Cited by 1,070Metabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase SignalingPancreatic function and diabetes

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

Ellis, Leland, Clauser, Eric, Morgan, David O., Edery, Marc, Roth, Richard A., Rutter, William J.·1986·Cell

DOI 10.1016/0092-8674(86)90786-5

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1016/0092-8674(86)90786-5

Cites

54 of 54 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?

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
Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors
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
Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
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
Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter.
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
PROTEIN-TYROSINE KINASES
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

Show all 57 references

Sorted by citations

Items 101–200 of 1,000

Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells.
Belkin, A. M., Zhidkova, N. I., Balzac, F., Altruda, F., Tomatis, D., Maier, A., Tarone, G., Koteliansky, V., & Burridge, K. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.132.1.211 · Cited by 227
Expression of tau protein in non-neuronal cells: microtubule binding and stabilization
Lee, G. S., & Rook, S. L. (1992) · Journal of Cell Science · doi:10.1242/jcs.102.2.227 · Cited by 226
An HMG-like protein that can switch a transcriptional activator to a repressor
Lehming, N., Thanos, D., Brickman, J. M., Ma, J., Maniatis, T., & Ptashne, M. (1994) · Nature · doi:10.1038/371175a0 · Cited by 225
Primary Structure of a Putative Receptor for a Ligand of the Insulin Family
Shier, P., & Watt, V. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63737-8 · Cited by 224
Acute insulin action requires insulin receptor kinase activity: introduction of an inhibitory monoclonal antibody into mammalian cells blocks the rapid effects of insulin.
Morgan, D. O., & Roth, R. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.1.41 · Cited by 221
Self-citation
The geminivirus nuclear shuttle protein is a virulence factor that suppresses transmembrane receptor kinase activityPreprint
Fontes, E. P. B., dos Santos, A. A., Luz, D. F., Waclawovsky, A. J., & Chory, J. (2004) · Genes & Development · doi:10.1101/gad.1245904 · Cited by 219
Catenin-dependent and -independent Functions of Vascular Endothelial Cadherin
Navarro, P., Caveda, L., Breviario, F., Mânduțeanu, I., Lampugnani, M. G., & Dejana, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.52.30965 · Cited by 218
Molecular analysis of signal transduction by growth factors
Yarden, Y., & Ullrich, A. (1988) · Biochemistry · doi:10.1021/bi00409a001 · Cited by 218
Human Connexin 32, a gap junction protein altered in the X-linked form of Charcot-Marie-Tooth disease, is directly regulated by the transcription factor SOX10
Bondurand, N. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.24.2783 · Cited by 209
INCENP Centromere and Spindle Targeting: Identification of Essential Conserved Motifs and Involvement of Heterochromatin Protein HP1
Ainsztein, A. M., Kandels-Lewis, S. E., Mackay, A. M., & Earnshaw, W. C. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1763 · Cited by 215
Polar Residues in the Transmembrane Domains of the Type 1 Angiotensin II Receptor Are Required for Binding and Coupling
Monnot, C., Bihoreau, C., Conchon, S., Curnow, K. M., Corvol, P. L., & Clauser, É. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1507 · Cited by 215
Cloning and characterization of the human V3 pituitary vasopressin receptor
de Keyzer, Y., Auzan, C., Lenne, F., Beldjord, C., Thibonnier, M., Bertagna, X., & Clauser, E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01268-7 · Cited by 209
All Autophosphorylation Sites of Epidermal Growth Factor (EGF) Receptor and HER2/neu Are Located in Their Carboxyl-terminal Tails
Margolis, B. L., Lax, I., Kris, R., Dombalagian, M., Honegger, A., Howk, R. S., Givol, D., Ullrich, A., & Schlessinger, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81674-x · Cited by 211
Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm.
Loewinger, L., & McKeon, F. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03073.x · Cited by 209
GAL4 fusion vectors for expression in yeast or mammalian cells
Sadowski, I., Bell, B., Broad, P. M., & Hollis, M. (1992) · Gene · doi:10.1016/0378-1119(92)90261-m · Cited by 209
The molecular and cell biology of glycosyltransferases
KLEENE, R. B., & Berger, E. G. (1993) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(93)90003-7 · Cited by 208
Trans-activation of the human immunodeficiency virus long terminal repeat by the hepatitis B virus X protein.
Seto, E., Yen, T. S. B., Peterlin, B. M., & Ou, J.-H. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.8286 · Cited by 208
Extrajunctional distribution of N-cadherin in cultured human endothelial cells
Salomon, D., Ayalon, O., Patel, R., Hynes, R. O., & Geiger, B. (1992) · Journal of Cell Science · doi:10.1242/jcs.102.1.7 · Cited by 207
Characterization of insulin/IGF hybrid receptors: contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation
Benyoucef, S., Surinya, K. H., Hadaschik, D., & Siddle, K. (2007) · Biochemical Journal · doi:10.1042/bj20061709 · Cited by 203
Structural Determinants for High-Affinity Binding of Insulin-Like Growth Factor II to Insulin Receptor (IR)-A, the Exon 11 Minus Isoform of the IR
Denley, A., Bonython, E. R., Booker, G. W., Cosgrove, L. J., Forbes, B. E., Ward, C. W., & Wallace, J. C. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0183 · Cited by 203
Protein kinases 1988: a current perspective
Blackshear, P. J., Nairn, A. C., & Kuo, J. F. (1988) · The FASEB Journal · doi:10.1096/fasebj.2.14.2972578 · Cited by 200
Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells
Wang, L., Fraley, C. D., Faridi, J. S., Kornberg, A., & Roth, R. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1534805100 · Cited by 197
Self-citation
Insulin receptor signaling. Activation of multiple serine kinases.
Czech, M. P., Klarlund, J. K., Yagaloff, K. A., Bradford, A. P., & Lewis, R. E. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37908-0 · Cited by 197
Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina.
Lutz, R. J., Trujillo, M. A., Denham, K. S., Wenger, L., & Sinensky, M. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.3000 · Cited by 196
14-3-3 (ϵ) Interacts with the Insulin-like Growth Factor I Receptor and Insulin Receptor Substrate I in a Phosphoserine-dependent Manner
Craparo, A., Freund, R., & Gustafson, T. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11663 · Cited by 196
Purification and partial sequence analysis of pp185, the major cellular substrate of the insulin receptor tyrosine kinase
Rothenberg, P., Lane, W. S., Karasik, A., Backer, J., White, M. F., & Kahn, C. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92976-5 · Cited by 196
Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes.
Wei, L., Alhenc‐Gelas, F., Soubrier, F., Michaud, A., Corvol, P. L., & Clauser, É. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67628-3 · Cited by 194
Reversibility of defective adipocyte insulin receptor kinase activity in non-insulin-dependent diabetes mellitus. Effect of weight loss.
Freidenberg, G. R., Reichart, D. R., Olefsky, J. M., & Henry, R. R. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113744 · Cited by 196
Phosphorylation of Insulin Receptor Substrate-1 (IRS-1) by Protein Kinase B Positively Regulates IRS-1 Function
Paz, K., Liu, Y., Shorer, H., Hemi, R., LeRoith, D., Quan, M., Kanety, H., Seger, R., & Zick, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28816 · Cited by 194
Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization
Dougher, M. M., & Terman, B. I. (1999) · Oncogene · doi:10.1038/sj.onc.1202478 · Cited by 194
Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase.
Konishi, H., Matsuzaki, H., Tanaka, M., Ono, Y., Tokunaga, C., Kuroda, S., & Kikkawa, U. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7639 · Cited by 190
GATA and Ets cis-Acting Sequences Mediate Megakaryocyte-Specific Expression
Lemarchandel, V., Ghysdael, J., Mignotte, V., Rahuel, C., & Roméo, P. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.668-676.1993 · Cited by 195
Recombinant myelin-associated glycoprotein confers neural adhesion and neurite outgrowth function
Johnson, P. W., Abramow-Newerly, W., Seilheimer, B., Sadoul, R., Tropak, M. B., Arquint, M., Dunn, R. J., Schachner, M., & Roder, J. (1989) · Neuron · doi:10.1016/0896-6273(89)90262-6 · Cited by 190
Identification of a Human Akt3 (Protein Kinase B γ) Which Contains the Regulatory Serine Phosphorylation Site
Nakatani, K., Sakaue, H., Thompson, D. A., Weigel, R. J., & Roth, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0559 · Cited by 190
Self-citation
Alpha-thrombin, epidermal growth factor, and okadaic acid activate the Na+/H+ exchanger, NHE-1, by phosphorylating a set of common sites.
Sardet, C., Fafournoux, P., & Pouysségur, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54977-2 · Cited by 187
The tyrosine kinase encoded by the MET proto-oncogene is activated by autophosphorylation.
Naldini, L., Vigna, E., Ferracini, R., Longati, P., Gandino, L., Prat, M., & Comoglio, P. M. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.1793 · Cited by 185
Stress-activated protein kinases (JNK and p38/HOG) are essential for vascular endothelial growth factor mRNA stability
Pagès, G., Berra, E., Milanini, J., Levy, A. P., & Pouysségur, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002104200 · Cited by 184
A mutation at tyrosine 1062 in MEN2A-Ret and MEN2B-Ret impairs their transforming activity and association with shc adaptor proteins
Asai, N., Murakami, H., Iwashita, T., & Takahashi, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17644 · Cited by 184
In Vivo Regulation of Alternative Pre-mRNA Splicing by the Clk1 Protein Kinase
Duncan, P. I., Stojdl, D. F., Marius, R. M., & Bell, J. C. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.10.5996 · Cited by 184
Activating and Inhibitory Mutations in Adjacent Tyrosines in the Kinase Domain of ZAP-70
Wange, R. L., Guitián, R., Isakov, N., Watts, J. D., Aebersold, R. H., & Samelson, L. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18730 · Cited by 183
A prolactin-dependent immune cell line (Nb2) expresses a mutant form of prolactin receptor.
Ali, S., Pellegrini, I., & Kelly, P. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54897-3 · Cited by 183
A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain.
Johnson, J. D., Edman, J. C., & Rutter, W. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.12.5677 · Cited by 182
Self-citation
Identification of insulin receptor tyrosine residues autophosphorylated in vitro.
Tornqvist, H. E., Pierce, M., Frackelton, A. R., Nemenoff, R. A., & Avruch, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61100-7 · Cited by 180
Identification of c-fos sequences involved in induction by insulin and phorbol esters.
Stumpo, D. J., Stewart, T., Gilman, M. Z., & Blackshear, P. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77921-6 · Cited by 180
ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.
Itin, C., Roche, A. C., Monsigny, M., & Hauri, H. P. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.3.483 · Cited by 179
c-myc Inhibition of MyoD and Myogenin-Initiated Myogenic Differentiation
Miner, J. H., & Wold, B. J. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2842 · Cited by 179
Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes.
Bernier, M., Laird, D. M., & Lane, M. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.7.1844 · Cited by 179
Peroxide(s) of vanadium : A novel and potent insulin-mimetic agent which activates the insulin receptor kinase
Kadota, S., Fantus, I. G., Deragon, G., Guyda, H. J., Hersh, B., & Posner, B. I. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(87)80115-8 · Cited by 177
Vanadate normalizes hyperglycemia in two mouse models of non-insulin-dependent diabetes mellitus.
Meyerovitch, J., Rothenberg, P., Shechter, Y., Bonner‐Weir, S., & Kahn, C. R. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115131 · Cited by 177
Characterization of an Interaction between Insulin Receptor Substrate 1 and the Insulin Receptor by Using the Two-Hybrid System
O’Neill, T. J., Craparo, A., & Gustafson, T. A. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6433 · Cited by 172
Expression of normal and mutant avian integrin subunits in rodent cells [published erratum appears in J Cell Biol 1989 Oct;109(4 Pt 1):1187]
Solowska, J. M. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.2.853 · Cited by 176
Evidence that Na+/H+ exchanger isoforms NHE1 and NHE3 exist as stable dimers in membranes with a high degree of specificity for homodimers.
Fafournoux, P., Noël, J., & Pouysségur, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41985-5 · Cited by 175
Steroid 17 alpha-hydroxylase and 17,20-lyase activities of P450c17: contributions of serine106 and P450 reductase
Lin, D., Black, S. M., Nagahama, Y., & Miller, W. L. (1993) · Endocrinology · doi:10.1210/endo.132.6.8504753 · Cited by 174
A protein‐arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor
Abramovich, C., Yakobson, B., Chebath, J., & Revel, M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.260 · Cited by 175
Profound ligand-independent kinase activation of fibroblast growth factor receptor 3 by the activation loop mutation responsible for a lethal skeletal dysplasia, thanatophoric dysplasia type II
Webster, M. K., d'Avis, P. Y., Robertson, S. C., & Donoghue, D. J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4081 · Cited by 177
A T‐cell specific TCR delta DNA binding protein is a member of the human GATA family.
Joulin, V., Bories, D., Eléouët, J., Labastie, M.-C., Chrétien, S., Mattéi, M., & Roméo, P. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07706.x · Cited by 172
Human hepatitis delta antigen is a nuclear phosphoprotein with RNA-binding activity
Chang, M., Baker, S. C., Soe, L. H., Kamahora, T., Keck, J., Makino, S., Govindarajan, S., & Lai, M. M. C. (1988) · Journal of Virology · doi:10.1128/jvi.62.7.2403-2410.1988 · Cited by 171
Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation.
Cooper, J. A., & MacAuley, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4232 · Cited by 170
Identification and sequence analysis of a second form of prolactin receptor by molecular cloning of complementary DNA from rabbit mammary gland.
Edery, M., Jolicoeur, C., Lévi-Meyrueis, C., Dusanter‐Fourt, I., Petridou, B., Boutin, J., Lesueur, L., Kelly, P. A., & Djiane, J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.6.2112 · Cited by 168
Self-citation
A point mutation of the Na+/H+ exchanger gene (NHE1) and amplification of the mutated allele confer amiloride resistance upon chronic acidosis.
Counillon, L., Franchi, A. J., & Pouysségur, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.10.4508 · Cited by 167
Inhibition of PDGF β Receptor Signal Transduction by Coexpression of a Truncated Receptor
Ueno, H., Colbert, H. A., Escobedo, J. A., & Williams, L. T. (1991) · Science · doi:10.1126/science.1851331 · Cited by 167
Mutation of Asp74 of the rat angiotensin II receptor confers changes in antagonist affinities and abolishes G-protein coupling.
Bihoreau, C., Monnot, C., Davies, E., Teutsch, B., Bernstein, K. E., Corvol, P. L., & Clauser, É. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5133 · Cited by 166
Tryptic activation of the insulin receptor. Proteolytic truncation of the alpha-subunit releases the beta-subunit from inhibitory control.
Shoelson, S. E., White, M. F., & Kahn, C. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68864-7 · Cited by 165
GMAP-210, A Cis-Golgi Network-associated Protein, Is a Minus End Microtubule-binding Protein
Infante, C., Ramos‐Morales, F., Fedriani, C., Bornens, M., & Rios, R. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.1.83 · Cited by 165
Functional Properties of Two Naturally Occurring Isoforms of the Human Insulin Receptor in Chinese Hamster Ovary Cells*
Yamaguchi, Y., Flier, J. S., YOKOTA, A., Benecke, H., Backer, J., & Moller, D. E. (1991) · Endocrinology · doi:10.1210/endo-129-4-2058 · Cited by 165
The biochemistry of diabetes
Taylor, R., & Agius, L. (1988) · Biochemical Journal · doi:10.1042/bj2500625 · Cited by 166
Overexpression of protein kinase C isoenzymes alpha, beta I, gamma, and epsilon in cells overexpressing the insulin receptor. Effects on receptor phosphorylation and signaling.
Chin, J. E., Dickens, M., Tavaré, J. M., & Roth, R. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53258-0 · Cited by 164
Self-citation
Hepatitis C Virus Core Protein Interacts with Cellular Putative RNA Helicase
You, L., Chen, C., Yeh, T.-S., Tsai, T.-Y., Mai, R.-T., Lin, C.-H., & Lee, Y. W. (1999) · Journal of Virology · doi:10.1128/jvi.73.4.2841-2853.1999 · Cited by 163
The transcription factor PU.1 is involved in macrophage proliferation.
Celada, A., Borràs, F. E., Soler, C., Lloberas, J., Klemsz, M., van Beveren, C., McKercher, S., & Maki, R. A. (1996) · The Journal of experimental medicine · doi:10.1084/jem.184.1.61 · Cited by 152
Brain Insulin Receptor Causes Activity-Dependent Current Suppression in the Olfactory Bulb Through Multiple Phosphorylation of Kv1.3
Fadool, D. A., Tucker, K. R., Phillips, J. J., & Simmen, J. A. (2000) · Journal of Neurophysiology · doi:10.1152/jn.2000.83.4.2332 · Cited by 166
Phosphorylation of serine 985 negatively regulates the hepatocyte growth factor receptor kinase.
Gandino, L., Longati, P., Médico, E., Prat, M., & Comoglio, P. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42099-0 · Cited by 160
Modulation of the trans-suppression activity of hepatitis C virus core protein by phosphorylation
Shih, C. M., Chen, C., Chen, S., & Lee, Y. W. (1995) · Journal of Virology · doi:10.1128/jvi.69.2.1160-1171.1995 · Cited by 158
Mutation of Asn111 in the Third Transmembrane Domain of the AT1A Angiotensin II Receptor Induces Its Constitutive Activation
Groblewski, T., Maigret, B., Larguier, R., Lombard, C., Bonnafous, J., & Marie, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.1822 · Cited by 157
Autophosphorylation of the insulin receptor in vitro. Designation of phosphorylation sites and correlation with receptor kinase activation.
Herrera, R., & Rosen, O. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67190-x · Cited by 157
Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide.
Hayes, G. R., & Lockwood, D. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.8115 · Cited by 155
Insulin inhibits pertussis toxin-catalyzed ADP-ribosylation of G-proteins. Evidence for a novel interaction between insulin receptors and G-proteins.
Rothenberg, P., & Kahn, C. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37623-9 · Cited by 156
Binding, internalization, and intracellular localization of interleukin-1 beta in human diploid fibroblasts.
Qwarnström, E. E., Page, R. C., Gillis, S. A., & Dower, S. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68472-8 · Cited by 155
HLH forced dimers: Tethering MyoD to E47 generates a dominant positive myogenic factor insulated from negative regulation by Id
Neuhold, L. A., & Wold, B. J. (1993) · Cell · doi:10.1016/0092-8674(93)90725-6 · Cited by 152
Inverted repeats are necessary for circularization of the mouse testis Sry transcript
Dubin, R. A., Kazmi, M. A., & D, H. O. M. (1995) · Gene · doi:10.1016/0378-1119(95)00639-7 · Cited by 154
Detection of an Alteration in the Insulin-Receptor Gene in a Patient with Insulin Resistance, Acanthosis Nigricans, and the Polycystic Ovary Syndrome (Type A Insulin Resistance)
Moller, D. E., & Flier, J. S. (1988) · New England Journal of Medicine · doi:10.1056/nejm198812083192306 · Cited by 154
Microinjection of a protein-tyrosine-phosphatase inhibits insulin action in Xenopus oocytes.
Cicirelli, M. F., Tonks, N. K., Diltz, C. D., Weiel, J. E., Fischer, E. H., & Krebs, E. G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5514 · Cited by 152
Characterisation of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin
WOOD, C. K., Turner, C. E., Jackson, P., & Critchley, D. R. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.2.709 · Cited by 151
High-level expression of human insulin receptor cDNA in mouse NIH 3T3 cells.
Whittaker, J., Okamoto, A., THYS, R., Bell, G. I., Steiner, D. F., & Hofmann, C. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5237 · Cited by 151
A Dominant Mutant of Inner Centromere Protein (INCENP), a Chromosomal Protein, Disrupts Prometaphase Congression and Cytokinesis
Mackay, A. M., Ainsztein, A. M., Eckley, D. M., & Earnshaw, W. C. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.5.991 · Cited by 150
Molecular mechanism of signal sequence orientation in the endoplasmic reticulum
Goder, V., & Spiess, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg361 · Cited by 149
The NF‐kappa B precursor p105 and the proto‐oncogene product Bcl‐3 are I kappa B molecules and control nuclear translocation of NF‐kappa B.
Naumann, M., Wulczyn, F. G., & Scheidereit, C. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05647.x · Cited by 149
Second Messengers of Insulin Action
Saltiel, A. R. (1990) · Diabetes Care · doi:10.2337/diacare.13.3.244 · Cited by 148
An Immunological Renal Disease in Transgenic Mice That Overexpress Fli-1 , a Member of the ets Family of Transcription Factor Genes
Zhang, L., Eddy, A. A., Teng, Y. A., Fritzler, M. J., Klüppel, M., Mélet, F., & Bernstein, A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.6961 · Cited by 148
Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression.
Turowski, P., Fernandez, A., Favre, B., Lamb, N. J. C., & Hemmings, B. A. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.2.397 · Cited by 147
Stimulation of insulin-like growth factor II receptor binding and insulin receptor kinase activity in rat adipocytes. Effects of vanadate and H2O2.
Kadota, S., Fantus, I. G., Deragon, G., Guyda, H. J., & Posner, B. I. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47556-4 · Cited by 147
The arginine-rich domain of hepatitis B virus precore and core proteins contains a signal for nuclear transport
Yeh, C., Liaw, Y., & Ou, J.-H. J. (1990) · Journal of Virology · doi:10.1128/jvi.64.12.6141-6147.1990 · Cited by 146
Autophosphorylation of Activation Loop Tyrosines Regulates Signaling by the TRK Nerve Growth Factor Receptor
Cunningham, M. E., Stephens, R. M., Kaplan, D. R., & Greene, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10957 · Cited by 149
Identification of the major autophosphorylation site of the Met/hepatocyte growth factor receptor tyrosine kinase.
Ferracini, R., Longati, P., Naldini, L., Vigna, E., & Comoglio, P. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55031-6 · Cited by 143
Alternatively spliced forms in the cytoplasmic domain of the human growth hormone (GH) receptor regulate its ability to generate a soluble GH-binding protein.
Moal, F., Sobrier, M., Duquesnoy, P., Duriez, B., Goossens, M., & Amselem, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10723 · Cited by 143
Multiple Determinants Direct the Orientation of Signal–Anchor Proteins: The Topogenic Role of the Hydrophobic Signal Domain
Wahlberg, J. M., & Spiess, M. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.3.555 · Cited by 143
Charged residues are major determinants of the transmembrane orientation of a signal-anchor sequence.
Beltzer, J. P., Fiedler, K., Fuhrer, C., Geffen, I., Handschin, C., Wessels, H. P., & Spiess, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35269-9 · Cited by 143
Insulin activates the kinase activity of the Raf-1 proto-oncogene by increasing its serine phosphorylation.
Kovacina, K. S., Yonezawa, K., Brautigan, D. L., Tonks, N. K., Rapp, U. R., & Roth, R. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38315-2 · Cited by 143
Self-citation
Identification of the insulin receptor tyrosine residues undergoing insulin-stimulated phosphorylation in intact rat hepatoma cells.
Tornqvist, H. E., Gunsalus, J. R., Nemenoff, R. A., Frackelton, A. R., Pierce, M., & Avruch, J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57400-2 · Cited by 143
Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function.
Wilden, P. A., Kahn, C. R., Siddle, K., & White, M. F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42053-4 · Cited by 144
Properties of a human insulin receptor with a COOH-terminal truncation. II. Truncated receptors have normal kinase activity but are defective in signaling metabolic effects.
Maegawa, H., McClain, D. A., Freidenberg, G. R., Olefsky, J. M., Napier, M. A., Lipari, T., Dull, T. J., Lee, J., & Ullrich, A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68394-2 · Cited by 142

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)
ORCID: Morgan, David O.
Roth, Richard A.
Venue: Cell
Publisher: Elsevier BV
Published: 1986-06
Volume: 45
Issue: 5
Pages: 721-732
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(86)90786-5
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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

Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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