The Hsp60-(p.V98I) mutation associated with hereditary spastic paraplegia SPG13 compromises chaperonin function both in vitro and in vivo.
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Disease-Associated Mutations in the HSPD1 Gene Encoding the Large Subunit of the Mitochondrial HSP60/HSP10 Chaperonin ComplexDelving into the complexity of hereditary spastic paraplegias: how unexpected phenotypes and inheritance modes are revolutionizing their nosologyIncreased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathyNovel Homozygous Missense Mutation in SPG20 Gene Results in Troyer Syndrome Associated with Mitochondrial Cytochrome c Oxidase Deficiency.Hereditary spastic paraplegia: clinico-pathologic features and emerging molecular mechanisms.An ATPase promotes autophosphorylation of the pattern recognition receptor XA21 and inhibits XA21-mediated immunity.Loss of Miro1-directed mitochondrial movement results in a novel murine model for neuron disease.Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors.The Chemical Biology of Molecular Chaperones--Implications for Modulation of ProteostasisMitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy.Effects of a Mutation in the HSPE1 Gene Encoding the Mitochondrial Co-chaperonin HSP10 and Its Potential Association with a Neurological and Developmental Disorder.Mitochondrial protein quality control in health and disease.Dysregulation of axonal transport and motorneuron diseases.Mitochondrial quality control: a matter of life and death for neurons.Mitochondrial proteomics--a tool for the study of metabolic disorders.Cellular pathways of hereditary spastic paraplegia.Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseasesHsp60 chaperonopathies and chaperonotherapy: targets and agents.Barcoding heat shock proteins to human diseases: looking beyond the heat shock responseMolecular chaperones and neuronal proteostasis.A cell model to study different degrees of Hsp60 deficiency in HEK293 cells.LON is the master protease that protects against protein aggregation in human mitochondria through direct degradation of misfolded proteins.The MitCHAP-60 disease is due to entropic destabilization of the human mitochondrial Hsp60 oligomer.Heterozygosity for an in-frame deletion causes glutaryl-CoA dehydrogenase deficiency in a patient detected by newborn screening: investigation of the effect of the mutant allele.Frataxin-deficient neurons and mice models of Friedreich ataxia are improved by TAT-MTScs-FXN treatment.Chaperonin of Group I: Oligomeric Spectrum and Biochemical and Biological Implications.Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics.ACO2 homozygous missense mutation associated with complicated hereditary spastic paraplegia.
P2860
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P2860
The Hsp60-(p.V98I) mutation associated with hereditary spastic paraplegia SPG13 compromises chaperonin function both in vitro and in vivo.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
The Hsp60-(p.V98I) mutation as ...... ion both in vitro and in vivo.
@en
type
label
The Hsp60-(p.V98I) mutation as ...... ion both in vitro and in vivo.
@en
prefLabel
The Hsp60-(p.V98I) mutation as ...... ion both in vitro and in vivo.
@en
P2093
P2860
P356
P1476
The Hsp60-(p.V98I) mutation as ...... ion both in vitro and in vivo.
@en
P2093
Costa Georgopoulos
Debbie Ang
Jakob Hansen
Jane Hvarregaard Christensen
Johan Palmfeldt
Kåre Lehmann Nielsen
Marit Nyholm Nielsen
Mogens Kruhøffer
Niels Gregersen
Peter Bross
P2860
P304
15694-15700
P356
10.1074/JBC.M800548200
P407
P577
2008-04-08T00:00:00Z