Ancient weapons: NK-lysin is a mammalian homologue to pore forming peptides of a protozoan parasite
Article Abstract:
NK-lysin, a effector molecule found in pig cytotoxic lymphocytes, is a homologue to amoebapore, a pore-forming peptide found in the parasitic protozoa Enamoeba histolytica. NK-lysin and amoebapore gene sequences are about 20-30% identical. About 44% percent of residues on NK-lysin match positions for the same residue on amoebapore. Primary structural similarities are mirrored in secondary peptide structure. Functional similarities include location in granules of the producing cells, antibacterial activity, and inefficient erythrocyte lysing. Large concentrations of each are needed to eliminate eukaryotic target cells.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Finding a partner in a crowd: neuronal diversity and synaptogenesis
Article Abstract:
A possibility was discussed that cadherins may play a vital role in synaptic specificity. The possibility was made after research findings showed that members of the cadherin family of cell-adhesion proteins are present in synapses. They are found to possess genes that are arranged in a globulin-like manner which makes them very likely candidate molecules for ensuring that neuronal diversity is used in particular, selective synaptic connections.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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A key role for TRPM7 channels in anoxic neuronal death
Article Abstract:
Research elucidates the mechanism by which excitotoxicity in brain ischemia triggers neuronal death by L-glutamate neurotransmitter. Results show that neurons under prolonged oxygen glucose deprivation causes antiexcitotoxic therapy unmasksing a death mechanism mediated by calcium permeable cation conductance, in which TRPM7 channels play an important role.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
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