DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate
about
Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenanceThermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNAMutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activitiesArchitectural role of mitochondrial transcription factor A in maintenance of human mitochondrial DNAIdentification of RNA Binding Proteins Associated with Dengue Virus RNA in Infected Cells Reveals Temporally Distinct Host Factor RequirementsCross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and DiseaseMultitasking in the mitochondrion by the ATP-dependent Lon proteaseStructure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activityStructural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon proteaseCleavage site selection within a folded substrate by the ATP-dependent lon protease.The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures.Tetramethylpyrazine blocks TFAM degradation and up-regulates mitochondrial DNA copy number by interacting with TFAM.Mitochondrial Nucleoid: Shield and Switch of the Mitochondrial Genome.Does mtDNA nucleoid organization impact aging?Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease.Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging.Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer.Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases.Nuclear cytoplasmic trafficking of proteins is a major response of human fibroblasts to oxidative stressCODAS syndrome is associated with mutations of LONP1, encoding mitochondrial AAA+ Lon protease.Inhibition of Lon blocks cell proliferation, enhances chemosensitivity by promoting apoptosis and decreases cellular bioenergetics of bladder cancer: potential roles of Lon as a prognostic marker and therapeutic target in baldder cancer.The mitochondrial ATP-dependent Lon protease: a novel target in lymphoma death mediated by the synthetic triterpenoid CDDO and its derivatives.Matrix proteases in mitochondrial DNA function.Quality control of mitochondria: protection against neurodegeneration and ageing.Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates.Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulationThe mitochondrial nucleoid: integrating mitochondrial DNA into cellular homeostasisChaperones and proteases--guardians of protein integrity in eukaryotic organelles.Applications of isothermal titration calorimetry in biophysical studies of G-quadruplexes.Impaired TCA cycle flux in mitochondria in skeletal muscle from type 2 diabetic subjects: marker or maker of the diabetic phenotype?A matter of life, death and diseases: mitochondria from a proteomic perspective.New roles for mitochondrial proteases in health, ageing and disease.Mitochondrial Quality Control Proteases in Neuronal Welfare.Mitochondrial Lon protease is a human stress protein.Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1.Identification of the proteasome inhibitor MG262 as a potent ATP-dependent inhibitor of the Salmonella enterica serovar Typhimurium Lon protease.Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease FunctionThe role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.Functional domains of Brevibacillus thermoruber lon protease for oligomerization and DNA binding: role of N-terminal and sensor and substrate discrimination domains.
P2860
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P2860
DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate
description
2004 nî lūn-bûn
@nan
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
DNA and RNA binding by the mit ...... cleotide and protein substrate
@ast
DNA and RNA binding by the mit ...... cleotide and protein substrate
@en
DNA and RNA binding by the mit ...... cleotide and protein substrate
@en-gb
DNA and RNA binding by the mit ...... cleotide and protein substrate
@nl
type
label
DNA and RNA binding by the mit ...... cleotide and protein substrate
@ast
DNA and RNA binding by the mit ...... cleotide and protein substrate
@en
DNA and RNA binding by the mit ...... cleotide and protein substrate
@en-gb
DNA and RNA binding by the mit ...... cleotide and protein substrate
@nl
prefLabel
DNA and RNA binding by the mit ...... cleotide and protein substrate
@ast
DNA and RNA binding by the mit ...... cleotide and protein substrate
@en
DNA and RNA binding by the mit ...... cleotide and protein substrate
@en-gb
DNA and RNA binding by the mit ...... cleotide and protein substrate
@nl
P2093
P2860
P921
P3181
P356
P1476
DNA and RNA binding by the mit ...... cleotide and protein substrate
@en
P2093
Carolyn K Suzuki
Eva Kutejová
Gabriela Ondrovicová
P2860
P304
P3181
P356
10.1074/JBC.M309642200
P407
P577
2004-04-02T00:00:00Z