Dr. Adarsh Kumar

Transforming Protein Structures into Therapeutic Breakthroughs | Structural Biology | Drug Discovery | Crystallographic Fragment Screening | Molecular Biology | Biochemistry

The catalytic domain of free or ligand bound histone deacetylase 4 occurs in solution predominantly in closed conformation


Journal article


Markus Schweipert, Thomas Nehls, Anton Frühauf, Cecilé Debarnot, Adarsh Kumar, Stefan Knapp, Frederik Lermyte, Franz-Josef Meyer-Almes
Protein Science, vol. 33, 2024, pp. e4917


Cite

Cite

APA   Click to copy
Schweipert, M., Nehls, T., Frühauf, A., Debarnot, C., Kumar, A., Knapp, S., … Meyer-Almes, F.-J. (2024). The catalytic domain of free or ligand bound histone deacetylase 4 occurs in solution predominantly in closed conformation. Protein Science, 33, e4917. https://doi.org/10.1002/pro.4917


Chicago/Turabian   Click to copy
Schweipert, Markus, Thomas Nehls, Anton Frühauf, Cecilé Debarnot, Adarsh Kumar, Stefan Knapp, Frederik Lermyte, and Franz-Josef Meyer-Almes. “The Catalytic Domain of Free or Ligand Bound Histone Deacetylase 4 Occurs in Solution Predominantly in Closed Conformation.” Protein Science 33 (2024): e4917.


MLA   Click to copy
Schweipert, Markus, et al. “The Catalytic Domain of Free or Ligand Bound Histone Deacetylase 4 Occurs in Solution Predominantly in Closed Conformation.” Protein Science, vol. 33, 2024, p. e4917, doi:10.1002/pro.4917.


BibTeX   Click to copy

@article{schweipert2024a,
  title = {The catalytic domain of free or ligand bound histone deacetylase 4 occurs in solution predominantly in closed conformation},
  year = {2024},
  journal = {Protein Science},
  pages = {e4917},
  volume = {33},
  doi = {10.1002/pro.4917},
  author = {Schweipert, Markus and Nehls, Thomas and Frühauf, Anton and Debarnot, Cecilé and Kumar, Adarsh and Knapp, Stefan and Lermyte, Frederik and Meyer-Almes, Franz-Josef}
}



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