Page last updated: 2024-09-05

phosphatidylcholines and pardaxin

phosphatidylcholines has been researched along with pardaxin in 5 studies

Compound Research Comparison

Studies
(phosphatidylcholines)
Trials
(phosphatidylcholines)
Recent Studies (post-2010)
(phosphatidylcholines)
Studies
(pardaxin)
Trials
(pardaxin)
Recent Studies (post-2010) (pardaxin)
32,2044435,59372012

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19901 (20.00)18.7374
1990's3 (60.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Barrow, CJ; Nakanishi, K; Tachibana, K1
Nagaraj, R; Saberwal, G2
Nir, S; Peled, R; Rapaport, D; Shai, Y1
Hallock, KJ; Lee, DK; Mosberg, HI; Omnaas, J; Ramamoorthy, A1

Other Studies

5 other study(ies) available for phosphatidylcholines and pardaxin

ArticleYear
Structure and activity studies of pardaxin and analogues using model membranes of phosphatidylcholine.
    Biochimica et biophysica acta, 1992, Dec-09, Volume: 1112, Issue:2

    Topics: Amino Acid Sequence; Chemical Phenomena; Chemistry, Physical; Electrochemistry; Fish Venoms; Isoleucine; Leucine; Lipid Bilayers; Liposomes; Lysine; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Phosphatidylcholines; Proline; Protein Structure, Secondary; Solutions; Structure-Activity Relationship

1992
A synthetic peptide corresponding to the hydrophobic amino terminal region of pardaxin can perturb model membranes of phosphatidyl choline and serine.
    Biochimica et biophysica acta, 1989, Sep-18, Volume: 984, Issue:3

    Topics: Amino Acid Sequence; Fish Venoms; Light; Membrane Lipids; Molecular Sequence Data; Peptides; Phosphatidylcholines; Phosphatidylserines; Protein Conformation; Scattering, Radiation; Spectrometry, Fluorescence; Structure-Activity Relationship

1989
Interaction of hydrophobic peptides with model membranes: slow binding to membranes and not subtle variations in pore structure is responsible for the gradual release of entrapped solutes.
    Biochimica et biophysica acta, 1993, Sep-05, Volume: 1151, Issue:1

    Topics: Amino Acid Sequence; Fish Venoms; Fluoresceins; Membranes; Molecular Sequence Data; Peptides; Phosphatidylcholines

1993
Reversible surface aggregation in pore formation by pardaxin.
    Biophysical journal, 1996, Volume: 70, Issue:6

    Topics: Amino Acid Sequence; Biophysical Phenomena; Biophysics; Cholesterol; Fish Venoms; Fluoresceins; Fluorescent Dyes; Kinetics; Liposomes; Models, Chemical; Molecular Sequence Data; Phosphatidylcholines; Phosphatidylserines; Surface Properties; Temperature

1996
Membrane composition determines pardaxin's mechanism of lipid bilayer disruption.
    Biophysical journal, 2002, Volume: 83, Issue:2

    Topics: Animals; Calorimetry, Differential Scanning; Cell Membrane; Cholesterol; Fish Venoms; Fishes; Lipid Bilayers; Magnetic Resonance Spectroscopy; Membranes; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylglycerols; Temperature

2002