(Q33186099)

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Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes

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scholarly article

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Europe PubMed Central

PubMed publication ID

23 July 2017

Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes (English)

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

1

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Jörg Andrä

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author name string

Rosa Herbst

2

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

Matthias Leippe

3

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

language of work or name

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publication date

1 April 2003

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Europe PubMed Central

PubMed publication ID

23 July 2017

Developmental and Comparative Immunology

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Europe PubMed Central

PubMed publication ID

23 July 2017

27

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Europe PubMed Central

PubMed publication ID

23 July 2017

4

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

291-304

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Europe PubMed Central

PubMed publication ID

23 July 2017

Peptide antibiotics and their role in innate immunity

1 reference

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Antimicrobial peptides of multicellular organisms

1 reference

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Cationic peptides: a new source of antibiotics

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Magainins: a new family of membrane-active host defense peptides

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Sequence and specificity of two antibacterial proteins involved in insect immunity

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cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava

1 reference

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Antibacterial peptides from pig intestine: isolation of a mammalian cecropin

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Antimicrobial and cytolytic polypeptides of amoeboid protozoa--effector molecules of primitive phagocytes

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Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica

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Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica.

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Antisense inhibition of amoebapore expression in Entamoeba histolytica causes a decrease in amoebic virulence.

1 reference

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Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes

1 reference

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A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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Ultrasensitive assays for endogenous antimicrobial polypeptides

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Diffusion potential cascade. Convenient detection of transferable membrane pores

1 reference

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Liposomes with a large trapping capacity prepared by freezing and thawing of sonicated phospholipid mixtures

1 reference

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A molecular model of membrane excitability

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A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from Moses sole fish Pardachirus marmoratus

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Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays

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Purification and molecular cloning of a major antibacterial protein of the protozoan parasite Entamoeba histolytica with lysozyme-like properties

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Molecular characterization of an exceptionally acidic lysozyme-like protein from the protozoon Entamoeba histolytica

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Acid intracellular vesicles and the cytolysis of mammalian target cells by Entamoeba histolytica trophozoites

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Defensins: endogenous antibiotic peptides of animal cells

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Interaction of cationic antimicrobial peptides with model membranes

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Pore-forming peptide of pathogenic Entamoeba histolytica

1 reference

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Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides

1 reference

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Statistical analysis of alamethicin channels in black lipid membranes

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Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles.

1 reference

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Membrane pores induced by magainin

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Magainins as paradigm for the mode of action of pore forming polypeptides

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NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity.

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Identifiers

10.1016/S0145-305X(02)00106-4

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 July 2017

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