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Disease on EC 3.4.24.B18 - m-AAA protease

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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Regulation of mitochondrial plasticity by the i-AAA protease YME1L.
Ataxia
A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy.
A Novel Frameshift Mutation in the AFG3L2 Gene in a Patient with Spinocerebellar Ataxia.
A Novel Missense Mutation in AFG3L2 Associated with Late Onset and Slow Progression of Spinocerebellar Ataxia Type 28.
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
Early onset and slow progression of SCA28, a rare dominant ataxia in a large four-generation family with a novel AFG3L2 mutation.
Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia.
Genome-wide expression profiling and functional characterization of SCA28 lymphoblastoid cell lines reveal impairment in cell growth and activation of apoptotic pathways.
Loss of paraplegin drives spasticity rather than ataxia in a cohort of 241 patients with SPG7.
Mice harbouring a SCA28 patient mutation in AFG3L2 develop late-onset ataxia associated with enhanced mitochondrial proteotoxicity.
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Spastic ataxia with eye-of-the-tiger-like sign in 4 siblings due to novel compound heterozygous AFG3L2 mutation.
Spinocerebellar Ataxia Type 28-Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2.
Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases.
Cerebellar Ataxia
Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia.
Missense mutations in the AFG3L2 proteolytic domain account for ?1.5% of European autosomal dominant cerebellar ataxias.
SCA28: Novel Mutation in the AFG3L2 Proteolytic Domain Causes a Mild Cerebellar Syndrome with Selective Type-1 Muscle Fiber Atrophy.
Cerebellar Diseases
Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration.
SCA28: Novel Mutation in the AFG3L2 Proteolytic Domain Causes a Mild Cerebellar Syndrome with Selective Type-1 Muscle Fiber Atrophy.
The mitochondrial protease AFG3L2 is essential for axonal development.
Coronary Artery Disease
In Silico Investigation of Traditional Chinese Medicine for Potential Lead Compounds as SPG7 Inhibitors against Coronary Artery Disease.
Demyelinating Diseases
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
Epilepsy
A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy.
Astrocyte-specific deletion of the mitochondrial m-AAA protease reveals glial contribution to neurodegeneration.
Friedreich Ataxia
Mitochondria and degenerative disorders.
Heart Failure
'Mitotherapy' for Heart Failure.
Enhancing fatty acid utilization ameliorates mitochondrial fragmentation and cardiac dysfunction via rebalancing OPA1 processing in the failing heart.
Regulation of mitochondrial plasticity by the i-AAA protease YME1L.
Hepatolenticular Degeneration
Mitochondria and degenerative disorders.
Intellectual Disability
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
m-aaa protease deficiency
Intramuscular viral delivery of paraplegin rescues peripheral axonopathy in a model of hereditary spastic paraplegia.
Loss of Drosophila i-AAA protease, dYME1L, causes abnormal mitochondria and apoptotic degeneration.
Mitochondrial Function in Hereditary Spastic Paraplegia: Deficits in SPG7 but Not SPAST Patient-Derived Stem Cells.
Respiratory dysfunction by AFG3L2 deficiency causes decreased mitochondrial calcium uptake via organellar network fragmentation.
The m-AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria.
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia.
Microcephaly
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Mitochondrial Diseases
Spinocerebellar Ataxia Type 28-Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2.
Multiple Sclerosis
A new paraplegin mutation in a patient with primary progressive multiple sclerosis.
Multiple Sclerosis, Chronic Progressive
A new paraplegin mutation in a patient with primary progressive multiple sclerosis.
Muscle Spasticity
A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy.
AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival.
Correction: Whole-Exome Sequencing Identifies Homozygous AFG3L2 Mutations in a Spastic Ataxia-Neuropathy Syndrome Linked to Mitochondrial m-AAA Proteases.
Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia.
Mitochondria and degenerative disorders.
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Spastic ataxia with eye-of-the-tiger-like sign in 4 siblings due to novel compound heterozygous AFG3L2 mutation.
Spinocerebellar Ataxia Type 28-Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2.
Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases.
Muscular Atrophy
Down-regulation of the mitochondrial i-AAA protease Yme1L induces muscle atrophy via FoxO3a and myostatin activation.
Muscular Atrophy, Spinal
Bovine spinal muscular atrophy: AFG3L2 is not a positional candidate gene.
Myoclonus
An atypical form of AOA2 with myoclonus associated with mutations in SETX and AFG3L2.
nadh:ubiquinone reductase (h+-translocating) deficiency
Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.
Neoplasms
Lipid signalling drives proteolytic rewiring of mitochondria by YME1L.
Neurodegenerative Diseases
A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy.
A Novel Frameshift Mutation in the AFG3L2 Gene in a Patient with Spinocerebellar Ataxia.
Autocatalytic processing of m-AAA protease subunits in mitochondria.
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Emerging roles of mitochondrial proteases in neurodegeneration.
Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration.
Identification and characterization of AFG3L2, a novel paraplegin-related gene.
Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.
Mice harbouring a SCA28 patient mutation in AFG3L2 develop late-onset ataxia associated with enhanced mitochondrial proteotoxicity.
Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease.
Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.
Pathogenic variants in the AFG3L2 proteolytic domain cause SCA28 through haploinsufficiency and proteostatic stress-driven OMA1 activation.
Purkinje neuron Ca2+ influx reduction rescues ataxia in SCA28 model.
Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1.
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.
Neuroinflammatory Diseases
Astrocyte-specific deletion of the mitochondrial m-AAA protease reveals glial contribution to neurodegeneration.
Nystagmus, Pathologic
Patterns and modulations of Pendular nystagmus in a family with hereditary spastic paraplegia.
Ophthalmoplegia
Adult-onset Mendelian PEO Associated with Mitochondrial Disease.
Optic Atrophy
A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy.
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Optic Atrophy, Autosomal Dominant
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
Down-regulation of the mitochondrial i-AAA protease Yme1L induces muscle atrophy via FoxO3a and myostatin activation.
Multi-site control and regulation of mitochondrial energy production.
Mutations in the m-AAA proteases AFG3L2 and SPG7 are causing isolated dominant optic atrophy.
Optic Nerve Diseases
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
ATPase Domain AFG3L2 Mutations Alter OPA1 Processing and Cause Optic Neuropathy.
Paraparesis, Spastic
A clinical, genetic, and biochemical characterization of SPG7 mutations in a large cohort of patients with hereditary spastic paraplegia.
Hereditary spastic paraplegia caused by the novel mutation 1047insC in the SPG7 gene.
Investigation of mitochondrial function in hereditary spastic paraparesis.
Paraplegin gene analysis in hereditary spastic paraparesis (HSP) pedigrees in northeast England.
Paraplegin mutations in sporadic adult-onset upper motor neuron syndromes.
Spastin and paraplegin gene analysis in selected cases of motor neurone disease (MND).
Paraplegia
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
Hereditary spastic paraplegia caused by the novel mutation 1047insC in the SPG7 gene.
In Silico Investigation of Traditional Chinese Medicine for Potential Lead Compounds as SPG7 Inhibitors against Coronary Artery Disease.
Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential.
Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein.
Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease.
Multi-site control and regulation of mitochondrial energy production.
Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.
Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease.
Spastic paraplegia gene 7 in patients with spasticity and/or optic neuropathy.
Spastic paraplegia type 7 is associated with multiple mitochondrial DNA deletions.
Parkinsonian Disorders
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Seizures
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Spastic Paraplegia, Hereditary
A clinical, genetic and biochemical study of SPG7 mutations in hereditary spastic paraplegia.
A novel phenotype of hereditary spastic paraplegia type 7 associated with a compound heterozygous mutation in paraplegin.
Abnormal Paraplegin Expression in Swollen Neurites, ?- and ?-Synuclein Pathology in a Case of Hereditary Spastic Paraplegia SPG7 with an Ala510Val Mutation.
Alternative splicing of Spg7, a gene involved in hereditary spastic paraplegia, encodes a variant of paraplegin targeted to the endoplasmic reticulum.
ATPase and Protease Domain Movements in the Bacterial AAA+ Protease FtsH Are Driven by Thermal Fluctuations.
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7.
Functional evaluation of paraplegin mutations by a yeast complementation assay.
Genetic interaction between the m-AAA protease isoenzymes reveals novel roles in cerebellar degeneration.
Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration.
Hereditary spastic paraplegia: respiratory choke or unactivated substrate?
Impaired flickering of the permeability transition pore causes SPG7 spastic paraplegia.
Intramuscular viral delivery of paraplegin rescues peripheral axonopathy in a model of hereditary spastic paraplegia.
Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.
m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration.
Mitochondrial proteins in neuronal degeneration.
Molecular basis of inherited spastic paraplegias.
Mutation analysis of the paraplegin gene (SPG7) in patients with hereditary spastic paraplegia.
Systematic isolation and characterization of cDNAs encoding AAA proteins from human brain.
The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria.
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
The mitochondrial protease AFG3L2 is essential for axonal development.
Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia.
Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia.
Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases.
Spinocerebellar Ataxias
A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy.
A novel AFG3L2 mutation in a Somalian patient with spinocerebellar ataxia type 28.
A Novel Frameshift Mutation in the AFG3L2 Gene in a Patient with Spinocerebellar Ataxia.
A Novel Missense Mutation in AFG3L2 Associated with Late Onset and Slow Progression of Spinocerebellar Ataxia Type 28.
AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival.
Astrocyte-specific deletion of the mitochondrial m-AAA protease reveals glial contribution to neurodegeneration.
ATPase Domain AFG3L2 Mutations Alter OPA1 Processing and Cause Optic Neuropathy.
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Deletion of AFG3L2 associated with spinocerebellar ataxia type 28 in the context of multiple genomic anomalies.
Evidence for Non-Mendelian Inheritance in Spastic Paraplegia 7.
Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia.
Genotype-phenotype correlations in spastic paraplegia type 7: a study in a large Dutch cohort.
Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration.
Loss of the m-AAA protease subunit AFG3L2 causes mitochondrial transport defects and tau hyperphosphorylation.
m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration.
Mice harbouring a SCA28 patient mutation in AFG3L2 develop late-onset ataxia associated with enhanced mitochondrial proteotoxicity.
Missense mutations in the AFG3L2 proteolytic domain account for ?1.5% of European autosomal dominant cerebellar ataxias.
Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease.
Partial deletion of AFG3L2 causing spinocerebellar ataxia type 28.
Pathogenic variants in the AFG3L2 proteolytic domain cause SCA28 through haploinsufficiency and proteostatic stress-driven OMA1 activation.
Purkinje neuron Ca2+ influx reduction rescues ataxia in SCA28 model.
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Respiratory dysfunction by AFG3L2 deficiency causes decreased mitochondrial calcium uptake via organellar network fragmentation.
SCA28: Novel Mutation in the AFG3L2 Proteolytic Domain Causes a Mild Cerebellar Syndrome with Selective Type-1 Muscle Fiber Atrophy.
Spinocerebellar ataxia 28: a novel AFG3L2 mutation in a German family with young onset, slow progression and saccadic slowing.
Spinocerebellar Ataxia Type 28-Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2.
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases.
Spinocerebellar Degenerations
Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.
Yet another gene mutation: dysfunction in mitochondrial protein quality control causing hereditary ataxia.
Starvation
Lipid signalling drives proteolytic rewiring of mitochondria by YME1L.
Stroke
The alternating power stroke of a 6-cylinder AAA protease chaperone engine.