(Q27936117)

GOA release 2020-03-11

author

Bernard Guiard

5

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author name string

Birgit von Janowsky

1

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Karin Knapp

2

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Tamara Major

3

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Martin Krayl

4

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Wolfgang Voos

Mitochondrial DNA instability mutants of the bifunctional protein Ilv5p have altered organization in mitochondria and are targeted for degradation by Hsp78 and the Pim1p protease

6

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language of work or name

English

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publication date

December 2005

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1 reference

1 December 2016

386

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issue

12

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page(s)

1307-17

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cites work

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Delivery of ubiquitinated substrates to protein-unfolding machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Two distinct mechanisms drive protein translocation across the mitochondrial outer membrane in the late step of the cytochrome b(2) import pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Unfolding of preproteins upon import into mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Chaperone rings in protein folding and degradation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The role of the ClpA chaperone in proteolysis by ClpAP

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Regulated protein degradation in mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Cleavage site selection within a folded substrate by the ATP-dependent lon protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Proteasomes and their kin: proteases in the machine age

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

An unstructured initiation site is required for efficient proteasome-mediated degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The role of protein degradation in mitochondrial function and biogenesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Targeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Lon and Clp family proteases and chaperones share homologous substrate-recognition domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

ATP-dependent proteases that also chaperone protein biogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Substitution of PIM1 protease in mitochondria by Escherichia coli Lon protease.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The green fluorescent protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

The ATPase and protease domains of yeast mitochondrial Lon: roles in proteolysis and respiration-dependent growth

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Autocatalytic processing of the ATP-dependent PIM1 protease: crucial function of a pro-region for sorting to mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Themes and variations on ubiquitylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Molecular structure of flavocytochrome b2 at 2.4 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Repeat sequence of Epstein-Barr virus-encoded nuclear antigen 1 protein interrupts proteasome substrate processing

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Proteasomes begin ornithine decarboxylase digestion at the C terminus

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149

Mitochondria Unfold Precursor Proteins by Unraveling Them From Their N-termini

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.149