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Cytosolic proteostasis through importing of misfolded proteins into mitochondria.
Ruan L, Zhou C, Jin E, Kucharavy A, Zhang Y, Wen Z, Florens L, Li R. Ruan L, et al. Nature. 2017 Mar 16;543(7645):443-446. doi: 10.1038/nature21695. Epub 2017 Mar 1. Nature. 2017. PMID: 28241148 Free PMC article.
Here we show that, in yeast, cytosolic proteins prone to aggregation are imported into mitochondria for degradation. ...Defects in cytosolic Hsp70s leads to enhanced entry of misfolded proteins into mitochondria and elevated …
Here we show that, in yeast, cytosolic proteins prone to aggregation are imported into mitochondria for degradat …
Mitochondrial control of cellular protein homeostasis.
Mohanraj K, Nowicka U, Chacinska A. Mohanraj K, et al. Biochem J. 2020 Aug 28;477(16):3033-3054. doi: 10.1042/BCJ20190654. Biochem J. 2020. PMID: 32845275 Review.
The majority of mitochondrial proteins are coded by nuclear DNA. Constant import of proteins from the cytosol is a prerequisite for the efficient functioning of the organelle. The protein import into mitochondria is mediated by div …
The majority of mitochondrial proteins are coded by nuclear DNA. Constant import of proteins from the cytosol is …
Consequences of inner mitochondrial membrane protein misfolding.
Coyne LP, Chen XJ. Coyne LP, et al. Mitochondrion. 2019 Nov;49:46-55. doi: 10.1016/j.mito.2019.06.001. Epub 2019 Jun 10. Mitochondrion. 2019. PMID: 31195097 Free PMC article. Review.
Maintaining the folding state of these proteins is therefore of the utmost importance, and this is ensured by IMM chaperones and proteases that refold and degrade unassembled and misfolded proteins. ...Finally, we summarize the mounting evidence that IMM prot …
Maintaining the folding state of these proteins is therefore of the utmost importance, and this is ensured by IMM chaperones and prot …
Mitochondrial Quality Control and Cellular Proteostasis: Two Sides of the Same Coin.
Quiles JM, Gustafsson ÅB. Quiles JM, et al. Front Physiol. 2020 May 25;11:515. doi: 10.3389/fphys.2020.00515. eCollection 2020. Front Physiol. 2020. PMID: 32528313 Free PMC article. Review.
Almost all of the mitochondrial proteins are encoded by the nuclear genome and the trafficking of these nuclear-encoded proteins necessitates significant cross-talk with the cytosolic protein QC machinery to ensure that only functional proteins
Almost all of the mitochondrial proteins are encoded by the nuclear genome and the trafficking of these nuclear-encoded proteins
Mitochondrial carrier protein overloading and misfolding induce aggresomes and proteostatic adaptations in the cytosol.
Liu Y, Wang X, Coyne LP, Yang Y, Qi Y, Middleton FA, Chen XJ. Liu Y, et al. Mol Biol Cell. 2019 May 15;30(11):1272-1284. doi: 10.1091/mbc.E19-01-0046. Epub 2019 Mar 20. Mol Biol Cell. 2019. PMID: 30893019 Free PMC article.
The data suggest that the import of mitochondrial proteins is saturable and that the cytosol is limited in degrading unimported mitochondrial proteins. ...In summary, our work captured a profound effect of unimported mitochondrial proteins on …
The data suggest that the import of mitochondrial proteins is saturable and that the cytosol is limited in degrading un …
Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins.
Nowicka U, Chroscicki P, Stroobants K, Sladowska M, Turek M, Uszczynska-Ratajczak B, Kundra R, Goral T, Perni M, Dobson CM, Vendruscolo M, Chacinska A. Nowicka U, et al. Elife. 2021 Jul 20;10:e65484. doi: 10.7554/eLife.65484. Elife. 2021. PMID: 34292154 Free PMC article.
Mitochondria are organelles with their own genomes, but they rely on the import of nuclear-encoded proteins that are translated by cytosolic ribosomes. ...Here, we report that upon impairments in mitochondrial protein import, high-risk pr
Mitochondria are organelles with their own genomes, but they rely on the import of nuclear-encoded proteins that are tr
Ribosomal mistranslation leads to silencing of the unfolded protein response and increased mitochondrial biogenesis.
Shcherbakov D, Teo Y, Boukari H, Cortes-Sanchon A, Mantovani M, Osinnii I, Moore J, Juskeviciene R, Brilkova M, Duscha S, Kumar HS, Laczko E, Rehrauer H, Westhof E, Akbergenov R, Böttger EC. Shcherbakov D, et al. Commun Biol. 2019 Oct 17;2:381. doi: 10.1038/s42003-019-0626-9. eCollection 2019. Commun Biol. 2019. PMID: 31637312 Free PMC article.
Here, we present a global and comprehensive picture of the cellular changes in response to translational accuracy in mammalian ribosomes impaired by genetic manipulation. In addition to affecting established protein quality control pathways, such as elevated transcript lev …
Here, we present a global and comprehensive picture of the cellular changes in response to translational accuracy in mammalian ribosomes imp …
Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis.
Finka A, Goloubinoff P. Finka A, et al. Cell Stress Chaperones. 2013 Sep;18(5):591-605. doi: 10.1007/s12192-013-0413-3. Epub 2013 Feb 21. Cell Stress Chaperones. 2013. PMID: 23430704 Free PMC article.
Nevertheless, young cells effectively express a network of molecular chaperones and folding enzymes, termed here "the chaperome," which can prevent formation of potentially harmful misfolded protein conformers and use the energy of adenosine triphosphate (ATP) to re …
Nevertheless, young cells effectively express a network of molecular chaperones and folding enzymes, termed here "the chaperome," which can …
Allosteric activation of Hsp70 reduces mutant huntingtin levels, the clustering of N-terminal fragments, and their nuclear accumulation.
Pinho BR, Almeida LM, Duchen MR, Oliveira JMA. Pinho BR, et al. Life Sci. 2021 Nov 15;285:120009. doi: 10.1016/j.lfs.2021.120009. Epub 2021 Oct 1. Life Sci. 2021. PMID: 34600937
AIMS: Huntington's disease (HD) is caused by a mutant huntingtin protein that misfolds, yields toxic N-terminal fragments, aggregates, and disrupts proteostasis. ...Mechanistically, YM-1 increases the Hsp70 affinity for substrates, promoting their prot …
AIMS: Huntington's disease (HD) is caused by a mutant huntingtin protein that misfolds, yields toxic N-terminal fragmen …