English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

The typically disordered n-terminus of PKA can fold as a helix and project the myristoylation site into solution

MPS-Authors
/persons/resource/persons77810

Breitenlechner,  C.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77940

Engh,  R. A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Breitenlechner, C., Engh, R. A., Huber, R., Kinzel, V., Bossemeyer, D., & Gassel, M. (2004). The typically disordered n-terminus of PKA can fold as a helix and project the myristoylation site into solution. Biochemistry, 43(24), 7743-7749.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-6908-6
Abstract
There is no abstract available