Lon protease inactivation in causes unfolded protein stress and inhibition of mitochondrial translation

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Lon protease inactivation in causes unfolded protein stress and inhibition of mitochondrial translation

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wetenschappelijk artikel

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наукова стаття, опублікована у 2018

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Lon protease inactivation in c ...... n of mitochondrial translation

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Lon protease inactivation in c ...... n of mitochondrial translation

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Lon protease inactivation in c ...... n of mitochondrial translation

@en

Lon protease inactivation in c ...... n of mitochondrial translation

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Lon protease inactivation in c ...... n of mitochondrial translation

@en

Lon protease inactivation in c ...... n of mitochondrial translation

@nl

P1476

Lon protease inactivation in c ...... n of mitochondrial translation

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P2093

David R Morris

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Evelyn S Vincow

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Gautam Pareek

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Leo J Pallanck

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Ruth E Thomas

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P2860

MTERF4 regulates translation by targeting the methyltransferase NSUN4 to the mammalian mitochondrial ribosome

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

PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix

Signal integration in the endoplasmic reticulum unfolded protein response

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

Adapting proteostasis for disease intervention

The unfolded protein response: from stress pathway to homeostatic regulation

Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants

A Drosophila model of mitochondrial disease caused by a complex I mutation that uncouples proton pumping from electron transfer.

Methods for studying metabolism in Drosophila

P2888

s41420-018-0110-1

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scholarly article

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10.1038/S41420-018-0110-1

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English

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P478

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P577

2018-01-01T00:00:00Z

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30374414

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P921

mitochondrion

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6197249

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