Identification of potential mitochondrial CLPXP protease interactors and substrates suggests its central role in energy metabolism

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Scientific reports, 5.2015, Nr. 18375. doi: 10.1038/srep18375

Classification: Biowissenschaften, Biologie

Event: Veröffentlichung

(where): Frankfurt am Main

(who): Universitätsbibliothek Johann Christian Senckenberg

(when): 2016

Creator: Fischer, Fabian
Langer, Julian D.
Osiewacz, Heinz D.

URN: urn:nbn:de:hebis:30:3-419024

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:57 AM CEST

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Associated

Fischer, Fabian
Langer, Julian D.
Osiewacz, Heinz D.
Universitätsbibliothek Johann Christian Senckenberg

Time of origin

2016

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Identification of potential mitochondrial CLPXP protease interactors and substrates suggests its central role in energy metabolism

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Other Objects (12)

A multiomic approach to identify new substrates of the mitochondrial m-AAA protease

Role of the mitochondrial ATP-dependent Clp protease in mammalian metabolism

Proteolytic regulation of mitochondrial phospholipid metabolism by the i-AAA protease Yme1

Pathogenic p62/SQSTM1 mutations impair energy metabolism through limitation of mitochondrial substrates

Identification of pancreatic cancer-specific protease substrates for protease-dependent targeted delivery

Author Correction: Pathogenic p62/SQSTM1 mutations impair energy metabolism through limitation of mitochondrial substrates

Complete mitochondrial genome suggests diapsid affinities of turtles

Structure and Dynamics of Intramembrane Protease Substrates by NMR Spectroscopy

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Function and substrates of the Alzheimer´s disease protease BACE1

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A multiomic approach to identify new substrates of the mitochondrial m-AAA protease

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Proteolytic regulation of mitochondrial phospholipid metabolism by the i-AAA protease Yme1

Pathogenic p62/SQSTM1 mutations impair energy metabolism through limitation of mitochondrial substrates

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Author Correction: Pathogenic p62/SQSTM1 mutations impair energy metabolism through limitation of mitochondrial substrates

Complete mitochondrial genome suggests diapsid affinities of turtles

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Function and substrates of the Alzheimer´s disease protease BACE1

A Photocrosslinking Probe to Capture the Substrates of Caseinolytic Protease P

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Proteolytic regulation of mitochondrial phospholipid metabolism by the i-AAA protease Yme1

Pathogenic p62/SQSTM1 mutations impair energy metabolism through limitation of mitochondrial substrates

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Author Correction: Pathogenic p62/SQSTM1 mutations impair energy metabolism through limitation of mitochondrial substrates

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