Barth syndrome mutations that cause tafazzin complex lability. - Test2 - elhamkhani - TriplyDB

Barth syndrome mutations that cause tafazzin complex lability.

Barth syndrome mutations that cause tafazzin complex lability.

http://www.wikidata.org/entity/Q35003569

about

Cardiolipin signaling mechanisms: collapse of asymmetry and oxidation Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development Barth Syndrome: From Mitochondrial Dysfunctions Associated with Aberrant Production of Reactive Oxygen Species to Pluripotent Stem Cell Studies The Role of Cardiolipin in Cardiovascular Health Successful management of Barth syndrome: a systematic review highlighting the importance of a flexible and multidisciplinary approach Deacylation on the matrix side of the mitochondrial inner membrane regulates cardiolipin remodeling.Phosphatidylserine decarboxylase 1 autocatalysis and function does not require a mitochondrial-specific factor.Mechanism for Remodeling of the Acyl Chain Composition of Cardiolipin Catalyzed by Saccharomyces cerevisiae Tafazzin Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization Mitochondrial protein quality control: the mechanisms guarding mitochondrial health YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress LPS impairs oxygen utilization in epithelia by triggering degradation of the mitochondrial enzyme Alcat1 Defining functional classes of Barth syndrome mutation in humans Disorders of phospholipid metabolism: an emerging class of mitochondrial disease due to defects in nuclear genes The complexity of cardiolipin in health and disease Stress-triggered activation of the metalloprotease Oma1 involves its C-terminal region and is important for mitochondrial stress protection in yeast Yeast as a system for modeling mitochondrial disease mechanisms and discovering therapies.Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life.Seven functional classes of Barth syndrome mutation The power of yeast to model diseases of the powerhouse of the cell.The Taz1p transacylase is imported and sorted into the outer mitochondrial membrane via a membrane anchor domain.Structural and functional analyses of Barth syndrome-causing mutations and alternative splicing in the tafazzin acyltransferase domain.Lipidomics Characterization of Biosynthetic and Remodeling Pathways of Cardiolipins in Genetically and Nutritionally Manipulated Yeast Cells Overexpression of mitochondrial oxodicarboxylate carrier (ODC1) preserves oxidative phosphorylation in a yeast model of Barth syndrome.The Assembly Factor Pet117 Couples Heme a Synthase Activity to Cytochrome Oxidase Assembly.Stendomycin selectively inhibits TIM23-dependent mitochondrial protein import.Loss of function of SLC25A46 causes lethal congenital pontocerebellar hypoplasia.Multitiered and Cooperative Surveillance of Mitochondrial Phosphatidylserine Decarboxylase 1.Metalloproteases of the Inner Mitochondrial Membrane.Cardiomyopathy-associated mutation in the ADP/ATP carrier reveals translation-dependent regulation of cytochrome c oxidase activity.Tafazzin knockdown interrupts cell cycle progression in cultured neonatal ventricular fibroblasts.

P2860

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P2860

Barth syndrome mutations that cause tafazzin complex lability.

http://www.wikidata.org/entity/Q35003569

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

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2011年论文

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name

Barth syndrome mutations that cause tafazzin complex lability.

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Barth syndrome mutations that cause tafazzin complex lability.

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type

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Barth syndrome mutations that cause tafazzin complex lability.

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Barth syndrome mutations that cause tafazzin complex lability.

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Barth syndrome mutations that cause tafazzin complex lability.

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Barth syndrome mutations that cause tafazzin complex lability.

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P1433

Journal of Cell Biology

P1476

Barth syndrome mutations that cause tafazzin complex lability.

@en

P2093

Carla M Koehler

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

Kevin Whited

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

Santi Srijumnong

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

Steven M Claypool

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

Xianlin Han

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

P2860

Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients

The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant. Implications for Barth syndrome

Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism

A case of severe hypermetabolism of nonthyroid origin with a defect in the maintenance of mitochondrial respiratory control: a correlated clinical, biochemical, and morphological study

The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome

A mitochondrial protein compendium elucidates complex I disease biology

Shotgun lipidomics of cardiolipin molecular species in lipid extracts of biological samples

The proteome of Saccharomyces cerevisiae mitochondria.

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g.

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447-462

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10.1083/JCB.201008177

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3

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192

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