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1 - 25 of 28 results for author:"Pines O." in Literature citations

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Infantile Cerebellar-Retinal Degeneration Associated with a Mutation in Mitochondrial Aconitase, ACO2.

Spiegel R., Pines O., Ta-Shma A., Burak E., Shaag A., Halvardson J., Edvardson S., Mahajna M., Zenvirt S., Saada A. et al.

Am. J. Hum. Genet. 90:518-523(2012) · UniProtKB (1) · Mapped (8)

Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins.

Muhlenhoff U., Richter N., Pines O., Pierik A.J., Lill R.

J. Biol. Chem. 286:41205-41216(2011)

The aconitase C-terminal domain is an independent dual targeting element.

Ben-Menachem R., Regev-Rudzki N., Pines O.

J. Mol. Biol. 409:113-123(2011) · Mapped (1)

Infantile cerebral and cerebellar atrophy is associated with a mutation in the MED17 subunit of the transcription preinitiation mediator complex.

Kaufmann R., Straussberg R., Mandel H., Fattal-Valevski A., Ben-Zeev B., Naamati A., Shaag A., Zenvirt S., Konen O., Mimouni-Bloch A. et al.

Am. J. Hum. Genet. 87:667-670(2010) · UniProtKB (1) · Mapped (2)

Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response.

Yogev O., Yogev O., Singer E., Shaulian E., Goldberg M., Fox T.D., Pines O.

PLoS Biol. 8:e1000328-e1000328(2010) · Mapped (5)

Tom20 mediates localization of mRNAs to mitochondria in a translation-dependent manner.

Eliyahu E., Pnueli L., Melamed D., Scherrer T., Gerber A.P., Pines O., Rapaport D., Arava Y.

Mol. Cell. Biol. 30:284-294(2010) · Mapped (7)

SLC25A19 mutation as a cause of neuropathy and bilateral striatal necrosis.

Spiegel R., Shaag A., Edvardson S., Mandel H., Stepensky P., Shalev S.A., Horovitz Y., Pines O., Elpeleg O.

Ann. Neurol. 66:419-424(2009) · UniProtKB (1) · Mapped (3)

Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55.

Naamati A., Regev-Rudzki N., Galperin S., Lill R., Pines O.

J. Biol. Chem. 284:30200-30208(2009) · UniProtKB (1) · Mapped (1)

Dual localization of fumarase is dependent on the integrity of the glyoxylate shunt.

Regev-Rudzki N., Battat E., Goldberg I., Pines O.

Mol. Microbiol. 72:297-306(2009) · Mapped (5)

Mutations in LPIN1 cause recurrent acute myoglobinuria in childhood.

Zeharia A., Shaag A., Houtkooper R.H., Hindi T., de Lonlay P., Erez G., Hubert L., Saada A., de Keyzer Y., Eshel G. et al.

Am. J. Hum. Genet. 83:489-494(2008) · UniProtKB (1) · Mapped (6)

The mitochondrial targeting sequence tilts the balance between mitochondrial and cytosolic dual localization.

Regev-Rudzki N., Yogev O., Pines O.

J. Cell. Sci. 121:2423-2431(2008) · Mapped (1)

Translation-coupled translocation of yeast fumarase into mitochondria in vivo.

Yogev O., Karniely S., Pines O.

J. Biol. Chem. 282:29222-29229(2007) · Mapped (3)

Eclipsed distribution: a phenomenon of dual targeting of protein and its significance.

Regev-Rudzki N., Pines O.

Bioessays 29:772-782(2007) · Mapped (2)

Location-specific depletion of a dual-localized protein.

Shlevin L., Regev-Rudzki N., Karniely S., Pines O.

Traffic 8:169-176(2007) · Mapped (1)

Alpha-complementation as a probe for dual localization of mitochondrial proteins.

Karniely S., Rayzner A., Sass E., Pines O.

Exp. Cell Res. 312:3835-3846(2006) · Mapped (11)

The presequence of fumarase is exposed to the cytosol during import into mitochondria.

Karniely S., Regev-Rudzki N., Pines O.

J. Mol. Biol. 358:396-405(2006) · Mapped (4)

Yeast aconitase in two locations and two metabolic pathways: seeing small amounts is believing.

Regev-Rudzki N., Karniely S., Ben-Haim N.N., Pines O.

Mol. Biol. Cell 16:4163-4171(2005) · Mapped (2)

Single translation--dual destination: mechanisms of dual protein targeting in eukaryotes.

Karniely S., Pines O.

EMBO Rep. 6:420-425(2005) · Mapped (5)

Folding of fumarase during mitochondrial import determines its dual targeting in yeast.

Sass E., Karniely S., Pines O.

J. Biol. Chem. 278:45109-45116(2003) · Mapped (5)

External pH and nitrogen source affect secretion of pectate lyase by Colletotrichum gloeosporioides.

Drori N., Kramer-Haimovich H., Rollins J.A., Dinoor A., Okon Y., Pines O., Prusky D.

Appl. Environ. Microbiol. 69:3258-3262(2003) · UniProtKB (1)

Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini.

Sass E., Blachinsky E., Karniely S., Pines O.

J. Biol. Chem. 276:46111-46117(2001) · Mapped (1)

Import into mitochondria, folding and retrograde movement of fumarase in yeast.

Knox C., Sass E., Neupert W., Pines O.

J. Biol. Chem. 273:25587-25593(1998) · Mapped (1)

Overexpression of cytosolic malate dehydrogenase (MDH2) causes overproduction of specific organic acids in Saccharomyces cerevisiae.

Pines O., Shemesh S., Battat E., Goldberg I.

Appl. Microbiol. Biotechnol. 48:248-255(1997) · Mapped (2)

Comparative topology studies in Saccharomyces cerevisiae and in Escherichia coli. The N-terminal half of the yeast ABC protein Ste6.

Geller D., Taglicht D., Edgar R., Tam A., Pines O., Michaelis S., Bibi E.

J. Biol. Chem. 271:13746-13753(1996) · UniProtKB (1)

The single translation product of the FUM1 gene (fumarase) is processed in mitochondria before being distributed between the cytosol and mitochondria in Saccharomyces cerevisiae.

Stein I., Peleg Y., Even-Ram S., Pines O.

Mol. Cell. Biol. 14:4770-4778(1994) · Mapped (1)

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