Cited by 550Regulation of Appetite and ObesityAdipokines, Inflammation, and Metabolic DiseasesHypothalamic control of reproductive hormones

The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.

Molecular and anatomical determinants of central leptin resistance

Münzberg, Heike, Myers, Martin G·2005·Nature Neuroscience

DOI 10.1038/nn1454

Open this paper in CoChat — free account

Abstract

The increasing incidence of obesity in developed nations is an ever-growing challenge to health care, promoting diabetes and other diseases. The hormone leptin, which is derived from adipose tissue, regulates feeding and energy expenditure. Most forms of obesity are associated with diminished responsiveness to the appetite-suppressing effects of leptin. Here we review the mechanisms by which leptin activates intracellular signals, the roles of these signals in leptin action in vivo, and mechanisms that may attenuate leptin signaling, limiting its action in obese individuals. We highlight data regarding the expression of SOCS3 (a potential mediator of leptin resistance) in the arcuate nucleus of the hypothalamus.

Integrity signals

Registry

Crossref · 10.1038/nn1454

Cites

66 of 66 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Central nervous system control of food intake
Schwartz, M. W., Woods, S. C., Porte, D., Seeley, R. J., & Baskin, D. G. (2000) · Nature · doi:10.1038/35007534 · Cited by 6,451
Leptin and the regulation of body weight in mammals
Friedman, J. M., & Halaas, J. L. (1998) · Nature · doi:10.1038/27376 · Cited by 5,405
Leptin activates anorexigenic POMC neurons through a neural network in the arcuate nucleus
Cowley, M. A., Smart, J. L., Rubinstein, M., Cerdán, M. G., Diano, S., Horvath, T. L., Cone, R. D., & Low, M. J. (2001) · Nature · doi:10.1038/35078085 · Cited by 2,356
Leptin levels reflect body lipid content in mice: Evidence for diet-induced resistance to leptin action
Frederich, R. C., Hamann, A., Anderson, S., Löllmann, B., Lowell, B. B., & Flier, J. S. (1995) · Nature Medicine · doi:10.1038/nm1295-1311 · Cited by 1,660
Beneficial effects of leptin on obesity, T cell hyporesponsiveness, and neuroendocrine/metabolic dysfunction of human congenital leptin deficiency
Farooqi, I. S., Matarese, G., Lord, G. M., Keogh, J. M., Lawrence, E., Agwu, C., Sanna, V., Jebb, S. A., Perna, F., Fontana, S., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15693 · Cited by 1,374
The Leptin Receptor
Tartaglia, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6093 · Cited by 1,289
Leptin-Replacement Therapy for Lipodystrophy
Oral, E. A., Simha, V., Ruiz, E., Andewelt, A., Premkumar, A., Snell, P., Wagner, A. J., DePaoli, A. M., Reitman, M. L., Taylor, S. I., et al. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa012437 · Cited by 1,247 · cited 1×
“, and it ameliorates the hyperphagia and endocrine abnormalities associated with very low body-fat content caused by a number of lipodystrophic and eating disorder”
Background
From Lesions to Leptin
Elmquist, J. K., Elias, C. F., & Saper, C. B. (1999) · Neuron · doi:10.1016/s0896-6273(00)81084-3 · Cited by 1,160
Beneficial effects of leptin on obesity, T cell hyporesponsiveness, and neuroendocrine/metabolic dysfunction of human congenital leptin deficiency
Farooqi, I. S., Matarese, G., Lord, G. M., Keogh, J. M., Lawrence, E., Agwu, C., Sanna, V., Jebb, S. A., Perna, F., Fontana, S., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215693 · Cited by 1,105
Leptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy
Shimomura, I., Hammer, R. E., Ikemoto, S., Brown, M. S., & Goldstein, J. L. (1999) · Nature · doi:10.1038/43448 · Cited by 1,038
Identification of SOCS-3 as a Potential Mediator of Central Leptin Resistance
Bjørbæk, C., Elmquist, J. K., Frantz, J. D., Shoelson, S. E., & Flier, J. S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80062-3 · Cited by 1,014
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
Self-citation
Jaks and Stats in signaling by the cytokine receptor superfamily.
Ihle, J., & Kerr, I. (1995) · Trends in Genetics · doi:10.1016/s0168-9525(00)89000-9 · Cited by 953
Leptin receptor signaling in POMC neurons is required for normal body weight homeostasis
Balthasar, N., Coppari, R., McMinn, J., Liu, S. M., Lee, C. E., Tang, V., Kenny, C. D., McGovern, R. A., Chua, S. C., Elmquist, J. K., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.004 · Cited by 935
Leptin Differentially Regulates NPY and POMC Neurons Projecting to the Lateral Hypothalamic Area
Elias, C. F., Aschkenasi, C., Lee, C., Kelly, J., Ahima, R. S., Bjorbæk, C., Flier, J. S., Saper, C. B., & Elmquist, J. K. (1999) · Neuron · doi:10.1016/s0896-6273(01)80035-0 · Cited by 924
Recombinant human leptin in women with hypothalamic amenorrhea
Welt, C. K., Chan, J. L., Bullen, J., Murphy, R., Smith, P., DePaoli, A. M., Karalis, A., & Mantzoros, C. S. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040388 · Cited by 908
Specificity of Leptin Action on Elevated Blood Glucose Levels and Hypothalamic Neuropeptide Y Gene Expression in ob/ob Mice
Schwartz, M. W., Baskin, D. G., Bukowski, T. R., Kuijper, J. L., Foster, D., Lasser, G., Prunkard, D. E., Porte, D., Woods, S. C., Seeley, R. J., et al. (1996) · Diabetes · doi:10.2337/diab.45.4.531 · Cited by 904 · cited 1×
“Leptin also regulates insulin sensitivity and glucose homeostasis by two mechanisms: first, by controlling energy balance and body fat (increased body adiposity leads to insulin resistance) and, second, through an adiposity-independent pathway mediated by the CNS control of hepatic glucose outpu”
Background
SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2
Rui, L., Yuan, M., Frantz, D., Shoelson, S., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200444200 · Cited by 904
Two defects contribute to hypothalamic leptin resistance in mice with diet-induced obesity
El-Haschimi, K., Pierroz, D. D., Hileman, S. M., Bjørbæk, C., & Flier, J. S. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9842 · Cited by 887
PTP1B Regulates Leptin Signal Transduction In Vivo
Zabolotny, J. M., Bence, K. K., Stricker‐Krongrad, A., Haj, F. G., Wang, Y., Minokoshi, Y., Kim, Y., Elmquist, J. K., Tartaglia, L. A., Kahn, B. B., et al. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00148-x · Cited by 818
Activation of Downstream Signals by the Long Form of the Leptin Receptor
Banks, A. S., Davis, S. M., Bates, S. H., & Myers, M. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14563 · Cited by 797
Self-citation
Diet-induced obese mice develop peripheral, but not central, resistance to leptin.
van Heek, M., Compton, D. S., France, C. F., Tedesco, R. P., Fawzi, A. B., Graziano, M. P., Sybertz, E. J., Strader, C. D., & Davis, H. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119171 · Cited by 765
Region-Specific Leptin Resistance within the Hypothalamus of Diet-Induced Obese Mice
Münzberg, H., Flier, J. S., & Bjørbæk, C. (2004) · Endocrinology · doi:10.1210/en.2004-0726 · Cited by 737
Self-citation
Acute stimulation of glucose metabolism in mice by leptin treatment
Kamohara, S., Burcelin, R., Halaas, J. L., Friedman, J. M., & Charron, M. J. (1997) · Nature · doi:10.1038/38717 · Cited by 708
Suppressor of Cytokine Signaling 1 (SOCS-1) and SOCS-3 Cause Insulin Resistance through Inhibition of Tyrosine Phosphorylation of Insulin Receptor Substrate Proteins by Discrete Mechanisms
Ueki, K., Kondo, T., & Kahn, C. R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5434-5446.2004 · Cited by 686
Socs3 deficiency in the brain elevates leptin sensitivity and confers resistance to diet-induced obesity
Mori, H., Hanada, R., Hanada, T., Aki, D., Mashima, R., Nishinakamura, H., Torisu, T., Chien, K. R., Yasukawa, H., & Yoshimura, A. (2004) · Nature Medicine · doi:10.1038/nm1071 · Cited by 651
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
Self-citation
Attenuation of Leptin Action and Regulation of Obesity by Protein Tyrosine Phosphatase 1B
Cheng, A., Uetani, N., Simoncic, P. D., Chaubey, V. P., Lee-Loy, A., McGlade, C. J., Kennedy, B. P., & Tremblay, M. L. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00149-1 · Cited by 545
SOCS3 Mediates Feedback Inhibition of the Leptin Receptor via Tyr985
Bjørbæk, C., Lavery, H. J., Bates, S. H., Olson, R. K., Davis, S. M., Flier, J. S., & Myers, M. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007577200 · Cited by 537
Self-citation
Phenotypic effects of leptin replacement on morbid obesity, diabetes mellitus, hypogonadism, and behavior in leptin-deficient adults
Licinio, J., Caglayan, S., Ozata, M., Yildiz, B. O., de Miranda, P. B., O'Kirwan, F., Whitby, R., Liang, L., Cohen, P., Bhasin, S., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308767101 · Cited by 505
Enhanced leptin sensitivity and attenuation of diet-induced obesity in mice with haploinsufficiency of Socs3
Howard, J. K., Cave, B. J., Oksanen, L. J., Tzameli, I., Bjørbæk, C., & Flier, J. S. (2004) · Nature Medicine · doi:10.1038/nm1072 · Cited by 490
Hypothalamic sensing of fatty acids
Lam, T. K. T., Schwartz, G. J., & Rossetti, L. (2005) · Nature Neuroscience · doi:10.1038/nn1456 · Cited by 478
Insulin Activation of Phosphatidylinositol 3-Kinase in the Hypothalamic Arcuate Nucleus
Niswender, K. D., Morrison, C. D., Clegg, D. J., Olson, R., Baskin, D. G., Myers, M. G., Seeley, R. J., & Schwartz, M. W. (2003) · Diabetes · doi:10.2337/diabetes.52.2.227 · Cited by 476
Self-citation
IRS-2 pathways integrate female reproduction and energy homeostasis
Burks, D. J., de Mora, J. F., Schubert, M., Withers, D. J., Myers, M. G., Towery, H. H., Altamuro, S. L., Flint, C. L., & White, M. F. (2000) · Nature · doi:10.1038/35030105 · Cited by 462
Self-citation
The hypothalamic arcuate nucleus: A key site for mediating leptin’s effects on glucose homeostasis and locomotor activity
Coppari, R., Ichinose, M., Lee, C. E., Pullen, A. E., Kenny, C. D., McGovern, R. A., Tang, V., Liu, S. M., Ludwig, T., Chua, S. C., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.004 · Cited by 457
SOCS-3 Inhibits Insulin Signaling and Is Up-regulated in Response to Tumor Necrosis Factor-α in the Adipose Tissue of Obese Mice
Emanuelli, B., Peraldi, P., Filloux, C., Carine Chavey, A., Freidinger, K., Hilton, D. J., Hotamışlıgil, G. S., & OBBERGHEN, E. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104602200 · Cited by 449
Disruption of neural signal transducer and activator of transcription 3 causes obesity, diabetes, infertility, and thermal dysregulation
Gao, Q., Wolfgang, M. J., Neschen, S., Morino, K., Horvath, T. L., Shulman, G. I., & Fu, X.-Y. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0303992101 · Cited by 385
Recombinant human leptin in women with hypothalamic amenorrhea.
Welt, C., Chan, J., Bullen, J., Murphy, R., Smith, P. C., DePaoli, A., Karalis, A., & Mantzoros, C. (2004) · New England Journal of Medicine · doi:10.1097/01.ogx.0000151645.22134.0b · Cited by 366
Divergent Roles of SHP-2 in ERK Activation by Leptin Receptors
Bjørbæk, C., Buchholz, R. M., Davis, S. M., Bates, S. H., Pierroz, D. D., Gu, H., Neel, B. G., Myers, M. G., & Flier, J. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007439200 · Cited by 364
Self-citation
Activation of Jak2 Catalytic Activity Requires Phosphorylation of Y 1007 in the Kinase Activation Loop
Feng, J., Witthuhn, B. A., Matsuda, T., Kohlhuber, F., Kerr, I. M., & Ihle, J. N. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.5.2497 · Cited by 358
CIS3/SOCS-3 Suppresses Erythropoietin (EPO) Signaling by Binding the EPO Receptor and JAK2
Sasaki, A. T., Yasukawa, H., Shouda, T., Kitamura, T., Đikić, I., & Yoshimura, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003456200 · Cited by 341
Role of signal transducer and activator of transcription 3 in regulation of hypothalamic proopiomelanocortin gene expression by leptin
Münzberg, H., Huo, L., Nillni, E. A., Hollenberg, A. N., & Bjørbæk, C. (2003) · Endocrinology · doi:10.1210/en.2002-221037 · Cited by 328
Self-citation
Leptin Receptor (OB-R) Signaling
White, D. W., Kuropatwinski, K. K., Devos, R., Baumann, H., & Tartaglia, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4065 · Cited by 295
A second look at the barriers of the medial basal hypothalamus
Peruzzo, B., Pastor, F., Blázquez, J. L., Schoebitz, K., Peláez, B., Amat, P., & Rodríguez, E. M. (2000) · Experimental Brain Research · doi:10.1007/s002219900289 · Cited by 273
Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism
Zhang, E. E., Chapeau, E. A., Hagihara, K., & Feng, G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405041101 · Cited by 270
Obesity-prone rats have normal blood-brain barrier transport but defective central leptin signaling before obesity onset
Levin, B. E., Dunn-Meynell, A. A., & Banks, W. A. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00393.2003 · Cited by 269
The role of leptin receptor signaling in feeding and neuroendocrine function
Bates, S. H., & Myers, M. G. (2003) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2003.10.003 · Cited by 245
Self-citation
Growth Hormone, Interferon-γ, and Leukemia Inhibitory Factor Promoted Tyrosyl Phosphorylation of Insulin Receptor Substrate-1
Argetsinger, L. S., Hsu, G. W., Myers, M. G., Billestrup, N., White, M. F., & Carter‐Su, C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14685 · Cited by 244
Self-citation
Regulation of Jak Kinases by Intracellular Leptin Receptor Sequences
Kloek, C. E., Haq, A. K., Dunn, S. L., Lavery, H. J., Banks, A. S., & Myers, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205148200 · Cited by 236
Self-citation
The melanocortin receptors: Lessons from knockout models
Butler, A. A., & Cone, R. D. (2002) · Neuropeptides · doi:10.1054/npep.2002.0890 · Cited by 222
Intracerebroventricular Leptin Regulates Hepatic but Not Peripheral Glucose Fluxes
Liu, L., Karkanias, G. B., Morales, J. C., Hawkins, M., Barzilai, N., Wang, J., & Rossetti, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.31160 · Cited by 222
Roles for leptin receptor/STAT3-dependent and -independent signals in the regulation of glucose homeostasis
Bates, S. H., Kulkarni, R. N., Seifert, M., & Myers, M. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.02.001 · Cited by 173
Self-citation
Arcuate Nucleus-Specific Leptin Receptor Gene Therapy Attenuates the Obesity Phenotype of Koletsky (fak/fak) Rats
Morton, G. J., Niswender, K. D., Rhodes, C. J., Myers, M. G., Blevins, J. E., Baskin, D. G., & Schwartz, M. W. (2003) · Endocrinology · doi:10.1210/en.2002-0115 · Cited by 158
Self-citation
Feedback Inhibition of Leptin Receptor/Jak2 Signaling via Tyr1138 of the Leptin Receptor and Suppressor of Cytokine Signaling 3
Dunn, S. L., Björnholm, M., Bates, S. H., Chen, Z., Seifert, M. M., & Myers, M. G. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0353 · Cited by 157
Self-citation
The many lives of leptin
Banks, W. A. (2004) · Peptides · doi:10.1016/j.peptides.2004.02.014 · Cited by 153
Autophosphorylation of JAK2 on Tyrosines 221 and 570 Regulates Its Activity
Argetsinger, L. S., Kouadio, J.-L. K., Steen, H., Stensballe, A., Jensen, O. N., & Carter‐Su, C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4955-4967.2004 · Cited by 147
LRb-STAT3 Signaling Is Required for the Neuroendocrine Regulation of Energy Expenditure by Leptin
Bates, S. H., Dundon, T. A., Seifert, M., Carlson, M., Maratos-Flier, E., & Myers, M. G. (2004) · Diabetes · doi:10.2337/diabetes.53.12.3067 · Cited by 139
Self-citation
Leptin as a Therapeutic Agent--Trials and Tribulations
Mantzoros, C. S., & Flier, J. S. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.85.11.7062 · Cited by 117
Tyrosine Phosphorylation of Jak2 in the JH2 Domain Inhibits Cytokine Signaling
Feener, E. P., Rosario, F., Dunn, S. L., Stancheva, Z. S., & Myers, M. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4968-4978.2004 · Cited by 114
Self-citation
Tyrosine 813 Is a Site of JAK2 Autophosphorylation Critical for Activation of JAK2 by SH2-Bβ
Kurzer, J. H., Argetsinger, L. S., Zhou, Y.-J., Kouadio, J.-L. K., O’Shea, J. J., & Carter‐Su, C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4557-4570.2004 · Cited by 107
Photoperiodic Regulation of Leptin Sensitivity in the Siberian Hamster, Phodopus sungorus, Is Reflected in Arcuate Nucleus SOCS-3 (Suppressor of Cytokine Signaling) Gene Expression
Tups, A., Ellis, C., Moar, K. M., Logie, T. J., Adam, C. L., Mercer, J. G., & Klingenspor, M. (2003) · Endocrinology · doi:10.1210/en.2003-1382 · Cited by 102
Acute intravenous leptin infusion increases glucose turnover but not skeletal muscle glucose uptake in ob/ob mice.
Burcelin, R., Kamohara, S., Li, J., Tannenbaum, G. S., Charron, M. J., & Friedman, J. M. (1999) · Diabetes · doi:10.2337/diabetes.48.6.1264 · Cited by 92
The functional and structural border of the neurohemal region of the median eminence
Krisch, B., Leonhardt, H., & Buchheim, W. (1978) · Cell and Tissue Research · doi:10.1007/bf00220750 · Cited by 80
Identification, cDNA Cloning, and Targeted Deletion of p70, a Novel, Ubiquitously Expressed SH3 Domain-Containing Protein
Carpino, N., Kobayashi, R., Zang, H., Takahashi, Y., Jou, S.-T., Feng, J., Nakajima, H., & Ihle, J. N. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7491-7500.2002 · Cited by 75
Exogenous Glutamate Enhances Glutamate Receptor Subunit Expression during Selective Neuronal Injury in the Ventral Arcuate Nucleus of Postnatal Mice
Hu, L., Fernstrom, J. D., & Goldsmith, P. C. (1998) · Neuroendocrinology · doi:10.1159/000054353 · Cited by 38
Untitled work
Matsuzawa, Y. (1997) · doi:10.1002/(sici)1099-0895(199703)13:1

Flagged first, then by citations

Sorted by citations

Adipose tissue dysfunction in obesity, diabetes, and vascular diseases
Hajer, G. R., van Haeften, T. W., & Visseren, F. L. J. (2008) · European Heart Journal · doi:10.1093/eurheartj/ehn387 · Cited by 1,410
Obesity-Induced Hypertension: Interaction of Neurohumoral and Renal Mechanisms
Hall, J. E., do Carmo, J. M., da Silva, A. A., Wang, Z., & Hall, M. E. (2015) · Circulation Research · doi:10.1161/circresaha.116.305697 · Cited by 1,360
Hypothalamic IKKβ/NF-κB and ER Stress Link Overnutrition to Energy Imbalance and Obesity
Zhang, X., Zhang, G., Zhang, H., Karin, M., Bai, H., & Cai, D. (2008) · Cell · doi:10.1016/j.cell.2008.07.043 · Cited by 1,350
Saturated fatty acids produce an inflammatory response predominantly through the activation of TLR4 signaling in hypothalamus: implications for the pathogenesis of obesity
Milanski, M., Degasperi, G., Coope, A., Morari, J., Denis, R., Cintra, D. E., Tsukumo, D. M. L., Anhe, G., Amaral, M. E., Takahashi, H. K., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2760-08.2009 · Cited by 1,125
Adipokines and Insulin Resistance
Rabe, K., Lehrke, M., Parhofer, K. G., & Broedl, U. C. (2008) · Molecular Medicine · doi:10.2119/2008-00058.rabe · Cited by 828

See all 550

Authors: Münzberg, H., & Myers, M. G.
Affiliations: University of Michigan (US)
Corresponding author: Myers, Martin G
ORCID: Münzberg, Heike
Myers, Martin G
Venue: Nature Neuroscience
Publisher: Springer Science and Business Media LLC
Published: 2005-04-26
Volume: 8
Issue: 5
Pages: 566-570
ISSN: 1097-6256 (ISSN-L)
1546-1726
DOI: 10.1038/nn1454
OpenAlex: W2042893069
Semantic Scholar: 71b5dabe299be6d5e8f778fa2686a524e8e2be92
Cited by: 550
References: 66
Citations by year: 2026: 8 · 2025: 7 · 2024: 12 · 2023: 9 · 2022: 8 · 2021: 13 · 2020: 16 · 2019: 18 · 2018: 10 · 2017: 18 · 2016: 27 · 2015: 36 · 2014: 40 · 2013: 29 · 2012: 30
FWCI: 4.48
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Neuroscience (publishedVersion)
PubMed (publishedVersion)
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
Health Sciences › Medicine › Reproductive Medicine › Hypothalamic control of reproductive hormones
Keywords: leptin resistance, leptin signaling, obesity, SOCS3, arcuate nucleus, hypothalamus, appetite regulation, energy expenditure, intracellular signaling
MeSH terms: Suppressor of Cytokine Signaling 3 Protein, Adipose Tissue, Animals, Appetite Regulation, Energy Metabolism, Humans, Hypothalamus, Obesity, Receptors, Cell Surface, Repressor Proteins, Transcription Factors, Signal Transduction, Leptin, Suppressor of Cytokine Signaling Proteins, Receptors, Leptin

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

Molecular and anatomical determinants of central leptin resistance

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks