Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Sergio de la Fuente van Bentem"'
Autor:
Melina Zourelidou, Birgit Absmanner, Benjamin Weller, Inês CR Barbosa, Björn C Willige, Astrid Fastner, Verena Streit, Sarah A Port, Jean Colcombet, Sergio de la Fuente van Bentem, Heribert Hirt, Bernhard Kuster, Waltraud X Schulze, Ulrich Z Hammes, Claus Schwechheimer
Publikováno v:
eLife, Vol 3 (2014)
The development and morphology of vascular plants is critically determined by synthesis and proper distribution of the phytohormone auxin. The directed cell-to-cell distribution of auxin is achieved through a system of auxin influx and efflux transpo
Externí odkaz:
https://doaj.org/article/48e58217bfb74bf5b92e82d841bd45d8
Autor:
Fatma Lecourieux, Celine Forzani, Sergio de la Fuente van Bentem, Alessandro Carreri, David Lecourieux, Heribert Hirt
Publikováno v:
FEBS Journal. 278:1126-1136
In Arabidopsis thaliana, the serine/threonine protein kinase oxidative signal-inducible 1 (OXI1), mediates oxidative stress signalling. Its activity is required for full activation of the mitogen-activated protein kinases (MAPKs), MPK3 and MPK6, in r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e87b0479dd993efa0fdb7b14b4cf0fd
https://doi.org/10.1111/j.1742-4658.2011.08033.x
https://doi.org/10.1111/j.1742-4658.2011.08033.x
Autor:
Sergio de la Fuente van Bentem, Florence Gonnet, Alberto de la Fuente, Heribert Hirt, Delphine Pflieger
Publikováno v:
Mass Spectrometry Reviews. 30:268-297
Proteomes are intricate. Typically, thousands of proteins interact through physical association and post-translational modifications (PTMs) to give rise to the emergent functions of cells. Understanding these functions requires one to study proteomes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13d421df709787ea9b726467f4e5d125
https://doi.org/10.1002/mas.20278
https://doi.org/10.1002/mas.20278
Publikováno v:
Trends in Plant Science. 14:71-76
Protein phosphorylation in eukaryotes predominantly occurs on serine (Ser) and threonine (Thr) residues, whereas phosphorylation on tyrosine (Tyr) residues is less abundant. Plants lack classic Tyr kinases, such as the epidermal growth factor recepto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22a7bb1aa5a702eb780b9164eb5355c5
https://doi.org/10.1016/j.tplants.2008.11.003
https://doi.org/10.1016/j.tplants.2008.11.003
Autor:
Andreas Verhounig, Edina Csaszar, Celine Forzani, David Lecourieux, Sergio de la Fuente van Bentem, Andrea Barta, Jos Joore, Zdravko J. Lorković, Heribert Hirt, Ilse Dohnal, Elisabeth Roitinger, Dorothea Anrather, Joshua Buijnink, Claudia Jonak, Alessandro Carreri
Publikováno v:
Journal of Proteome Research. 7:2458-2470
An estimated one-third of all proteins in higher eukaryotes are regulated by phosphorylation by protein kinases (PKs). Although plant genomes encode more than 1000 PKs, the substrates of only a small fraction of these kinases are known. By mass spect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38937f95dde6a22753fbb829b4368006
https://doi.org/10.1021/pr8000173
https://doi.org/10.1021/pr8000173
Publikováno v:
Trends in Plant Science. 12:404-411
To ensure appropriate responses to stimuli, organisms have evolved signalling networks that rely on post-translational modifications of their components. Among these, protein phosphorylation has a prominent role and much research in plants has focuse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a399bfe469526eedde1d11c7e3c2687
https://doi.org/10.1016/j.tplants.2007.08.007
https://doi.org/10.1016/j.tplants.2007.08.007
Autor:
Dorothea Anrather, Elisabeth Roitinger, Edina Csaszar, Heribert Hirt, Sergio de la Fuente van Bentem
Publikováno v:
Physiologia Plantarum. 126:110-119
Reversible phosphorylation of proteins plays a key role in many regulatory processes that lie at the basis of life. With plants, much research has focused on protein kinases that are involved in the adaptation to different stress conditions, such as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7f7a6cda4d7dcb146efdd0189160526
https://doi.org/10.1111/j.1399-3054.2006.00615.x
https://doi.org/10.1111/j.1399-3054.2006.00615.x
Autor:
Jack H. Vossen, Theodorus W. J. Gadella, Josephus E.M. Vermeer, Marianne J. de Vroomen, Ben J. C. Cornelissen, Michel A. Haring, Sergio de la Fuente van Bentem
Publikováno v:
Plant Physiology, 133, 702-712. American Society of Plant Biologists
Protein serine/threonine phosphatase 5 (PP5) plays an important role in signal transduction in animal cells, but in plants, knowledge about PP5 is scarce. Here, we describe the isolation of a full-length cDNA encoding tomato (Lycopersicon esculentum)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebeac832b06086128685479e57ad6afc
https://doi.org/10.1104/pp.103.026617
https://doi.org/10.1104/pp.103.026617
Autor:
Birgit Absmanner, Inês C. R. Barbosa, Björn C. Willige, Ulrich Z. Hammes, Waltraud X. Schulze, Sarah A. Port, Heribert Hirt, Verena Streit, Sergio de la Fuente van Bentem, Melina Zourelidou, Bernhard Kuster, Astrid Fastner, Benjamin Weller, Jean Colcombet, Claus Schwechheimer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::92401e710e792807f3adf5f72ae3b253
https://doi.org/10.7554/elife.02860.035
https://doi.org/10.7554/elife.02860.035
Autor:
Celine, Forzani, Alessandro, Carreri, Sergio, de la Fuente van Bentem, David, Lecourieux, Fatma, Lecourieux, Heribert, Hirt
Publikováno v:
The FEBS journal. 278(7)
In Arabidopsis thaliana, the serine/threonine protein kinase oxidative signal-inducible 1 (OXI1), mediates oxidative stress signalling. Its activity is required for full activation of the mitogen-activated protein kinases (MAPKs), MPK3 and MPK6, in r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a894172b1b9888a7c9e40489fdb8116a
https://pubmed.ncbi.nlm.nih.gov/21276203
https://pubmed.ncbi.nlm.nih.gov/21276203