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

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

Item
http://www.wikidata.org/entity/Q24642289
Erythropoietic protoporphyriaBiology of Heme in Mammalian Erythroid Cells and Related DisordersErythroid heme biosynthesis and its disordersInfluence of meteorological data on sun tolerance in patients with erythropoietic protoporphyria in France.Targeting the active site gate to yield hyperactive variants of 5-aminolevulinate synthase.5-aminolevulinate synthase: catalysis of the first step of heme biosynthesisUnstable reaction intermediates and hysteresis during the catalytic cycle of 5-aminolevulinate synthase: implications from using pseudo and alternate substrates and a promiscuous enzyme variant.Erythropoietic protoporphyria in Sweden: demographic, clinical, biochemical and genetic characteristics.Liver disease and erythropoietic protoporphyria: a concise review.Maternal and fetal outcome in Swedish women with erythropoietic protoporphyria.X-linked dominant protoporphyria: a new porphyria.Identification of the Mitochondrial Heme Metabolism Complex.Clinically important features of porphyrin and heme metabolism and the porphyrias.Molecular enzymology of 5-aminolevulinate synthase, the gatekeeper of heme biosynthesis.Red cells from ferrochelatase-deficient erythropoietic protoporphyria patients are resistant to growth of malarial parasites.UK experience of liver transplantation for erythropoietic protoporphyria.Targeted deletion of the mouse Mitoferrin1 gene: from anemia to protoporphyria.Abnormal mitoferrin-1 expression in patients with erythropoietic protoporphyria.Expression of murine 5-aminolevulinate synthase variants causes protoporphyrin IX accumulation and light-induced mammalian cell deathCatalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthaseAsn-150 of Murine Erythroid 5-Aminolevulinate Synthase Modulates the Catalytic Balance between the Rates of the Reversible ReactionLiver transplantation in the management of porphyria.X-chromosomal inactivation directly influences the phenotypic manifestation of X-linked protoporphyria.Cellular and mitochondrial iron homeostasis in vertebratesHuman Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.Ambient Light Promotes Selective Subcellular Proteotoxicity after Endogenous and Exogenous Porphyrinogenic StressOne ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoansMurine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysisX-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).Porphyria Diagnostics-Part 1: A Brief Overview of the Porphyrias.Protoporphyrin IX: the Good, the Bad, and the Ugly.Pitfalls in Erythrocyte Protoporphyrin Measurement for Diagnosis and Monitoring of Protoporphyrias.Establishing a network of specialist Porphyria centres - effects on diagnostic activities and services.Afamelanotide for Erythropoietic Protoporphyria.Synthesis, delivery and regulation of eukaryotic heme and Fe-S cluster cofactors.Molecular expression and characterization of erythroid-specific 5-aminolevulinate synthase gain-of-function mutations causing X-linked protoporphyriaA precursor-inducible zebrafish model of acute protoporphyria with hepatic protein aggregation and multiorganelle stress.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 ofMammalian iron metabolism and its control by iron regulatory proteinsIdentification of FECH gene multiple variations in two Chinese patients with erythropoietic protoporphyria and a review.
P2860
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P2860

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

Item
http://www.wikidata.org/entity/Q24642289
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
C-terminal deletions in the AL ...... ithout anemia or iron overload
@ast
C-terminal deletions in the AL ...... ithout anemia or iron overload
@en
C-terminal deletions in the AL ...... ithout anemia or iron overload
@nl
type
label
C-terminal deletions in the AL ...... ithout anemia or iron overload
@ast
C-terminal deletions in the AL ...... ithout anemia or iron overload
@en
C-terminal deletions in the AL ...... ithout anemia or iron overload
@nl
prefLabel
C-terminal deletions in the AL ...... ithout anemia or iron overload
@ast
C-terminal deletions in the AL ...... ithout anemia or iron overload
@en
C-terminal deletions in the AL ...... ithout anemia or iron overload
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P932
P356
P1433
P1476
C-terminal deletions in the AL ...... ithout anemia or iron overload
@en
P2093
P2860
P304
P31
P356
10.1016/J.AJHG.2008.08.003
P407
P433
P478
P50
P577
P5875
P698
P932