The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Editor

Share

Personal info

View

Links

Table of contents

About

Terms

 

Chemical Compound Review: 

AG-G-56450     2-anthracen-9- ylcarbonyloxyhexadecanoic acid

Synonyms: AC1O5BNG, CTK2F4181, 2AP Compound, 67708-96-7, 2-(9-Anthroyloxy)palmitate, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on 2AP Compound

  • Transfer of 2AP from HFABP mutants involving K22, located on alpha-helix I (alpha-I) of the helical cap region, was 3-fold slower than transfer from wild-type protein, whereas rates from a mutant involving the K59 residue, located on the beta 2-turn of the barrel near the helical cap, were 2-fold faster than those of wild type [1].
  • By using a resonance energy transfer assay, transfer of 2-(9-anthroyloxy)palmitate (2AP) from acetylated HFABP to membranes was significantly slower than transfer from native HFABP [1].
  • Transfer of 2-(9-anthroyloxy)palmitate (2AP) from acetylated A-FABP to small unilamellar vesicles (SUV) was 35-fold slower than from native protein [2].
 

Anatomical context of 2AP Compound

  • In addition, in distinct contrast to transfer from native protein, the 2AP transfer rate from acetylated HFABP was not increased to acceptor membranes of increased negative charge [1].

References

  1. Role of portal region lysine residues in electrostatic interactions between heart fatty acid binding protein and phospholipid membranes. Herr, F.M., Aronson, J., Storch, J. Biochemistry (1996) [Pubmed]
  2. Surface lysine residues modulate the collisional transfer of fatty acid from adipocyte fatty acid binding protein to membranes. Herr, F.M., Matarese, V., Bernlohr, D.A., Storch, J. Biochemistry (1995) [Pubmed]
Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities