Page last updated: 2024-09-05

bactenecin and pyrrhocoricin protein, pyrrhocoris apterus

bactenecin has been researched along with pyrrhocoricin protein, pyrrhocoris apterus in 2 studies

Compound Research Comparison

Studies
(bactenecin)
Trials
(bactenecin)
Recent Studies (post-2010)
(bactenecin)
Studies
(pyrrhocoricin protein, pyrrhocoris apterus)
Trials
(pyrrhocoricin protein, pyrrhocoris apterus)
Recent Studies (post-2010) (pyrrhocoricin protein, pyrrhocoris apterus)
780272305

Research

Studies (2)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's2 (100.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Arenz, S; Graf, M; Innis, CA; Mardirossian, M; Nguyen, F; Pérébaskine, N; Scocchi, M; Seefeldt, AC; Wilson, DN1
Florin, T; Gagnon, MG; Lomakin, IB; Mankin, AS; Roy, RN; Steitz, TA1

Other Studies

2 other study(ies) available for bactenecin and pyrrhocoricin protein, pyrrhocoris apterus

ArticleYear
Structure of the mammalian antimicrobial peptide Bac7(1-16) bound within the exit tunnel of a bacterial ribosome.
    Nucleic acids research, 2016, Mar-18, Volume: 44, Issue:5

    Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Binding Sites; Binding, Competitive; Cattle; Crystallography, X-Ray; Erythromycin; Escherichia coli; Heteroptera; Insect Proteins; Models, Molecular; Molecular Sequence Data; Peptides, Cyclic; Protein Binding; Protein Biosynthesis; Ribosomes; RNA, Messenger; RNA, Transfer; Species Specificity; Thermus thermophilus

2016
Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition.
    Nucleic acids research, 2016, Mar-18, Volume: 44, Issue:5

    Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Binding Sites; Cattle; Crystallography, X-Ray; Escherichia coli; Insect Proteins; Models, Molecular; Molecular Sequence Data; Peptides, Cyclic; Protein Binding; Protein Biosynthesis; Ribosomes; RNA, Messenger; RNA, Transfer; Species Specificity; Thermus thermophilus

2016