability in MYCN-driven leukemogenesis.The potential role of cell penetrating peptides in the intracellular delivery of proteins for therapy of erythroid related disorders.Iron metabolism in erythroid cells and patients with congenital sideroblastic anemia.Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme.Glutamine via α-ketoglutarate dehydrogenase provides succinyl-CoA for heme synthesis during erythropoiesis

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P2860

X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).

http://www.wikidata.org/entity/Q36217252

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

@yue

2012年論文

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2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

X-linked sideroblastic anemia ...... cinyl-CoA synthetase (SUCLA2).

@ast

X-linked sideroblastic anemia ...... cinyl-CoA synthetase (SUCLA2).

@en

type

label

X-linked sideroblastic anemia ...... cinyl-CoA synthetase (SUCLA2).

@ast

X-linked sideroblastic anemia ...... cinyl-CoA synthetase (SUCLA2).

@en

prefLabel

X-linked sideroblastic anemia ...... cinyl-CoA synthetase (SUCLA2).

@ast

X-linked sideroblastic anemia ...... cinyl-CoA synthetase (SUCLA2).

@en

P1433

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P356

JBC.M111.306423

P1433

Journal of Biological Chemistry

P1476

X-linked sideroblastic anemia ...... cinyl-CoA synthetase (SUCLA2).

@en

P2093

A Victor Hoffbrand

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

David F Bishop

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Marie E Fraser

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Steven Margolis

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

Vassili Tchaikovskii

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P2860

Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia

The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis

Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion

Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.

C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload

Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome

Recent advances in the understanding of inherited sideroblastic anaemia

Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24-->q25 by in situ hybridization

Targeting the active site gate to yield hyperactive variants of 5-aminolevulinate synthase.

New SUCLG1 patients expanding the phenotypic spectrum of this rare cause of mild methylmalonic aciduria.

P304

28943-28955

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scholarly article

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10.1074/JBC.M111.306423

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P433

34

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287

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2012-06-27T00:00:00Z

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22740690

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3436539

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