Structural dynamics in cellular communication

Related content

• Projects

• Dynamics of toxin-antitoxin stress response networks: an interdisciplinarycomputational and in-vivo approach.

  Project: Fundamental

• Regulatory mechanisms in bacterial toxin-antitoxin modules

  Project: Fundamental

• Bacterial toxin-antitoxin modules as drug targets

  Project: Fundamental

• Molecular mechanisms of intrinsically disordered proteins

  Project: Fundamental

• Research output

• Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.

  Research output: Contribution to journal › Article › peer-review

• Doc of prophage P1 is inhibited by its antitoxin partner Phd though fold complementation

  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

• 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

• The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

  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

• Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding

  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

• Energetic basis of uncoupling folding from binding for an intrinsically disordered protein

  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