Výsledky vyhledávání - "D H, Gonzalez"

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On the nature of the hard X-ray sources SWIFTJ1907.3-2050, IGRJ12123-5802 and IGRJ19552+0044

Autor: Bernardini, F., de Martino, D., Mukai, K., Falanga, M., Andruchow, I., Bonnet-Bidaud, J. -M., Masetti, N., Buitrago, D. H. Gonzalez, Mouchet, M., Tovmassian, G.

The INTEGRAL and Swift hard X-ray surveys have identified a large number of new sources, among which many are proposed as Cataclysmic Variables (CVs). Here we present the first detailed study of three X-ray selected CVs, Swift J1907.3-2050, IGRJ12123

Externí odkaz: http://arxiv.org/abs/1308.1230

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Positively charged residues at the N-terminal arm of the homeodomain are required for efficient DNA binding by homeodomain-leucine zipper proteins

Autor: C M, Palena, A E, Tron, C W, Bertoncini, D H, Gonzalez, R L, Chan

Publikováno v: Journal of molecular biology. 308(1)

Plant homeodomain-leucine zipper proteins, unlike most animal homeodomains, bind DNA efficiently only as dimers. In the present work, we report that the deletion of the homeodomain N-terminal arm (first nine residues) of the homeodomain-leucine zippe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::81d4a8a891695ecea72c92e5a47d9c55
https://pubmed.ncbi.nlm.nih.gov/11302705

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A monomer-dimer equilibrium modulates the interaction of the sunflower homeodomain leucine-zipper protein Hahb-4 with DNA

Autor: C M, Palena, D H, Gonzalez, R L, Chan

Publikováno v: The Biochemical journal. 341

We have analysed the interaction of the sunflower homeodomain leucine-zipper (Hd-Zip) protein Hahb-4 with DNA. The complete Hd-Zip domain from Hahb-4 was able to select specific sequences from a random oligonucleotide mixture that contained a 9-bp co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9a6899e40dfed799645d7b502432cc4c
https://pubmed.ncbi.nlm.nih.gov/10377247

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A gene involved in the biogenesis of c-type cytochromes is co-transcribed with a ribosomal protein gene in wheat mitochondria [corrected]

Autor: D H, Gonzalez, G, Bonnard, J M, Grienenberger

Publikováno v: Current genetics. 24(3)

Sequence analysis of a transcribed region of the wheat mitochondrial (mt) genome revealed two open reading frames (orfs) coding for proteins of 589 and 174 amino acids. Both genes are co-transcribed in a 2.6-kb RNA. The largest orf codes for a hydrop

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8e7d1693b602de0f7a63ecd5ed1132fa
https://pubmed.ncbi.nlm.nih.gov/8221934

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Carboxylation and dephosphorylation of phosphoenol-3-fluoropyruvate by maize leaf phosphoenolpyruvate carboxylase

Autor: C S Andreo, D H Gonzalez

Publikováno v: The Biochemical journal. 253(1)

The analogue (Z)-phosphoenol-3-fluoropyruvate [(Z)-3-fluoro-2-(phosphono-oxy)propenoic acid] was tested as substrate of maize leaf phosphoenolpyruvate carboxylase. Studies with NaH14CO3 indicate that the analogue is carboxylated by the enzyme. Howeve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed36e1c24c86d8da71bbe910b995c9ef
https://pubmed.ncbi.nlm.nih.gov/3421944

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The Ionic Strength Changes the Quaternary Structure of Phosphoenolpyruvate Carboxylase from Maize Leaves

Autor: D. H. Gonzalez, R. Wagner, F. E. Podesta, Carlos S. Andreo

Publikováno v: Progress in Photosynthesis Research ISBN: 9789401705189

Phosphoenolpyruvate (Pep) carboxylase (E.C. 4.1.1.31) is the enzyme responsible for the primary CO2 fixation in maize and other C4 plants (1).

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::76671abaa861870b8c4f0905d0e97540
https://doi.org/10.1007/978-94-017-0516-5_113

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