About: Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets

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scientific article published on 01 November 1999

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1999 (uk) im November 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 November 1999 (en) artículu científicu espublizáu en payares de 1999 (ast)
publication date	wds:Q73157267-E30EDAAA-8FB1-451E-BBC4-69D18290A5E8
publication date	1999-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73157267-0FBF020B-E7A3-48EA-9014-A36AEA415128
language of work or name	English
author name string	wds:Q73157267-18E7DCC3-C8D2-4A10-BF88-FC3598C5BFEC wds:Q73157267-3DAECE3B-2D5D-40A7-8C19-7FDB47E97402 wds:Q73157267-6F60C84C-9190-424B-8F4D-BC6651A65CEC wds:Q73157267-84CB6C46-A652-4D25-B18B-A96F77603805
author name string	P Tempst A Nazarian M Castle S S Yi
rdfs:label	Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets (en) Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets (nl)
skos:prefLabel	Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets (en) Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets (nl)
name	Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets (en) Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets (nl)
title	wds:Q73157267-B4641160-D366-40AA-84D5-3C2CF70C8E02
title	Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets (en)
page(s)	wds:Q73157267-132CE119-F352-430D-91BB-650396FB7CE5
page(s)	32555-32564
instance of	wds:Q73157267-B0516E79-534B-44D0-9B89-F5A18CB61EF2
instance of	scholarly article
main subject	wds:Q73157267-15AF3E66-6584-4103-95B5-6DA1CC2D47DE wds:Q73157267-8C18AB15-2D96-43C9-B1FA-26620D1A6E7F
main subject	Escherichia coli molecular interaction
PubMed ID	wds:Q73157267-0F4288F8-3116-4090-BC28-2C23295F56AB
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10551808
PubMed ID	10551808
published in	wds:Q73157267-58286F4D-7704-4085-89FA-0621DF0220F8
published in	Journal of Biological Chemistry
issue	wds:Q73157267-DD40DE57-1A9A-4C8A-8386-3E6E5301CEA8
volume	wds:Q73157267-717C4A2C-6AC3-4760-A392-025F3CE637BF
issue	46
volume	274
DOI	wds:Q73157267-DF5B139F-D87D-46B3-B35A-4DF19765B6C7
DOI	http://dx.doi.org/10.1074/JBC.274.46.32555
DOI	10.1074/JBC.274.46.32555
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73157267
is cites work of	Cell-penetrating peptides and antimicrobial peptides: how different are they? Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action. Prediction of antibacterial activity from physicochemical properties of antimicrobial peptides. Insect antimicrobial peptides show potentiating functional interactions against Gram-negative bacteria. Through the looking glass, mechanistic insights from enantiomeric human defensins Intracellular toxicity of proline-rich antimicrobial peptides shuttled into mammalian cells by the cell-penetrating peptide penetratin Cell-penetrating antimicrobial peptides - prospectives for targeting intracellular infections Antimicrobial peptides Antimicrobial peptides: modes of mechanism, modulation of defense responses Initial Insights into Structure-Activity Relationships of Avian Defensins Dermcidin-derived peptides show a different mode of action than the cathelicidin LL-37 against Staphylococcus aureus Mirror image proteins iTRAQ-coupled 2-D LC-MS/MS analysis of membrane protein profile in Escherichia coli incubated with apidaecin IB. Antimicrobial peptides: a new class of antimalarial drugs? Two functional motifs define the interaction, internalization and toxicity of the cell-penetrating antifungal peptide PAF26 on fungal cells Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system Porphyrin-apidaecin conjugate as a new broad spectrum antibacterial agent Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C Pro-domain. In vivo target exploration of apidaecin based on Acquired Resistance induced by Gene Overexpression (ARGO assay) Non-Lytic Antibacterial Peptides That Translocate Through Bacterial Membranes to Act on Intracellular Targets An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome. Genome-wide effects of the antimicrobial peptide apidaecin on translation termination in bacteria Proline-Rich Antimicrobial Peptides in Medicinal Maggots of Lucilia sericata Interact With Bacterial DnaK But Do Not Inhibit Protein Synthesis Fragments of the Nonlytic Proline-Rich Antimicrobial Peptide Bac5 Kill Escherichia coli Cells by Inhibiting Protein Synthesis. High-level heterologous production and Functional Secretion by recombinant Pichia pastoris of the shortest proline-rich antibacterial honeybee peptide Apidaecin Bioactive Natural Peptides Glycosylated analogs of formaecin I and drosocin exhibit differential pattern of antibacterial activity Trypanosoma cruzi: synergistic cytotoxicity of multiple amphipathic anti-microbial peptides to T. cruzi and potential bacterial hosts Design of a functionally equivalent nonglycosylated analog of the glycopeptide antibiotic formaecin I.
is cites work of	wds:Q39653098-A538181A-2E29-46A0-8D79-162DCED2D157 wds:Q42121285-7D9F5D54-9179-4E97-8AA6-8CE975F29C38 wds:Q90459715-479110CC-2CB4-49DF-86A7-DD31F758A13C wds:Q33932751-74F35057-166E-4AE3-BBEF-FA8B0B1DD9B9 wds:Q37918722-0DD69CA3-E3E1-4A46-95FA-CD587808456E wds:Q39159024-5953B55F-F5C9-4ECC-B161-2032B5871D2F wds:Q39304670-CB05C966-2E02-4349-AD93-1D60DCE914F9 wds:Q35302104-5DBBA3F0-94B8-4D1A-8E71-369F6C50F02B wds:Q45045398-2AF29D33-A4A2-4BEF-8415-137616C56998 wds:Q42362914-C5F4C036-E568-46BE-A265-D4E51B760EC1 wds:Q52642991-78140599-1539-4451-88A6-2A03C629FD03 wds:Q51363895-F631C8A4-1E46-46E1-9ACB-565F314420CC wds:Q36586917-3F3D8E10-7266-40B5-9217-435B81545887 wds:Q37877177-3F589F2B-9AAC-49AC-B359-12385AAA27AB wds:Q44063337-B748C19C-43EF-4B39-9D39-5D8A01C98CEE wds:Q24652382-7FF85DF7-B340-4A54-9C05-5FE191DAE6AE wds:Q34110097-F3DC9365-A670-45B5-B65D-1D51FF5340DB wds:Q41208099-EF040CF1-60C1-4E09-AB6E-29BF665BF27E wds:Q57890248-21FEEA65-3821-4B12-9E85-DEE05E1EBE2B wds:Q55982720-3B56BAE9-A572-49E1-A98F-87532B461E0C wds:Q27318277-97F6C536-96D5-470D-8783-6F874EF26AE7 wds:Q36388148-D653FB12-6A26-472D-9659-B05A8DC46BC8

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