A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance-Reference-Cited by-同舟云学术

A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance

Published:1993-05 Issue:2 Volume:1163 Page:209-216
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Tamamura Hirokazu,Kuroda Masataka,Masuda Masao,Otaka Akira,Funakoshi Susumu,Nakashima Hideki,Yamamoto Naoki,Waki Michinori,Matsumoto Akiyoshi,Lancelin Jean M.,Kohda Daisuke,Tate Shinichi,Inagaki Fuyuhiko,Fujii Nobutaka

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference23 articles.

1. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure.

2. Antimicrobial Peptides, Isolated from Horseshoe Crab Hemocytes, Tachyplesin II, and Polyphemusins I and II: Chemical Structures and Biological Activity1

3. Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action

4. Direct Virus Inactivation of Tachyplesin I and Its Isopeptides from Horseshoe Crab Hemocytes

5. Inhibitory Effect of Tachyplesin I on the Proliferation of Human Immunodeficiency Virus in vitro

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