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Results: 1 to 20 of 138

Similar articles for PubMed (Select 16239145)

1.

The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria.

Nolden M, Ehses S, Koppen M, Bernacchia A, Rugarli EI, Langer T.

Cell. 2005 Oct 21;123(2):277-89.

2.

Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia.

Rugarli EI, Langer T.

Trends Mol Med. 2006 Jun;12(6):262-9. Epub 2006 May 2. Review.

PMID:
16647881
3.

Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia.

Koppen M, Metodiev MD, Casari G, Rugarli EI, Langer T.

Mol Cell Biol. 2007 Jan;27(2):758-67. Epub 2006 Nov 13.

4.

Hereditary spastic paraplegia: respiratory choke or unactivated substrate?

Claypool SM, Koehler CM.

Cell. 2005 Oct 21;123(2):183-5.

5.

Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.

Atorino L, Silvestri L, Koppen M, Cassina L, Ballabio A, Marconi R, Langer T, Casari G.

J Cell Biol. 2003 Nov 24;163(4):777-87. Epub 2003 Nov 17.

6.

Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria.

Bonn F, Tatsuta T, Petrungaro C, Riemer J, Langer T.

EMBO J. 2011 May 24;30(13):2545-56. doi: 10.1038/emboj.2011.169.

7.

Hereditary spastic paraplegia: mitochondrial metalloproteases of yeast.

Pearce DA.

Hum Genet. 1999 Jun;104(6):443-8. Review.

PMID:
10453730
8.

Genetic interaction between the m-AAA protease isoenzymes reveals novel roles in cerebellar degeneration.

Martinelli P, La Mattina V, Bernacchia A, Magnoni R, Cerri F, Cox G, Quattrini A, Casari G, Rugarli EI.

Hum Mol Genet. 2009 Jun 1;18(11):2001-13. doi: 10.1093/hmg/ddp124. Epub 2009 Mar 16.

9.

ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae.

Van Dyck L, Langer T.

Cell Mol Life Sci. 1999 Nov 30;56(9-10):825-42. Review.

PMID:
11212342
10.

Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases.

Koppen M, Langer T.

Crit Rev Biochem Mol Biol. 2007 May-Jun;42(3):221-42. Review.

PMID:
17562452
11.

OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria.

Duvezin-Caubet S, Koppen M, Wagener J, Zick M, Israel L, Bernacchia A, Jagasia R, Rugarli EI, Imhof A, Neupert W, Langer T, Reichert AS.

Mol Biol Cell. 2007 Sep;18(9):3582-90. Epub 2007 Jul 5.

12.

The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria.

Suppanz IE, Wurm CA, Wenzel D, Jakobs S.

Mol Biol Cell. 2009 Jan;20(2):572-80. doi: 10.1091/mbc.E07-11-1112. Epub 2008 Nov 19.

13.

A genomewide screen for petite-negative yeast strains yields a new subunit of the i-AAA protease complex.

Dunn CD, Lee MS, Spencer FA, Jensen RE.

Mol Biol Cell. 2006 Jan;17(1):213-26. Epub 2005 Nov 2.

14.

The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease.

Arlt H, Steglich G, Perryman R, Guiard B, Neupert W, Langer T.

EMBO J. 1998 Aug 17;17(16):4837-47.

16.

Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease.

Leonhard K, Stiegler A, Neupert W, Langer T.

Nature. 1999 Mar 25;398(6725):348-51.

PMID:
10192337
17.
18.

Substrate specific consequences of central pore mutations in the i-AAA protease Yme1 on substrate engagement.

Graef M, Langer T.

J Struct Biol. 2006 Oct;156(1):101-8. Epub 2006 Feb 21.

PMID:
16527490
19.

Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease.

Lee S, Augustin S, Tatsuta T, Gerdes F, Langer T, Tsai FT.

J Biol Chem. 2011 Feb 11;286(6):4404-11. doi: 10.1074/jbc.M110.158741. Epub 2010 Dec 8.

20.

Functional evaluation of paraplegin mutations by a yeast complementation assay.

Bonn F, Pantakani K, Shoukier M, Langer T, Mannan AU.

Hum Mutat. 2010 May;31(5):617-21. doi: 10.1002/humu.21226.

PMID:
20186691
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