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    • Article
    Sélectionner

    Heterodimer formation between thioredoxin f and fructose 1,6-bisphosphatase from spinach chloroplasts

    Balmer, Yves
    Schürmann, Peter
    FEBS Letters. - 2001/492/1-2/58-61
    2001
    Disponible
    Plus…
    Titre: Heterodimer formation between thioredoxin f and fructose 1,6-bisphosphatase from spinach chloroplasts
    Auteur: Balmer, Yves
    Contributeur: Schürmann, Peter
    Date: 2001
    Sujet: Spinach - Fructose 1,6-Bisphosphatase - Thioredoxin f - Site-directed mutagenesis - Intermolecular disulfide - Heterodimer
    Description: Chloroplast fructose 1,6-bisphosphatase (FBPase) is activated by reduction of a regulatory disulfide through thioredoxin f (Trx f). In the course of this reduction a transient mixed disulfide is formed linking covalently Trx f with FBPase, which possesses three Cys on a loop structure, two of them forming the redox-active disulfide bridge. The goal of this study was to identify the Cys involved in the transient mixed disulfide. To stabilize this reaction intermediate, mutant proteins with modified active sites were used. We identified Cys-155 of the FBPase as the one engaged in the formation of the mixed disulfide intermediate with Cys-46 of Trx f.
    Publication en relation: FEBS Letters. - 2001/492/1-2/58-61
    Document hôte: FEBS Letters
    Identifiant: 10.1016/S0014-5793(01)02229-3 (DOI)

    • Article
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    Canal 9 et son rédacteur en chef Yves Balmer, un mariage réussi : [interview]

    Balmer, Yves
    In: Regards : journal régional indépendant : Sierre, Anniviers, Noble-Contrée. - Sion. - No 67(septembre 2010), p. 4-5 : ill.
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    Titre: Canal 9 et son rédacteur en chef Yves Balmer, un mariage réussi : [interview]
    Auteur: Balmer, Yves
    Sujet RERO: Canal 9
    Sujet RERO - forme: [Entretiens]
    Publication en relation: In: Regards : journal régional indépendant : Sierre, Anniviers, Noble-Contrée. - Sion. - No 67(septembre 2010), p. 4-5 : ill.
    Document hôte: Regards : journal régional indépendant : Sierre, Anniviers, Noble-Contrée
    Classification: vs-bvs-sys 09.07.03
    No RERO: R005535625
    Permalien:
    http://data.rero.ch/01-R005535625/html?view=VS_V1

    • Plusieurs versions

    Proteomics Uncovers Proteins Interacting Electrostatically with Thioredoxin in Chloroplasts

    Balmer, Yves, Koller, Antonius, Val, Greg, Schürmann, Peter, Buchanan, Bob
    Photosynthesis Research, 2004, Vol.79(3), pp.275-280 [Revue évaluée par les pairs]

    • Article
    Sélectionner

    Proteomics gives insight into the regulatory function of chloroplast thioredoxins

    Balmer, Yves, Koller, Antonius, Del Val, Gregorio, Manieri, Wanda, Schürmann, Peter, Buchanan, Bob B
    Proceedings of the National Academy of Sciences of the United States of America, 07 January 2003, Vol.100(1), pp.370-5 [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
    Disponible
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    Titre: Proteomics gives insight into the regulatory function of chloroplast thioredoxins
    Auteur: Balmer, Yves; Koller, Antonius; Del Val, Gregorio; Manieri, Wanda; Schürmann, Peter; Buchanan, Bob B
    Sujet: Proteomics ; Chloroplasts -- Genetics ; Thioredoxins -- Genetics
    Description: Thioredoxins are small multifunctional redox active proteins widely if not universally distributed among living organisms. In chloroplasts, two types of thioredoxins (f and m) coexist and play central roles in regulating enzyme activity. Reduction of thioredoxins in chloroplasts is catalyzed by an iron-sulfur disulfide enzyme, ferredoxin-thioredoxin reductase, that receives photosynthetic electrons from ferredoxin, thereby providing a link between light and enzyme activity. Chloroplast thioredoxins function in the regulation of the Calvin cycle and associated processes. However, the relatively small number of known thioredoxin-linked proteins (about 16) raised the possibility that others remain to be identified. To pursue this opportunity, we have mutated thioredoxins f and m, such that the buried cysteine of the active disulfide has been replaced by serine or alanine, and bound them to affinity columns to trap target proteins of chloroplast stroma. The covalently linked proteins were eluted...
    Fait partie de: Proceedings of the National Academy of Sciences of the United States of America, 07 January 2003, Vol.100(1), pp.370-5
    Identifiant: 0027-8424 (ISSN); 12509500 Version (PMID)

    • Plusieurs versions

    Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria

    Balmer, Yves, Gelhaye, Éric, Rouhier, Nicolas, Jacquot, Jean-Pierre, Manieri, Wanda, Schü, Peter, Droux, Michel
    Proceedings of the National Academy of Sciences - PNAS, 2004, Vol.101(8), p.2642–2647 [Revue évaluée par les pairs]

    • Article
    Sélectionner

    Proteomics gives insight into the regulatory function of chloroplast thioredoxins

    Balmer, Yves
    Koller, Antonius, del Val, Gregorio, Manieri, Wanda, Schürmann, Peter, Buchanan, Bob B
    Proceedings of the National Academy of Sciences of the United States of America (PNAS). - 2003/100/1/370-375
    2003-01-07
    Disponible
    Plus…
    Titre: Proteomics gives insight into the regulatory function of chloroplast thioredoxins
    Auteur: Balmer, Yves
    Contributeur: Koller, Antonius; del Val, Gregorio; Manieri, Wanda; Schürmann, Peter; Buchanan, Bob B
    Date: 2003-01-07
    Description: Thioredoxins are small multifunctional redox active proteins widely if not universally distributed among living organisms. In chloroplasts, two types of thioredoxins (f and m) coexist and play central roles in regulating enzyme activity. Reduction of thioredoxins in chloroplasts is catalyzed by an iron-sulfur disulfide enzyme, ferredoxin-thioredoxin reductase, that receives photosynthetic electrons from ferredoxin, thereby providing a link between light and enzyme activity. Chloroplast thioredoxins function in the regulation of the Calvin cycle and associated processes. However, the relatively small number of known thioredoxin-linked proteins (about 16) raised the possibility that others remain to be identified. To pursue this opportunity, we have mutated thioredoxins f and m, such that the buried cysteine of the active disulfide has been replaced by serine or alanine, and bound them to affinity columns to trap target proteins of chloroplast stroma. The covalently linked proteins were eluted with DTT, separated on gels, and identified by mass spectrometry. This approach led to the identification of 15 potential targets that function in 10 chloroplast processes not known to be thioredoxin linked. Included are proteins that seem to function in plastid-to-nucleus signaling and in a previously unrecognized type of oxidative regulation. Approximately two-thirds of these targets contained conserved cysteines. We also identified 11 previously unknown and 9 confirmed target proteins that are members of pathways known to be regulated by thioredoxin. In contrast to results with individual enzyme assays, specificity for thioredoxin f or m was not observed on affinity chromatography.
    Publication en relation: Proceedings of the National Academy of Sciences of the United States of America (PNAS). - 2003/100/1/370-375
    Document hôte: Proceedings of the National Academy of Sciences of the United States of America (PNAS)
    Identifiant: 10.1073/pnas.232703799 (DOI)

    • Article
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    Canal9 = Kanal9

    Schnyder, Fabienne
    Balmer, Yves
    In: Almanach du Valais. - Sion. - Année 111(2011), p. 35-38 : ill.
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    Titre: Canal9 = Kanal9 / par Fabienne Schnyder et Yves Balmer
    Auteur: Schnyder, Fabienne
    Contributeur: Balmer, Yves
    Sujet RERO: Télévision - Canal 9 - Valais (Suisse)
    Publication en relation: In: Almanach du Valais. - Sion. - Année 111(2011), p. 35-38 : ill.
    Document hôte: Almanach du Valais
    Classification: vs-bvs-sys 09.07.03
    No RERO: R005711111
    Permalien:
    http://data.rero.ch/01-R005711111/html?view=VS_V1

    • Article
    Sélectionner

    Proteomics Uncovers Proteins Interacting Electrostatically with Thioredoxin in Chloroplasts

    Balmer, Yves
    Koller, Antonius, del Val, Greg, Schürmann, Peter, Buchanan, Bob B
    Photosynthesis Research. - 2004/79/3/275-280
    2004
    Disponible
    Plus…
    Titre: Proteomics Uncovers Proteins Interacting Electrostatically with Thioredoxin in Chloroplasts
    Auteur: Balmer, Yves
    Contributeur: Koller, Antonius; del Val, Greg; Schürmann, Peter; Buchanan, Bob B
    Date: 2004
    Sujet: complex - electrostatic - non-covalent - thioredoxin f
    Description: The ability of thioredoxin f to form an electrostatic (non-covalent) complex, earlier found with fructose-1,6-bisphosphatase, was extended to include 27 previously unrecognized proteins functional in 11 processes of chloroplasts. The proteins were identified by combining thioredoxin f affinity chromatography with proteomic analysis using tandem mass spectrometry. The results provide evidence that an association with thioredoxin enables the interacting protein to achieve an optimal conformation, so as to facilitate: (i) the transfer of reducing equivalents from the ferredoxin/ferredoxin—thioredoxin reductase complex to a target protein; (ii) in some cases, to enable the channeling of metabolite substrates; (iii) to function as a subunit in the formation of multienzyme complexes.
    Publication en relation: Photosynthesis Research. - 2004/79/3/275-280
    Document hôte: Photosynthesis Research
    Identifiant: 10.1023/B:PRES.0000017207.88257.d4 (DOI)

    • Film
    Sélectionner

    Grand Maman Marie : le 16:9 du 8 septembre 2006

    Balmer, Marie
    Simoncini, Jannick, Balmer, Yves
    Sierre [etc.] : Canal 9
    2006
    Recherche de la disponibilité
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    Erreur de chargement
    Titre: Grand Maman Marie : le 16:9 du 8 septembre 2006 / [réalisation, images, interviews Yves Balmer] ; [montage Jannick Simoncini]
    Auteur: Balmer, Marie
    Contributeur: Simoncini, Jannick; Balmer, Yves
    Editeur: Sierre [etc.] : Canal 9
    Date: 2006
    Collation: 1 DVD-vidéo
    Collection: 16:9 ; [29]
    Documents dans cette collection: 16:9. Canal 9
    Sujet RERO: vie quotidienne - 20e siècle (début) - Femmes - Grands-mères - Histoires de vie - Saint-Luc (Suisse, VS)
    Sujet RERO - forme: [DVD vidéo] - [document]
    Description: Concerne: Marie Balmer
    Note: Données vidéo
    Classification: vs-bvs-sys 02.05
    cdu-vsmart 305
    cdu-vsbcvm 305(494)
    No RERO: R004238301
    Permalien:
    http://data.rero.ch/01-R004238301/html?view=VS_V1

    • Article
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    A complete ferredoxin/thioredoxin system regulates fundamental processes in amyloplasts

    Balmer, Yves, Vensel, William H, Cai, Nick, Manieri, Wanda, Schürmann, Peter, Hurkman, William J, Buchanan, Bob B
    Proceedings of the National Academy of Sciences of the United States of America, 21 February 2006, Vol.103(8), pp.2988-93 [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
    Disponible
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    Titre: A complete ferredoxin/thioredoxin system regulates fundamental processes in amyloplasts
    Auteur: Balmer, Yves; Vensel, William H; Cai, Nick; Manieri, Wanda; Schürmann, Peter; Hurkman, William J; Buchanan, Bob B
    Sujet: Ferredoxins -- Physiology ; Plant Proteins -- Analysis ; Plastids -- Metabolism ; Starch -- Metabolism ; Thioredoxins -- Metabolism ; Triticum -- Metabolism
    Description: A growing number of processes throughout biology are regulated by redox via thiol-disulfide exchange. This mechanism is particularly widespread in plants, where almost 200 proteins have been linked to thioredoxin (Trx), a widely distributed small regulatory disulfide protein. The current study extends regulation by Trx to amyloplasts, organelles prevalent in heterotrophic plant tissues that, among other biosynthetic activities, catalyze the synthesis and storage of copious amounts of starch. Using proteomics and immunological methods, we identified the components of the ferredoxin/Trx system (ferredoxin, ferredoxin-Trx reductase, and Trx), originally described for chloroplasts, in amyloplasts isolated from wheat starchy endosperm. Ferredoxin is reduced not by light, as in chloroplasts, but by metabolically generated NADPH via ferredoxin-NADP reductase. However, once reduced, ferredoxin appears to act as established for chloroplasts, i.e., via ferredoxin-Trx reductase and a Trx (m-type)....
    Fait partie de: Proceedings of the National Academy of Sciences of the United States of America, 21 February 2006, Vol.103(8), pp.2988-93
    Identifiant: 0027-8424 (ISSN); 16481623 Version (PMID)