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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.
Ataxia
A Novel Frameshift Mutation in the AFG3L2 Gene in a Patient with Spinocerebellar Ataxia.
Ataxia
A Novel Missense Mutation in AFG3L2 Associated with Late Onset and Slow Progression of Spinocerebellar Ataxia Type 28.
Ataxia
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
Ataxia
Early onset and slow progression of SCA28, a rare dominant ataxia in a large four-generation family with a novel AFG3L2 mutation.
Ataxia
Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia.
Ataxia
Genome-wide expression profiling and functional characterization of SCA28 lymphoblastoid cell lines reveal impairment in cell growth and activation of apoptotic pathways.
Ataxia
Loss of paraplegin drives spasticity rather than ataxia in a cohort of 241 patients with SPG7.
Ataxia
Mice harbouring a SCA28 patient mutation in AFG3L2 develop late-onset ataxia associated with enhanced mitochondrial proteotoxicity.
Ataxia
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Ataxia
Spastic ataxia with eye-of-the-tiger-like sign in 4 siblings due to novel compound heterozygous AFG3L2 mutation.
Ataxia
Spinocerebellar Ataxia Type 28-Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2.
Ataxia
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.
Cerebellar Ataxia
Missense mutations in the AFG3L2 proteolytic domain account for ?1.5% of European autosomal dominant cerebellar ataxias.
Cerebellar Ataxia
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.
Cerebellar Diseases
SCA28: Novel Mutation in the AFG3L2 Proteolytic Domain Causes a Mild Cerebellar Syndrome with Selective Type-1 Muscle Fiber Atrophy.
Cerebellar Diseases
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.
Epilepsy
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.
Heart Failure
Enhancing fatty acid utilization ameliorates mitochondrial fragmentation and cardiac dysfunction via rebalancing OPA1 processing in the failing heart.
Heart Failure
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.
m-aaa protease deficiency
Loss of Drosophila i-AAA protease, dYME1L, causes abnormal mitochondria and apoptotic degeneration.
m-aaa protease deficiency
Mitochondrial Function in Hereditary Spastic Paraplegia: Deficits in SPG7 but Not SPAST Patient-Derived Stem Cells.
m-aaa protease deficiency
Respiratory dysfunction by AFG3L2 deficiency causes decreased mitochondrial calcium uptake via organellar network fragmentation.
m-aaa protease deficiency
The m-AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria.
m-aaa protease deficiency
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
m-aaa protease deficiency
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.
Muscle Spasticity
AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival.
Muscle Spasticity
Correction: Whole-Exome Sequencing Identifies Homozygous AFG3L2 Mutations in a Spastic Ataxia-Neuropathy Syndrome Linked to Mitochondrial m-AAA Proteases.
Muscle Spasticity
Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia.
Muscle Spasticity
Mitochondria and degenerative disorders.
Muscle Spasticity
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Muscle Spasticity
Spastic ataxia with eye-of-the-tiger-like sign in 4 siblings due to novel compound heterozygous AFG3L2 mutation.
Muscle Spasticity
Spinocerebellar Ataxia Type 28-Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2.
Muscle Spasticity
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.
Neurodegenerative Diseases
A Novel Frameshift Mutation in the AFG3L2 Gene in a Patient with Spinocerebellar Ataxia.
Neurodegenerative Diseases
Autocatalytic processing of m-AAA protease subunits in mitochondria.
Neurodegenerative Diseases
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Neurodegenerative Diseases
Emerging roles of mitochondrial proteases in neurodegeneration.
Neurodegenerative Diseases
Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration.
Neurodegenerative Diseases
Identification and characterization of AFG3L2, a novel paraplegin-related gene.
Neurodegenerative Diseases
Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.
Neurodegenerative Diseases
Mice harbouring a SCA28 patient mutation in AFG3L2 develop late-onset ataxia associated with enhanced mitochondrial proteotoxicity.
Neurodegenerative Diseases
Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease.
Neurodegenerative Diseases
Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.
Neurodegenerative Diseases
Pathogenic variants in the AFG3L2 proteolytic domain cause SCA28 through haploinsufficiency and proteostatic stress-driven OMA1 activation.
Neurodegenerative Diseases
Purkinje neuron Ca2+ influx reduction rescues ataxia in SCA28 model.
Neurodegenerative Diseases
Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1.
Neurodegenerative Diseases
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
Neurodegenerative Diseases
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.
Optic Atrophy
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
Optic Atrophy
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.
Optic Atrophy, Autosomal Dominant
Down-regulation of the mitochondrial i-AAA protease Yme1L induces muscle atrophy via FoxO3a and myostatin activation.
Optic Atrophy, Autosomal Dominant
Multi-site control and regulation of mitochondrial energy production.
Optic Atrophy, Autosomal Dominant
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.
Optic Nerve Diseases
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.
Paraparesis, Spastic
Hereditary spastic paraplegia caused by the novel mutation 1047insC in the SPG7 gene.
Paraparesis, Spastic
Investigation of mitochondrial function in hereditary spastic paraparesis.
Paraparesis, Spastic
Paraplegin gene analysis in hereditary spastic paraparesis (HSP) pedigrees in northeast England.
Paraparesis, Spastic
Paraplegin mutations in sporadic adult-onset upper motor neuron syndromes.
Paraparesis, Spastic
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.
Paraplegia
Hereditary spastic paraplegia caused by the novel mutation 1047insC in the SPG7 gene.
Paraplegia
In Silico Investigation of Traditional Chinese Medicine for Potential Lead Compounds as SPG7 Inhibitors against Coronary Artery Disease.
Paraplegia
Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential.
Paraplegia
Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein.
Paraplegia
Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease.
Paraplegia
Multi-site control and regulation of mitochondrial energy production.
Paraplegia
Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.
Paraplegia
Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease.
Paraplegia
Spastic paraplegia gene 7 in patients with spasticity and/or optic neuropathy.
Paraplegia
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.
Spastic Paraplegia, Hereditary
A novel phenotype of hereditary spastic paraplegia type 7 associated with a compound heterozygous mutation in paraplegin.
Spastic Paraplegia, Hereditary
Abnormal Paraplegin Expression in Swollen Neurites, ?- and ?-Synuclein Pathology in a Case of Hereditary Spastic Paraplegia SPG7 with an Ala510Val Mutation.
Spastic Paraplegia, Hereditary
Alternative splicing of Spg7, a gene involved in hereditary spastic paraplegia, encodes a variant of paraplegin targeted to the endoplasmic reticulum.
Spastic Paraplegia, Hereditary
ATPase and Protease Domain Movements in the Bacterial AAA+ Protease FtsH Are Driven by Thermal Fluctuations.
Spastic Paraplegia, Hereditary
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Spastic Paraplegia, Hereditary
Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7.
Spastic Paraplegia, Hereditary
Functional evaluation of paraplegin mutations by a yeast complementation assay.
Spastic Paraplegia, Hereditary
Genetic interaction between the m-AAA protease isoenzymes reveals novel roles in cerebellar degeneration.
Spastic Paraplegia, Hereditary
Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration.
Spastic Paraplegia, Hereditary
Hereditary spastic paraplegia: respiratory choke or unactivated substrate?
Spastic Paraplegia, Hereditary
Impaired flickering of the permeability transition pore causes SPG7 spastic paraplegia.
Spastic Paraplegia, Hereditary
Intramuscular viral delivery of paraplegin rescues peripheral axonopathy in a model of hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration.
Spastic Paraplegia, Hereditary
Mitochondrial proteins in neuronal degeneration.
Spastic Paraplegia, Hereditary
Molecular basis of inherited spastic paraplegias.
Spastic Paraplegia, Hereditary
Mutation analysis of the paraplegin gene (SPG7) in patients with hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
Systematic isolation and characterization of cDNAs encoding AAA proteins from human brain.
Spastic Paraplegia, Hereditary
The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria.
Spastic Paraplegia, Hereditary
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
Spastic Paraplegia, Hereditary
The mitochondrial protease AFG3L2 is essential for axonal development.
Spastic Paraplegia, Hereditary
Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
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.
Spinocerebellar Ataxias
A novel AFG3L2 mutation in a Somalian patient with spinocerebellar ataxia type 28.
Spinocerebellar Ataxias
A Novel Frameshift Mutation in the AFG3L2 Gene in a Patient with Spinocerebellar Ataxia.
Spinocerebellar Ataxias
A Novel Missense Mutation in AFG3L2 Associated with Late Onset and Slow Progression of Spinocerebellar Ataxia Type 28.
Spinocerebellar Ataxias
AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival.
Spinocerebellar Ataxias
Astrocyte-specific deletion of the mitochondrial m-AAA protease reveals glial contribution to neurodegeneration.
Spinocerebellar Ataxias
ATPase Domain AFG3L2 Mutations Alter OPA1 Processing and Cause Optic Neuropathy.
Spinocerebellar Ataxias
Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Spinocerebellar Ataxias
Deletion of AFG3L2 associated with spinocerebellar ataxia type 28 in the context of multiple genomic anomalies.
Spinocerebellar Ataxias
Evidence for Non-Mendelian Inheritance in Spastic Paraplegia 7.
Spinocerebellar Ataxias
Expanding the phenotype of AFG3L2 mutations: Late-onset autosomal recessive spinocerebellar ataxia.
Spinocerebellar Ataxias
Genotype-phenotype correlations in spastic paraplegia type 7: a study in a large Dutch cohort.
Spinocerebellar Ataxias
Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration.
Spinocerebellar Ataxias
Loss of the m-AAA protease subunit AFG3L2 causes mitochondrial transport defects and tau hyperphosphorylation.
Spinocerebellar Ataxias
m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration.
Spinocerebellar Ataxias
Mice harbouring a SCA28 patient mutation in AFG3L2 develop late-onset ataxia associated with enhanced mitochondrial proteotoxicity.
Spinocerebellar Ataxias
Missense mutations in the AFG3L2 proteolytic domain account for ?1.5% of European autosomal dominant cerebellar ataxias.
Spinocerebellar Ataxias
Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease.
Spinocerebellar Ataxias
Partial deletion of AFG3L2 causing spinocerebellar ataxia type 28.
Spinocerebellar Ataxias
Pathogenic variants in the AFG3L2 proteolytic domain cause SCA28 through haploinsufficiency and proteostatic stress-driven OMA1 activation.
Spinocerebellar Ataxias
Purkinje neuron Ca2+ influx reduction rescues ataxia in SCA28 model.
Spinocerebellar Ataxias
Recessive AFG3L2 Mutation Causes Progressive Microcephaly, Early Onset Seizures, Spasticity, and Basal Ganglia Involvement.
Spinocerebellar Ataxias
Respiratory dysfunction by AFG3L2 deficiency causes decreased mitochondrial calcium uptake via organellar network fragmentation.
Spinocerebellar Ataxias
SCA28: Novel Mutation in the AFG3L2 Proteolytic Domain Causes a Mild Cerebellar Syndrome with Selective Type-1 Muscle Fiber Atrophy.
Spinocerebellar Ataxias
Spinocerebellar ataxia 28: a novel AFG3L2 mutation in a German family with young onset, slow progression and saccadic slowing.
Spinocerebellar Ataxias
Spinocerebellar Ataxia Type 28-Phenotypic and Molecular Characterization of a Family with Heterozygous and Compound-Heterozygous Mutations in AFG3L2.
Spinocerebellar Ataxias
The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying.
Spinocerebellar Ataxias
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.
Spinocerebellar Degenerations
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.
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Rugarli, E.I.; Langer, T.
Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia
Trends Mol. Med.
12
262-269
2006
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
brenda
Martinelli, P.; La Mattina, V.; Bernacchia, A.; Magnoni, R.; Cerri, F.; Cox, G.; Quattrini, A.; Casari, G.; Rugarli, E.I.
Genetic interaction between the m-AAA protease isoenzymes reveals novel roles in cerebellar degeneration
Hum. Mol. Genet.
18
2001-2013
2009
Homo sapiens (Q9UQ90), Homo sapiens (Q9Y4W6), Homo sapiens, Mus musculus (Q3ULF4), Mus musculus (Q8JZQ2)
brenda
Bonn, F.; Pantakani, K.; Shoukier, M.; Langer, T.; Mannan, A.U.
Functional evaluation of paraplegin mutations by a yeast complementation assay
Hum. Mutat.
31
617-621
2010
Homo sapiens (Q9UQ90), Homo sapiens
brenda
Ehses, S.; Raschke, I.; Mancuso, G.; Bernacchia, A.; Geimer, S.; Tondera, D.; Martinou, J.C.; Westermann, B.; Rugarli, E.I.; Langer, T.
Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1
J. Cell Biol.
187
1023-1036
2009
Homo sapiens (Q9Y4W6), Homo sapiens, Mus musculus
brenda
Karlberg, T.; van den Berg, S.; Hammarstroem, M.; Sagemark, J.; Johansson, I.; Holmberg-Schiavone, L.; Schueler, H.
Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7
PLoS ONE
4
e6975
2009
Homo sapiens (Q9UQ90), Homo sapiens
brenda
Smakowska, E.; Czarna, M.; Janska, H.
Mitochondrial ATP-dependent proteases in protection against accumulation of carbonylated proteins
Mitochondrion
19
245-251
2014
Homo sapiens
brenda
Kasashima, K.; Sumitani, M.; Endo, H.
Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX
Exp. Cell Res.
318
2335-2343
2012
Homo sapiens
brenda
Ramelot, T.A.; Yang, Y.; Sahu, I.D.; Lee, H.W.; Xiao, R.; Lorigan, G.A.; Montelione, G.T.; Kennedy, M.A.
NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer
FEBS Lett.
587
3522-3528
2013
Homo sapiens, Homo sapiens (Q9Y4W6)
brenda
Lowth, B.; Kirstein-Miles, J.; Saiyed, T.; Brtz-Oesterhelt, H.; Morimoto, R.; Truscott, K.; Dougan, D.
Substrate recognition and processing by a Walker B mutant of the human mitochondrial AAA+ protein CLPX
J. Struct. Biol.
179
193-201
2012
Homo sapiens
brenda
Lu, B.; Lee, J.; Nie, X.; Li, M.; Morozov, Y.I.; Venkatesh, S.; Bogenhagen, D.F.; Temiakov, D.; Suzuki, C.K.
Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease
Mol. Cell
49
121-132
2013
Homo sapiens
brenda
Cesnekova, J.; Rodinova, M.; Hansikova, H.; Zeman, J.; Stiburek, L.
Loss of mitochondrial AAA proteases AFG3L2 and YME1L impairs mitochondrial structure and respiratory chain biogenesis
Int. J. Mol. Sci.
19
e9288
2018
Homo sapiens (Q9Y4W6 and Q96TA2)
brenda
Hurst, S.; Baggett, A.; Csordas, G.; Sheu, S.S.
SPG7 targets the m-AAA protease complex to process MCU for uniporter assembly, Ca2+ influx, and regulation of mitochondrial permeability transition pore opening
J. Biol. Chem.
294
10807-10818
2019
Homo sapiens (Q9UQ90 and Q9Y4W6)
brenda
Puchades, C.; Ding, B.; Song, A.; Wiseman, R.; Lander, G.; Glynn, S.
Unique structural features of the mitochondrial AAA+ protease AFG3L2 reveal the molecular basis for activity in health and disease
Mol. Cell.
75
1073-1085
2019
Homo sapiens (Q9Y4W6), Homo sapiens
brenda