Ancient weapons: NK-lysin, is a mammalian homolog to pore-forming peptides of a protozoan parasite.
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A short guided tour through functional and structural features of saposin-like proteinsIgVH genes from different anatomical regions, with different histopathological patterns, of a rheumatoid arthritis patient suggest cyclic re-entry of mature synovial B-cells in the hypermutation processLegionella pneumophila: The Paradox of a Highly Sensitive Opportunistic Waterborne Pathogen Able to Persist in the EnvironmentSaposin fold revealed by the NMR structure of NK-lysinEvolution of Cell-Autonomous Effector Mechanisms in Macrophages versus Non-Immune CellsPore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.Reciprocal Interactions between Nematodes and Their Microbial EnvironmentsPathogenesis of intestinal amebiasis: from molecules to disease.Two distinct hemolytic activities in Xenorhabdus nematophila are active against immunocompetent insect cells.Antimicrobial peptides: properties and applicability.A Sequential Model of Host Cell Killing and Phagocytosis by Entamoeba histolytica.Antimicrobial peptides and proteins of the horse--insights into a well-armed organism.Mechanisms of endotoxin neutralization by synthetic cationic compounds.The immunological functions of saposins.Peptide-based treatment of sepsis.Pore-forming toxins from pathogenic amoebae.Antimicrobial effectors in the nematode Caenorhabditis elegans: an outgroup to the Arthropoda.The invasiveness of Entamoeba histolytica - a continuing enigma.Shortened amoebapore analogs with enhanced antibacterial and cytolytic activity.Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica.Pore-forming peptides of Entamoeba dispar. Similarity and divergence to amoebapores in structure, expression and activity.Interaction of NK lysin, a peptide produced by cytolytic lymphocytes, with endotoxin.Entamoeba histolytica induces host cell death in amebic liver abscess by a non-Fas-dependent, non-tumor necrosis factor alpha-dependent pathway of apoptosisAn endogenous peptide isolated from the gut, NK-lysin, stimulates insulin secretion without changes in cytosolic free Ca2+ concentration.Molecular structures and interactions of pulmonary surfactant components.Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis.Saposin-like proteins from the intestine of the blood-feeding hookworm, Ancylostoma caninum.Biochemical characteristics of Eiseniapore, a pore-forming protein in the coelomic fluid of earthworms.Antisense inhibition of amoebapore expression in Entamoeba histolytica causes a decrease in amoebic virulence.Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis.
P2860
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P2860
Ancient weapons: NK-lysin, is a mammalian homolog to pore-forming peptides of a protozoan parasite.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh-hant
name
Ancient weapons: NK-lysin, is ...... tides of a protozoan parasite.
@en
Ancient weapons: NK-lysin, is ...... tides of a protozoan parasite.
@nl
type
label
Ancient weapons: NK-lysin, is ...... tides of a protozoan parasite.
@en
Ancient weapons: NK-lysin, is ...... tides of a protozoan parasite.
@nl
prefLabel
Ancient weapons: NK-lysin, is ...... tides of a protozoan parasite.
@en
Ancient weapons: NK-lysin, is ...... tides of a protozoan parasite.
@nl
P1433
P1476
Ancient weapons: NK-lysin, is ...... tides of a protozoan parasite.
@en
P2093
P356
10.1016/0092-8674(95)90229-5
P407
P577
1995-10-01T00:00:00Z