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Lonnie P. Wollmuth

Researcher at Stony Brook University

Publications -  91
Citations -  7326

Lonnie P. Wollmuth is an academic researcher from Stony Brook University. The author has contributed to research in topics: AMPA receptor & Gating. The author has an hindex of 36, co-authored 84 publications receiving 6325 citations. Previous affiliations of Lonnie P. Wollmuth include University of Washington & Max Planck Society.

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Glutamate Receptor Ion Channels: Structure, Regulation, and Function

TL;DR: This review discusses International Union of Basic and Clinical Pharmacology glutamate receptor nomenclature, structure, assembly, accessory subunits, interacting proteins, gene expression and translation, post-translational modifications, agonist and antagonist pharmacology, allosteric modulation, mechanisms of gating and permeation, roles in normal physiological function, as well as the potential therapeutic use of pharmacological agents acting at glutamate receptors.
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Structure, function, and allosteric modulation of NMDA receptors.

TL;DR: The relationship between NMDA receptor structure and function is reviewed with an emphasis on emerging atomic resolution structures, which begin to explain unique features of this receptor.
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Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines

TL;DR: The structure of the NMDA receptor channel M2 segment was investigated by probing the extracellular and cytoplasmic faces of cysteine-substituted NR1-NR2C channels with charged sulfhydryl-specific reagents to suggest a channel-lining loop originating and ending on the cytopLasmic side of the channel.
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Microglia actively regulate the number of functional synapses.

TL;DR: It is shown that the frequency of excitatory postsynaptic current increases in microglia-depleted brain slices, consistent with a higher synaptic density, and that this enhancement ensures from the loss ofmicroglia since it is reversed when the microglias are replenished.
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Structure and gating of the glutamate receptor ion channel

TL;DR: Crystal structures are now available for the ligand-binding domain, but the structure of the ion channel itself remains unknown, and differences are emerging in the glutamate receptor ion channel.