ArticleThe Journal of physiology1996
Activation and blockade of mouse muscle nicotinic channels by antibodies directed against the binding site of the acetylcholine receptor.
Article in The Journal of physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 38 citations in OpenAlex.
- Longitudinal Improvement in Respiratory Function Following Plasma Exchange in Patients with Severe Myasthenia Gravis.Neurocritical care · 2025Article
- A Functional Human-on-a-Chip Autoimmune Disease Model of Myasthenia Gravis for Development of Therapeutics.Frontiers in cell and developmental biology · 2021Article
- Myasthenia gravis AChR antibodies inhibit function of rapsyn-clustered AChRs.Journal of neurology, neurosurgery, and psychiatry · 2020Article
- Effect of sera from seronegative myasthenia gravis patients on neuromuscular junctions.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2013Article
- Neuronal MHC class I molecules are involved in excitatory synaptic transmission at the hippocampal mossy fiber synapses of marmoset monkeys.Cellular and molecular neurobiology · 2010Article
- Current and future standards in treatment of myasthenia gravis.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2008Review
- Progress in the treatment of myasthenia gravis.Therapeutic advances in neurological disorders · 2008Article
- Activation of heteroliganded mouse muscle nicotinic receptors.The Journal of physiology · 2005Article
- Identification of the Kv2.1 K+ channel as a major component of the delayed rectifier K+ current in rat hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. Using the patch-clamp technique, we have found that mouse muscle nicotinic acetylcholine receptor (nAChR) channels can be activated by low concentrations of a monoclonal antibody (MoAb), referred to as WF6, which is directed against the acetylcholine (ACh) binding site. Similar effects were seen using IgG or F(ab)2 fragments from the sera of patients with myasthenia gravis (MG), which contain polyclonal anti-nAChR antibodies. 2. The mean open times of MoAb and the slope conductance of single WF6-activated single channels were similar to those of ACh-activated channels under the same experimental conditions. 3. On outside-out patches, single channel activity was elicited by MoAb WF6 and MG F(ab)2 fragments, and was blocked by (+)-tubocurarine. We therefore concluded that MoAb WF6 and the MG F(ab)2 fragments activate the nAChR. 4. MoAb WF6 and MG F(ab)2 fragments blocked the current activated by pulsed application of 10(-4) M ACh to a significant extent. The block was partly reversible. The rate constants for the binding and dissociation of MoAb WF6 from the receptor were determined quantitatively.
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