Melatonin Target Proteins: Too Many or Not Enough?
Open accessAbstract
The neurohormone N-acetyl-5-methoxytryptamine, better known as melatonin, is a tryptophan derivative with a wide range of biological effects that is present in many organisms. These effects are believed to rely either on the chemical properties of melatonin itself as scavenger of free radicals or on the binding of melatonin to protein targets. More than fifteen proteins, including receptors (MT1, MT2, Mel1c, CAND2, ROR, VDR), enzymes (QR2, MMP-9, pepsin, PP2A, PR-10 proteins), pores (mtPTP), transporters (PEPT1/2, Glut1) and other proteins (HBS, CaM, tubulin, calreticuline), have been suggested to interact with melatonin at sub-nanomolar to millimolar melatonin concentrations. In this review we assemble for the first time the available information on proposed melatonin targets and discuss them in a comprehensive manner to evaluate the robustness of these findings in terms of methodology, physiological relevance and independent replication.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Melatonin can bind several target proteins, including enzymes, receptors, pores, and transporters.
“For example, it has been demonstrated that melatonin can bind several target proteins, including enzymes, receptors, pores, and transporters [17].”
From Is Melatonin the “Next Vitamin D”?: A Review of Emerging Science, Clinical Uses, Safety, and Dietary Supplements (2022) · cites this paper as [17]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Trends in the Use of Complementary Health Approaches Among Adults in the United States
Jackson, C. (2015) · Holistic Nursing Practice · doi:10.1097/hnp.0000000000000088 · Cited by 1,174 · see citing works
Extrapineal melatonin: sources, regulation, and potential functions
Acuña-Castroviejo, D., Escames, G., Venegas, C., Díaz-Casado, M. E., Lima‐Cabello, E., López, L. C., Rosales‐Corral, S., Tan, D., & Reiter, R. J. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1579-2 · Cited by 1,086 · see citing works
Tan, D., Reiter, R. J., Manchester, L. C., Yan, M.-T., El-Sawi, M. R., Sainz, R. M., Mayo, J. C., Kohen, R., Allegra, M., & Hardelan, R. (2002) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026023394443 · Cited by 1,065 · see citing works
(2015) · PubMed · Cited by 926 · see citing works
Melatonin: A New Plant Hormone and/or a Plant Master Regulator?
Arnao, M. B., & Hernández‐Ruíz, J. (2018) · Trends in Plant Science · doi:10.1016/j.tplants.2018.10.010 · Cited by 903 · see citing works
New perspectives on the role of melatonin in human sleep, circadian rhythms and their regulation
Zisapel, N. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14116 · Cited by 893 · see citing works
Reppert, S. M., Godson, C., Mahle, C. D., Weaver, D. R., Slaugenhaupt, S. A., & Gusella, J. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.19.8734 · Cited by 882 · see citing works
Variants in MTNR1B influence fasting glucose levels
Prokopenko, I., Langenberg, C., Florez, J. C., Saxena, R., Soranzo, N., Þorleifsson, G., Loos, R. J. F., Manning, A. K., Jackson, A., Aulchenko, Y. S., et al. (2008) · Nature Genetics · doi:10.1038/ng.290 · Cited by 743 · see citing works
Lyssenko, V., Nagorny, C. L. F., Erdos, M. R., Wierup, N., Jonsson, A., Spégel, P., Bugliani, M., Saxena, R., Fex, M., Pulizzi, N., et al. (2009) · Nature Genetics · doi:10.1038/ng.288 · Cited by 742 · see citing works
Simonneaux, V., & Ribelayga, C. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.2.2 · Cited by 740 · see citing works
Melatonin Synthesis and Function: Evolutionary History in Animals and Plants
Zhao, D., Yu, Y., Shen, Y., Liu, Q., Zhao, Z., Sharma, R., & Reiter, R. J. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00249 · Cited by 703 · see citing works
Dubocovich, M. L., Delagrange, P., Krause, D. N., Sugden, D., Cardinali, D. P., & Olcese, J. (2010) · Pharmacological Reviews · doi:10.1124/pr.110.002832 · Cited by 636 · see citing works
Melatonin receptors: Localization, molecular pharmacology and physiological significance
Morgan, P. J., Barrett, P., Howell, H. E., & Helliwell, R. J. A. (1994) · Neurochemistry International · doi:10.1016/0197-0186(94)90100-7 · Cited by 623 · see citing works
Bouatia-Naji, N., Bonnefond, A., Cavalcanti-Proença, C., Sparsø, T., Holmkvist, J., Marchand, M., Delplanque, J., Lobbens, S., Rocheleau, G., Durand, E., et al. (2009) · Nature Genetics · doi:10.1038/ng.277 · Cited by 611 · see citing works
Identification of the Melatonin-binding SiteMT 3 as the Quinone Reductase 2
Nosjean, O., Ferro, M., Cogé, F., Beauverger, P., Henlin, J., Lefoulon, F., Fauchère, J., Delagrange, P., Canet, E., & Boutin, J. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005141200 · Cited by 604 · see citing works
Carrillo‐Vico, A., Calvo, J. R., Abreu, P. M., Lardone, P. J., García‐Mauriño, S., Reiter, R. J., & Guerrero, J. M. (2004) · The FASEB Journal · doi:10.1096/fj.03-0694fje · Cited by 457 · see citing works
Pineal gland hormone melatonin binds and activates an orphan of the nuclear receptor superfamily.
Becker-André, M., Wiesenberg, I., Schaeren‐Wiemers, N., André, E., Missbach, M., Saurat, J. ‐., & Carlberg, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61934-4 · Cited by 434 · see citing works
Expression cloning of a high-affinity melatonin receptor from Xenopus dermal melanophores.
Ebisawa, T., Karne, S., Lerner, M. R., & Reppert, S. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.6133 · Cited by 432 · see citing works
Phytomelatonin receptor PMTR 1‐mediated signaling regulates stomatal closure in Arabidopsis thaliana
Wei, J., Li, D., Zhang, J., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12500 · Cited by 432 · see citing works
Update on melatonin receptors: IUPHAR Review 20
Jockers, R., Delagrange, P., Dubocovich, M. L., Markus, R. P., Renault, N., Tosini, G., Cecon, E., & Zlotos, D. P. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13536 · Cited by 426 · see citing works
Self-citationSuofu, Y., Li, W., Jean‐Alphonse, F., Jia, J., Khattar, N. K., Li, J., Baranov, S. V., Leronni, D., Mihalik, A. C., He, Y., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705768114 · Cited by 415 · see citing works
Self-citationRare MTNR1B variants impairing melatonin receptor 1B function contribute to type 2 diabetes
The Meta-Analysis of Glucose and Insulin-Related Traits Consortium (MAGIC), Bonnefond, A., Clément, N., Fawcett, K., Yengo, L., Vaillant, E., Guillaume, J.-L., Dechaume, A., Payne, F., Roussel, R., et al. (2012) · Nature Genetics · doi:10.1038/ng.1053 · Cited by 363 · see citing works
Self-citationDietary Sources and Bioactivities of Melatonin
Meng, X., Li, Y., Li, S., Zhou, Y., Gan, R.-Y., Xu, D.-P., & Li, H.-B. (2017) · Nutrients · doi:10.3390/nu9040367 · Cited by 362 · see citing works
Davenport, A. P., Alexander, S. P. H., Sharman, J. L., Pawson, A. J., Benson, H. E., Monaghan, A. E., Liew, W. C., Mpamhanga, C. P., Bonner, T. I., Neubig, R. R., et al. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.007179 · Cited by 327 · see citing works
Andrabi, S. A., Sayeed, I., Siemen, D., Wolf, G. L., & Horn, T. F. W. (2004) · The FASEB Journal · doi:10.1096/fj.03-1031fje · Cited by 311 · see citing works
Slominski, A. T., Kim, T., Takeda, Y., Janjetović, Z., Brożyna, A. A., Skobowiat, C., Wang, J., Postlethwaite, A. E., Li, W., Tuckey, R. C., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-242040 · Cited by 271 · see citing works
Melatonin in type 2 diabetes mellitus and obesity
Karamitri, A., & Jockers, R. (2019) · Nature Reviews Endocrinology · doi:10.1038/s41574-018-0130-1 · Cited by 268 · see citing works
Self-citationHardeland, R. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8001-x · Cited by 253 · see citing works
High physiological levels of melatonin in the bile of mammals
Tan, D., Manchester, L. C., Reiter, R. J., Qi, W., Hanes, M. A., & Farley, N. J. (1999) · Life Sciences · doi:10.1016/s0024-3205(99)00519-6 · Cited by 233 · see citing works
Phytomelatonin: Recent advances and future prospects
Kanwar, M. K., Yu, J., & Zhou, J. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12526 · Cited by 214 · see citing works
Binding of 3H-melatonin to calmodulin
Benítez‐King, G., Huerto‐Delgadillo, L., & Antón‐Tay, F. (1993) · Life Sciences · doi:10.1016/0024-3205(93)90670-x · Cited by 211 · see citing works
Structural basis of ligand recognition at the human MT1 melatonin receptor
Stauch, B., Johansson, L. C., McCorvy, J. D., Patel, N., Han, G. W., Huang, X., Gati, C., Batyuk, A., Slocum, S. T., Ishchenko, A., et al. (2019) · Nature · doi:10.1038/s41586-019-1141-3 · Cited by 209 · see citing works
Melatonin Enters the Cerebrospinal Fluid through the Pineal Recess
Tricoire-Leignel, H., Locatelli, A., Chemineau, P., & Malpaux, B. (2002) · Endocrinology · doi:10.1210/endo.143.1.8585 · Cited by 206 · see citing works
Deacon, S., & Arendt, J. (1995) · Brain Research · doi:10.1016/0006-8993(95)96872-i · Cited by 203 · see citing works
Saeteaw, M., Johns, J. R., Johns, N. P., & Subongkot, S. (2012) · Journal of Pineal Research · doi:10.1111/jpi.12025 · Cited by 183 · see citing works
Melatonin and sirtuins: A “not-so unexpected” relationship
Mayo, J. C., Sainz, R. M., González Menéndez, P., Cepas, V., Tan, D., & Reiter, R. J. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12391 · Cited by 175 · see citing works
Thirty four years since the discovery of gastrointestinal melatonin.
Bubenik, G. A. (2008) · PubMed · Cited by 175 · see citing works
Carrillo‐Vico, A., Lardone, P. J., Fernández-Santos, J. M., Martín‐Lacave, I., Calvo, J. R., Karasek, M., & Guerrero, J. M. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1429 · Cited by 168 · see citing works
Reiter, R. J., Tan, D. X., Kim, S. J., & Cruz, M. H. C. (2014) · Brain Structure and Function · doi:10.1007/s00429-014-0719-7 · Cited by 163 · see citing works
Huo, X., Wang, C., Yu, Z., Peng, Y., Wang, S., Feng, S., Zhang, S., Tian, X., Sun, C., Liu, K., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12390 · Cited by 155 · see citing works
XFEL structures of the human MT2 melatonin receptor reveal the basis of subtype selectivity
Johansson, L. C., Stauch, B., McCorvy, J. D., Han, G. W., Patel, N., Huang, X., Batyuk, A., Gati, C., Slocum, S. T., Li, C., et al. (2019) · Nature · doi:10.1038/s41586-019-1144-0 · Cited by 153 · see citing works
Binding of Melatonin to Human and Rat Plasma Proteins
Cardinali, D. P., Lynch, H. J., & Wurtman, R. J. (1972) · Endocrinology · doi:10.1210/endo-91-5-1213 · Cited by 148 · see citing works
Melatonin uptake through glucose transporters: a new target for melatonin inhibition of cancer
Hevia, D., González‐Menéndez, P., Quirós-González, I., Miar, A., Rodríguez‐García, A., Tan, D. X., Reiter, R. J., Mayo, J. C., & Sainz, R. M. (2015) · Journal of Pineal Research · doi:10.1111/jpi.12210 · Cited by 144 · see citing works
Night/Day Changes in Pineal Expression of >600 Genes
Bailey, M. J., Coon, S. L., Carter, D., Humphries, A., Kim, J., Shi, Q., Gaildrat, P., Morin, F., Ganguly, S., Hogenesch, J. B., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808394200 · Cited by 142 · see citing works
Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., Zanda, M., Bode, W., & Goettig, P. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.068 · Cited by 142 · see citing works
In vitro inhibition of Ca2+/calmodulin-dependent kinase II activity by melatonin
Benítez‐King, G., Rı́os, A., Martı́nez-Hernández, A., & Antón‐Tay, F. (1996) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(96)00025-6 · Cited by 137 · see citing works
GPR50 is the mammalian ortholog of Mel1c: Evidence of rapid evolution in mammals
Dufourny, L., Levasseur, A., Migaud, M., Callebaut, I., Pontarotti, P., Malpaux, B., & Monget, P. (2008) · BMC Evolutionary Biology · doi:10.1186/1471-2148-8-105 · Cited by 136 · see citing works
Pharmacological characterization of human recombinant melatonin mt1 and MT2 receptors
Browning, C., Beresford, I. J. M., Fraser, N., & Giles, H. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703130 · Cited by 136 · see citing works
Mercolini, L., Mandrioli, R., & Raggi, M. A. (2011) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2011.00967.x · Cited by 135 · see citing works
Duncan, M. J., Takahashi, J. S., & Dubocovich, M. L. (1988) · Endocrinology · doi:10.1210/endo-122-5-1825 · Cited by 134 · see citing works
Huerto‐Delgadillo, L., Antón‐Tay, F., & Benítez‐King, G. (1994) · Journal of Pineal Research · doi:10.1111/j.1600-079x.1994.tb00114.x · Cited by 132 · see citing works
Reppert, S. M., Tsai, T., Roca, A. L., & Saumant, I. (1994) · Neuron · doi:10.1016/0896-6273(94)90054-x · Cited by 132 · see citing works
León, J., Macías, M. J., Escames, G., Camacho, E., Khaldy, H., Martı́n, M., Espinosa, A., Gallo, M. Á., & Acuña-Castroviejo, D. (2000) · Molecular Pharmacology · doi:10.1124/mol.58.5.967 · Cited by 132 · see citing works
Pontes, G. N., Cardoso, E. C., Carneiro-Sampaio, M. M. S., & Markus, R. P. (2006) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2006.00345.x · Cited by 129 · see citing works
Alluri, H., Wilson, R. L., Shaji, C. A., Wiggins-Dohlvik, K. C., Patel, S. V., Liu, Y., Peng, X., Beeram, M., Davis, M. L., Huang, J. H., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0154427 · Cited by 128 · see citing works
Melatonin inhibits matrix metalloproteinase‐9 activity by binding to its active site
Rudra, D. S., Pal, U., Maiti, N. C., Reiter, R. J., & Swarnakar, S. (2012) · Journal of Pineal Research · doi:10.1111/jpi.12034 · Cited by 125 · see citing works
Zhao, Q., Yang, X., Holtzclaw, W. D., & Talalay, P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1669 · Cited by 121 · see citing works
Evidence of melatonin synthesis and release by mast cells. Possible modulatory role on inflammation
y Aibar, M. D. M., Mora‐Santos, M., Naji, L., Carrascosa-Salmoral, M. P., Naranjo, M. C., & Calvo, J. R. (2009) · Pharmacological Research · doi:10.1016/j.phrs.2009.11.014 · Cited by 110 · see citing works
Quinone reductase 2 as a promising target of melatonin therapeutic actions
Boutin, J. A. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1091882 · Cited by 108 · see citing works
Pharmacokinetics of orally administered melatonin in critically ill patients
Mistraletti, G., Sabbatini, G., Taverna, M., Figini, M. A., Umbrello, M., Magni, P., Ruscica, M., Dozio, E., Esposti, R., Demartini, G., et al. (2010) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2009.00737.x · Cited by 108 · see citing works
Endogenous Melatonin Levels and the Fate of Exogenous Melatonin: Age Effects
Zhdanova, I. V., Wurtman, R. J., Balcioglu, A., Kartashov, A. I., & Lynch, H. J. (1998) · The Journals of Gerontology Series A · doi:10.1093/gerona/53a.4.b293 · Cited by 107 · see citing works
Chaste, P., Clément, N., Mercati, O., Guillaume, J., Delorme, R., Goubran‐Botros, H., Pagan, C., Périvier, S., Scheid, I., Nygren, G., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011495 · Cited by 103 · see citing works
Self-citationCalamini, B., Santarsiero, B. D., Boutin, J. A., & Mesecar, A. D. (2008) · Biochemical Journal · doi:10.1042/bj20071373 · Cited by 101 · see citing works
Macías, M. J., Escames, G., León, J., Coto‐Montes, A. M., Sbihi, Y., Osuna, A., & Acuña-Castroviejo, D. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03430.x · Cited by 100 · see citing works
Benítez‐King, G., Huerto‐Delgadillo, L., & Antón‐Tay, F. (1991) · Brain Research · doi:10.1016/0006-8993(91)90146-m · Cited by 96 · see citing works
High membrane permeability for melatonin
Yu, H., Dickson, E. J., Jung, S., et al. (2015) · The Journal of General Physiology · doi:10.1085/jgp.201511526 · Cited by 94 · see citing works
Melatonin identified in meats and other food stuffs: potentially nutritional impact
Tan, D. X., Zanghi, B. M., Manchester, L. C., & Reiter, R. J. (2014) · Journal of Pineal Research · doi:10.1111/jpi.12152 · Cited by 92 · see citing works
Cloning and functional analysis of a polymorphic variant of the ovine Mel 1a melatonin receptor
Barrett, P., Conway, S., Jockers, R., Strosberg, A. D., Lemaître, B. J., Delagrange, P., & Morgan, P. J. (1997) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(96)00179-6 · Cited by 81 · see citing works
Self-citationMontilla-López, P., Muñoz-Águeda, M. C., Feijóo, M., Muñoz-Castañeda, J. R., Bujalance, I., & Túnez‐Fiñana, I. (2002) · European Journal of Pharmacology · doi:10.1016/s0014-2999(02)02151-9 · Cited by 75 · see citing works
Structure-activity relationships of melatonin and related indoleamines
Heward, C. B., & Hadley, M. E. (1975) · Life Sciences · doi:10.1016/0024-3205(75)90340-9 · Cited by 74 · see citing works
Legros, C., Chesneau, D., Boutin, J. A., Barc, C., & Malpaux, B. (2014) · Journal of Neuroendocrinology · doi:10.1111/jne.12134 · Cited by 73 · see citing works
Cardinali, D. P., & Freire, F. N. (1975) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(75)90019-2 · Cited by 72 · see citing works
Lapa, M. A. P. C., Tamura, E. K., Salustiano, E. M. A., & Markus, R. P. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12066 · Cited by 72 · see citing works
Is There Sufficient Evidence that the Melatonin Binding Site MT Is Quinone Reductase 2?
Boutin, J. A., & Ferry, G. (2018) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.118.253260 · Cited by 72 · see citing works
Tryptophan consumption and indoleamines production by peritoneal cavity macrophages
Martins, E., Ferreira, A. C. F., Skorupa, A. L., Afeche, S. C., Cipolla‐Neto, J., & Rosa, L. F. B. P. C. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.1203614 · Cited by 71 · see citing works
Swarnakar, S., Mishra, A., Ganguly, K., & Sharma, A. V. (2007) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2007.00443.x · Cited by 69 · see citing works
Chaste, P., Clement, N., Botros, H. G., Guillaume, J.-L., Konyukh, M., Pagan, C., Scheid, I., Nygren, G., Anckarsäter, H., Rastam, M., et al. (2011) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2011.00902.x · Cited by 67 · see citing works
Self-citationEsposito, E., Mazzon, E., Riccardi, L., Caminiti, R., Meli, R., & Cuzzocrea, S. (2008) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2008.00572.x · Cited by 63 · see citing works
Bondi, C., McKeon, R. M., Bennett, J. M., Ignatius, P. F., Brydon, L., Jockers, R., Melan, M. A., & Witt‐Enderby, P. A. (2007) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2007.00525.x · Cited by 61 · see citing works
Self-citationGanguly, K., Maity, P., Reiter, R. J., & Swarnakar, S. (2005) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2005.00250.x · Cited by 61 · see citing works
Design and validation of the first cell‐impermeant melatonin receptor agonist
Gbahou, F., Cecon, E., Viault, G., Gerbier, R., Jean‐Alphonse, F., Karamitri, A., Guillaumet, G., Delagrange, P., Friedlander, R. M., Vilardaga, J., et al. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13856 · Cited by 61 · see citing works
Self-citationMelatonin receptor structures shed new light on melatonin research
Cecon, E., Liu, L., & Jockers, R. (2019) · Journal of Pineal Research · doi:10.1111/jpi.12606 · Cited by 60 · see citing works
Self-citationMelatonin - From Molecules to Therapy
Pandi-Perumal, S. R. (2007) · Cited by 57 · see citing works
Membrane‐bound calmodulin in Xenopus laevis oocytes as a novel binding site for melatonin
Romero, M., García‐Pergañeda, A., Guerrero, J. M., et al. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.13.1401 · Cited by 55 · see citing works
NMR and molecular dynamics studies of the interaction of melatonin with calmodulin
Turjanski, A. G., Estrin, D. A., Rosenstein, R. E., McCormick, J. E., Martin, S. R., Pastore, A., Biekofsky, R. R., & Martorana, V. (2004) · Protein Science · doi:10.1110/ps.04611404 · Cited by 54 · see citing works
Melatonin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemical studies
Ouyang, H. X., & Vogel, H. J. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00157-x · Cited by 53 · see citing works
RORα is not a receptor for melatonin (response to DOI 10.1002/bies.201600018)
Slominski, A. T., Zmijewski, M. A., & Jetten, A. M. (2016) · BioEssays · doi:10.1002/bies.201600204 · Cited by 53 · see citing works
Śliwiak, J., Sikorski, M., & Jaskólski, M. (2018) · FEBS Journal · doi:10.1111/febs.14455 · Cited by 50 · see citing works
Crystal Structure of Hyp-1, a Hypericum perforatum PR-10 Protein, in Complex with Melatonin
Śliwiak, J., Dauter, Z., & Jaskólski, M. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00668 · Cited by 49 · see citing works
Identification of a novel melatonin-binding nuclear receptor: Vitamin D receptor
Fang, N., Hu, C., Sun, W., Xu, Y., Gu, Y., Wu, L., Peng, Q., Reiter, R. J., & Liu, L. (2020) · Journal of Pineal Research · doi:10.1111/jpi.12618 · Cited by 46 · see citing works
Self-citationMelatonin Uptake by Cells: An Answer to Its Relationship with Glucose?
Mayo, J. C., Aguado, A. I. W., Cernuda‐Cernuda, R., Álvarez-Artime, A., Cepas, V., Quirós-González, I., Hevia, D., & Sainz, R. M. (2018) · Molecules · doi:10.3390/molecules23081999 · Cited by 41 · see citing works
Binding of glutathione and melatonin to human serum albumin: A comparative study
Li, X., & Wang, S. (2014) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2014.11.023 · Cited by 38 · see citing works
Pineal gland hormone melatonin binds and activates an orphan of the nuclear receptor superfamily.
Becker-André, M., Wiesenberg, I., Schaeren‐Wiemers, N., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16707 · Cited by 37 · see citing works
Pharmacogenetics of the G Protein-Coupled Receptors
Thompson, M. D., Cole, D. E. C., Capra, V., Siminovitch, K. A., Rovati, G. E., Burnham, W. M., & Rana, B. K. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-0956-8_9 · Cited by 34 · see citing works
Clément, N., Renault, N., Guillaume, J., Cecon, E., Journé, A., Laurent, X., Tadagaki, K., Cogé, F., Gohier, A., Delagrange, P., et al. (2017) · British Journal of Pharmacology · doi:10.1111/bph.14029 · Cited by 34 · see citing works
Self-citationβ-Adrenoceptors Trigger Melatonin Synthesis in Phagocytes
Lapa, M. A. P. C., Carvalho‐Sousa, C. E., Cecon, E., Fernandes, P. A. C. M., & Markus, R. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082182 · Cited by 32 · see citing works
Self-citationLajarín-Cuesta, R., Nanclares, C., Arranz-Tagarro, J.-A., González‐Lafuente, L., Arribas, R. L., de Brito, M. A., Gandı́a, L., & Rı́os, C. D. L. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00478 · Cited by 30 · see citing works
Characterization of the Mel1c melatoninergic receptor in platypus (Ornithorhynchus anatinus)
Gautier, C., Guenin, S., Riest‐Fery, I., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191904 · Cited by 30 · see citing works
Arribas, R. L., Romero, A., Egea, J., et al. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14365 · Cited by 25 · see citing works
Detection of Melatonin Production from the Intestinal Epithelium Using Electrochemical Methods
Bertrand, P., Polglaze, K., Bertrand, R. L., Sandow, S. L., & Pozo, M. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612819666131119105421 · Cited by 24 · see citing works
Hardeland, R. (2018) · Melatonin Research · doi:10.32794/mr11250005 · Cited by 24 · see citing works
Binding of glutathione and melatonin to pepsin occurs via different binding mechanisms
Li, X., & Ni, T. (2015) · European Biophysics Journal · doi:10.1007/s00249-015-1085-y · Cited by 22 · see citing works
Kim, S., & Lee, S. (2013) · Life Sciences · doi:10.1016/j.lfs.2013.11.013 · Cited by 21 · see citing works
Dupré, C., Bruno, O., Bonnaud, A., Giganti, A., Nosjean, O., Legros, C., & Boutin, J. A. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.11.022 · Cited by 21 · see citing works
GA-binding protein is involved in altered expression of ribosomal protein L32 gene
Ćurčić, D., Glibetić, M., Larson, D. E., & Sells, B. H. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19970601)65:3 · Cited by 19 · see citing works
The Binding of Methoxyindoles to Human Plasma Proteins
Laud, C. A., & Smith, I. R. (1979) · Progress in brain research · doi:10.1016/s0079-6123(08)62958-1 · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Minich, D. M., Henning, M., Darley, C., Fahoum, M., Schuler, C. B., & Frame, J. (2022) · Nutrients · doi:10.3390/nu14193934 · Cited by 176 · see citing works
“For example, it has been demonstrated that melatonin can bind several target proteins, including enzymes, receptors, pores, and transporters [17].”
Background
- Authors
- Liu, L., Labani, N., Cecon, E., & Jockers, R.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Jockers, Ralf
- Venue
- Frontiers in Endocrinology
- Publisher
- Frontiers Media SA
- Published
- 2019-11-15
- Volume
- 10
- Pages
- 791-791
- ISSN
- 1664-2392 (ISSN-L)
- PMC
- PMC6872631
- OpenAlex
- W2989558653
- Cited by
- 102
- References
- 106
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 13 · 2023: 20 · 2022: 19 · 2021: 21 · 2020: 13 · 2019: 1 · 2018: 1
- FWCI
- 1.65
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Endocrinology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Agence Nationale de la Recherche (ANR-19-CE16-0025, FRM 2019, ANR‐19)
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- Topics
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- melatonin, melatonin receptors, MT1 receptor, MT2 receptor, ROR, vitamin D receptor, MMP-9, pepsin, protein phosphatase 2A, PR-10 proteins, mitochondrial permeability transition pore, GLUT1, calmodulin, tubulin, calreticulin, protein-protein interaction
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
