The DOI matches its Crossref record; 205 of the 206 references it cites were found in a registry or an index.
Melatonin: A Mitochondrial Targeting Molecule Involving Mitochondrial Protection and Dynamics
Open accessAbstract
Melatonin has been speculated to be mainly synthesized by mitochondria. This speculation is supported by the recent discovery that aralkylamine N-acetyltransferase/serotonin N-acetyltransferase (AANAT/SNAT) is localized in mitochondria of oocytes and the isolated mitochondria generate melatonin. We have also speculated that melatonin is a mitochondria-targeted antioxidant. It accumulates in mitochondria with high concentration against a concentration gradient. This is probably achieved by an active transportation via mitochondrial melatonin transporter(s). Melatonin protects mitochondria by scavenging reactive oxygen species (ROS), inhibiting the mitochondrial permeability transition pore (MPTP), and activating uncoupling proteins (UCPs). Thus, melatonin maintains the optimal mitochondrial membrane potential and preserves mitochondrial functions. In addition, mitochondrial biogenesis and dynamics is also regulated by melatonin. In most cases, melatonin reduces mitochondrial fission and elevates their fusion. Mitochondrial dynamics exhibit an oscillatory pattern which matches the melatonin circadian secretory rhythm in pinealeocytes and probably in other cells. Recently, melatonin has been found to promote mitophagy and improve homeostasis of mitochondria.
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“Recently obtained results indicate that mitochondria play an important role in the production, metabolism, and activity of melatonin (Tan et al. 2016; Tan and Reiter 2019).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Tan et al. 2016
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2 retracted
San‐Miguel, B., Crespo, I., Sánchez, D. I., González‐Fernández, B., de Urbina, J. J. O., Tuñón, M. J., & González‐Gallego, J. (2015) · Journal of Pineal Research · doi:10.1111/jpi.12247 · Cited by 96
RetractedKashani, I. R., Rajabi, Z., Akbari, M., Hassanzadeh, G., Mohseni, A., Eramsadati, M. K., Rafiee, K., Beyer, C., Kipp, M., & Zendedel, A. (2014) · Experimental Brain Research · doi:10.1007/s00221-014-3946-5 · Cited by 56
RetractedUttara, B., Singh, A., Zamboni, P., & Mahajan, R. (2009) · Current Neuropharmacology · doi:10.2174/157015909787602823 · Cited by 3,378
Pineal Melatonin: Cell Biology of Its Synthesis and of Its Physiological Interactions*
REITER, R. J. (1991) · Endocrine Reviews · doi:10.1210/edrv-12-2-151 · Cited by 2,192
Self-citationDynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
On the origin of mitosing cells
Sagan, L. (1967) · Journal of Theoretical Biology · doi:10.1016/0022-5193(67)90079-3 · Cited by 1,870
Melatonin as an antioxidant: under promises but over delivers
Reiter, R. J., Mayo, J. C., Tan, D. X., Sainz, R. M., Alatorre-Jiménez, M. A., & Qin, L. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12360 · Cited by 1,777
Self-citationMelatonin : a potent, endogenous hydroxyl radical scavenger
Tan, D. (1993) · Endocrine Journal · Cited by 1,659
Self-citationTan, D., Manchester, L. C., Terron, M. P., Flores, L. J., & Reiter, R. J. (2007) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2006.00407.x · Cited by 1,601
Self-citationThe Haber–Weiss reaction and mechanisms of toxicity
Kehrer, J. P. (2000) · Toxicology · doi:10.1016/s0300-483x(00)00231-6 · Cited by 1,418
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Items 401–402 of 402
Mui, W.-C., Hou¹, Y.-C., Liao, Y., & Lu, K. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1960152
Lei, X., Liu, G., Duan, Y., Dong, Y., Chen, F., Li, Z., Liu, Y., & Shou, S. (2026) · Science Progress · doi:10.1177/00368504261501651
Metadata
- Authors
- Tan, D.-X., Manchester, L., Qin, L., & Reiter, R.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- Corresponding author
- Tan, Dun-Xian
- Reiter, Russel
- ORCID
- Reiter, Russel
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2016-12-16
- Volume
- 17
- Issue
- 12
- Pages
- 2124
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC5187924
- OpenAlex
- W2563008150
- Cited by
- 402
- References
- 206
- Citations by year
- 2026: 23 · 2025: 38 · 2024: 51 · 2023: 51 · 2022: 46 · 2021: 50 · 2020: 43 · 2019: 33 · 2018: 33 · 2017: 32
- FWCI
- 3.48
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Keywords
- melatonin, mitochondrial targeting, mitochondrial protection, mitochondrial dynamics, mitochondrial fission and fusion, mitochondrial biogenesis, mitochondrial permeability transition pore, uncoupling proteins, reactive oxygen species scavenging, mitochondrial membrane potential, mitophagy, acetyltransferase, oocytes, pinealocytes, circadian rhythm
- MeSH terms
- Mitochondrial Uncoupling Proteins, Mitochondrial Permeability Transition Pore, Animals, Antioxidants, Circadian Rhythm, Enzyme Activation, Humans, Melatonin, Mitochondria, Plants, Reactive Oxygen Species, Mitochondrial Membrane Transport Proteins, Membrane Potential, Mitochondrial, Mitochondrial Dynamics, Mitophagy
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