VOLUME 279 (2004) PAGES 33480–33491
This article has been withdrawn by the authors (although Rocío Jorge, Susana García-Vargas, and Silvia Gutiérrez-Eisman could not be reached, and Natalia Martínez passed away). The authors have become aware of errors in the preparation of Figs. 2A and 3C, where some lanes were erroneously cropped, as well as the Figs. 6A and 8A where some images appear duplicated. The authors state that although replicated experiments performed at the time of the article support the results and conclusions presented in this published paper, they consider that the responsible course of action is to withdraw the article in the interests of maintaining the publication standards of the journal. The authors apologize for any inconvenience they may have caused. The paper with the corrected figures can be obtained by contacting the authors.
Article Info
Publication History
Published online: July 20, 2018
Identification
Copyright
© 2018 by The American Society for Biochemistry and Molecular Biology, Inc.
User License
Creative Commons Attribution (CC BY 4.0) | How you can reuse 
Elsevier's open access license policy
Creative Commons Attribution (CC BY 4.0)
Permitted
- Read, print & download
- Redistribute or republish the final article
- Text & data mine
- Translate the article
- Reuse portions or extracts from the article in other works
- Sell or re-use for commercial purposes
Elsevier's open access license policy
ScienceDirect
Access this article on ScienceDirectLinked Article
- The P34G Mutation Reduces the Transforming Activity of K-Ras and N-Ras in NIH 3T3 Cells but Not of H-RasJournal of Biological ChemistryVol. 279Issue 32
- PreviewRas proteins (H-, N-, and K-Ras) operate as molecular switches in signal transduction cascades controlling cell proliferation, differentiation, or apoptosis. The interaction of Ras with its effectors is mediated by the effector-binding loop, but different data about Ras location to plasma membrane subdomains and new roles for some docking/scaffold proteins point to signaling specificities of the different Ras proteins. To investigate the molecular mechanisms for these specificities, we compared an effector loop mutation (P34G) of three Ras isoforms (H-, N-, and K-Ras4B) for their biological and biochemical properties.
- Full-Text
- Preview
