Studies of synthetic peptide analogs of the amphipathic helix. Effect of charge distribution, hydrophobicity, and secondary structure on lipid association and lecithin:cholesterol acyltransferase activation.-Reference-Cited by-同舟云学术

Studies of synthetic peptide analogs of the amphipathic helix. Effect of charge distribution, hydrophobicity, and secondary structure on lipid association and lecithin:cholesterol acyltransferase activation.

Published:1987-07 Issue:19 Volume:262 Page:9389-9396
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Epand R M,Gawish A,Iqbal M,Gupta K B,Chen C H,Segrest J P,Anantharamaiah G M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. A molecular theory of lipid-protein interactions in the plasma lipoproteins

2. Studies of synthetic peptide analogs of the amphipathic helix. Structure of complexes with dimyristoyl phosphatidylcholine.

3. [36] Synthetic peptide analogs of apolipoproteins

4. Studies of synthetic peptide analogs of the amphipathic helix. Correlation of structure with function.

5. Studies of synthetic peptide analogs of the amphipathic helix. Competitive displacement of exchangeable apolipoproteins from native lipoproteins.

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