Page last updated: 2024-08-17

histidine and alloferon

histidine has been researched along with alloferon in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's3 (75.00)24.3611
2020's1 (25.00)2.80

Authors

AuthorsStudies
Kowalik-Jankowska, T; Kuczer, M; Pietruszka, M1
Czarniewska, E; Kowalik-Jankowska, T; Kuczer, M; Matusiak, A; Rosiński, G1
Czarniewska, E; Kowalik-Jankowska, T; Kuczer, M; Matusiak, A; Rosiński, G; Urbański, A1
Draghi, S; Dudek, D; Matera-Witkiewicz, A; Mikołajczyk, A; Miller, A; Rowińska-Żyrek, M; Stokowa-Sołtys, K; Valensin, D; Witkowska, D1

Other Studies

4 other study(ies) available for histidine and alloferon

ArticleYear
Copper(II) complex formation processes of alloferon I with point mutation H1K; combined spectroscopic and potentiometric studies.
    Journal of inorganic biochemistry, 2012, Volume: 111

    Topics: Acetylation; Amino Acid Sequence; Copper; Histidine; Hydrogen-Ion Concentration; Kinetics; Lysine; Mass Spectrometry; Molecular Structure; Mutant Proteins; Organomercury Compounds; Peptides; Point Mutation; Potentiometry; Protons; Spectrophotometry

2012
Copper(II) complexes of alloferon 1 with point mutations (H1A) and (H9A) stability structure and biological activity.
    Journal of inorganic biochemistry, 2014, Volume: 138

    Topics: Amino Acid Sequence; Animals; Apoptosis; Coordination Complexes; Copper; Drug Stability; Heart; Hemocytes; Histidine; Male; Monophenol Monooxygenase; Organometallic Compounds; Peptides; Point Mutation; Tenebrio

2014
Copper(II) complexes of terminally free alloferon peptide mutants containing two different histidyl (H(1) and H(6) or H(9) or H(12)) binding sites Structure Stability and Biological Activity.
    Journal of inorganic biochemistry, 2015, Volume: 151

    Topics: Animals; Apoptosis; Binding Sites; Coleoptera; Coordination Complexes; Copper; Drug Stability; Enzyme Activation; Histidine; Molecular Structure; Monophenol Monooxygenase; Mutation; Peptides

2015
Zn(II)-alloferon complexes - Similar sequence, different coordination modes, no antibacterial activity.
    Journal of inorganic biochemistry, 2020, Volume: 213

    Topics: Amino Acid Sequence; Anti-Bacterial Agents; Coordination Complexes; Histidine; Ligands; Mass Spectrometry; Microbial Sensitivity Tests; Peptides; Proton Magnetic Resonance Spectroscopy; Structure-Activity Relationship; Thermodynamics; Zinc

2020