T
Tiago M. Bandeiras
Researcher at Universidade Nova de Lisboa
Publications - 49
Citations - 1661
Tiago M. Bandeiras is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: AAA proteins & RUVBL2. The author has an hindex of 19, co-authored 46 publications receiving 1459 citations. Previous affiliations of Tiago M. Bandeiras include University of Lisbon.
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New Insights into Type II NAD(P)H:Quinone Oxidoreductases
TL;DR: The knowledge of these proteins has expanded in the past decade, as a result of contributions at the biochemical level and the sequencing of the genomes from several organisms, which showed that most organisms contain genes that potentially encode NDH-2.
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Dissimilatory oxidation and reduction of elemental sulfur in thermophilic archaea.
TL;DR: The current knowledge on the composition and properties of the aerobic and anaerobic pathways of dissimilatory elemental sulfur metabolism in thermophilic archaea is summarized in this contribution.
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Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase.
TL;DR: Oxygen consumption was measured in membrane fractions upon thiosulphate addition, thus linking thiosULphate oxidation to dioxygen reduction, in what constitutes a novel activity among Archaea.
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Structural and functional insights into sulfide:quinone oxidoreductase.
José A. Brito,Filipa L. Sousa,Meike Stelter,Tiago M. Bandeiras,Clemens Vonrhein,Miguel Teixeira,Manuela M. Pereira,Margarida Archer +7 more
TL;DR: A sulfide:quinone oxidoreductase (SQR) was isolated from the membranes of the hyperthermoacidophilic archaeon Acidianus ambivalens, and its X-ray structure revealed the presence of a chain of three sulfur atoms bridging those two cysteine residues.
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Structural and functional insights into a dodecameric molecular machine - the RuvBL1/RuvBL2 complex.
Sabine Gorynia,Tiago M. Bandeiras,Filipa G. Pinho,Colin E. McVey,Clemens Vonrhein,Adam Round,Dmitri I. Svergun,Peter Donner,Peter Donner,Pedro M. Matias,Maria Arménia Carrondo +10 more
TL;DR: The first three-dimensional crystal structure of the human RuvBL complex with a truncated domain II is solved and it is shown that this complex is competent for helicase activity, suggesting that in vivo activities of these highly interesting therapeutic drug targets are regulated by cofactors inducing conformational changes via domain II in order to modulate the enzyme complex into its active state.