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Elke Brosens
Researcher at Vrije Universiteit Brussel
Publications - 18
Citations - 592
Elke Brosens is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Arsenate reductase & Active site. The author has an hindex of 10, co-authored 16 publications receiving 560 citations. Previous affiliations of Elke Brosens include Flanders Institute for Biotechnology.
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Journal ArticleDOI
Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax.
Wim Versées,Klaas Decanniere,Roger Pelle,J. Depoorter,Elke Brosens,David W. Parkin,Jan Steyaert +6 more
TL;DR: The purine salvage pathway of parasitic protozoa is currently considered as a target for drug development because these organisms cannot synthesize purines de novo, and insight into the structure and mechanism of the involved enzymes can aid in the development of potent inhibitors, leading to new curative drugs.
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The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine.
Lieven Buts,Julie Bouckaert,Erwin De Genst,Remy Loris,Stefan Oscarson,Martina Lahmann,Joris Messens,Elke Brosens,Lode Wyns,Henri De Greve +9 more
TL;DR: F Fold comparisons with pilin and chaperone structures of the chaper one/usher pathway highlight the central role of the C‐terminal β‐strand G of the immunoglobulin‐like fold and provides new insights into pilus assembly, function and adhesion.
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The oxidase DsbA folds a protein with a nonconsecutive disulfide.
Joris Messens,Joris Messens,Jean-François Collet,Karolien Van Belle,Karolien Van Belle,Elke Brosens,Elke Brosens,Remy Loris,Remy Loris,Lode Wyns,Lode Wyns +10 more
TL;DR: Periplasmic ribonuclease I from Escherichia coli is presented as a new endogenous substrate for the study of oxidative protein folding and shows that DsbA is a sufficient catalyst for correct disulfide formation in vivo and in vitro.
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All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
Joris Messens,José C. Martins,Karolien Van Belle,Elke Brosens,Aline Desmyter,Marjan De Gieter,Jean-Michel Wieruszeski,Rudolph Willem,Lode Wyns,Ingrid Zegers +9 more
TL;DR: The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate reduction, involving its P-loop structural motif and three redox active cysteines, has been unraveled and Steady-state kinetics of ArsC mutants gives a view of the crucial residues for catalysis.
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The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin.
Goedele Roos,Abel Garcia-Pino,Karolien Van Belle,Elke Brosens,Khadija Wahni,Guy Vandenbussche,Lode Wyns,Remy Loris,Joris Messens +8 more
TL;DR: The active site proline in thioredoxin determines the driving potential for substrate reduction, and the oxidized form of wild-type Sa_Trx is far more stable than the reduced form over the whole temperature range.