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Alexandre Wohlkonig
Researcher at Vrije Universiteit Brussel
Publications - 47
Citations - 2544
Alexandre Wohlkonig is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Ethionamide & Mycobacterium tuberculosis. The author has an hindex of 19, co-authored 46 publications receiving 1975 citations. Previous affiliations of Alexandre Wohlkonig include Université libre de Bruxelles & VU University Amsterdam.
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Journal ArticleDOI
Characterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmission.
Elian Dupré,Alexandre Wohlkonig,Julien Herrou,Camille Locht,Françoise Jacob-Dubuisson,Rudy Antoine +5 more
TL;DR: It is proposed that a major function of the BvgS PAS domain is to maintain conformational signals arising from mechanical strain generated by the periplasmic domain.
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Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion
Romany Abskharon,Fei Wang,Alexandre Wohlkonig,Juxin Ruan,Sameh H. Soror,Sameh H. Soror,Gabriele Giachin,Els Pardon,Wen-Quan Zou,Giuseppe Legname,Jiyan Ma,Jan Steyaert +11 more
TL;DR: X-ray crystal structures of mouse (Mo) prion protein (PrP) in complex with a nanobody (Nb484) are reported, providing the first structure-function evidence supporting a crucial role of the hydrophobic region of PrP in forming an infectious prion.
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Crystallization and initial crystallographic analysis of covalent DNA-cleavage complexes of Staphyloccocus aureus DNA gyrase with QPT-1, moxifloxacin and etoposide
Velupillai Srikannathasan,Alexandre Wohlkonig,Anthony Shillings,Onkar M. P. Singh,Pan F. Chan,Jianzhong Huang,Michael N. Gwynn,Andrew P. Fosberry,Paul Homes,Martin Hibbs,Andrew J. Theobald,Claus Spitzfaden,Benjamin D. Bax +12 more
TL;DR: A G/T mismatch introduced at the ends of the DNA duplexes facilitated the crystallization of slightly asymmetric complexes of the inherently flexible DNA-cleavage complexes of S. aureus DNA gyrase.
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The Mycobacterium tuberculosis transcriptional repressor EthR is negatively regulated by Serine/Threonine phosphorylation.
Jade Leiba,Séverine Carrère-Kremer,Nicolas Blondiaux,Martin Moune Dimala,Alexandre Wohlkonig,Alain R. Baulard,Laurent Kremer,Laurent Kremer,Virginie Molle +8 more
TL;DR: It is demonstrated that the Mycobacterium tuberculosis EthR, a transcriptional repressor that regulates the activation process of the antitubercular drug ethionamide, is a specific substrate of the mycobacterial kinase PknF, and phosphorylation negatively affects its DNA-binding activity, which may impact ETH resistance levels in M. tb.
Journal ArticleDOI
Combining in-situ proteolysis and microseed matrix screening to promote crystallization of PrPc-nanobody complexes.
Romany Abskharon,Sameh H. Soror,Sameh H. Soror,Els Pardon,Hassan El Hassan,Giuseppe Legname,Jan Steyaert,Alexandre Wohlkonig +7 more
TL;DR: In-situ proteolysis with automated microseed matrix screening (MMS) is combined to crystallize two different PrP(C)-nanobody (Nb) complexes, which are single-domain antibodies derived from heavy-chain-only antibodies of camelids and could be exploited for the crystallization of other difficult antigen-antibody complexes.