The DOI matches its Crossref record; 62 of the 67 references it cites were found in a registry or an index, and 5 are not checked yet.
Leptin signaling
Open accessAbstract
Leptin is secreted by adipose tissue and regulates energy homeostasis, glucose and lipid metabolism, immune function, and other systems. The binding of leptin to its specific receptor activates various intracellular signaling pathways, including Janus kinase 2 (JAK2)/ signal transducer and activator of transcription 3 (STAT3), insulin receptor substrate (IRS)/phosphatidylinositol 3 kinase (PI3K), SH2-containing protein tyrosine phosphatase 2 (SHP2)/mitogen-activated protein kinase (MAPK), and 5' adenosine monophosphate-activated protein kinase (AMPK)/ acetyl-CoA carboxylase (ACC), in the central nervous system and peripheral tissues. Understanding of leptin signaling provides insights into its roles in health and disease.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Leptin binds to its specific receptor, LepRb, on cells in the central nervous system (CNS) and peripheral tissues, including skeletal muscle, placenta, ovary, pituitary gland, and lymphoid tissue”
From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as Park and Ahima, 2014
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Leptin Induces CD40 Expression through the Activation of Akt in Murine Dendritic Cells
Lam, Q. L. K., Zheng, B., Jin, D., Cao, X., & Lu, L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704579200 · Cited by 41
RetractedLeptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
Minokoshi, Y., Kim, Y.-B., Peroni, O. D., Fryer, L. G. D., Müller, C., Carling, D., & Kahn, B. B. (2002) · Nature · doi:10.1038/415339a · Cited by 2,053
AMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus
Minokoshi, Y., Alquier, T., Furukawa, N., Kim, Y.-B., Lee, A., Xue, B., Mu, J., Foufelle, F., Ferré, P., Birnbaum, M. J., et al. (2004) · Nature · doi:10.1038/nature02440 · Cited by 1,637
Hypothalamic mTOR Signaling Regulates Food Intake
Cota, D., Proulx, K., Smith, K. A. B., Kozma, S. C., Thomas, G., Woods, S. C., & Seeley, R. J. (2006) · Science · doi:10.1126/science.1124147 · Cited by 1,278
STAT3 signalling is required for leptin regulation of energy balance but not reproduction
Bates, S. H., Stearns, W. H., Dundon, T. A., Schubert, M., Tso, A. W. K., Wang, Y., Banks, A. S., Lavery, H. J., Haq, A. K., Maratos-Flier, E., et al. (2003) · Nature · doi:10.1038/nature01388 · Cited by 1,010 · cited 2×
“STAT3-mediated signaling are involved in leptin ’ s effect on glucose homeostasis [8,11,13].”
BackgroundNarrative Review: The Role of Leptin in Human Physiology: Emerging Clinical Applications
Kelesidis, T., Kelesidis, I., Chou, S. H.-H., & Mantzoros, C. S. (2010) · Annals of Internal Medicine · doi:10.7326/0003-4819-152-2-201001190-00008 · Cited by 693
A Key Role of Leptin in the Control of Regulatory T Cell Proliferation
Rosa, V. D., Procaccini, C., Calı̀, G., Pirozzi, G., Fontana, S., Zappacosta, S., Cava, A. L., & Matarese, G. (2007) · Immunity · doi:10.1016/j.immuni.2007.01.011 · Cited by 646
Key enzyme in leptin-induced anorexia
Niswender, K. D., Morton, G. J., Stearns, W. H., Rhodes, C. J., Myers, M. G., & Schwartz, M. W. (2001) · Nature · doi:10.1038/35101657 · Cited by 585
Recent advances in understanding leptin signaling and leptin resistance
Morris, D. L., & Rui, L. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00274.2009 · Cited by 484
Forkhead protein FoxO1 mediates Agrp-dependent effects of leptin on food intake
Kitamura, T., Feng, Y., Kitamura, Y., Chua, S. C., Xu, A. W., Barsh, G. S., Rossetti, L., & Accili, D. (2006) · Nature Medicine · doi:10.1038/nm1392 · Cited by 458
Flagged first, then by citations
Cited by
Sorted by citations
The mechanistic target of rapamycin: the grand conducTOR of metabolism and aging
Kennedy, B. K., & Lamming, D. W. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.009 · Cited by 544
Bharadwaj, U., Kasembeli, M. M., Robinson, P., & Tweardy, D. J. (2020) · Pharmacological Reviews · doi:10.1124/pr.119.018440 · Cited by 314
STAT3 in the systemic inflammation of cancer cachexia
Zimmers, T. A., Fishel, M. L., & Bonetto, A. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.02.009 · Cited by 231
Leptin action in normal and pathological pregnancies
Pérez‐Pérez, A., Toro, A. R., Vilariño‐García, T., Maymó, J. L., Guadix, P., Dueñas, J. L., Sánchez, M. F., Varone, C. L., & Sánchez‐Margalet, V. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13369 · Cited by 217
Lysosome: The metabolic signaling hub
Lamming, D. W., & Bar‐Peled, L. (2019) · Traffic · doi:10.1111/tra.12617 · Cited by 173
The central moTOR of metabolism
Simcox, J., & Lamming, D. W. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.02.024 · Cited by 174
Molecular Mechanisms of Cancer-Induced Sleep Disruption
Walker, W. H., II, & Borniger, J. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112780 · Cited by 149
Barnes, M. A., Carson, M. J., & Nair, M. G. (2015) · Cytokine · doi:10.1016/j.cyto.2015.01.008 · Cited by 110
Cognitive and autonomic determinants of energy homeostasis in obesity
Richard, D. (2015) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.103 · Cited by 113
Rocca, A., Moscato, S., Ronca, F., Nitti, S., Mattoli, V., Gıorgı, M., & Ciofani, G. (2015) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2015.05.001 · Cited by 102
Leptin in Atherosclerosis: Focus on Macrophages, Endothelial and Smooth Muscle Cells
Raman, P., & Khanal, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115446 · Cited by 99
Role of Leptin in Non-Alcoholic Fatty Liver Disease
Jiménez‐Cortegana, C., García-Galey, A., Tami, M., Bellido, P. D. P., Carmona, I., López, S., Álba, G., & Sánchez‐Margalet, V. (2021) · Biomedicines · doi:10.3390/biomedicines9070762 · Cited by 100
Exploring the emerging complexity in transcriptional regulation of energy homeostasis
Lempradl, A. M., Pospisilik, J. A., & Penninger, J. M. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3941 · Cited by 100
Adipocytes, aldosterone and obesity-related hypertension
Cat, A. N. D., Friederich‐Persson, M., White, A. D., & Touyz, R. M. (2016) · Journal of Molecular Endocrinology · doi:10.1530/jme-16-0025 · Cited by 94
Shpakov, A. O., Derkach, K. V., & Berstein, L. M. (2015) · Future Science OA · doi:10.4155/fso.15.23 · Cited by 93
Gao, Q., Jia, Y., Yang, G., Zhang, X., Boddu, P. C., Petersen, B. E., Narsingam, S., Zhu, Y.-J., Thimmapaya, B., Kanwar, Y. S., et al. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.01.018 · Cited by 93
Leptin and Nutrition in Gestational Diabetes
Pérez‐Pérez, A., Vilariño‐García, T., Guadix, P., Dueñas, J. L., & Sánchez‐Margalet, V. (2020) · Nutrients · doi:10.3390/nu12071970 · Cited by 95
Beneficial Effects of Anti-Inflammatory Diet in Modulating Gut Microbiota and Controlling Obesity
Bagheri, S., Zolghadri, S., & Stanek, A. (2022) · Nutrients · doi:10.3390/nu14193985 · Cited by 98
Diminished mTOR signaling: a common mode of action for endocrine longevity factors
Lamming, D. W. (2014) · SpringerPlus · doi:10.1186/2193-1801-3-735 · Cited by 71
Leptin in osteoarthritis and rheumatoid arthritis: Player or bystander?
Ait Eldjoudi, D., Cordero Barreal, A., Gonzalez-Rodríguez, M., Ruiz-Fernández, C., Farrag, Y., Farrag, M., Lago, F., Capuozzo, M., Gonzalez-Gay, M. A., Mera Varela, A., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052859 · Cited by 72
Coronell‐Tovar, A., Pardo, J. P., Rodríguez‐Romero, A., Sosa‐Peinado, A., Vásquez-Bochm, L. X., Cano‐Sánchez, P., Álvarez‐Añorve, L. I., & González‐Andrade, M. (2024) · FEBS Letters · doi:10.1002/1873-3468.14901 · Cited by 72
The role of leptin and obesity on male infertility
Khodamoradi, K., Parmar, M., Khosravizadeh, Z., Kuchakulla, M., Manoharan, M., & Arora, H. (2020) · Current Opinion in Urology · doi:10.1097/mou.0000000000000762 · Cited by 69
Leptin, Both Bad and Good Actor in Cancer
Jiménez‐Cortegana, C., López-Saavedra, A., Sánchez-Jiménez, F., Pérez‐Pérez, A., Castiñeiras, J., Virizuela-Echaburu, J. A., de la Cruz‐Merino, L., & Sánchez‐Margalet, V. (2021) · Biomolecules · doi:10.3390/biom11060913 · Cited by 69
Modulation of leptin resistance by food compounds
Aragonès, G., Ardid‐Ruiz, A., Ibars, M., Suárez, M., & Bladé, C. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500964 · Cited by 69
STAT3: The art of multi-tasking of metabolic and immune functions in obesity
Hu, W., Lv, J., Han, M., Yang, Z. P., Li, T. X., Jiang, S., & Yang, Y. (2018) · Progress in Lipid Research · doi:10.1016/j.plipres.2018.04.002 · Cited by 64
Zhang, B., Yang, L., Zeng, Z., Feng, Y., Wang, X., Wu, X., Luo, H., Zhang, J., Zhang, M., Pakvasa, M., et al. (2020) · Stem Cells and Development · doi:10.1089/scd.2019.0292 · Cited by 63
Li, C., Meng, F., Lei, Y., Liu, J., Liu, J., Zhang, J., Liu, F., Liu, C., Guo, M., & Lu, X. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-00922-0 · Cited by 62
Derkach, K. V., Zakharova, I. O., Zorina, I. I., Bakhtyukov, A. A., Romanova, I. V., Bayunova, L. V., & Shpakov, A. O. (2019) · PLoS ONE · doi:10.1371/journal.pone.0213779 · Cited by 60
Bhardwaj, P., Iyengar, N. M., Zahid, H., Carter, K. M., Byun, D. J., Choi, M. H., Sun, Q., Savenkov, O., Louka, C., Liu, C., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.ade1857 · Cited by 58
Leptin signaling and leptin resistance
Liu, J., Lai, F., Hou, Y., & Zheng, R. (2022) · Medical Review · doi:10.1515/mr-2022-0017 · Cited by 61
A Review of Recent Developments in the Molecular Mechanisms of Bone Healing
Rodriguez-Merchan, E. C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020767 · Cited by 57
Leptin as a Key between Obesity and Cardiovascular Disease
Kang, K., Ok, M., & Lee, S. (2020) · Journal of Obesity & Metabolic Syndrome · doi:10.7570/jomes20120 · Cited by 53
Leptin in normal physiology and leptin resistance
Li, S., & Li, X. (2015) · 中国科学通报:英文版 · doi:10.1007/s11434-015-0951-4 · Cited by 52
The Role of Adipokines in Intervertebral Disc Degeneration
Sharma, A. (2018) · Medical Sciences · doi:10.3390/medsci6020034 · Cited by 51
Adlanmérini, M., Nguyen, H. C. B., Krusen, B. M., Teng, C. W., Geisler, C. E., Peed, L. C., Carpenter, B. J., Hayes, M. R., & Lazar, M. A. (2020) · Journal of Clinical Investigation · doi:10.1172/jci140424 · Cited by 52
Exploring the Homeostatic and Sensory Roles of the Immune System
Marques, R. E., Marques, P. E., Guabiraba, R., & Teixeira, M. M. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00125 · Cited by 52
Leptin-Activity Modulators and Their Potential Pharmaceutical Applications
Greco, M., Santo, M. D., Comandé, A., Belsito, E. L., Andò, S., Liguori, A., & Leggio, A. (2021) · Biomolecules · doi:10.3390/biom11071045 · Cited by 49
Metabolic Impact on the Hypothalamic Kisspeptin-Kiss1r Signaling Pathway
Wahab, F., Atika, B., Ullah, F., Shahab, M., & Behr, R. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00123 · Cited by 48
Saeidi, A., Haghighi, M. M., Kolahdouzi, S., Daraei, A., Abderrahman, A. B., Essop, M. F., Laher, I., Hackney, A. C., & Zouhal, H. (2020) · Obesity Reviews · doi:10.1111/obr.13090 · Cited by 50
la Paz, S. M., Pérez‐Pérez, A., Vilariño‐García, T., Jiménez‐Cortegana, C., Muriana, F. J. G., Millán-Linares, M. C., & Sánchez‐Margalet, V. (2020) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2020.108561 · Cited by 46
Novel Biomolecules in the Pathogenesis of Gestational Diabetes Mellitus
Ruszała, M., Niebrzydowska-Tatus, M., Pilszyk, A., Kimber-Trojnar, Ż., Trojnar, M. P., & Leszczyńska‐Gorzelak, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111578 · Cited by 47
Kudo, M., Yoshitomi, H., Momoo, M., Suguro, S., Yamagishi, Y., & Gao, M. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b16-01002 · Cited by 44
Melnik, B. C., John, S. M., Carrera‐Bastos, P., & Schmitz, G. (2020) · Cancers · doi:10.3390/cancers12082111 · Cited by 44
Regulation of placental amino acid transport in health and disease
Shimada, H., Powell, T. L., & Jansson, T. (2024) · Acta Physiologica · doi:10.1111/apha.14157 · Cited by 47
Koskinen-Kolasa, A., Vuolteenaho, K., Korhonen, R., Moilanen, T. P. S., & Moilanen, E. (2016) · Arthritis Research & Therapy · doi:10.1186/s13075-016-1112-0 · Cited by 42
Babaei, S., Sáez-Arteaga, A., Caballero‐Solares, A., Fernández, F., Baanante, I. V., & Metón, I. (2016) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2016.10.003 · Cited by 40
D’Occhio, M. J., Campanile, G., & Baruselli, P. S. (2020) · Biology of Reproduction · doi:10.1093/biolre/ioaa135 · Cited by 41
New Actors Driving the Epithelial–Mesenchymal Transition in Cancer: The Role of Leptin
Olea‐Flores, M., Juárez-Cruz, J. C., Zuñiga‐Eulogio, M. D., Acosta, E., García-Rodríguez, E., Zacapala-Gómez, A. E., Catalán, M. A. M., Ortiz‐Ortiz, J., Ortuño‐Pineda, C., & Navarro‐Tito, N. (2020) · Biomolecules · doi:10.3390/biom10121676 · Cited by 41
20years of leptin: Role of leptin in cardiomyocyte physiology and physiopathology
Feijóo‐Bandín, S., Portolés, M., Roselló‐Lletí, E., Rivera, M., González‐Juanatey, J. R., & Lago, F. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.02.016 · Cited by 39
Niwczyk, O., Grymowicz, M., Szczęsnowicz, A., Hajbos, M., Kostrzak, A., Budzik, M. P., Maciejewska-Jeske, M., Bala, G., Smolarczyk, R., & Męczekalski, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076840 · Cited by 39
Pregnancy-induced adaptation of central sensitivity to leptin and insulin
Aung, Z. K., Grattan, D. R., & Ladyman, S. R. (2020) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2020.110933 · Cited by 57
Sato, A., Kamekura, R., Kawata, K., Kawada, M., Jitsukawa, S., Yamashita, K., Sato, N., Himi, T., & Ichimiya, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158408 · Cited by 33
Freitag, H., Christen, F., Lewens, F., Grass, I., Briest, F., Iwaszkiewicz, S., Siegmund, B., & Grabowski, P. (2016) · Neuroendocrinology · doi:10.1159/000448843 · Cited by 34
Translating Mechanism-Based Strategies to Break the Obesity−Cancer Link: A Narrative Review
Smith, L. A., O’Flanagan, C. H., Bowers, L. W., Allott, E. H., & Hursting, S. D. (2017) · Journal of the Academy of Nutrition and Dietetics · doi:10.1016/j.jand.2017.08.112 · Cited by 33
SUMO-specific protease 2 mediates leptin-induced fatty acid oxidation in skeletal muscle
Koo, Y. D., Lee, J. S., Lee, S., Quaresma, P. G. F., Bhat, R. V., Haynes, W. G., Park, Y. J., Kim, Y., Chung, S. S., & Park, K. S. (2019) · Metabolism · doi:10.1016/j.metabol.2019.03.004 · Cited by 30
Ignatieva, E. V., Afonnikov, D. A., Saik, O., Rogaev, E. I., & Kolchanov, N. A. (2016) · BMC Genetics · doi:10.1186/s12863-016-0466-2 · Cited by 28
Guan, D., Men, Y., Bartlett, A., Hernández, M. A. S., Xu, J., Yi, X., Li, H.-S., Kong, D., Mazitschek, R., & Özcan, U. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.02.007 · Cited by 28
Ma, S., Zhang, K., Shi, S., Li, X., Che, C., Chen, P., & Liu, H. (2022) · Poultry Science · doi:10.1016/j.psj.2022.102441 · Cited by 27
Ritze, Y., Schollenberger, A. E., Sinno, M. H., Bühler, N. E. M., Böhle, M., Bárdos, G., Sauer, H., Mack, I., Enck, P., Zipfel, S., et al. (2016) · Neurogastroenterology & Motility · doi:10.1111/nmo.12773 · Cited by 26
de Lima, R. M. S., Barth, B., Arcego, D. M., Filho, E. J. D. M., Patel, S. H., Wang, Z., Pokhvisneva, I., Parent, C. I., Levitan, R. D., Kobor, M. S., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03992-8 · Cited by 23
Khoramipour, K., Rezaei, M. H., Madadizadeh, E., Hosseini, M. S., Soltani, Z., Schierbauer, J., & Moser, O. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01421-w · Cited by 23
Xu, J., Chen, L., Tang, L., Chang, L., Liu, S., Tan, J., Chen, Y., Ren, Y., Liang, F., & Cui, J. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0667-7 · Cited by 22
Altered intestinal neuroendocrine gene expression in humans with obesity
Ritze, Y., Hengelhaupt, C., Bárdos, G., Ernst, B., Thurnheer, M., D’Haese, J. G., Bischoff, S. C., & Schultes, B. (2015) · Obesity · doi:10.1002/oby.21253 · Cited by 23
Molecular targeting of obesity pathways in cancer
Surmacz, E., & Otvos, L. J. (2015) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2015-0007 · Cited by 22
Choi, J., Kim, M.-K., Yeo, S., & Kim, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-78166-9 · Cited by 22
Zhang, X., Tian, L., Majumdar, A., & Scheller, E. L. (2024) · Comprehensive physiology · doi:10.1002/cphy.c230016 · Cited by 23
Overexpression of Na+/Mg2+ exchanger SLC41A1 attenuates pro-survival signaling
Sponder, G., Abdulhanan, N., Fröhlich, N., Mastrototaro, L., Aschenbach, J. R., Röntgen, M., Pilchová, I., Cibulka, M., Račay, P., & Kolísek, M. (2017) · Oncotarget · doi:10.18632/oncotarget.23598 · Cited by 21
Pražienková, V., Funda, J., Pirník, Z., Karnošová, A., Hrubá, L., Kořínková, L., Neprašová, B., Janovská, P., Benzce, M., Kadlecová, M., et al. (2021) · Gene · doi:10.1016/j.gene.2021.145427 · Cited by 20
Reschke, L. D., Afrin, S., Sabah, M. E., Charewycz, N., Miyashita‐Ishiwata, M., & Borahay, M. A. (2022) · F&S Science · doi:10.1016/j.xfss.2022.05.001 · Cited by 19
Zhang, X., Tian, L., Majumdar, A., & Scheller, E. L. (2024) · Comprehensive Physiology · doi:10.1002/j.2040-4603.2024.tb00300.x · Cited by 18
JAK inhibitors: an evidence-based choice of the most appropriate molecule
Antonioli, L., Armuzzi, A., Fantini, M. C., & Fornai, M. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1494901 · Cited by 18
Kang, N., Oh, S., Kim, S.-Y., Ahn, H., Son, M., Heo, S., Byun, K., & Jeon, Y. (2021) · Algal Research · doi:10.1016/j.algal.2021.102533 · Cited by 18
miRNA and leptin signaling in metabolic diseases and at extreme environments
Mondal, S., Rathor, R., Singh, S. N., & Suryakumar, G. (2024) · Pharmacology Research & Perspectives · doi:10.1002/prp2.1248 · Cited by 18
Jiménez‐Cortegana, C., Gutiérrez‐García, C., Sánchez-Jiménez, F., Vilariño‐García, T., Flores-Campos, R., Pérez‐Pérez, A., Garnacho, C., Sánchez‐León, M., García-Domínguez, D. J., Hontecillas‐Prieto, L., et al. (2024) · International Journal of Oncology · doi:10.3892/ijo.2024.5667 · Cited by 17
Awèdé, B., Adovoekpe, D., Adehan, G., MacFarlane, N. G., Azonbakin, S. A., Dossou, E., Amoussou-Guenou, M., & Djrolo, F. (2018) · Physiological Reports · doi:10.14814/phy2.13718 · Cited by 17
Kusuhara, M., Maruyama, K., Ishii, H., Masuda, Y., Sakurai, K., Tamai, E., & Urakami, K. (2019) · Integrative Cancer Therapies · doi:10.1177/1534735419845139 · Cited by 17
Leptin: an unappreciated key player in SLE
Yuan, Q., Chen, H., Li, X., & Wei, J. (2019) · Clinical Rheumatology · doi:10.1007/s10067-019-04831-8 · Cited by 18
Leptin and Its Role in Oxidative Stress and Apoptosis: An Overview
Gelen, V., Kükürt, A., Şengül, E., & Deveci, H. A. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.101237 · Cited by 16
Adipocyte and Adipokines Promote a Uterine Leiomyoma Friendly Microenvironment
Afrin, S., Ramaiyer, M. S., Begum, U. A. M., & Borahay, M. A. (2023) · Nutrients · doi:10.3390/nu15030715 · Cited by 16
Murayama, S., Yamamoto, K., Fujita, S., Takei, H., Inui, T., Ogiso, B., & Kobayashi, M. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.02.021 · Cited by 15
Alkhaleq, H. A., Kornowski, R., Waldman, M., Levy, E., Zemel, R. R., Nudelman, V., Shainberg, A., Miskin, R., & Hochhauser, E. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112373 · Cited by 15
Adipokines regulate mesenchymal stem cell osteogenic differentiation
Xu, Z., Xiong, C.-W., Miao, K., Yu, Z.-T., Zhang, J., Yu, C., Huang, Y., & Zhou, X. (2023) · World Journal of Stem Cells · doi:10.4252/wjsc.v15.i6.502 · Cited by 15
Carey, A. N., Pintea, G. I., Leuven, S. V., Gildawie, K. R., Squiccimara, L., Fine, E., Rovnak, A., & Harrington, M. (2019) · Nutritional Neuroscience · doi:10.1080/1028415x.2019.1641284 · Cited by 14
Alkhaleq, H. A., Kornowski, R., Waldman, M., Zemel, R. R., Lev, D., Shainberg, A., Miskin, R., & Hochhauser, E. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112647 · Cited by 15
Tawfik, M. K., Badran, D. I., Keshawy, M. M., Makary, S., & Abdo, M. (2022) · Archives of Medical Science · doi:10.5114/aoms/158534 · Cited by 14
Chronic exposure to methylmercury enhances the anorexigenic effects of leptin in C57BL/6J male mice
Ferrer, B., Prince, L. M., Tinkov, A. A., Santamarı́a, A., Farina, M., da Rocha, J. B. T., Bowman, A. B., & Aschner, M. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111924 · Cited by 14
Weight Regain after Metabolic Surgery: Beyond the Surgical Failure
Salazar, J. J., Durán, P., Garrido, B., Parra, H., Hernández, M., Cano, C., Áñez, R., García-Pacheco, H., Cubillos-Valencia, G., Vasquez, N., et al. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13041143 · Cited by 14
Hammersjö, R., Roth, B., Höglund, P., & Ohlsson, B. (2016) · The Review of Diabetic Studies · doi:10.1900/rds.2016.13.79 · Cited by 13
Cellular and molecular overview of gestational diabetes mellitus: Is it predictable and preventable?
Lim, P.-Q., Lai, Y.-J., Ling, P., & Chen, K.-H. (2023) · World Journal of Diabetes · doi:10.4239/wjd.v14.i11.1693 · Cited by 12
Chen, J., Xu, X., Dalhaimer, P., & Zhao, L. (2022) · Animals · doi:10.3390/ani12192680 · Cited by 12
Obesity and Risk for Lymphoma: Possible Role of Leptin
Jiménez‐Cortegana, C., Hontecillas‐Prieto, L., García-Domínguez, D. J., Zapata, F., Carrión, N. P., Sánchez-León, M. L., Tami, M., Pérez‐Pérez, A., Sánchez-Jiménez, F., Vilariño‐García, T., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415530 · Cited by 12
Dobrakowski, M., Kasperczyk, A., Czuba, Z. P., Machoń‐Grecka, A., Szlacheta, Z., & Kasperczyk, S. (2016) · Human & Experimental Toxicology · doi:10.1177/0960327116658106 · Cited by 12
Taşkın, A. C., Kocabay, A., Ebrahımı, A., Karahüseyinoğlu, S., Şahin, G. N., Özçimen, B., Ruacan, A., & Önder, T. T. (2019) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-019-00367-y · Cited by 11
Hua, K., Li, L.-H., Yu, H.-C., Wong, W.-T., & Hsu, H.-T. (2023) · Journal of Inflammation Research · doi:10.2147/jir.s431026 · Cited by 11
Increased Permeability of the Blood–Brain Barrier in a Diabetic Mouse Model (Leprdb/db Mice)
Alshammari, M. A., Alshehri, A. O., Alqahtani, F., Khan, M. R., Bakhrebah, M. A., Alasmari, F. F., Alshammari, T. K., & AlSharari, S. D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147768 · Cited by 11
Leptin-dependent neurotoxicity via induction of apoptosis in adult rat neurogenic cells
Segura, S., Efthimiadi, L., Porcher, C., Courtes, S., Coronas, V., Krantic, S. M., & Moyse, E. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00350 · Cited by 12
Mangini, V., Maggi, V., Trianni, A., Melle, F., Luca, E. D., Pennetta, A., Sole, R. D., Ventura, G., Cataldi, T. R. I., & Fiammengo, R. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00748 · Cited by 10
Tomaszewska, E., Prost, Ł., Dobrowolski, P., Chand, D. K. P., Donaldson, J., Czech, A., Klebaniuk, R., Fabjanowska, J., & Muszyński, S. (2021) · Annals of Animal Science · doi:10.2478/aoas-2021-0075 · Cited by 10
Yan, J. Y., Wang, X., Tao, H., Wang, Y., Luo, M., & Lin, F. (2015) · Obesity Research & Clinical Practice · doi:10.1016/j.orcp.2015.01.002 · Cited by 10
Paolucci, M., Coccia, E., Imperatore, R., & Varricchio, E. (2019) · Fish Physiology and Biochemistry · doi:10.1007/s10695-019-00720-8 · Cited by 10
Metadata
- Authors
- Park, H.-K., & Ahima, R. S.
- Affiliations
- Soonchunhyang University (KR)
- University of Pennsylvania (US)
- Corresponding author
- Ahima, Rexford S.
- ORCID
- Ahima, Rexford S.
- Venue
- F1000Prime Reports
- Publisher
- H1 Connect
- Published
- 2014-09-04
- Volume
- 6
- Pages
- 73-73
- ISSN
- 2051-7599 (ISSN-L)
- PMC
- PMC4166933
- OpenAlex
- W4252710559
- Cited by
- 171
- References
- 62
- Citations by year
- 2026: 6 · 2025: 18 · 2024: 18 · 2023: 15 · 2022: 20 · 2021: 16 · 2020: 23 · 2019: 13 · 2018: 5 · 2017: 7 · 2016: 14 · 2015: 15 · 2014: 1
- FWCI
- 1.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- F1000Prime Reports (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (DK049210, DK 19525)
- National Institute of Diabetes and Digestive and Kidney Diseases (P01DK049210, P30DK019525)
- National Institute of Neurological Disorders and Stroke (R01NS084965)
- Topics
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Regulation of Appetite and Obesity
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Keywords
- leptin, leptin signaling, leptin receptor, energy homeostasis, glucose metabolism, lipid metabolism, immune function, JAK2/STAT3 signaling, adipose tissue, central nervous system
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