| Period | 9 Feb 2015 → 10 Feb 2015 |
|---|---|
| Event type | Other |
| Sponsor | Flanders Institute for Biotechnology |
Related content
-
Projects
-
Molecular mechanisms of intrinsically disordered proteins
Project: Fundamental
-
Regulatory mechanisms in bacterial toxin-antitoxin modules
Project: Fundamental
-
Bacterial toxin-antitoxin modules as drug targets
Project: Fundamental
-
Research output
-
Doc of prophage P1 is inhibited by its antitoxin partner Phd though fold complementation
Research output: Contribution to journal › Article › peer-review
-
Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain
Research output: Contribution to journal › Article › peer-review
-
The Intrinsically Disordered Domain of the Antitoxin Phd Chaperones the Toxin Doc Against Irreversible Inactivation and Misfolding
Research output: Contribution to journal › Article › peer-review
-
The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu
Research output: Contribution to journal › Article › peer-review
-
Disorder- and Dynamics-Based Regulatory Mechanisms in Toxin-Antitoxin Modules.
Research output: Contribution to journal › Article › peer-review
-
Driving Forces of Gyrase Recognition by the Addiction Toxin
Research output: Contribution to journal › Article › peer-review
-
Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.
Research output: Contribution to journal › Article › peer-review
-
Energetic basis of uncoupling folding from binding for an intrinsically disordered protein
Research output: Contribution to journal › Article › peer-review
-
Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding
Research output: Contribution to journal › Article › peer-review
-
Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability and influence on interactions with DNA
Research output: Contribution to journal › Article › peer-review