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BCS1L encodes a homolog of the S. Zusätzlich bieten wir Ihnen BCS1-Like (S. Cerevisiae) Antikörper (26) und BCS1-Like (S. Cerevisiae) Kits (6) und viele weitere Produktgruppen zu diesem Protein an.
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The BCSIL gene mutation is responsible for GRACILE syndrome, Bjornstad syndrome and complex III deficiency. Bjomstad syndrome is characterized by sensorineural hearing loss and abnormal flat twisted hair shafts. The case is GRACILE syndrome with Bjomstad phenotype in neonatal period due to BCSL1 gene mutation.
We report the first Italian patients with Bjornstad syndrome, two siblings with pili torti and sensorineural hearing loss, in whom we detected two novel compound heterozygous mutations in BCS1L
* Description of a novel homozygous mutation in BCS1L with transient neonatal acidosis and persistent de Toni-Debre-Fanconi-type tubulopathy. * The long survival of patients with phenotypic presentation of severe complex III deficiency is uncommon.
Extensive statistical and cluster analyses revealed a protein profile characteristic for the BCS1L mutant fibroblasts that included alterations in energy metabolism, cell signaling and gene expression regulation, cytoskeleton formation and maintenance.
Exome sequencing revealed novel BCS1L mutations in two siblings with Bjornstad syndrome characterized by hearing loss and hypotrichosis.
A novel behavioral and psychiatric phenotype associated with a p.Gly129Arg BCS1L mutation.
This region encompasses the BCS1L gene.
These results provide new insights into the role of pathogenic BCS1L mutations in mitochondrial function and dynamics.
GRACILE syndrome, a lethal metabolic disorder with iron overload, is caused by a point mutation in BCS1L
a function of BCS1L is to promote the maturation of complex III and the incorporation of the Rieske iron-sulfur protein into the nascent complex. Defective BCS1L leads to the formation of a catalytically inactive, structurally unstable complex III.
assessed whether 232A-->G or other BCS1L mutations were present in infants (n = 21) of Finnish origin with severe, lethal disease compatible with mitochondrial disorder
BCS1L stimulates the assembly of the LETM1 complex. BCS1L knockdown caused disassembly of the respiratory chains as well as LETM1 downregulation and induced distinct changes in mitochondrial morphology.
The severity of the complex III enzyme defect correlated with decreased amounts of BCS1L and respiratory chain complex III. This supports a pathogenic role for the novel BCS1L mutation in a patient with a singular clinical phenotype.
The g.1181A>G mutation generated an alternative splicing site in the BCS1L transcript, causing a 19-nucleotides deletion in its 5'UTR region and Complex III deficiency.
mitochondrial complex III deficiency caused by mutations in the BCS1L gene
COX7A2L/SCAFI and Pre-Complex III Modify Respiratory Chain Supercomplex Formation in Different Mouse Strains with a Bcs1l Mutation.
Studies in the yeast BCS1 ortholog indicate that the Bcs1 protein is anchored in the mitochondrial inner membrane, despite the absence of an N-terminal targeting sequence. Targeting occurs via charged amino acids near the transmembrane domain that act as an internal targeting signal.
Metabolite profiles reveal energy failure and impaired beta-oxidation in liver of mice with complex III deficiency due to a BCS1L mutation.
The GRACILE mutation introduced into Bcs1l causes postnatal complex III deficiency and is a viable mouse model for mitochondrial hepatopathy.
The predominant expression of BCS1L in the floor plate of the neural tube region, together with its presence in peripheral ganglia from E13 onwards, indicates a role for BCS1L in the development of neural structures.
This gene encodes a homolog of the S. cerevisiae bcs1 protein which is involved in the assembly of complex III of the mitochondrial respiratory chain. The encoded protein does not contain a mitochondrial targeting sequence but experimental studies confirm that it is imported into mitochondria. Mutations in this gene are associated with mitochondrial complex III deficiency and the GRACILE syndrome. Five alternatively spliced transcripts encoding the same protein have been described.
, mitochondrial chaperone BCS1
, mitochondrial complex III assembly
, mitochondrial chaperone bcs1
, BC1 (ubiquinol-cytochrome c reductase) synthesis-like