ReviewInternational journal of molecular sciences2016
Zinc as Allosteric Ion Channel Modulator: Ionotropic Receptors as Metalloproteins.
Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 50 citations in OpenAlex.
- Human CTR1 Through the Ages: Milestones and Emerging Roles in Disease and Therapy.Biomolecules · 2025Review
- Somatic Mosaicism Patterns Define Clinical-Surgical Subtypes of Focal Cortical Dysplasia Through Cell-Type-Specific Expression.medRxiv : the preprint server for health sciences · 2025Article
- Zrt-Irt-like Proteins (ZIP) Family Zinc Transporters: Emerging Players in Pancreatic β Cell Function and Insulin Regulation.The Journal of nutrition · 2025Review
- Preferential allosteric modulation of Otop1 channels by small molecule compounds.Communications biology · 2025Article
- Zinc inhibits the voltage-gated proton channel HCNL1.Biophysical journal · 2024Article
- The Concise Guide to PHARMACOLOGY 2023/24: Ion channels.British journal of pharmacology · 2023Article
- Zinc activation of OTOP proton channels identifies structural elements of the gating apparatus.eLife · 2023Article
- The Role of Zinc in Modulating Acid-Sensing Ion Channel Function.Biomolecules · 2023Review
- Interplay between ZnInternational journal of molecular sciences · 2022Review
- Control of coronary vascular resistance by eicosanoids via a novel GPCR.American journal of physiology. Cell physiology · 2022Article
- TRPM2 Non-Selective Cation Channels in Liver Injury Mediated by Reactive Oxygen Species.Antioxidants (Basel, Switzerland) · 2021Review
- Hybrid QM/MM Simulations Confirm Zn(II) Coordination Sphere That Includes Four Cysteines from the P2 × 4R Head Domain.International journal of molecular sciences · 2021Article
- Zinc is an important inter-kingdom signal between the host and microbe.Veterinary research · 2021Review
- Differential Expression of Myogenic and Calcium Signaling-Related Genes in Broilers Affected With White Striping.Frontiers in physiology · 2021Article
- New Insights of the Zn(II)-Induced P2 × 4R Positive Allosteric Modulation: Role of Head Receptor Domain SS2/SS3, E160 and D170.International journal of molecular sciences · 2020Article
- Copper-mediated thiol potentiation and mutagenesis-guided modeling suggest a highly conserved copper-binding motif in human OR2M3.Cellular and molecular life sciences : CMLS · 2020Article
- ZnScientific reports · 2019Article
- The Versatile Role of Matrix Metalloproteinase for the Diverse Results of Fibrosis Treatment.Molecules (Basel, Switzerland) · 2019Review
- Interactions of nanomaterials with ion channels and related mechanisms.British journal of pharmacology · 2019Review
- Zinc Inhibits TRPV1 to Alleviate Chemotherapy-Induced Neuropathic Pain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zinc is an essential metal to life. This transition metal is a structural component of many proteins and is actively involved in the catalytic activity of cell enzymes. In either case, these zinc-containing proteins are metalloproteins. However, the amino acid residues that serve as ligands for metal coordination are not necessarily the same in structural proteins compared to enzymes. While crystals of structural proteins that bind zinc reveal a higher preference for cysteine sulfhydryls rather than histidine imidazole rings, catalytic enzymes reveal the opposite, i.e., a greater preference for the histidines over cysteines for catalysis, plus the influence of carboxylic acids. Based on this paradigm, we reviewed the putative ligands of zinc in ionotropic receptors, where zinc has been described as an allosteric modulator of channel receptors. Although these receptors do not strictly qualify as metalloproteins since they do not normally bind zinc in structural domains, they do transitorily bind zinc at allosteric sites, modifying transiently the receptor channel's ion permeability. The present contribution summarizes current information showing that zinc allosteric modulation of receptor channels occurs by the preferential metal coordination to imidazole rings as well as to the sulfhydryl groups of cysteine in addition to the carboxyl group of acid residues, as with enzymes and catalysis. It is remarkable that most channels, either voltage-sensitive or transmitter-gated receptor channels, are susceptible to zinc modulation either as positive or negative regulators.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.