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17 results for author:"Heazlewood J.L."Drop in Literature Citations

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Novel proteins, putative membrane transporters, and an integrated metabolic network are revealed by quantitative proteomic analysis of Arabidopsis cell culture peroxisomes.

Eubel H., Meyer E.H., Taylor N.L., Bussell J.D., O'Toole N., Heazlewood J.L., Castleden I., Small I.D., Smith S.M., Millar A.H.

Plant Physiol. 148:1809-1829(2008) · Mapped (86)

Analysis of the Arabidopsis cytosolic ribosome proteome provides detailed insights into its components and their post-translational modification.

Carroll A.J., Heazlewood J.L., Ito J., Millar A.H.

Mol. Cell Proteomics 7:347-369(2008) · Mapped (210)

Mitochondrial acyl carrier proteins in Arabidopsis thaliana are predominantly soluble matrix proteins and none can be confirmed as subunits of respiratory Complex I.

Meyer E.H., Heazlewood J.L., Millar A.H.

Plant Mol. Biol. 64:319-327(2007) · Mapped (17)

Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix.

Ito J., Heazlewood J.L., Millar A.H.

J. Proteome Res. 5:3459-3469(2006) · Mapped (52)

Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis.

Heazlewood J.L., Tonti-Filippini J., Verboom R.E., Millar A.H.

Plant Physiol. 139:598-609(2005) · Mapped (19)

Untangling multi-gene families in plants by integrating proteomics into functional genomics.

Sappl P.G., Heazlewood J.L., Millar A.H.

Phytochemistry 65:1517-1530(2004) · Mapped (13)

Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis.

Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.

Plant Physiol. 134:838-848(2004) · UniProtKB (5) · Mapped (13)

A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor.

Chew O., Lister R., Qbadou S., Heazlewood J.L., Soll J., Schleiff E., Millar A.H., Whelan J.

FEBS Lett. 557:109-114(2004) · Mapped (1)

A transcriptomic and proteomic characterization of the Arabidopsis mitochondrial protein import apparatus and its response to mitochondrial dysfunction.

Lister R., Chew O., Lee M.-N., Heazlewood J.L., Clifton R., Parker K.L., Millar A.H., Whelan J.

Plant Physiol. 134:777-789(2004) · UniProtKB (1) · Mapped (52)

Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.

Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.

Plant Cell 16:241-256(2004) · UniProtKB (119) · Mapped (276)

Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells.

Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R., Leaver C.J., Sweetlove L.J.

Plant Cell 15:2140-2151(2003) · UniProtKB (2) · Mapped (9)

Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant-specific subunits.

Heazlewood J.L., Howell K.A., Millar A.H.

Biochim. Biophys. Acta 1604:159-169(2003) · Mapped (34)

The products of the mitochondrial orf25 and orfB genes are F(0) components in the plant F(1)F(0) ATP synthase.

Heazlewood J.L., Whelan J., Millar A.H.

FEBS Lett. 540:201-205(2003) · UniProtKB (2) · Mapped (9)

Proteomic identification of divalent metal cation binding proteins in plant mitochondria.

Herald V.L., Heazlewood J.L., Day D.A., Millar A.H.

FEBS Lett. 537:96-100(2003) · Mapped (14)

Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis.

Millar A.H., Heazlewood J.L.

Plant Physiol. 131:443-453(2003) · Mapped (29)

The impact of oxidative stress on Arabidopsis mitochondria.

Sweetlove L.J., Heazlewood J.L., Herald V., Holtzapffel R., Day D.A., Leaver C.J., Millar A.H.

Plant J. 32:891-904(2002) · UniProtKB (2) · Mapped (31)

Expansin-like molecules: novel functions derived from common domains.

Ludidi N.N., Heazlewood J.L., Seoighe C., Irving H.R., Gehring C.A.

J. Mol. Evol. 54:587-594(2002) · UniProtKB (3)

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