Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease. - Wikidata - awgldk - TriplyDB

Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease.

Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease.

http://www.wikidata.org/entity/Q42114093

about

Cell death and survival through the endoplasmic reticulum-mitochondrial axis Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation Multitasking in the mitochondrion by the ATP-dependent Lon protease Mitochondrial quality control: decommissioning power plants in neurodegenerative diseases Diversification, evolution and sub-functionalization of 70kDa heat-shock proteins in two sister species of antarctic krill: differences in thermal habitats, responses and implications under climate change Regulation of mitochondrial pyruvate uptake by alternative pyruvate carrier complexes.Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria.Mitochondrial Lon protease in human disease and aging: Including an etiologic classification of Lon-related diseases and disorders Sending Out an SOS: Mitochondria as a Signaling Hub F-box protein 7 mutations promote protein aggregation in mitochondria and inhibit mitophagy Loss of Nardilysin, a Mitochondrial Co-chaperone for α-Ketoglutarate Dehydrogenase, Promotes mTORC1 Activation and Neurodegeneration Stress-triggered activation of the metalloprotease Oma1 involves its C-terminal region and is important for mitochondrial stress protection in yeast Profiling the mitochondrial proteome of Leber's Hereditary Optic Neuropathy (LHON) in Thailand: down-regulation of bioenergetics and mitochondrial protein quality control pathways in fibroblasts with the 11778G>A mutation Mitochondrial protein synthesis, import, and assembly.Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging.Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.Methionine sulfoxide reductase 2 reversibly regulates Mge1, a cochaperone of mitochondrial Hsp70, during oxidative stress MitoTimer: a novel protein for monitoring mitochondrial turnover in the heart.Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation.Abrogation of MMP-9 gene protects against the development of retinopathy in diabetic mice by preventing mitochondrial damage.Mitochondrial quality control: Easy come, easy go Matrix proteases in mitochondrial DNA function.Spatial and temporal dynamics of the cardiac mitochondrial proteome.Mitochondrial dysfunction induced by heat stress in cultured rat CNS neurons.Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation Oxidative stress adaptation with acute, chronic, and repeated stress.Mitochondrial Proteome Studies in Seeds during Germination.Quality control of mitochondrial proteostasis.Crosstalk between mitochondrial (dys)function and mitochondrial abundance.Mitochondrial quality control: a matter of life and death for neurons.The Biological Foundation of the Genetic Association of TOMM40 with Late-onset Alzheimer's disease.Riboflavin transport and metabolism in humans.A LON-ClpP Proteolytic Axis Degrades Complex I to Extinguish ROS Production in Depolarized Mitochondria.The deafness gene DFNA5 induces programmed cell death through mitochondria and MAPK-related pathways Mitochondrial SSBP1 protects cells from proteotoxic stresses by potentiating stress-induced HSF1 transcriptional activity.Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?Proteins interacting with mitochondrial ATP-dependent Lon protease (MAP1) in Magnaporthe oryzae are involved in rice blast disease.LON is the master protease that protects against protein aggregation in human mitochondria through direct degradation of misfolded proteins.The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.Peroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone.

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P2860

Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease.

http://www.wikidata.org/entity/Q42114093

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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name

Mitochondrial enzymes are prot ...... nes and the Pim1/LON protease.

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Mitochondrial enzymes are prot ...... nes and the Pim1/LON protease.

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type

label

Mitochondrial enzymes are prot ...... nes and the Pim1/LON protease.

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Mitochondrial enzymes are prot ...... nes and the Pim1/LON protease.

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prefLabel

Mitochondrial enzymes are prot ...... nes and the Pim1/LON protease.

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Mitochondrial enzymes are prot ...... nes and the Pim1/LON protease.

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P356

MBC.E10-08-0718

P1433

Molecular Biology of the Cell

P1476

Mitochondrial enzymes are prot ...... nes and the Pim1/LON protease.

@en

P2093

Catherina Baitzel

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

Ilka Lewrenz

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

Sebastian Franken

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

Tom Bender

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

Wolfgang Voos

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P2860

Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death

Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism

The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress.

A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase.

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system.

Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria.

Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.

Mitochondrial Hsp70 Ssc1: role in protein folding.

Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1.

P304

541-554

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10.1091/MBC.E10-08-0718

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5

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22

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2011-01-05T00:00:00Z

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49731772

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P698

21209324

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P921

molecular chaperones

P932

3046053

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