The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Abnormal splicing of the leptin receptor in diabetic mice
Abstract
Mutations in the mouse diabetes (db) gene result in obesity and diabetes in a syndrome resembling morbid human obesity. Previous data suggest that the db gene encodes the receptor for the obese (ob) gene product, leptin. A leptin receptor was recently cloned from choroid plexus and shown to map to the same 6-cM interval on mouse chromosome 4 as db. This receptor maps to the same 300-kilobase interval as db, and has at least six alternatively spliced forms. One of these splice variants is expressed at a high level in the hypothalamus, and is abnormally spliced in C57BL/Ks db/db mice. The mutant protein is missing the cytoplasmic region, and is likely to be defective in signal transduction. This suggests that the weight-reducing effects of leptin may be mediated by signal transduction through a leptin receptor in the hypothalamus.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“It was subsequently shown that leptin receptor RNA was alternatively spliced and that only one of the splice variants, referred to as ObRb at the time (also known as LepR-l), was mutant in C57Bl/Ks db/db mice (25,26).”
From Leptin at 14 y of age: an ongoing story (2009) · cites this paper as [25]
In the citing paper
“ObRb is the only receptor isoform that expresses all the protein motifs required for cytokine receptor signaling.”
From Leptin at 14 y of age: an ongoing story (2009) · cites this paper as [25]
In the citing paper
“These mutant mice show an identical phenotype to animals with null mutations of the leptin receptor or leptin itself (25,26).”
From Leptin at 14 y of age: an ongoing story (2009) · cites this paper as [25]
In the citing paper
“ObRb was highly enriched in the hypothalamus in precisely those nuclei that alter body weight when lesioned (25,27).”
From Leptin at 14 y of age: an ongoing story (2009) · cites this paper as [25]
In the citing paper
“mice that lack only LepRb (e.g. db/db mice) exhibit a phenotype similar to leptin-deficient ob/ob mice (100).”
From Leptin and the Central Nervous System Control of Glucose Metabolism (2011) · cites this paper as [100]
In the citing paper
“Among the various isoforms of LepR, only the “long”, or “signaling” form, LepRb, appears to be competent for intracellular signal transduction and is critical for energy homeostasis.”
From Leptin and the Central Nervous System Control of Glucose Metabolism (2011) · cites this paper as [100]
In the citing paper
“The absence of leptin or leptin receptors in Lepob/ob mice or Leprdb/db mice respectively, results in morbid obesity, hyperphagia, severe hyperglycemia and insulin resistance, and marked hypoactivity (Chen et al., 1996; Coleman, 1978; Lee et al., 1996; Pelleymounter et al., 1995; Tartaglia et al., 1995; Zhang et al., 1994).”
From Leptin-Dependent Control of Glucose Balance and Locomotor Activity by POMC Neurons (2009) · cites this paper as Lee et al., 1996
Citations
Cites
Positional cloning of the mouse obese gene and its human homologue
Zhang, Y., Proenca, R., Maffei, M., Barone, M., Leopold, L., & Friedman, J. M. (1994) · Nature · doi:10.1038/372425a0 · Cited by 13,419
Self-citationLodish, H. F. (1986) · Cited by 5,650
Weight-Reducing Effects of the Plasma Protein Encoded by the obese Gene
Halaas, J. L., Gajiwala, K. S., Maffei, M., Cohen, S. L., Chait, B. T., Rabinowitz, D., Lallone, R. L., Burley, S. K., & Friedman, J. M. (1995) · Science · doi:10.1126/science.7624777 · Cited by 4,451
Self-citationEffects of the obese Gene Product on Body Weight Regulation in ob / ob Mice
Pelleymounter, M. A., Cullen, M. J., Baker, M. B., Hecht, R., Winters, D., Boone, T., & Collins, F. (1995) · Science · doi:10.1126/science.7624776 · Cited by 4,017
Identification and expression cloning of a leptin receptor, OB-R.
Tartaglia, L. A., Dembski, M., Weng, X., Deng, N., Culpepper, J., Devos, R., Richards, G. J., Campfield, L. A., Clark, F. T., Deeds, J., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90151-5 · Cited by 3,496
Campfield, L. A., Smith, F. J., Guisez, Y., Devos, R., & Burn, P. (1995) · Science · doi:10.1126/science.7624778 · Cited by 3,243
A role for glucagon-like peptide-1 in the central regulation of feeding
Turton, M. D., O'Shea, D., Gunn, I., Beak, S. A., Edwards, C. M. B., Meeran, K., Choi, S. J., Taylor, G. M., Heath, M. M., Lambert, P. D., et al. (1996) · Nature · doi:10.1038/379069a0 · Cited by 1,950
Shizuya, H., Birren, B. W., Kim, U. J., Mancino, V., Slepak, T. I., Tachiiri, Y., & Simon, M. I. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.18.8794 · Cited by 1,672
The role of neuropeptide Y in the antiobesity action of the obese gene product
Stephens, T. W., Basinski, M., Bristow, P. K., Bue-Valleskey, J. M., Burgett, S. G., Craft, L., Hale, J., Hoffmann, J., Hsiung, H. M., Kriauciunas, A., et al. (1995) · Nature · doi:10.1038/377530a0 · Cited by 1,498
Kishimoto, T., Taga, T., & Akira, S. (1994) · Cell · doi:10.1016/0092-8674(94)90333-6 · Cited by 1,318
Flagged first, then by citations
Research works printed but not linked: 1
- Hartl, D. L. & Nurminsky, D. I. Bio Techniques 15, 201–208 (1993).
Cited by
Sorted by citations
Items 201–300 of 1,006
Simopoulou, T., Malizos, Κ. Ν., Iliopoulos, D., Stefanou, N., Papatheodorou, L. K., Ιωάννου, Μ., & Tsezou, A. (2007) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2007.01.018 · Cited by 287
Role of Leptin in the Regulation of Glucagon-Like Peptide-1 Secretion
Anini, Y., & Brubaker, P. L. (2003) · Diabetes · doi:10.2337/diabetes.52.2.252 · Cited by 287
Leal, V. D. O., & Mafra, D. (2013) · Clinica Chimica Acta · doi:10.1016/j.cca.2013.02.003 · Cited by 287
Leptin Effects on Pancreatic β-Cell Gene Expression and Function
Seufert, J. (2004) · Diabetes · doi:10.2337/diabetes.53.2007.s152 · Cited by 284
Leptin Function and Regulation
Zhang, Y., & Chua, S. C. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160041 · Cited by 284
The adipocyte as an endocrine organ in the regulation of metabolic homeostasis
Harwood, H. J. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.12.010 · Cited by 282
The Molecular Genetics of Rodent Single Gene Obesities
Leibel, R. L., Chung, W. K., & Chua, S. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.31937 · Cited by 279
Genetics and epigenetics of eating disorders
Bulik, C., Yilmaz, Z., & HArdaway, A. (2015) · Advances in Genomics and Genetics · doi:10.2147/agg.s55776 · Cited by 278
Bornstein, S. R., Schuppenies, A., Wong, M., & Licinio, J. (2006) · Molecular Psychiatry · doi:10.1038/sj.mp.4001873 · Cited by 278
The role of leptin in regulating bone metabolism
Upadhyay, J., Farr, O. M., & Mantzoros, C. S. (2014) · Metabolism · doi:10.1016/j.metabol.2014.10.021 · Cited by 277
Strain-Specific Response to 3-Adrenergic Receptor Agonist Treatment of Diet-Induced Obesity in Mice
Collins, S., Daniel, K. W., Petro, A. E., & Surwit, R. S. (1997) · Endocrinology · doi:10.1210/endo.138.1.4829 · Cited by 276
Kadowaki, T., Yamauchi, T., & Kubota, N. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.070 · Cited by 274
Hileman, S. M., Pierroz, D. D., Masuzaki, H., Bjørbæk, C., El-Haschimi, K., Banks, W. A., & Flier, J. S. (2002) · Endocrinology · doi:10.1210/endo.143.3.8669 · Cited by 274
Leptin at 14 y of age: an ongoing story
Friedman, J. M. (2009) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2008.26788b · Cited by 272
Self-citationSweeney, G. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(02)00006-2 · Cited by 271
Mattioli, B., Straface, E., Quaranta, M. G., Giordani, L., & Viora, M. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.11.6820 · Cited by 271
Obesity – is it a genetic disorder?
Loos, R. J. F., & Bouchard, C. (2003) · Journal of Internal Medicine · doi:10.1046/j.1365-2796.2003.01242.x · Cited by 271
Modulation of Circulating Leptin Levels by Its Soluble Receptor
Huang, L., Wang, Z., & Cai, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009795200 · Cited by 269
Kazak, L., Chouchani, E. T., Lu, G. Z., Jedrychowski, M. P., Bare, C. J., Mina, A. I., Kumari, M., Zhang, S., Vučković, I., Laznik-Bogoslavski, D., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.009 · Cited by 269
Frühbeck, G., Aguado, M., & Martínez, J. A. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7716 · Cited by 268
The MC4 receptor and control of appetite
Adan, R. A. H., Tiesjema, B., Hillebrand, J. J., la Fleur, S. E., Kas, M. J., & de Krom, M. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706929 · Cited by 267
Neuroendocrine Responses to Starvation and Weight Loss
Schwartz, M. W., & Seeley, R. J. (1997) · New England Journal of Medicine · doi:10.1056/nejm199706193362507 · Cited by 265
Towards a pro-inflammatory and immunomodulatory emerging role of leptin
Otero, M., Lago, R., Gómez, R., Diéguez, C., Lago, F., Gómez-Reino, J. J., & Gualillo, O. (2006) · Rheumatology · doi:10.1093/rheumatology/kel157 · Cited by 263
Genetics of the metabolic syndrome
Groop, L. (2000) · British Journal Of Nutrition · doi:10.1017/s0007114500000945 · Cited by 262
Testosterone Substitution Normalizes Elevated Serum Leptin Levels in Hypogonadal Men
Jockenhövel, F., Blum, W. F., Vogel, E., Englaro, P., Müller-Wieland, D., Reinwein, D., Rascher, W., & Krone, W. (1997) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.82.8.4174 · Cited by 261
Leptin: physiology and pathophysiology
Frühbeck, G., Jebb, S. A., & Prentice, A. M. (1998) · Clinical Physiology · doi:10.1046/j.1365-2281.1998.00129.x · Cited by 261
Uotani, S., Bjørbæk, C., Tornøe, J., & Flier, J. S. (1999) · Diabetes · doi:10.2337/diabetes.48.2.279 · Cited by 259
Papathanassoglou, E., El-Haschimi, K., Li, X. C., Matarese, G., Strom, T., & Mantzoros, C. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.12.7745 · Cited by 258
Reduced expression of PDGF and PDGF receptors during impaired wound healing
Beer, H.-D., Longaker, M. T., & Werner, S. (1997) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12319188 · Cited by 257
20 YEARS OF LEPTIN: Leptin at 20: an overview
Friedman, J. M. (2014) · Journal of Endocrinology · doi:10.1530/joe-14-0405 · Cited by 257
Self-citationThe adipocyte as an active participant in energy balance and metabolism
Badman, M. K., & Flier, J. S. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.03.058 · Cited by 256
Identification of Five Phytosterols from Aloe Vera Gel as Anti-diabetic Compounds
Tanaka, M., Misawa, E., Ito, Y., Habara, N., Nomaguchi, K., Yamada, M., Toida, T., Hayasawa, H., Takase, M., Inagaki, M., et al. (2006) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.29.1418 · Cited by 255
Plasma leptin is partly cleared by the kidney and is elevated in hemodialysis patients
Sharma, K., Considine, R. V., Michael, B., Dunn, S., Weisberg, L. S., Kurnik, B. R. C., Kurnik, P. B., O'Connor, J., Sinha, M. K., & Caro, J. F. (1997) · Kidney International · doi:10.1038/ki.1997.269 · Cited by 255
Advances in understanding the interrelations between leptin resistance and obesity
Pan, H., Guo, J., & Su, Z. (2014) · Physiology & Behavior · doi:10.1016/j.physbeh.2014.04.003 · Cited by 257
Tissue-Specific Effects of Leptin on Glucose and Lipid Metabolism
Pereira, S., Cline, D. L., Glavas, M. M., Covey, S. D., & Kieffer, T. J. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa027 · Cited by 256
Regulation of leptin production: sympathetic nervous system interactions
Rayner, D. V., & Trayhurn, P. (2001) · Journal of Molecular Medicine · doi:10.1007/s001090100198 · Cited by 250
Mushroom bodies of the cockroach: Their participation in place memory
Mizunami, M., Weibrecht, J. M., & Strausfeld, N. J. (1998) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19981228)402:4 · Cited by 289
Leptin‐induced signal transduction pathways
Hegyi, K., Fülöp, K., Kovács, K., Tóth, S., & Falus, A. (2004) · Cell Biology International · doi:10.1016/j.cellbi.2003.12.003 · Cited by 250
Hypothalamic pathways underlying the endocrine, autonomic, and behavioral effects of leptin
Elmquist, J. K. (2001) · Physiology & Behavior · doi:10.1016/s0031-9384(01)00613-8 · Cited by 249
Morioka, T., Asilmaz, E., Hu, J., Dishinger, J. F., Kurpad, A. J., Elias, C. F., Li, H., Elmquist, J. K., Kennedy, R. T., & Kulkarni, R. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30910 · Cited by 249
ADIPOCYTE DIFFERENTIATION AND LEPTIN EXPRESSION
Hwang, C.-S., Loftus, T. M., Mandrup, S., & Lane, M. D. (1997) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.13.1.231 · Cited by 249
Considine, R. V., Caro, J. F., Considine, E. L., Williams, C. J., & Hyde, T. M. (1996) · Diabetes · doi:10.2337/diab.45.7.992 · Cited by 248
Lam, Q. L. K., & Lu, L. (2007) · PubMed · Cited by 247
Kim, Y., Uotani, S., Pierroz, D. D., Flier, J. S., & Kahn, B. B. (2000) · Endocrinology · doi:10.1210/endo.141.7.7536 · Cited by 246
Evolution of Leptin Structure and Function
Denver, R. J., Bonett, R. M., & Boorse, G. C. (2011) · Neuroendocrinology · doi:10.1159/000328435 · Cited by 245
Chan, J. L., Blüher, S., Yiannakouris, N., Suchard, M. A., Kratzsch, J., & Mantzoros, C. S. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2105 · Cited by 245
Leptin stimulates rat aortic smooth muscle cell proliferation and migration.
Oda, A., Taniguchi, T., & Yokoyama, M. (2001) · PubMed · doi:10.24546/00082677 · Cited by 245
Evidence for Leptin Binding to Proteins in Serum of Rodents and Humans: Modulation With Obesity
Houseknecht, K. L., Mantzoros, C. S., Kuliawat, R., Hadro, E., Flier, J. S., & Kahn, B. B. (1996) · Diabetes · doi:10.2337/diab.45.11.1638 · Cited by 245
Haft, C. R., de la Luz Sierra, M., Barr, V. A., Haft, D. H., & Taylor, S. I. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7278 · Cited by 244
Gavrilova, O., Barr, V. A., Marcus‐Samuels, B., & Reitman, M. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30546 · Cited by 244
Diabetes mellitus and the peripheral nervous system: Manifestations and mechanisms
Zochodne, D. W. (2007) · Muscle & Nerve · doi:10.1002/mus.20785 · Cited by 243
Trayhurn, P., Hoggard, N., Mercer, J., & Rayner, D. V. (1999) · International Journal of Obesity · doi:10.1038/sj.ijo.0800791 · Cited by 243
20 YEARS OF LEPTIN: Connecting leptin signaling to biological function
Allison, M. B., & Myers, M. G. (2014) · Journal of Endocrinology · doi:10.1530/joe-14-0404 · Cited by 242
Immunohistochemical Localization of Leptin and Uncoupling Protein in White and Brown Adipose Tissue
Cinti, S., Frederich, R. C., Zingaretti, M. C., Matteis, R. D., Flier, J. S., & Lowell, B. B. (1997) · Endocrinology · doi:10.1210/endo.138.2.4908 · Cited by 242
Relatively low plasma leptin concentrations precede weight gain in Pima Indians
Ravussin, É., Pratley, R. E., Maffei, M., Wang, H., Friedman, J. M., Bennett, P. H., & Bogardus, C. (1997) · Nature Medicine · doi:10.1038/nm0297-238 · Cited by 240
Self-citationIndependent and Additive Effects of Central POMC and Leptin Pathways on Murine Obesity
Boston, B. A., Blaydon, K. M., Varnerin, J. P., & Cone, R. D. (1997) · Science · doi:10.1126/science.278.5343.1641 · Cited by 239
BROWN ADIPOSE TISSUE, β3-ADRENERGIC RECEPTORS, AND OBESITY
Lowell, M., & Flier, M. (1997) · Annual Review of Medicine · doi:10.1146/annurev.med.48.1.307 · Cited by 237
van Dielen, F., Veer, C. V. ′., Schols, A. M. W. J., Soeters, P. B., Buurman, W. A., & Greve, J.-W. M. (2001) · International Journal of Obesity · doi:10.1038/sj.ijo.0801825 · Cited by 237
The Importance of Leptin to Reproduction
Childs, G. V., Odle, A. K., MacNicol, M. C., & MacNicol, A. M. (2020) · Endocrinology · doi:10.1210/endocr/bqaa204 · Cited by 237
Obese Gene Expression Alters the Ability of 30A5 Preadipocytes to Respond to Lipogenic Hormones
Bai, Y., Zhang, S., Kim, K., Lee, J.-K., & Kim, K.-H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.13939 · Cited by 237
Self-citationLeptin Induces Insulin-like Signaling That Antagonizes cAMP Elevation by Glucagon in Hepatocytes
Zhao, A. Z., Shinohara, M. M., Huang, D., Shimizu, M., Eldar-Finkelman, H., Krebs, E. G., Beavo, J. A., & Bornfeldt, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.11348 · Cited by 237
Expression of leptin receptor in lung: leptin as a growth factor
Tsuchiya, T., Shimizu, H., Horie, T., & Mori, M. (1999) · European Journal of Pharmacology · doi:10.1016/s0014-2999(98)00884-x · Cited by 237
Leptin receptor signaling and the regulation of mammalian physiology
Villanueva, E. C., & Myers, M. G. (2008) · International Journal of Obesity · doi:10.1038/ijo.2008.232 · Cited by 237
Castellucci, M. (2000) · Molecular Human Reproduction · doi:10.1093/molehr/6.10.951 · Cited by 236
Zimmet, P., Boyko, E. J., Collier, G. R., & de Courten, M. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07783.x · Cited by 234
Molecular disruption of hypothalamic nutrient sensing induces obesity
He, W., Lam, T. K. T., Obici, S., & Rossetti, L. (2006) · Nature Neuroscience · doi:10.1038/nn1626 · Cited by 233
Leptin and its receptors: regulators of whole-body energy homeostasis
Houseknecht, K. L., & Portocarrero, C. P. (1998) · Domestic Animal Endocrinology · doi:10.1016/s0739-7240(98)00035-6 · Cited by 232
Leptin secretion from adipose tissue in women. Relationship to plasma levels and gene expression.
Lönnqvist, F., Nordfors, L., Jansson, M., Thörne, A., Schalling, M., & Arner, P. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119422 · Cited by 232
Leptin Action in Intestinal Cells
Morton, N. M., Emilsson, V., Liu, Y.-L., & Cawthorne, M. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26194 · Cited by 231
RAGE modulates vascular inflammation and atherosclerosis in a murine model of type 2 diabetes
Wendt, T., Harja, E., Bucciarelli, L. G., Qu, W., Lu, Y., Rong, L., Jenkins, D. G., Stein, G., Schmidt, A. M., & Yan, S. F. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.06.013 · Cited by 229
Control of energy homeostasis by insulin and leptin: Targeting the arcuate nucleus and beyond
Könner, A. C., Klöckener, T., & Brüning, J. C. (2009) · Physiology & Behavior · doi:10.1016/j.physbeh.2009.03.027 · Cited by 230
From obesity genetics to the future of personalized obesity therapy
Moustafa, J. S. E.-S., & Froguel, P. (2013) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2013.57 · Cited by 228
Leptin and the regulation of body weight
Considine, R. V., & Caro, J. F. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(97)00050-2 · Cited by 228
Ren, D., Li, M., Duan, C., & Rui, L. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.07.004 · Cited by 227
Leptin-Dependent Control of Glucose Balance and Locomotor Activity by POMC Neurons
Huo, L., Gamber, K., Greeley, S., Silva, J., Huntoon, N., Leng, X.-H., & Bjørbæk, C. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.05.003 · Cited by 226
“The absence of leptin or leptin receptors in Lepob/ob mice or Leprdb/db mice respectively, results in morbid obesity, hyperphagia, severe hyperglycemia and insulin resistance, and marked hypoactivity (Chen et al., 1996; Coleman, 1978; Lee et al., 1996; Pelleymounter et al., 1995; Tartaglia et al., 1995; Zhang et al.,…”
Vaccination against weight gain
Zorrilla, E. P., Iwasaki, S., Moss, J. A., Chang, J. Y., Otsuji, J., Inoue, K., Meijler, M. M., & Janda, K. D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605376103 · Cited by 225
Buyse, M., Berlioz, F., Guilmeau, S., Tsocas, A., Voisin, T., Péranzi, G., Merlin, D., Laburthe, M., Lewin, M. J. M., Rozé, C., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13219 · Cited by 225
Wu-Peng, X. S., Chua, S. C., Okada, N. A., Liu, S.-M., Nicolson, M. A., & Leibel, R. L. (1997) · Diabetes · doi:10.2337/diab.46.3.513 · Cited by 224
Håkansson, de Lecea, L., Sutcliffe, Yanagisawa, & Meister (1999) · Journal of Neuroendocrinology · doi:10.1046/j.1365-2826.1999.00378.x · Cited by 223
Ross, R. J. M., Esposito, N., Shen, X. Y., Laue, S. V., Chew, S. L., Dobson, P. R. M., Postel-Vinay, M. C., & Finidori, J. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.3.9901 · Cited by 222
Leptin: a multifunctional hormone
Huang, L., & Cai, L. (2000) · Cell Research · doi:10.1038/sj.cr.7290038 · Cited by 221
Leptin expression and action: New experimental paradigms
Flier, J. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4242 · Cited by 221
The glucoregulatory actions of leptin
D'souza, A. M., Neumann, U. H., Glavas, M. M., & Kieffer, T. J. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.04.011 · Cited by 220
Uchida, T., Nakamura, T., Hashimoto, N., Matsuda, T., Kotani, K., Sakaue, H., Kido, Y., Hayashi, Y., Nakayama, K. I., White, M. F., et al. (2005) · Nature Medicine · doi:10.1038/nm1187 · Cited by 218
Steatohepatitis Induced by Intragastric Overfeeding in Mice *
Deng, Q.-G., She, H., Cheng, J. H., French, S. W., Koop, D. R., Xiong, S., & Tsukamoto, H. (2005) · Hepatology · doi:10.1002/hep.20877 · Cited by 218
Obesity is associated with a decreased leptin transport across the blood-brain barrier in rats.
Burguera, B. G., Couce, M., Curran, G. L., Jensen, M. D., Lloyd, R. V., Cleary, M. P., & Poduslo, J. F. (2000) · Diabetes · doi:10.2337/diabetes.49.7.1219 · Cited by 217
Sano, H., Nakamura, A., Texada, M. J., Truman, J. W., Ishimoto, H., Kamikouchi, A., Nibu, Y., Kume, K., Ida, T., & Kojima, M. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005209 · Cited by 211
Gloaguen, I., Costa, P., Demartis, A., Lazzaro, D., Marco, A. D., Graziani, R., Paonessa, G., Chen, F., Rosenblum, C. I., der Ploeg, L. H. T. V., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6456 · Cited by 215
Aneja, A. (2004) · Recent Progress in Hormone Research · doi:10.1210/rp.59.1.169 · Cited by 214
Apoptotic Pathways Are Inhibited by Leptin Receptor Activation in Neutrophils
Bruno, A., Conus, S., Schmid, I., & Simon, H. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.12.8090 · Cited by 214
The arcuate nucleus as a primary site of satiety effect of leptin in rats
Satoh, N., Ogawa, Y., Katsuura, G., Hayase, M., Tsuji, T., Imagawa, K., Yoshimasa, Y., Nishi, S., Hosoda, K., & Nakao, K. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00163-8 · Cited by 213
Differential Role of Leptin and Adiponectin in Cardiovascular System
Ghantous, C. M., Azrak, Z., Hanache, S., Abou-Kheir, W. G., & Zeidan, A. (2015) · International Journal of Endocrinology · doi:10.1155/2015/534320 · Cited by 211
Interleukin 1 Increases Serum Leptin Concentrations in Humans
Janik, J. E., Curti, B. D., Considine, R. V., Rager, H., Powers, G. C., Alvord, W. G., Smith, J. W., Gause, B. L., & Kopp, W. C. (1997) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.82.9.4214 · Cited by 211
Buyse, M., Ovesjö, M., Goïot, H., Guilmeau, S., Péranzi, G., Moizo, L., Walker, F., Lewin, M. J. M., Meister, B., & Bado, A. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01628.x · Cited by 210
Garza, J. C., Guo, M., Zhang, W., & Lu, X.-Y. (2012) · Molecular Psychiatry · doi:10.1038/mp.2011.161 · Cited by 209
Neuronal SH2B1 is essential for controlling energy and glucose homeostasis
Ren, D., Zhou, Y., Morris, D. L., Li, M., Li, Z., & Rui, L. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29417 · Cited by 209
Leptin Regulates Prothyrotropin-releasing Hormone Biosynthesis
Nillni, E. A., Vaslet, C. A., Harris, M., Hollenberg, A. N., Bjørbæk, C., & Flier, J. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003549200 · Cited by 209
Tsuji, K., Maeda, T., Kawane, T., Matsunuma, A., & Horiuchi, N. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.65 · Cited by 208
Nonsense mutation of leptin receptor in the obese spontaneously hypertensive Koletsky rat
Takaya, K., Ogawa, Y., Hiraoka, J., Hosoda, K., Yamori, Y., Nakao, K., & Koletsky, R. J. (1996) · Nature Genetics · doi:10.1038/ng1096-130 · Cited by 207
Dendritically targeted Bdnf mRNA is essential for energy balance and response to leptin
Liao, G., An, J. J., Gharami, K., Waterhouse, E. G., Vanevski, F., Jones, K. R., & Xu, B. (2012) · Nature Medicine · doi:10.1038/nm.2687 · Cited by 208
Metadata
- Authors
- Lee, G.-H., Proenca, R., Montez, J. M., Carroll, K. M., Darvishzadeh, J. G., Lee, J. I., & Friedman, J. M.
- Affiliations
- Howard Hughes Medical Institute (US)
- Rockefeller University (US)
- ORCID
- Friedman, J. M.
- Venue
- Nature
- Published
- 1996-02
- Volume
- 379
- Issue
- 6566
- Pages
- 632-635
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2016994959
- Cited by
- 2,327
- References
- 27
- Citations by year
- 2026: 12 · 2025: 22 · 2024: 17 · 2023: 20 · 2022: 36 · 2021: 46 · 2020: 35 · 2019: 47 · 2018: 38 · 2017: 46 · 2016: 58 · 2015: 62 · 2014: 88 · 2013: 88 · 2012: 83
- FWCI
- 56.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (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 receptor, alternative splicing, db/db mice, obesity, leptin, signal transduction, hypothalamus, obesity-related genes, chromosome 4, cytoplasmic domain, body weight regulation
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Chromosome Mapping, Diabetes Mellitus, Experimental, Mice, Inbred C57BL, Molecular Sequence Data, Mutation, Proteins, Receptors, Cell Surface, Tissue Distribution, Polymerase Chain Reaction, Alternative Splicing, DNA Primers, Leptin, Mice, 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