4.5 Article

Evaluation of protein farnesyltransferase substrate specificity using synthetic peptide libraries

Journal

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 17, Issue 20, Pages 5548-5551

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2007.08.024

Keywords

farnesyl; protein modification; protein farnesyltransferase; peptide synthesis; fluorescence assay

Funding

  1. NCI NIH HHS [R56 CA078819, R01 CA078819, R01 CA078819-05A2, P30CA21368, CA78819] Funding Source: Medline
  2. NIGMS NIH HHS [GM40602, R01 GM040602-18A1, R01 GM040602, T32 GM145304] Funding Source: Medline

Ask authors/readers for more resources

Farnesylation, catalyzed by protein farnesyltransferase (FTase), is an important post-translational modification guiding cellular localization. Recently predictive models for identifying FTase substrates have been reported. Here we evaluate these models through screening of dansylated-GCaaS peptides, which also provides new insights into the protein substrate selectivity of FTase. (c) 2007 Elsevier Ltd. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available