Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon.
about
Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid β-oxidation in peroxisomal matrixThermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNAThe XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factorTransmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon proteaseMultitasking in the mitochondrion by the ATP-dependent Lon proteaseStructural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1.Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis.Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functionsTurnover of matrix proteins in mammalian mitochondriaMaintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeastQuality control: from molecules to organelles.Lambda Xis degradation in vivo by Lon and FtsH.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Biological roles of the Podospora anserina mitochondrial Lon protease and the importance of its N-domain.Lon, a stress-induced ATP-dependent protease, is critically important for systemic Salmonella enterica serovar typhimurium infection of mice.CODAS syndrome is associated with mutations of LONP1, encoding mitochondrial AAA+ Lon protease.Down-regulating overexpressed human Lon in cervical cancer suppresses cell proliferation and bioenergetics.Dynamics of the Light-Dependent Transition of Plant Peroxisomes.Mitochondrial Lon regulates apoptosis through the association with Hsp60-mtHsp70 complex.Lon and Clp family proteases and chaperones share homologous substrate-recognition domains.Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunitsFunctional 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 regulationChaperones and proteases--guardians of protein integrity in eukaryotic organelles.Substrate sequestration by a proteolytically inactive Lon mutant.ATP-dependent proteases differ substantially in their ability to unfold globular proteinsThe ATPase and protease domains of yeast mitochondrial Lon: roles in proteolysis and respiration-dependent growth.Mitochondrial Lon is over-expressed in high-grade gliomas, and mediates hypoxic adaptation: potential role of Lon as a therapeutic target in glioma.The multifaceted role of Lon proteolysis in seedling establishment and maintenance of plant organelle function: living from protein destruction.Cytosolic proteostasis through importing of misfolded proteins into mitochondria.Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteinsIdentification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1.A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum.The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondriaChronic treatment with azide in situ leads to an irreversible loss of cytochrome c oxidase activity via holoenzyme dissociation.The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.Expression of the Saccharomyces cerevisiae gene YME1 in the petite-negative yeast Schizosaccharomyces pombe converts it to petite-positiveBiofilm research uncovers a novel nonenzymatic signal peptidase function in BacillusPeroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone.
P2860
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P2860
Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon.
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@ast
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@en
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@nl
type
label
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@ast
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@en
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@nl
prefLabel
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@ast
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@en
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@nl
P2093
P2860
P1433
P1476
Promotion of mitochondrial mem ...... olytically inactive yeast Lon.
@en
P2093
P2860
HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.
Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration.
P356
10.1126/SCIENCE.274.5284.103
P407
P577
1996-10-04T00:00:00Z