Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation
about
Protein misfolding is the molecular mechanism underlying MCADD identified in newborn screeningCrystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substratePurification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patientsMolecular characterization of variant alpha-subunit of electron transfer flavoprotein in three patients with glutaric acidemia type II--and identification of glycine substitution for valine-157 in the sequence of the precursor, producing an unstableA general introduction to the biochemistry of mitochondrial fatty acid β-oxidationCombined enzyme defect of mitochondrial fatty acid oxidationStructural organization of the human short-chain acyl-CoA dehydrogenase geneCharacterization of new ACADSB gene sequence mutations and clinical implications in patients with 2-methylbutyrylglycinuria identified by newborn screeningTargeted disruption of mouse long-chain acyl-CoA dehydrogenase gene reveals crucial roles for fatty acid oxidationFunctional studies of 18 heterologously expressed medium-chain acyl-CoA dehydrogenase (MCAD) variants.Rhabdomyolysis and acute encephalopathy in late onset medium chain acyl-CoA dehydrogenase deficiencyMetabolic cardiomyopathies.The domain-specific and temperature-dependent protein misfolding phenotype of variant medium-chain acyl-CoA dehydrogenaseThree RFLPs defining a haplotype associated with the common mutation in human medium-chain acyl-CoA dehydrogenase (MCAD) deficiency occur in Alu repeats.Estimation of the incidence of a rare genetic disease through a two-tier mutation surveyA rare disease-associated mutation in the medium-chain acyl-CoA dehydrogenase (MCAD) gene changes a conserved arginine, previously shown to be functionally essential in short-chain acyl-CoA dehydrogenase (SCAD).Identification of a new mutation in medium-chain acyl-CoA dehydrogenase (MCAD) deficiency.Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency.Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase geneHomozygous carnitine palmitoyltransferase 1b (muscle isoform) deficiency is lethal in the mouse221 newborn-screened neonates with medium-chain acyl-coenzyme A dehydrogenase deficiency: Findings from the Inborn Errors of Metabolism Collaborative.Mammalian mitochondrial beta-oxidation.Expanded newborn screening: Lessons learned from MCAD deficiency.A survey of the newborn populations in Belgium, Germany, Poland, Czech Republic, Hungary, Bulgaria, Spain, Turkey, and Japan for the G985 variant allele with haplotype analysis at the medium chain Acyl-CoA dehydrogenase gene locus: clinical and evolHigh risk of medium chain acyl-coenzyme A dehydrogenase deficiency among gypsies.Medium-chain acyl-CoA deficiency: outlines from newborn screening, in silico predictions, and molecular studies.TNF-alpha and IL-10 gene polymorphisms versus cardioimmunological responses in sudden infant death.Mitochondrial Fatty Acid Oxidation Disorders Associated with Short-Chain Enoyl-CoA Hydratase (ECHS1) Deficiency.
P2860
Q24312099-947B73EE-AD2B-48A6-9004-D90C8717EABDQ24561814-2B4D55A3-9F7D-450D-AAA5-AD467408BBF8Q24628908-3681CDB8-128C-4735-893E-61EC276CD10BQ24678683-56456127-557F-4D7E-81FC-0DC545FAAA41Q26699142-18E6251F-6C11-4994-99C6-ED93888AACC0Q28190578-91341632-7BB6-4FEF-94E2-FFCAC73F8BDAQ28255483-ED132332-841B-4110-9DFE-C275AE939A5BQ28285245-0C3AD985-5234-4141-BDEF-B2E59831A75DQ28588271-2C2BAC8D-4AD3-4DA4-A238-9FCBEB1F8E2AQ30363996-6A8C4374-89EB-4B10-A70E-401AD0150397Q33733702-0277B581-021C-462E-A7C4-487F50BB7CF3Q34216280-683DF575-713D-4058-B689-8B4CF520A00BQ35144068-BECF2444-2B1E-43BD-B0DD-94E7935EA39AQ35194683-4B358DD9-FE0A-44C1-ABA8-C9BD3303B285Q35194753-428E3E38-93B3-4BEA-B31B-0911339B43FAQ35195005-43332761-8591-4A39-9112-A369F7B2CBC9Q35195264-C613B3C1-C045-42F6-BC00-F1792B271222Q35204534-A9D72201-ECA9-4040-9E21-23F11C8B3230Q35889170-A9C500B8-8307-4FAC-949F-E0261C2FC782Q36501934-D81A859D-44D7-47D3-9872-26E3E035FB51Q39539724-81F39478-B399-45E2-B09D-E96D374DD669Q41280085-C25E7339-7CAD-4204-B975-22EEDAEDEFEAQ43079401-F6178316-AA9E-4F6D-A53C-612AB4D5B3C1Q43930177-AD7860CF-619D-4F60-A836-941B327031B7Q44577432-D8F29879-A098-40FD-92B5-8381E549DE4FQ51330620-2D0D7A87-4678-43DB-B5D0-CF3A4DEF7B18Q53465857-21DC6DD5-C948-4DB5-A6C3-AA7D8551938CQ55515392-0F784018-18A1-4FF9-9431-2666EBE03E71
P2860
Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation
description
1990 nî lūn-bûn
@nan
1990 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Molecular basis of medium chai ...... the single prevalent mutation
@ast
Molecular basis of medium chai ...... the single prevalent mutation
@en
Molecular basis of medium chai ...... the single prevalent mutation
@nl
type
label
Molecular basis of medium chai ...... the single prevalent mutation
@ast
Molecular basis of medium chai ...... the single prevalent mutation
@en
Molecular basis of medium chai ...... the single prevalent mutation
@nl
prefLabel
Molecular basis of medium chai ...... the single prevalent mutation
@ast
Molecular basis of medium chai ...... the single prevalent mutation
@en
Molecular basis of medium chai ...... the single prevalent mutation
@nl
P2093
P2860
P356
P1476
Molecular basis of medium chai ...... the single prevalent mutation
@en
P2093
P2860
P304
P356
10.1172/JCI114761
P407
P577
1990-09-01T00:00:00Z