Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Biochemie     Collection: Structure Research (R. Huber)     Display Documents



  history
ID: 222095.0, MPI für Biochemie / Structure Research (R. Huber)
The typically disordered n-terminus of PKA can fold as a helix and project the myristoylation site into solution
Authors:Breitenlechner, C.; Engh, R. A.; Huber, R.; Kinzel, V.; Bossemeyer, D.; Gassel, M.
Language:English
Date of Publication (YYYY-MM-DD):2004-06-22
Title of Journal:Biochemistry
Journal Abbrev.:Biochemistry
Volume:43
Issue / Number:24
Start Page:7743
End Page:7749
Review Status:Peer-review
Audience:Not Specified
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Affiliations:MPI für Biochemie/Structure Research (Huber)
External Affiliations:German Canc Res Ctr, Dept Pathochem, D-69120 Heidelberg, Germany.; Roche Diagnost GMBH, Dept Med Chem, D-82372 Penzberg, Germany.
Identifiers:ISI:000222063900011 [ID No:1]
ISSN:0006-2960 [ID No:2]
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.