Dipòsit Digital de Documents de la UAB 4 registres trobats  La cerca s'ha fet en 0.01 segons. 
1.
10 p, 2.0 MB Distinct pathways for zinc metabolism in the terrestrial slug Arion vulgaris / Dvorak, Martin (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Schnegg, Raimund (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Salvenmoser, Willy (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Palacios Bonilla, Òscar (Universitat Autònoma de Barcelona. Departament de Química) ; Lindner, Herbert (Innsbruck Medical University. Institute of Clinical Biochemistry. Biocenter) ; Zerbe, Oliver (University of Zurich. Department of Chemistry) ; Hansel, Armin (University of Innsbruck. Institute for Ion Physics and Applied Physics) ; Leiminger, Markus (University of Innsbruck. Institute for Ion Physics and Applied Physics) ; Steiner, Gerhard (University of Innsbruck. Institute for Ion Physics and Applied Physics) ; Dallinger, Reinhard (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Lackner, Reinhard (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences)
In most organisms, the concentration of free Zn is controlled by metallothioneins (MTs). In contrast, no significant proportions of Zn are bound to MTs in the slug, Arion vulgaris. Instead, this species possesses cytoplasmic low-molecular-weight Zn (LMW Zn) binding compound that divert these metal ions into pathways uncoupled from MT metabolism. [...]
2019 - 10.1038/s41598-019-56577-7
Scientific reports, Vol. 9 (December 2019) , art. 20089  
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15 p, 2.3 MB Biomphalaria glabrata metallothionein : Lacking metal specificity of the protein and missing gene upregulation suggest metal sequestration by exchange instead of through selective binding / Niederwanger, Michael (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences Innsbruck) ; Calatayud, Sara (Universitat de Barcelona. Departament de Biologia Evolutiva) ; Zerbe, Oliver (University of Zürich. Department of Chemistry) ; Atrian i Ventura, Sílvia (Universitat de Barcelona. Departament de Biologia Evolutiva) ; Albalat, Ricard (Universitat de Barcelona. Departament de Biologia Evolutiva) ; Capdevila Vidal, Mercè (Universitat Autònoma de Barcelona. Departament de Química) ; Palacios Bonilla, Òscar (Universitat Autònoma de Barcelona. Departament de Química) ; Dallinger, Reinhard (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences Innsbruck)
The wild-type metallothionein (MT) of the freshwater snail Biomphalaria glabrata and a natural allelic mutant of it in which a lysine residue was replaced by an asparagine residue, were recombinantly expressed and analyzed for their metal-binding features with respect to Cd, Zn and Cu, applying spectroscopic and mass-spectrometric methods. [...]
2017 - 10.3390/ijms18071457
International journal of molecular sciences, Vol. 18, Num. 7 (July 2017) , art. 1457  
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16 p, 2.3 MB Analysis of metal-binding features of the wild type and two domain-truncated mutant variants of Littorina littorea metallothionein reveals its cd-specific character / Palacios Bonilla, Òscar (Universitat Autònoma de Barcelona. Departament de Química) ; Jiménez Martí, Elena (Universitat de Barcelona. Departament de Genètica) ; Niederwanger, Michael (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Gil-Moreno, Selene (Universitat Autònoma de Barcelona. Departament de Química) ; Zerbe, Oliver (University of Zurich. Institute of Organic Chemistry) ; Atrian i Ventura, Sílvia (Universitat de Barcelona. Departament de Genètica) ; Dallinger, Reinhard (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Capdevila Vidal, Mercè (Universitat Autònoma de Barcelona. Departament de Química)
After the resolution of the 3D structure of the Cd9-aggregate of the Littorina littorea metallothionein (MT), we report here a detailed analysis of the metal binding capabilities of the wild type MT, LlwtMT, and of two truncated mutants lacking either the N-terminal domain, Lltr2MT, or both the N-terminal domain, plus four extra flanking residues (SSVF), Lltr1MT. [...]
2017 - 10.3390/ijms18071452
International journal of molecular sciences, Vol. 18 Núm. 7 (july 2017) , p. 1452  
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13 p, 1.3 MB Does Variation of the Inter-Domain Linker Sequence Modulate the Metal Binding Behaviour of Helix pomatia Cd-Metallothionein? / Gil-Moreno, Selene (Universitat Autònoma de Barcelona. Departament de Química) ; Jiménez Martí, Elena (Universitat de Barcelona. Departament de Genètica) ; Palacios Bonilla, Òscar (Universitat Autònoma de Barcelona. Departament de Química) ; Zerbe, Oliver (University of Zurich. Institute of Organic Chemistry) ; Dallinger, Reinhard (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Capdevila Vidal, Mercè (Universitat Autònoma de Barcelona. Departament de Química) ; Atrian i Ventura, Sílvia (Universitat de Barcelona. Departament de Genètica)
Snail metallothioneins (MTs) constitute an ideal model to study structure/function relationships in these metal-binding polypeptides. Helix pomatia harbours three MT isoforms: the highly specific CdMT and CuMT, and an unspecific Cd/CuMT, which represent paralogous proteins with extremely different metal binding preferences while sharing high sequence similarity. [...]
2016 - 10.3390/ijms17010006
International journal of molecular sciences, Vol. 17 Núm. 6 (2016) , p. 1-13  

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