The DOI matches its Crossref record; 54 of the 57 references it cites were found in a registry or an index.
Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
Abstract
Insulin stimulates the autophosphorylation of tyrosine residues of the beta subunit of the insulin receptor (IR); this modified insulin-independent kinase has increased activity toward exogenous substrates in vitro. We show here that replacement of one or both of the twin tyrosines (residues 1162 and 1163) with phenylalanine results in a dramatic reduction in or loss of insulin-activated autophosphorylation and kinase activity in vitro. In vivo, these mutations not only result in a substantial decrease in insulin-stimulated IR autophosphorylation but also in a parallel decrease in the insulin-activated uptake of 2-deoxyglucose. Furthermore, a truncated IR protein (lacking the last 112 amino acids) has an unstable beta subunit; this mutant has no kinase activity in vitro or in vivo and does not mediate insulin-stimulated uptake of 2-deoxyglucose. IR autophosphorylation is thus implicated in the regulation of IR activities, with tyrosines 1162 and 1163 as major sites of this regulation.
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
“Mutagenesis of any of the three major phosphorylation sites (at residues 1158, 1163, and 1162) impairs insulin receptor tyrosine kinase activity, leading to a decrease in the metabolic and growth-promoting effects of insulin [141, 142].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [141]
In the citing paper
“Inhibitors of PI3K impair glucose transport and block the activation of glycogen synthase and hexokinase- (HK-) II expression [138–146]”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [141]
Citations
Cites
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
Scatchard, G. (1949) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1949.tb27297.x · Cited by 19,724
Yanisch-Perron, C., Vieira, J., & Messing, J. W. (1985) · Gene · doi:10.1016/0378-1119(85)90120-9 · Cited by 14,909
Studies on transformation of Escherichia coli with plasmids
Hanahan, D. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80284-8 · Cited by 11,194
Ullrich, A., Coussens, L. M., Hayflick, J. S., Dull, T. J., Gray, A., Tam, A. W., Lee, J., Yarden, Y., Libermann, T. A., Schlessinger, J., et al. (1984) · Nature · doi:10.1038/309418a0 · Cited by 2,751
Southern, P. J., & Berg, P. R. (1982) · PubMed · Cited by 2,740
Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
Ullrich, A., Bell, J. R., Chen, E. Y., Herrera, R., Petruzzelli, L., Dull, T. J., Gray, A., Coussens, L. M., Liao, Y.-C., Tsubokawa, M., et al. (1985) · Nature · doi:10.1038/313756a0 · Cited by 2,251
Hunter, T. R., & Cooper, J. A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.004341 · Cited by 2,142
CELLULAR ONCOGENES AND RETROVIRUSES
Bishop, J. M. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.001505 · Cited by 1,666
The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling
Ebina, Y., Ellis, L., Jarnagin, K., Edery, M., Gráf, L., Clauser, É., Ou, J. J., Masiarz, F. R., Kan, Y. W., Goldfine, I. D., et al. (1985) · Cell · doi:10.1016/0092-8674(85)90334-4 · Cited by 1,477
Self-citation
Cited by
Sorted by citations
Items 801–900 of 1,000
Tavaré, J. M., Ramos, P., & Ellis, L. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)92353-y · Cited by 20
Self-citationJacob, K. K., Whittaker, J., & Stanley, F. M. (2002) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00674-8 · Cited by 19
Tavaré, J. M., & Dickens, M. (1991) · Biochemical Journal · doi:10.1042/bj2740173 · Cited by 19
Insulin receptor gene mutation: A molecular genetical and funtional analysis
Makino, H., Taira, M., Shimada, F., Hashimoto, N., Suzuki, Y., Nozaki, O., Hatanaka, Y., & Yoshida, S. (1992) · Cellular Signalling · doi:10.1016/0898-6568(92)90030-c · Cited by 18
Levy-Toledano, R., Accili, D., & Taylor, S. I. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(93)90090-c · Cited by 19
Magré, J., Grigorescu, F., Reynet, C., Caron, M., Capony, J., White, M. F., Picard, J., Mirouze, J., & Capeau, J. (1989) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-69-1-142 · Cited by 19
Falcioni, R., Perrotti, N., Piaggio, G., Kennel, S. K., & Sacchi, A. (1989) · Molecular Carcinogenesis · doi:10.1002/mc.2940020611 · Cited by 19
Sung, C. K. (1992) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240480106 · Cited by 19
Comparative studies of hepatitis B virus precore and core particles
Ou, J. J., & Bell, K. D. (1990) · Virology · doi:10.1016/0042-6822(90)90067-2 · Cited by 18
Lloberas, J. (1998) · International Immunology · doi:10.1093/intimm/10.5.593 · Cited by 18
Structural Differences between Repressed and Derepressed Forms of p60 c- src
MacAuley, A., & Cooper, J. A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.6.2648-2656.1989 · Cited by 18
Transforming activity of mutant human p53 alleles
Slingerland, J. M., & Benchimol, S. (1991) · Journal of Cellular Physiology · doi:10.1002/jcp.1041480309 · Cited by 18
Insulin Resistance: A Look at the Role of Insulin Receptor Kinase
Reddy, S. S. ‐., & Kahn, C. R. (1988) · Diabetic Medicine · doi:10.1111/j.1464-5491.1988.tb01069.x · Cited by 18
Identification of cultured cells expressing ligand-gated cationic channels
Rogers, S. W., Gahring, L. C., Papke, R. L., & Heinemann, S. (1991) · Protein Expression and Purification · doi:10.1016/1046-5928(91)90058-q · Cited by 18
Oliveira, E. D. A., Cheim, L. M. G., Veloso, R. V., Arantes, V. C., Reis, M. A. D. B., Carneiro, E. M., Boschero, A. C., & Latorraca, M. Q. (2007) · Nutrition · doi:10.1016/j.nut.2007.09.002 · Cited by 18
Stephens, D. J., & Banting, G. S. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01165-4 · Cited by 18
Properties of an insulin receptor with an IGF‐1 receptor loop exchange in the cysteine‐rich region
Hoyne, P. A., ELLEMAN, T. C., Adams, T. E., Richards, K. M., & Ward, C. W. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01237-0 · Cited by 18
Garofalo, R. S., & Rosen, O. M. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.7.2806-2817.1989 · Cited by 18
Evidence against insulin-stimulated phosphorylation of calmodulin in 3T3-L1 adipocytes
Blackshear, P. J., & Haupt, D. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84929-3 · Cited by 18
The Insulin Receptor Tyrosine Kinase
Rothenberg, P., White, M. F., & Kahn, C. R. (1990) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-74098-5_11 · Cited by 18
Kole, H. K., Liotta, A. S., Kole, S., Roth, J., Montrose‐Rafizadeh, C., & Bernier, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31619 · Cited by 18
Yap, H. M., Lee, Y. Z., Harith, H. H., Tham, C. L., Cheema, M. S., Shaari, K., & Israf, D. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-34847-0 · Cited by 17
A Computational Study of the Phosphorylation Mechanism of the Insulin Receptor Tyrosine Kinase
Zhou, B., & Wong, C. F. (2009) · The Journal of Physical Chemistry A · doi:10.1021/jp810827w · Cited by 17
Zolfaghari, R., Glick, J. M., & Fisher, E. A. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38682-x · Cited by 17
Shiba, T., Tobe, K., Koshio, O., Yamamoto, R., Shibasaki, Y., Matsumoto, N., Toyoshima, S., OSAWA, T., Akanuma, Y., Takaku, F., et al. (1990) · Biochemical Journal · doi:10.1042/bj2670787 · Cited by 17
Insulin‐antagonistic effects of counterregulatory hormones: Clinical and mechanistic aspects
Smith, U., & Lager, I. (1989) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610050604 · Cited by 18
Martin, A., Magnusson, R. P., Kendler, D. L., Concepcion, E. S., Ben‐Nun, A., & Davies, T. F. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116362 · Cited by 17
Endocytosis by the asialoglycoprotein receptor is independent of cytoplasmic serine residues.
Geffen, I., Fuhrer, C., & Spiess, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8425 · Cited by 17
Wahlberg, J. M., Geffen, I., Reymond, F., Simmen, T., & Spiess, M. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.2.285 · Cited by 17
Ny, T., Hansson, L., Lawrence, D. A., Leonardsson, G., & Åstedt, B. (1989) · Fibrinolysis and Proteolysis · doi:10.1016/0268-9499(89)90045-3 · Cited by 17
Khare, S., Holgren, C. W., & Samarel, A. M. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00008.2006 · Cited by 16
Brunetti, A., Maddux, B. A., Wong, K.-Y., Hofmann, C. A., Whittaker, J., Sung, C. K., & Goldfine, I. D. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91056-5 · Cited by 16
Castle, A. M., & Castle, J. D. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80752-2 · Cited by 16
Gimenez‐Roqueplo, A., Leconte, I., Cohen, P. A., Simon, D., Guyene, T. T., Célérier, J., Pau, B., Corvol, P. L., Clauser, É., & Jeunemaı̂tre, X. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9838 · Cited by 16
SCHAEFER, E. M., & Guimond, S. E. (1998) · Analytical Biochemistry · doi:10.1006/abio.1998.2716 · Cited by 16
Eléouët, J., & Roméo, P. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17716.x · Cited by 17
Nuclear proto-oncogene products transactivate the human papillomavirus type 16 promoter
Nürnberg, W., Artuc, M., Vorbrüggen, G., Kalkbrenner, F., Moelling, K., Czarnetzki, B. M., & Schadendorf, D. (1995) · British Journal of Cancer · doi:10.1038/bjc.1995.196 · Cited by 16
Rochet, N., Blanche, S., Carel, J., Fischer, A., Deist, F. L., Griscelli, C., OBBERGHEN, E. V., & MARCHAND‐BRUSTEL, Y. L. (1989) · Diabetologia · doi:10.1007/bf00265089 · Cited by 16
Cole, L.-A., Zirngibl, R. A., Craig, A. W., Jia, Z., & Greer, P. A. (1999) · Protein Engineering Design and Selection · doi:10.1093/protein/12.2.155 · Cited by 16
Macaulay, S. L., Polites, M., Hewish, D. R., & Ward, C. W. (1994) · Biochemical Journal · doi:10.1042/bj3030575 · Cited by 16
Mutations of the human insulin receptor gene
Taylor, S. I., Cama, A., Kadowaki, H., Kadowaki, T., & Accili, D. (1990) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(90)90024-w · Cited by 15
Vecchio, R. L. D., & Pilch, P. F. (1989) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(89)90270-8 · Cited by 15
Mutant p53 Tumor Suppressor Alleles Release ras -Induced Cell Cycle Growth Arrest
Hicks, G. G., Egan, S. E., Greenberg, A. H., & Mowat, M. R. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.3.1344-1352.1991 · Cited by 15
The Role of Glycosylphosphoinositides in Signal Transduction
Saltiel, A. R., Osterman, D. G., Darnell, J. C., Chan, B., & Sorbara-Cazan, L. R. (1989) · Elsevier eBooks · doi:10.1016/b978-0-12-571145-6.50011-x · Cited by 15
Metabolic and Molecular Pathogenesis of Type 2 Diabetes Mellitus
DeFronzo, R. A., Mandarino, L. J., & Ferrannini, E. (2003) · Wiley eBooks · doi:10.1002/0470862092.d0310 · Cited by 15
Synthesis of soluble myelin-associated glycoprotein in insect and mammalian cells
Johnson, P. W., Attia, J., Richardson, C. D., Roder, J., & Dunn, R. J. (1989) · Gene · doi:10.1016/0378-1119(89)90076-0 · Cited by 15
Tyrosine kinase activity of insulin receptors from an insulin-resistant patient with leprechaunism
Cama, A., & Taylor, S. I. (1987) · Diabetologia · doi:10.1007/bf00277320 · Cited by 15
Functional Analysis of Phosphorylation at Serine 532 of Human c-Myb by MAP Kinase
Vorbrüggen, G., Lovrić, J., & Moelling, K. (1996) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1996.377.11.721 · Cited by 15
Identification and Characterization of a Functional Murine FLT3 Isoform Produced by Exon Skipping
Lavagna, C., Marchetto, S., Birnbaum, D., & Rosnet, O. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3165 · Cited by 14
Insulin downregulates the steady-state level of its receptor's messenger ribonucleic acid
Rohilla, A. M. K., Anderson, C. M., Wood, W. M., & Berhanu, P. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91595-4 · Cited by 14
What is the role of the insulin receptor tyrosine kinase?
Espinal, J. (1988) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(88)90170-3 · Cited by 14
Camps, M., Gumà, A., Testar, X., Palacı́n, M., & Antonio Zorzano, A. (1990) · Endocrinology · doi:10.1210/endo-127-5-2561 · Cited by 13
Staugaitis, S. M., Bernier, L., Smith, P. R., & Colman, D. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490250413 · Cited by 14
Gryz, E. A., & Meakin, S. O. (2000) · Oncogene · doi:10.1038/sj.onc.1203330 · Cited by 14
Yu, K. T., Benjamin, W. B., Ramakrishna, S., Khalaf, N., & Czech, M. (1990) · Biochemical Journal · doi:10.1042/bj2680539 · Cited by 14
Lombardo, A. M., Costa, E., Chao, W. R., Toll, L., Hobbs, P. D., Jong, L., Lee, M. O., Pfahl, M., Ely, K. R., & Dawson, M. I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37283-6 · Cited by 14
A family of polypeptide substrates and inhibitors of insulin receptor kinase
Meyerovitch, J., Kahn, C. R., & Shechter, Y. (1990) · Biochemistry · doi:10.1021/bi00467a010 · Cited by 14
The Mechanisms of Insulin Action
White, M. F., & Copps, K. D. (2015) · Elsevier eBooks · doi:10.1016/b978-0-323-18907-1.00033-0 · Cited by 12
Huang, M., & Miller, W. L. (2001) · Endocrinology · doi:10.1210/endo.142.6.8206 · Cited by 13
Inhibitors of the insulin receptor tyrosine kinase
Srinivas, P. R., & Grunberger, G. (1994) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(94)90032-9 · Cited by 13
Bernier, M., Nadiv, O., & Kole, H. K. (1995) · Biochemistry · doi:10.1021/bi00026a017 · Cited by 13
Strout, H. V., Vicario, P. P., Saperstein, R., & Slater, E. E. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80328-0 · Cited by 13
A Murine fer Testis-Specific Transcript ( ferT) Encodes a Truncated Fer Protein
Fischman, K., Edman, J. C., Shackleford, G. M., Turner, J. A., Rutter, W. J., & Nir, U. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.1.146-153.1990 · Cited by 13
Self-citationExpression of the Insulin Receptor with a Recombinant Vaccinia Virus
Tauer, T. J., Volle, D. J., Rhode, S. L., & Lewis, R. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.331 · Cited by 13
Cadherin-Mediated Transmembrane Interactions
Levenberg, S., Sadot, E., Goichberg, P., & Geiger, B. (1998) · Cell Communication & Adhesion · doi:10.3109/15419069809004473 · Cited by 13
Hormonal regulation of protein tyrosine kinase activity
Ramachandran, J., & Ullrich, A. (1987) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(87)90030-7 · Cited by 13
Antibody-induced down-regulation of a mutated insulin receptor lacking an intact cytoplasmic domain
Morgan, D. O., Ellis, L., Rutter, W. J., & Roth, R. A. (1987) · Biochemistry · doi:10.1021/bi00385a001 · Cited by 13
Self-citationMolecular genetics of severe insulin resistance.
Elsas, L. J., Longo, N., Langley, S. D., Griffin, L. D., & Shuster, R. C. (1989) · PubMed Central · Cited by 12
Bovi, R. J. D., & Miller, W. T. (2017) · Analytical Biochemistry · doi:10.1016/j.ab.2017.08.011 · Cited by 12
Theoretical and Computational Studies of Peptides and Receptors of the Insulin Family
Vashisth, H. (2015) · Membranes · doi:10.3390/membranes5010048 · Cited by 14
The reversible and irreversible autophosphorylations of insulin receptor kinase.
Argetsinger, L. S., & Shafer, J. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41640-7 · Cited by 12
Jong, S. M., & Wang, L. H. (1991) · Journal of Virology · doi:10.1128/jvi.65.1.180-189.1991 · Cited by 12
Calı̀, G., Retta, S. F., Negri, R., Damiano, I., Gentile, R., Tarone, G., Nitsch, L., & Garbi, C. (1998) · European Journal of Cell Biology · doi:10.1016/s0171-9335(98)80053-8 · Cited by 12
Physical separation of ICAM-1 binding cells
Hedman, H., Brändén, H., & Lundgre, E. (1992) · Journal of Immunological Methods · doi:10.1016/0022-1759(92)90229-m · Cited by 12
Association and phosphorylation-dependent dissociation of proteins in the insulin receptor complex.
Zhang, W., Johnson, J. D., & Rutter, W. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11317 · Cited by 12
Self-citationHaft, C. R., & Taylor, S. I. (1994) · Biochemistry · doi:10.1021/bi00197a017 · Cited by 12
Kuratani, S., Matsuo, I., & Aizawa, S. (1997) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199706)209:2 · Cited by 116
Stone, J. C., Moran, M. F., & Pawson, T. J. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)00180-5 · Cited by 12
Yano, H., Wang, B.-E., Ahmad, I., Zhang, J., Abo, T., Nakayama, J., Krempen, K., & Kohwi, Y. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4603 · Cited by 11
Plaetinck, G., Combe, M. C., Corthésy, P., Seckinger, P., & Nabholz, M. (1989) · European Journal of Immunology · doi:10.1002/eji.1830190517 · Cited by 11
Reusch, J. E. B., Hsieh, P., Bhuripanyo, P., Carel, K. D., Leitner, J. W., Olefsky, J. M., & Draznin, B. (1995) · Endocrinology · doi:10.1210/en.136.6.2464 · Cited by 11
Klein, D. P., Jongstra‐Bilen, J., Ogryzlo, K., Chong, R., & Jongstra‐Bilen, J. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.7.3043-3048.1989 · Cited by 11
Naranda, T., D, A. G. M., & Olsson, L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11692 · Cited by 11
Vera, J. C., & Rosen, O. M. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.2.743-751.1990 · Cited by 11
Yan, P., Li, S., Liang, S. J., Giannini, S., & Fujita‐Yamaguchi, Y. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41549-9 · Cited by 11
Insulin-Sensitive Glucose Transport
Kôno, T. (1988) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60694-9 · Cited by 11
O’Brien, R. M., Houslay, M. D., Brindle, N. P. J., Milligan, G., Whittaker, J., & Siddle, K. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92784-8 · Cited by 11
Lesueur, L., Edery, M., Paly, J., Kelly, P. A., & Djiane, J. (1993) · Molecular Endocrinology · doi:10.1210/me.7.9.1178 · Cited by 11
Self-citationHsu, C., Shih, H. Y., Chang, Y. C., Huang, Z. L., Tsai, M. J., Chia, Y., Chen, C., Lai, Y., & Weng, C. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.01.033 · Cited by 10
Pavlopoulou, A., Karaca, E., Balestrazzi, A., & Georgakilas, A. G. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8683054 · Cited by 10
Ponzio, G., Debant, A., Contreres, J.-O., & Rossi, B. (1990) · Cellular Signalling · doi:10.1016/0898-6568(90)90068-l · Cited by 10
Looking for an insulin pill? Use the BRET methodology!
Issad, T., Boute, N., Boubekeur, S., Lacasa, D., & Siquier-Pernet, K. (2003) · Diabetes & Metabolism · doi:10.1016/s1262-3636(07)70016-2 · Cited by 10
Mutagenic structure/function analysis of the cytoplasmic cysteines of the insulin receptor
Macaulay, S. L., Polites, M., Frenkel, M. J., Hewish, D. R., & Ward, C. W. (1995) · Biochemical Journal · doi:10.1042/bj3060811 · Cited by 10
Weinmaster, G., Middlemas, D. S., & Hunter, T. R. (1988) · Journal of Virology · doi:10.1128/jvi.62.6.2016-2025.1988 · Cited by 10
Suzuki, Y., Hashimoto, N., Shimada, F., Taira, M., Mimura, M., Nozaki, O., Tawata, M., Onaya, T., Makino, H., & Yoshida, S. (1991) · Diabetologia · doi:10.1007/bf00500378 · Cited by 10
Rickles, R. J., Henry, P. A., Guan, W., Azimioara, M. D., Shakespeare, W. C., Violette, S. M., & Zoller, M. J. (1998) · Chemistry & Biology · doi:10.1016/s1074-5521(98)90112-0 · Cited by 10
Jonas, H. A., Eckardt, G. S., & Clark, S. (1990) · Endocrinology · doi:10.1210/endo-127-3-1301 · Cited by 10
Macaulay, S. L., Clark, S., & Larkins, R. G. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(92)90027-9 · Cited by 10
Roth, R. A. (1990) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-74098-5_9 · Cited by 10
Self-citationFunctional interactions of L-162,313 with angiotensin II receptor subtypes and mutants
Vianello, B., Clauser, É., Corvol, P. L., & Monnot, C. (1998) · European Journal of Pharmacology · doi:10.1016/s0014-2999(98)00081-8 · Cited by 9
Metadata
- Authors
- Ellis, L., Clauser, E., Morgan, D. O., Edery, M., Roth, R. A., & Rutter, W. J.
- Affiliations
- University of California, San Francisco (US)
- Stanford University (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1986-06
- Volume
- 45
- Issue
- 5
- Pages
- 721-732
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2030156849
- Cited by
- 1,070
- References
- 57
- Citations by year
- 2026: 1 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 4 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 4 · 2015: 6 · 2014: 4 · 2013: 1 · 2012: 5
- FWCI
- 34.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01am021344-09, 5r01am034926-02)
- National Institute of General Medical Sciences (GM 28520)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Keywords
- insulin receptor, insulin receptor beta-subunit, autophosphorylation, 2-deoxyglucose uptake, insulin signaling, point mutations
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Cricetulus, Deoxy Sugars, Deoxyglucose, DNA, Female, Gene Expression Regulation, Cricetinae, Humans, Insulin, Ovary, Phosphorylation, Protein-Tyrosine Kinases, Receptor, Insulin, Transfection, Tyrosine
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