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 701–800 of 1,006
Miyamoto, S., Yasui, Y., Tanaka, T., Ohigashi, H., & Murakami, A. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn080 · Cited by 85
Kálmán, K., Nguyen, A., Tseng-Crank, J., Dukes, I. D., Chandy, G., Hustad, C. M., Copeland, N. G., Jenkins, N. A., Mohrenweiser, H. W., Brandriff, B. F., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5851 · Cited by 85
Leptin depolarizes rat hypothalamic paraventricular nucleus neurons
Powis, J. E., Bains, J. S., & Ferguson, A. V. (1998) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1998.274.5.r1468 · Cited by 85
Ceddia, R. B., William, W. N., Lima, F. B., Flandin, P., Curi, R., & Giacobino, J. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01664.x · Cited by 84
Jeon, J. Y., Steadward, R. D., Wheeler, G. D., Bell, G. J., McCargar, L. J., & Harber, V. J. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-020939 · Cited by 84
Neuroprotective effects of leptin in the context of obesity and metabolic disorders
Davis, C., Mudd, J., & Hawkins, M. A. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.04.012 · Cited by 84
Role of S6K1 in regulation of SREBP1c expression in the liver
Li, S., Ogawa, W., Emi, A., Hayashi, K., Senga, Y., Nomura, K., Hara, K., Yu, D., & Kasuga, M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.07.038 · Cited by 84
Guo, M., Lu, Y., Garza, J. C., Li, Y., Chua, S. C., Zhang, W., Lu, B., & Lu, X.-Y. (2012) · Translational Psychiatry · doi:10.1038/tp.2012.9 · Cited by 84
Exogenous leptin controls the development of the small intestine in neonatal piglets
Woliński, J., Biernat, M., Guilloteau, P., Weström, B. R., & Zabielski, R. (2003) · Journal of Endocrinology · doi:10.1677/joe.0.1770215 · Cited by 84
Beshel, J., Dubnau, J., & Zhong, Y. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.12.013 · Cited by 84
Iqbal, J., Pompolo, S., Murakami, T., Grouzmann, E., Sakurai, T., Meister, B., & Clarke, I. J. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02932-8 · Cited by 84
Breidert, M. (1999) · Scandinavian Journal of Gastroenterology · doi:10.1080/003655299750025039 · Cited by 84
Leptin: its pharmacokinetics and tissue distribution
Hill, R., Margetic, S., Pegg, G. G., & Gazzola, C. (1998) · International Journal of Obesity · doi:10.1038/sj.ijo.0800656 · Cited by 84
Hypocretin as a Hub for Arousal and Motivation
Tyree, S. M., Borniger, J. C., & de Lecea, L. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00413 · Cited by 83
ABA Mediates Plant Development and Abiotic Stress via Alternative Splicing
Yang, X., Jia, Z., Pu, Q., Tian, Y., Zhu, F., & Liu, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073796 · Cited by 83
Nakashima, K., Narazaki, M., & Taga, T. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00013-6 · Cited by 83
The Leptin Receptor Mediates Apparent Autocrine Regulation of Leptin Gene Expression
Zhang, Y., Olbort, M., Schwarzer, K., Nuesslein‐Hildesheim, B., Nicolson, M. A., Murphy, E. M., Kowalski, T. J., Schmidt, I., & Leibel, R. L. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7622 · Cited by 83
Overeating of palatable food is associated with blunted leptin and ghrelin responses
Lindqvist, A., de la Cour, C. D., Stegmark, A., Håkanson, R., & Erlanson‐Albertsson, C. (2005) · Regulatory Peptides · doi:10.1016/j.regpep.2005.05.002 · Cited by 83
Appleton, D. J., Rand, J. S., & Sunvold, G. D. (2000) · Journal of Feline Medicine and Surgery · doi:10.1053/jfms.2000.0103 · Cited by 83
Acute Effect of Leptin on Hepatic Glycogenolysis and Gluconeogenesis in Perfused Rat Liver
Nemecz, M., Preininger, K., Englisch, R., Fürnsinn, C., Schneider, B., Waldhäusl, W., & Roden, M. (1999) · Hepatology · doi:10.1002/hep.510290110 · Cited by 83
El-Atat, F. A., Aneja, A., McFarlane, S. I., & Sowers, J. R. (2003) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/s0889-8529(03)00070-7 · Cited by 83
Leptin and Adiponectin: Emerging Therapeutic Targets in Breast Cancer
Surmacz, E. (2013) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-013-9302-8 · Cited by 82
Ogawa, T., Hirose, H., Yamamoto, Y., Nishikai, K., Miyashita, K., Nakamura, H., Saito, I., & Saruta, T. (2004) · Metabolism · doi:10.1016/j.metabol.2004.02.009 · Cited by 82
Morino, S., Kondo, T., Sasaki, K., Adachi, H., Suico, M. A., Sekimoto, E., Matsuda, T., Shuto, T., Araki, E., & Kai, H. (2008) · PLoS ONE · doi:10.1371/journal.pone.0004068 · Cited by 82
The association of gastric leptin with oesophageal inflammation and metaplasia
François, F., Roper, J., Goodman, A. J., Pei, Z., Ghumman, M., Mourad, M. S., de Perez, A. Z. O., Perez-Perez, G. I., Tseng, C., & Blaser, M. J. (2007) · Gut · doi:10.1136/gut.2007.131672 · Cited by 82
Mishra, R., Emancipator, S. N., Miller, C. M., Kern, T. S., & Simonson, M. S. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00323.2003 · Cited by 82
Shek, E. W., & Scarpace, P. J. (2000) · Regulatory Peptides · doi:10.1016/s0167-0115(00)00151-8 · Cited by 82
Roles of leptin in prenatal and perinatal brain development
Udagawa, J., Hatta, T., Hashimoto, R., & Otani, H. (2007) · Congenital Anomalies · doi:10.1111/j.1741-4520.2007.00150.x · Cited by 81
Amino Acid Variants in the Human Leptin Receptor: Lack of Association to Juvenile Onset Obesity
Echwald, S. M., Sørensen, T. D., Sørensen, T. I. A., Tybjærg‐Hansen, A., Andersen, T., Chung, W. K., Leibel, R. L., & Pedersen, O. B. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6430 · Cited by 81
Messinis, I. E. (1999) · Human Reproduction Update · doi:10.1093/humupd/5.1.52 · Cited by 81
Comparing the hypothalamic and extrahypothalamic actions of endogenous hyperleptinemia
Wang, Z.-W., Zhou, Y.-T., Kakuma, T., Lee, Y., Higa, M., Kalra, S. P., Dube, M. G., Kalra, P. S., & Unger, R. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10373 · Cited by 81
Serum leptin levels in the acquired immunodeficiency syndrome
Grünfeld, C., Pang, M., Shigenaga, J. K., Jensen, P. B., Lallone, R. L., Friedman, J. M., & Kr, F. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.81.12.8954039 · Cited by 81
Self-citationThe role of leptin-->STAT3 signaling in neuroendocrine function: an integrative perspective
Bates, S. H., & Myers, M. G. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0494-z · Cited by 81
Muñoz, G., Óvilo, C., Silio, L. F., Tomás, A., Noguera, J. L., & Rodríguez, M. C. (2008) · Journal of Animal Science · doi:10.2527/jas.2008-1127 · Cited by 80
Hua, P., Feng, W., Ji, S., Raij, L. R., & Jaimes, E. A. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00293.2010 · Cited by 80
Passage of leptin across the blood-testis barrier
Banks, W. A., McLay, R. N., Kastin, A. J., Sarmiento, U. M., & Scully, S. A. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.276.6.e1099 · Cited by 80
Leptin in the regulation of the immunometabolism of adipose tissue-macrophages
Monteiro, L. D. B., Pereira, J. A. D. S., Palhinha, L., & Moraes‐Vieira, P. M. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr1218-478r · Cited by 80
Central nervous system nitric oxide synthase activity regulates insulin secretion and insulin action
Shankar, R., Zhu, J. S., Ladd, B., Henry, D., Shen, H. Q., & Baron, A. D. (1998) · Journal of Clinical Investigation · doi:10.1172/jci3030 · Cited by 79
Translational value of animal models of obesity—Focus on dogs and cats
Osto, M., & Lutz, T. A. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.03.036 · Cited by 79
Glial cells as integrators of peripheral and central signals in the regulation of energy homeostasis
Nampoothiri, S. S., Nogueiras, R., Schwaninger, M., & Prévot, V. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00610-z · Cited by 82
Lin, X., Braymer, H. D., Bray, G. A., & York, D. A. (1998) · Life Sciences · doi:10.1016/s0024-3205(98)00250-1 · Cited by 79
Demozay, D., Rocchi, S., Mas, J.-C., Grillo, S., Pirola, L., Chavey, C., & OBBERGHEN, E. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312062200 · Cited by 79
Diamant, M., Rieneck, K., Mechti, N., Zhang, X., Svenson, M., Bendtzen, K., & Klein, B. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00750-3 · Cited by 79
Absence of Soluble Leptin Receptor in Plasma fromdbPas/dbPas and Otherdb/db Mice
Cai, L., Ioffe, E., Fidahusein, N., Connolly, E. P., & Friedman, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.10078 · Cited by 79
Self-citationGarcia, J. M., Splenser, A. E., Kramer, J. R., Alsarraj, A., Fitzgerald, S. J., Ramsey, D. J., & El‐Serag, H. B. (2013) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2013.07.038 · Cited by 78
Leptin Suppresses Mouse Taste Cell Responses to Sweet Compounds
Yoshida, R., Noguchi, K., Shigemura, N., Jyotaki, M., Takahashi, I., Margolskee, R. F., & Ninomiya, Y. (2015) · Diabetes · doi:10.2337/db14-1462 · Cited by 78
Soler, M. J., Riera, M., & BATLLE, D. C. (2012) · Experimental Diabetes Research · doi:10.1155/2012/616313 · Cited by 78
Tian, Y., Wang, S., Ma, Y., Lim, G., Kim, H., & Mao, J. (2011) · Pain · doi:10.1016/j.pain.2011.01.054 · Cited by 78
Serum leptin level in women with idiopathic intracranial hypertension
Lampl, Y. (2002) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.72.5.642 · Cited by 78
THE NEUROENDOCRINOLOGY OF CHILDHOOD OBESITY
Lustig, R. H. (2001) · Pediatric Clinics of North America · doi:10.1016/s0031-3955(05)70348-5 · Cited by 78
Physiological Role of Cholecystokinin B/Gastrin Receptor in Leptin Secretion
Attoub, S., Levasseur, S., Buyse, M., Goïot, H., Laigneau, J., Moizo, L., Hervatin, F., MARCHAND‐BRUSTEL, Y. L., Lewin, J. M. M., & Bado, A. (1999) · Endocrinology · doi:10.1210/endo.140.10.7079 · Cited by 78
Kapitonov, V. V., & Jurka, J. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00013153 · Cited by 78
da Silva, B. A., Bjørbæk, C., Uotani, S., & Flier, J. S. (1998) · Endocrinology · doi:10.1210/endo.139.9.6168 · Cited by 78
Brann, D. W., Wade, M. F., Dhandapani, K. M., Mahesh, V. B., & Buchanan, C. D. (2002) · Steroids · doi:10.1016/s0039-128x(01)00138-6 · Cited by 78
Hamann, U., Brauch, H. B., Garvin, A. M., Bastert, G., & Scott, R. J. (1997) · Genes Chromosomes and Cancer · doi:10.1002/(sici)1098-2264(199702)18:2 · Cited by 24
Sex Differences in Circulating Human Leptin Pulse Amplitude: Clinical Implications
Licinio, J. (1998) · Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.83.11.4140 · Cited by 77
Rationale for Leptin-Replacement Therapy for Severe Lipodystrophy
Oral, E. A., & Chan, J. L. (2010) · Endocrine Practice · doi:10.4158/ep09155.ra · Cited by 77
Zheng, F., Zeng, Y.-J., Plati, A. R., Elliot, S. J., Berho, M. E., Potier, M., Striker, L. J., & Striker, G. E. (2006) · Kidney International · doi:10.1038/sj.ki.5001578 · Cited by 77
Increased hypercholesterolemia and atherosclerosis in mice lacking both ApoE and leptin receptor
Wu, K. K., Wu, T.-J., Chin, J., Mitnaul, L. J., Hernandez, M., Cai, T., Ren, N., Waters, M. G., Wright, S. D., & Cheng, K. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.01.029 · Cited by 77
Islam, M. S., Morton, N. M., Hansson, A., & Emilsson, V. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7399 · Cited by 77
Tena‐Sempere, M., Pinilla, L., Zhang, F., González, L. C., Huhtaniemi, I. T., Casanueva, F. F., Diéguez, C., & Aguilar, E. (2001) · Biology of Reproduction · doi:10.1095/biolreprod64.2.634 · Cited by 77
Ranganathan, S., Ciaraldi, T. P., Henry, R. R., Mudaliar, S. R. D., & Kern, P. A. (1998) · Endocrinology · doi:10.1210/endo.139.5.5980 · Cited by 77
Leptin-dependent platelet aggregation in healthy, overweight and obese subjects
Corsonello, A., Perticone, F., Malara, A., Domenico, D. D., Loddo, S., Buemi, M., Ientile, R., & Corica, F. (2003) · International Journal of Obesity · doi:10.1038/sj.ijo.0802273 · Cited by 76
Gotoh, N., Nagao, K., Onoda, S., Shirouchi, B., Furuya, K., Nagai, T., Mizobe, H., Ichioka, K., Watanabe, H., Yanagita, T., et al. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9026553 · Cited by 76
An overview of mongenic and syndromic obesities in humans
Chung, W. K. (2011) · Pediatric Blood & Cancer · doi:10.1002/pbc.23372 · Cited by 76
Mazor, R., Friedmann‐Morvinski, D., Alsaigh, T., Kleifeld, O., Kistler, E. B., Rousso-Noori, L., Huang, C., Li, J. B., Verma, I. M., & Schmid‐Schönbein, G. W. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aah6324 · Cited by 76
Expression and Activity of Arginase Isoenzymes During Normal and Diabetes-Impaired Skin Repair
Kämpfer, H., Pfeilschifter, J. M., & Frank, S. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12610.x · Cited by 77
GPL, a Novel Cytokine Receptor Related to GP130 and Leukemia Inhibitory Factor Receptor
Diveu, C., Lelièvre, E., Perret, D., Lagrue-Lak-Hal, A.-H., Froger, J., Guillet, C., Chevalier, S., Rousseau, F., Wesa, A. K., Preisser, L., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307286200 · Cited by 76
Free and protein bound leptin are distinct and independently controlled factors in energy regulation
Brabant, G. E., Horn, R., Mühlen, A. V. Z., Mayr, B. M., Wurster, U., Heidenreich, F., Schnabel, D., Grüters‐Kieslich, A., Zimmermann‐Belsing, T., & Feldt‐Rasmussen, U. (2000) · Diabetologia · doi:10.1007/s001250051326 · Cited by 76
Thon, M., Hosoi, T., & Ozawa, K. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2016.00138 · Cited by 75
Taga, T. (1997) · Annals of Medicine · doi:10.3109/07853899708998744 · Cited by 75
Ontogenesis of Leptin Receptor in Rat Leydig Cells1
Caprio, M., Fabbrini, E., Ricci, G., Basciani, S., Gnessi, L., Arizzi, M., Carta, A. R., Martino, M. U. D., Isidori, A. M., Frajese, G. V., et al. (2003) · Biology of Reproduction · doi:10.1095/biolreprod.102.007831 · Cited by 75
Leptin and Leptin Receptor in Anterior Pituitary Function
Lloyd, R. V., Jin, L. G., Tsumanuma, I., Vidal, S., Kovács, K., Horváth, É., Scheithauer, B. W., Couce, M., & Burguera, B. G. (2001) · Pituitary · doi:10.1023/a:1012982626401 · Cited by 76
Wang, Y., Wan, R., & Hu, C. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00702-w · Cited by 74
PPAR α in Obesity: Sex Difference and Estrogen Involvement
Yoon, M. (2010) · PPAR Research · doi:10.1155/2010/584296 · Cited by 74
Structure-Function Studies of Human Leptin
Imagawa, K., Numata, Y., Katsuura, G., Sakaguchi, I., Morita, A., Kikuoka, S., Matumoto, Y., Tsuji, T., Tamaki, M., Sasakura, K., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35245 · Cited by 74
Leptin receptor modulation of adiposity and fertility
Israel, D. D., & Chua, S. C. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.07.004 · Cited by 74
Masuyama, T., Fuse, M., Yokoi, N., Shinohara, M., Tsujii, H., Kanazawa, M., Kanazawa, Y., Komeda, K., & TANIGUCHI, K. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00548-5 · Cited by 74
Mercer, J. G., Moar, K. M., Findlay, P. A., Hoggard, N., & Adam, C. L. (1998) · Regulatory Peptides · doi:10.1016/s0167-0115(98)00078-0 · Cited by 74
MacDonald, M. L. E., Singaraja, R. R., Bissada, N., Ruddle, P., Watts, R., Karasinska, J. M., Gibson, W. T., Fiévet, C., Vance, J. E., Staels, B., et al. (2007) · Journal of Lipid Research · doi:10.1194/jlr.m700478-jlr200 · Cited by 73
THE NEUROENDOCRINOLOGY OF OBESITY
Lustig, R. H. (2001) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/s0889-8529(05)70211-5 · Cited by 73
Doehner, W., Rauchhaus, M., Godsland, I. F., Egerer, K., Niebauer, J., Sharma, R., Cicoira, M., Florea, V. G., Coats, A. J. S., & Anker, S. D. (2002) · International Journal of Cardiology · doi:10.1016/s0167-5273(02)00022-0 · Cited by 73
Aberrant expression and possible involvement of the leptin receptor in endometrial cancer
Yuan, S. F., Tsai, K., Chung, Y.-F., Chan, T., Yeh, Y., Tsai, L., & Su, J. (2004) · Gynecologic Oncology · doi:10.1016/j.ygyno.2003.11.043 · Cited by 73
Obese (ob) Gene Defects are Rare in Human Obesity
Carlsson, B., Lindell, K., Gabrielsson, B. G., Karlsson, C., Bjarnason, R. G., Westphal, O., Karlsson, U., Sjöström, L., & Carlsson, L. M. S. (1997) · Obesity Research · doi:10.1002/j.1550-8528.1997.tb00280.x · Cited by 73
Leptin constrains acetylcholine-induced insulin secretion from pancreatic islets of ob/ob mice.
Chen, N.-G., Swick, A. G., & Romsos, D. R. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119629 · Cited by 73
Bryson, J. M., Phuyal, J. L., Swan, V., & Caterson, I. D. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.3.e417 · Cited by 73
LEPR hypomethylation is significantly associated with gastric cancer in males
Yu, H., Pan, R., Qi, Y., Zheng, Z., Li, J., Li, H., Ying, J., Xu, M., & Duan, S. (2020) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2020.104493 · Cited by 72
Ikegami, H., Babaya, N., & Noso, S. (2021) · Journal of Diabetes Investigation · doi:10.1111/jdi.13576 · Cited by 72
Animal Models of Diabetes Mellitus for Islet Transplantation
Sakata, N., Yoshimatsu, G., Tsuchiya, H., Egawa, S., & Unno, M. (2012) · Experimental Diabetes Research · doi:10.1155/2012/256707 · Cited by 72
Gastric leptin: a new manager of gastrointestinal function
Guilmeau, S., Buyse, M., & Bado, A. (2004) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2004.06.008 · Cited by 72
Role of Krüppel-like factor 15 in PEPCK gene expression in the liver
Teshigawara, K., Ogawa, W., Mori, T., Matsuki, Y., Watanabe, E., Hiramatsu, R., Inoue, H., Miyake, K., Sakaue, H., & Kasuga, M. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.096 · Cited by 72
Desai, M., Li, T., & Ross, M. G. (2011) · Endocrinology · doi:10.1210/en.2010-1217 · Cited by 72
Bennett, P. A., Sjöholm, K., Wilson, C., Carlsson, L. M. S., Carlsson, B., & Robinson, I. C. A. F. (1999) · Neuroendocrinology · doi:10.1159/000054444 · Cited by 72
Leptin and cancer: from cancer stem cells to metastasis
Park, J., & Scherer, P. E. (2011) · Endocrine Related Cancer · doi:10.1530/erc-11-0163 · Cited by 72
Rezonzew, G., Chumley, P. H., Feng, W., Hua, P., Siegal, G. P., & Jaimes, E. A. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00661.2011 · Cited by 72
Kapodistria, K., Tsilibary, E.-P. C., Kotsopoulou, E. S., Moustardas, P., & Kitsiou, P. V. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13259 · Cited by 72
Leptin Levels Are Associated with Fat Oxidation and Dietary‐Induced Weight Loss in Obesity
Verdich, C., Toubro, S., Buemann, B., Holst, J. J., Bülow, J., Simonsen, L., Søndergaard, S. B., Christensen, N. J., & Astrup, A. V. (2001) · Obesity Research · doi:10.1038/oby.2001.59 · Cited by 72
A human leptin mutant induces weight gain in normal mice
Verploegen, S. A. B. W., Plaetinck, G., Devos, R., der Heyden, J. V., & Guisez, Y. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00192-0 · Cited by 72
Doulberis, M., Papaefthymiou, A., Pοlyzos, S. A., Katsinelos, P., Grigoriadis, N., Srivastava, D., & Kountouras, J. (2020) · Minerva Endocrinology · doi:10.23736/s0391-1977.19.03058-x · Cited by 71
Kořínková, L., Pražienková, V., Černá, L., Karnošová, A., Železná, B., Kuneš, J., & Maletı́nská, L. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.597583 · Cited by 71
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