dimyristoylphosphatidylglycerol has been researched along with alpha-sarcin in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (20.00) | 18.7374 |
1990's | 2 (40.00) | 18.2507 |
2000's | 2 (40.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Gasset, M; Gavilanes, JG; Martinez del Pozo, A; Oñaderra, M | 1 |
Gasset, M; Gavilanes, JG; Lacadena, J; Mancheño, JM; Martínez del Pozo, A; Oñaderra, M; Ramón, F | 1 |
Albar, JP; Gavilanes, JG; Mancheño, JM; Martínez del Pozo, A; Oñaderra, M | 1 |
Bruix, M; de Antonio, C; Gavilanes, JG; Lacadena, J; Mancheño, JM; Martínez del Pozo, A; Martínez-Ruiz, A; Oñaderra, M; Pérez-Cañadillas, JM | 1 |
Alvarez-García, E; Bruix, M; García-Ortega, L; Gavilanes, JG; Martínez del Pozo, A; Verdún, Y | 1 |
5 other study(ies) available for dimyristoylphosphatidylglycerol and alpha-sarcin
Article | Year |
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Study of the interaction between the antitumour protein alpha-sarcin and phospholipid vesicles.
Topics: Animals; Aspergillus; Binding Sites; Endoribonucleases; Fungal Proteins; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Osmolar Concentration; Phosphatidylglycerols; Phospholipids; Protein Synthesis Inhibitors; Temperature | 1989 |
Kinetic study of the aggregation and lipid mixing produced by alpha-sarcin on phosphatidylglycerol and phosphatidylserine vesicles: stopped-flow light scattering and fluorescence energy transfer measurements.
Topics: Animals; Biophysical Phenomena; Biophysics; Cattle; Endoribonucleases; Energy Transfer; Fluorescence; Fungal Proteins; In Vitro Techniques; Kinetics; Light; Lipid Bilayers; Liposomes; Membrane Fusion; Phosphatidylglycerols; Phosphatidylserines; Ribosomes; Scattering, Radiation | 1994 |
A peptide of nine amino acid residues from alpha-sarcin cytotoxin is a membrane-perturbing structure.
Topics: Amino Acid Sequence; Aspergillus; Circular Dichroism; Cytotoxins; Diphenylhexatriene; Endoribonucleases; Fluorescence Polarization; Fluorescent Dyes; Fungal Proteins; Lipid Bilayers; Liposomes; Membrane Lipids; Peptide Fragments; Phosphatidylglycerols; Protein Conformation; Protein Structure, Secondary; Spectrometry, Fluorescence; Trifluoroethanol | 1998 |
Assignment of the contribution of the tryptophan residues to the spectroscopic and functional properties of the ribotoxin alpha-sarcin.
Topics: Anthracenes; Circular Dichroism; Cytotoxins; Endoribonucleases; Fluorescence Polarization; Fungal Proteins; Hot Temperature; Models, Molecular; Molecular Probes; Mutation; Mycotoxins; Nuclear Magnetic Resonance, Biomolecular; Phosphatidylglycerols; Protein Conformation; Protein Denaturation; Protein Synthesis Inhibitors; Recombinant Proteins; Spectrophotometry, Ultraviolet; Tryptophan | 2000 |
Tyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of alpha-sarcin.
Topics: Circular Dichroism; Endoribonucleases; Fungal Proteins; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Mutant Proteins; Phenylalanine; Phosphatidylglycerols; Protein Denaturation; Protein Structure, Tertiary; RNA, Fungal; Spectrometry, Fluorescence; Structure-Activity Relationship; Tyrosine | 2006 |