Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (649 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
Chemical agents that increase the permeability of biological or artificial lipid membranes to specific ions. Most ionophores are relatively small organic molecules that act as mobile carriers within membranes or coalesce to form ion permeable channels across membranes. Many are antibiotics, and many act as uncoupling agents by short-circuiting the proton gradient across mitochondrial membranes.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Ionophore.
Where it fits in the MeSH classification
- Broader topics
- Membrane Transport Modulators; Specialty Uses of Chemicals
- Narrower topics
- Calcium Ionophores; Potassium Ionophores; Proton Ionophores; Sodium Ionophores
- See also
- Cell Membrane Permeability
Research landscape
PubMed indexes 6,963 records tagged with the MeSH heading “Ionophores” (counts retrieved 2026-10-29). 487 of them (7.0%) were published from 2020 onward, and the busiest period so far is through 1999 with 2,970 records.
Reviews account for 226 records (3.2%) and meta-analyses for 8. Randomized controlled trials number 49 (0.7%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 2,970 |
| 2000-2009 | 2,427 |
| 2010-2019 | 1,079 |
| 2020 onward | 487 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 226 | 3.2% |
| Meta-analyses | 8 | 0.1% |
| Randomized controlled trials | 49 | 0.7% |
Method: PubMed query "Ionophores"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-29.
Reading the evidence in pharmacology
Drug evidence builds in layers: laboratory pharmacology describes how a compound acts, pharmacokinetic studies describe how the body handles it, and randomized trials test whether it helps and what harms it causes. Post-marketing surveillance and observational studies reveal rarer adverse effects but cannot prove causation. This page is educational and is not a recommendation to start, stop or change any medicine; decisions about treatment belong with a qualified clinician.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| A high quantum yield molecule-protein complex fluorophore for near-infrared II imaging | 2017 | Research article Design not recorded in structured metadata | 403 | cc by PMID 28524850 · DOI · PMC5454457 |
| Golgi organization is regulated by proteasomal degradation | 2020 | Research article Design not recorded in structured metadata | 107 | cc by PMID 31964869 · DOI · PMC6972958 |
| Superoxide drives progression of Parkin/PINK1-dependent mitophagy following translocation of Parkin to mitochondria | 2017 | Research article Design not recorded in structured metadata | 105 | cc by PMID 29022898 · DOI · PMC5680585 |
| Sunitinib enhances cuproptosis induced by copper ionophores via ROS-ATF3-SLC31A1 axis in thyroid Carcinoma | 2026 | Research article Design not recorded in structured metadata | 1 | cc by PMID 42225617 · DOI · PMC13434697 |
A high quantum yield molecule-protein complex fluorophore for near-infrared II imaging [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Fluorescence imaging in the second near-infrared window (NIR-II) allows visualization of deep anatomical features with an unprecedented degree of clarity.
- Closing excerpt
- In addition, we demonstrate that the NIR-II molecular complexes are superior to clinically approved ICG for lymph node imaging deep within the mouse body.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (150 words)
Fluorescence imaging in the second near-infrared window (NIR-II) allows visualization of deep anatomical features with an unprecedented degree of clarity. NIR-II fluorophores draw from a broad spectrum of materials spanning semiconducting nanomaterials to organic molecular dyes, yet unfortunately all water-soluble organic molecules with >1,000 nm emission suffer from low quantum yields that have limited temporal resolution and penetration depth. Here, we report tailoring the supramolecular assemblies of protein complexes with a sulfonated NIR-II organic dye (CH-4T) to produce a brilliant 110-fold increase in fluorescence, resulting in the highest quantum yield molecular fluorophore thus far. The bright molecular complex allowed for the fastest video-rate imaging in the second NIR window with ∼50-fold reduced exposure times at a fast 50 frames-per-second (FPS) capable of resolving mouse cardiac cycles. In addition, we demonstrate that the NIR-II molecular complexes are superior to clinically approved ICG for lymph node imaging deep within the mouse body.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 28524850 · DOI · PMC5454457
Golgi organization is regulated by proteasomal degradation [2]
Abstract reading summary — source excerpts
- Opening excerpt
- The Golgi is a dynamic organelle whose correct assembly is crucial for cellular homeostasis.
- Closing excerpt
- Taken together, this work reveals a mechanism of Golgi-localized proteasomal degradation, providing a functional link between proteostasis control and Golgi architecture, which may be critical in various secretion-related pathologies.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (150 words)
The Golgi is a dynamic organelle whose correct assembly is crucial for cellular homeostasis. Perturbations in Golgi structure are associated with numerous disorders from neurodegeneration to cancer. However, whether and how dispersal of the Golgi apparatus is actively regulated under stress, and the consequences of Golgi dispersal, remain unknown. Here we demonstrate that 26S proteasomes are associated with the cytosolic surface of Golgi membranes to facilitate Golgi Apparatus-Related Degradation (GARD) and degradation of GM130 in response to Golgi stress. The degradation of GM130 is dependent on p97/VCP and 26S proteasomes, and required for Golgi dispersal. Finally, we show that perturbation of Golgi homeostasis induces cell death of multiple myeloma in vitro and in vivo, offering a therapeutic strategy for this malignancy. Taken together, this work reveals a mechanism of Golgi-localized proteasomal degradation, providing a functional link between proteostasis control and Golgi architecture, which may be critical in various secretion-related pathologies.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 31964869 · DOI · PMC6972958
Superoxide drives progression of Parkin/PINK1-dependent mitophagy following translocation of Parkin to mitochondria [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Reactive oxygen species (ROS) and mitophagy are profoundly implicated in the pathogenesis of neurodegenerative diseases, such as Parkinson's disease (PD).
- Closing excerpt
- Together, our study sheds light on the link between ROS and mitophagy at a molecular level, and suggests the therapeutic potential of regulating mitophagy through the superoxide-p38-mitophagy axis.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (206 words)
Reactive oxygen species (ROS) and mitophagy are profoundly implicated in the pathogenesis of neurodegenerative diseases, such as Parkinson's disease (PD). Several studies have suggested that ROS are not involved in mitochondrial translocation of Parkin which primes mitochondria for autophagic elimination. However, whether ROS play a role in the execution of mitophagy is unknown. In the present study, we show that carbonyl cyanide m-chlorophenylhydrazone (CCCP) treatment induced both mitochondrial depolarization and generation of ROS that were needed for the mitophagy process. Cells failed to proceed to complete mitophagy if CCCP treatment was discontinued even after recruitment of Parkin and autophagy machinery to mitochondria. Notably, treatment of pro-oxidant was able to replace CCCP treatment to take mitophagy forward, while it alone was insufficient to induce translocation of Parkin to mitochondria or autophagic clearance of mitochondria. In addition, an SOD mimetic that attenuated the superoxide level suppressed mitophagy, while an SOD inhibitor accumulated cellular superoxide and promoted mitophagy. Furthermore, blockage of the p38 signaling pathway inhibited mitophagy induced by ROS, suggesting that it may contribute to the activation of ROS-mediated mitophagy. Together, our study sheds light on the link between ROS and mitophagy at a molecular level, and suggests the therapeutic potential of regulating mitophagy through the superoxide-p38-mitophagy axis.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 29022898 · DOI · PMC5680585
Sunitinib enhances cuproptosis induced by copper ionophores via ROS-ATF3-SLC31A1 axis in thyroid Carcinoma [4]
Abstract reading summary — source excerpts
- Opening excerpt
- The clinical management of advanced thyroid carcinoma presents substantial therapeutic challenges due to non-curative surgical outcomes and resistance to both radioiodine therapy and conventional chemotherapeutic agents.
- Closing excerpt
- Overall, these results demonstrate that Sunitinib and copper ionophores can induce synergistic cytotoxic effect, shedding light on therapeutic strategy for advanced thyroid carcinomas.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (143 words)
The clinical management of advanced thyroid carcinoma presents substantial therapeutic challenges due to non-curative surgical outcomes and resistance to both radioiodine therapy and conventional chemotherapeutic agents. Emerging evidence implicates copper dysregulation in thyroid cancer pathogenesis, yet monotherapy with copper ionophores demonstrates constrained efficacy due to tumor-intrinsic adaptive resistance mechanisms. In this study, we investigated the therapeutic potential of combining Sunitinib with copper ionophore Elesclomol as a novel strategy against thyroid carcinoma. Mechanically, we identified that Sunitinib treatment induces ROS accumulation, activating the stress-responsive transcription factor ATF3, which directly binds and transactivates the copper transporter gene SLC31A1. Clinically, TCGA analysis reveals SLC31A1 as a vulnerability in advanced thyroid cancer, with expression significantly downregulated in metastatic lesions, a deficit rescued by Sunitinib. Overall, these results demonstrate that Sunitinib and copper ionophores can induce synergistic cytotoxic effect, shedding light on therapeutic strategy for advanced thyroid carcinomas.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 42225617 · DOI · PMC13434697
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Biological applications of ionophores [5]
- Research article Microbial iron compounds [6]
- Research article Drug interactions at the GABA receptor-ionophore complex [7]
- Research article Transport of protons across membranes by weak acids [8]
- Research article Effect of ionophores on ruminal fermentation [9]
- Research article Ionophores: their effect on production efficiency and mode of action [10]
References
- Antaris AL, Chen H, Diao S, Ma Z, Zhang Z, Zhu S, et al.. A high quantum yield molecule-protein complex fluorophore for near-infrared II imaging. . 2017. PMID 28524850 · DOI · PMC5454457
- Eisenberg-Lerner A, Benyair R, Hizkiahou N, Nudel N, Maor R, Kramer MP, et al.. Golgi organization is regulated by proteasomal degradation. . 2020. PMID 31964869 · DOI · PMC6972958
- Xiao B, Deng X, Lim GGY, Xie S, Zhou ZD, Lim KL, et al.. Superoxide drives progression of Parkin/PINK1-dependent mitophagy following translocation of Parkin to mitochondria. . 2017. PMID 29022898 · DOI · PMC5680585
- Zhao D, Wang Y, Guan Q, Xu W, Yang Z, Li X, et al.. Sunitinib enhances cuproptosis induced by copper ionophores via ROS-ATF3-SLC31A1 axis in thyroid Carcinoma. . 2026. PMID 42225617 · DOI · PMC13434697
- Pressman BC. Biological applications of ionophores. Annu Rev Biochem. 1976. PMID 786156 · DOI
- Neilands JB. Microbial iron compounds. Annu Rev Biochem. 1981. PMID 6455965 · DOI
- Olsen RW. Drug interactions at the GABA receptor-ionophore complex. Annu Rev Pharmacol Toxicol. 1982. PMID 6282187 · DOI
- McLaughlin SG, Dilger JP. Transport of protons across membranes by weak acids. Physiol Rev. 1980. PMID 6248908 · DOI
- Russell JB, Strobel HJ. Effect of ionophores on ruminal fermentation. Appl Environ Microbiol. 1989. PMID 2650616 · DOI · PMC184044
- Bergen WG, Bates DB. Ionophores: their effect on production efficiency and mode of action. J Anim Sci. 1984. PMID 6378864 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-29.
See how EvidenceLib is built. Spotted an error? Email support@evidencehelix.com.
Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.