Insulinski receptor (Serbian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Insulinski receptor" in Serbian language version.

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20nih.gov

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20doi.org

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2archive.org

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1harvard.edu

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archive.org

Maddux BA, Goldfine ID (2000). „Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor alpha-subunit”. Diabetes. 49 (1): 13—9. PMID 10615944. doi:10.2337/diabetes.49.1.13.
Rosenzweig T, Braiman L, Bak A, Alt A, Kuroki T, Sampson SR (2002). „Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling”. Diabetes. 51 (6): 1921—30. PMID 12031982. doi:10.2337/diabetes.51.6.1921.

doi.org

Ward CW, Lawrence MC (2009). „Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor”. BioEssays. 31 (4): 422—34. PMID 19274663. doi:10.1002/bies.200800210.
Ebina Y, Ellis L (1985). „The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling.”. Cell. 40 (4): 747—58. PMID 2859121. doi:10.1016/0092-8674(85)90334-4.
Malaguarnera R, Belfiore A (2012). „Proinsulin Binds with High Affinity the Insulin Receptor Isoform A and Predominantly Activates the Mitogenic Pathway.”. Endocrinology. Epub (5): 2152—63. PMID 22355074. doi:10.1210/en.2011-1843.
Belfiore A, Frasca F (2009). „Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease.”. Endocr Rev. 30 (6): 586—623. PMID 19752219. doi:10.1210/er.2008-0047.
Maddux BA, Goldfine ID (2000). „Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor alpha-subunit”. Diabetes. 49 (1): 13—9. PMID 10615944. doi:10.2337/diabetes.49.1.13.
Langlais P, Dong LQ, Hu D, Liu F (2000). „Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family”. Oncogene. 19 (25): 2895—903. PMID 10871840. doi:10.1038/sj.onc.1203616.
Hansen H, Svensson U, Zhu J, Laviola L, Giorgino F, Wolf G, Smith RJ, Riedel H (1996). „Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus”. The Journal of Biological Chemistry. 271 (15): 8882—6. PMID 8621530. doi:10.1074/jbc.271.15.8882.
Liu F, Roth RA (1995). „Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function”. Proceedings of the National Academy of Sciences of the United States of America. 92 (22): 10287—91. Bibcode:1995PNAS...9210287L. PMC 40781 . PMID 7479769. doi:10.1073/pnas.92.22.10287.
He W, Rose DW, Olefsky JM, Gustafson TA (1998). „Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains”. The Journal of Biological Chemistry. 273 (12): 6860—7. PMID 9506989. doi:10.1074/jbc.273.12.6860.
Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE (1997). „Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains”. The Journal of Biological Chemistry. 272 (5): 2659—67. PMID 9006901. doi:10.1074/jbc.272.5.2659.
Kasus-Jacobi A, Béréziat V, Perdereau D, Girard J, Burnol AF (2000). „Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2”. Oncogene. 19 (16): 2052—9. PMID 10803466. doi:10.1038/sj.onc.1203469.
Aguirre V, Werner ED, Giraud J, Lee YH, Shoelson SE, White MF (2002). „Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action”. The Journal of Biological Chemistry. 277 (2): 1531—7. PMID 11606564. doi:10.1074/jbc.M101521200.
Sawka-Verhelle D, Tartare-Deckert S, White MF, Van Obberghen E (1996). „Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786”. The Journal of Biological Chemistry. 271 (11): 5980—3. PMID 8626379. doi:10.1074/jbc.271.11.5980.
O'Neill TJ, Zhu Y, Gustafson TA (1997). „Interaction of MAD2 with the carboxyl terminus of the insulin receptor but not with the IGFIR. Evidence for release from the insulin receptor after activation”. The Journal of Biological Chemistry. 272 (15): 10035—40. PMID 9092546. doi:10.1074/jbc.272.15.10035.
Braiman L, Alt A, Kuroki T, Ohba M, Bak A, Tennenbaum T, Sampson SR (2001). „Insulin induces specific interaction between insulin receptor and protein kinase C delta in primary cultured skeletal muscle”. Molecular Endocrinology. 15 (4): 565—74. PMID 11266508. doi:10.1210/mend.15.4.0612.
Rosenzweig T, Braiman L, Bak A, Alt A, Kuroki T, Sampson SR (2002). „Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling”. Diabetes. 51 (6): 1921—30. PMID 12031982. doi:10.2337/diabetes.51.6.1921.
Maegawa H, Ugi S, Adachi M, Hinoda Y, Kikkawa R, Yachi A, Shigeta Y, Kashiwagi A (1994). „Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro”. Biochemical and Biophysical Research Communications. 199 (2): 780—5. PMID 8135823. doi:10.1006/bbrc.1994.1297.
Kharitonenkov A, Schnekenburger J, Chen Z, Knyazev P, Ali S, Zwick E, White M, Ullrich A (1995). „Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction”. The Journal of Biological Chemistry. 270 (49): 29189—93. PMID 7493946. doi:10.1074/jbc.270.49.29189.
Kotani K, Wilden P, Pillay TS (1998). „SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase”. The Biochemical Journal. 335 ( Pt 1) (1): 103—9. PMC 1219757 . PMID 9742218. doi:10.1042/bj3350103.
Nelms K, O'Neill TJ, Li S, Hubbard SR, Gustafson TA, Paul WE (1999). „Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain”. Mammalian Genome. 10 (12): 1160—7. PMID 10594240. doi:10.1007/s003359901183.

harvard.edu

adsabs.harvard.edu

Liu F, Roth RA (1995). „Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function”. Proceedings of the National Academy of Sciences of the United States of America. 92 (22): 10287—91. Bibcode:1995PNAS...9210287L. PMC 40781 . PMID 7479769. doi:10.1073/pnas.92.22.10287.

nih.gov

ncbi.nlm.nih.gov

Ward CW, Lawrence MC (2009). „Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor”. BioEssays. 31 (4): 422—34. PMID 19274663. doi:10.1002/bies.200800210.
Ebina Y, Ellis L (1985). „The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling.”. Cell. 40 (4): 747—58. PMID 2859121. doi:10.1016/0092-8674(85)90334-4.
Malaguarnera R, Belfiore A (2012). „Proinsulin Binds with High Affinity the Insulin Receptor Isoform A and Predominantly Activates the Mitogenic Pathway.”. Endocrinology. Epub (5): 2152—63. PMID 22355074. doi:10.1210/en.2011-1843.
Belfiore A, Frasca F (2009). „Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease.”. Endocr Rev. 30 (6): 586—623. PMID 19752219. doi:10.1210/er.2008-0047.
Maddux BA, Goldfine ID (2000). „Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor alpha-subunit”. Diabetes. 49 (1): 13—9. PMID 10615944. doi:10.2337/diabetes.49.1.13.
Langlais P, Dong LQ, Hu D, Liu F (2000). „Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family”. Oncogene. 19 (25): 2895—903. PMID 10871840. doi:10.1038/sj.onc.1203616.
Hansen H, Svensson U, Zhu J, Laviola L, Giorgino F, Wolf G, Smith RJ, Riedel H (1996). „Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus”. The Journal of Biological Chemistry. 271 (15): 8882—6. PMID 8621530. doi:10.1074/jbc.271.15.8882.
Liu F, Roth RA (1995). „Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function”. Proceedings of the National Academy of Sciences of the United States of America. 92 (22): 10287—91. Bibcode:1995PNAS...9210287L. PMC 40781 . PMID 7479769. doi:10.1073/pnas.92.22.10287.
He W, Rose DW, Olefsky JM, Gustafson TA (1998). „Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains”. The Journal of Biological Chemistry. 273 (12): 6860—7. PMID 9506989. doi:10.1074/jbc.273.12.6860.
Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE (1997). „Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains”. The Journal of Biological Chemistry. 272 (5): 2659—67. PMID 9006901. doi:10.1074/jbc.272.5.2659.
Kasus-Jacobi A, Béréziat V, Perdereau D, Girard J, Burnol AF (2000). „Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2”. Oncogene. 19 (16): 2052—9. PMID 10803466. doi:10.1038/sj.onc.1203469.
Aguirre V, Werner ED, Giraud J, Lee YH, Shoelson SE, White MF (2002). „Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action”. The Journal of Biological Chemistry. 277 (2): 1531—7. PMID 11606564. doi:10.1074/jbc.M101521200.
Sawka-Verhelle D, Tartare-Deckert S, White MF, Van Obberghen E (1996). „Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786”. The Journal of Biological Chemistry. 271 (11): 5980—3. PMID 8626379. doi:10.1074/jbc.271.11.5980.
O'Neill TJ, Zhu Y, Gustafson TA (1997). „Interaction of MAD2 with the carboxyl terminus of the insulin receptor but not with the IGFIR. Evidence for release from the insulin receptor after activation”. The Journal of Biological Chemistry. 272 (15): 10035—40. PMID 9092546. doi:10.1074/jbc.272.15.10035.
Braiman L, Alt A, Kuroki T, Ohba M, Bak A, Tennenbaum T, Sampson SR (2001). „Insulin induces specific interaction between insulin receptor and protein kinase C delta in primary cultured skeletal muscle”. Molecular Endocrinology. 15 (4): 565—74. PMID 11266508. doi:10.1210/mend.15.4.0612.
Rosenzweig T, Braiman L, Bak A, Alt A, Kuroki T, Sampson SR (2002). „Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling”. Diabetes. 51 (6): 1921—30. PMID 12031982. doi:10.2337/diabetes.51.6.1921.
Maegawa H, Ugi S, Adachi M, Hinoda Y, Kikkawa R, Yachi A, Shigeta Y, Kashiwagi A (1994). „Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro”. Biochemical and Biophysical Research Communications. 199 (2): 780—5. PMID 8135823. doi:10.1006/bbrc.1994.1297.
Kharitonenkov A, Schnekenburger J, Chen Z, Knyazev P, Ali S, Zwick E, White M, Ullrich A (1995). „Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction”. The Journal of Biological Chemistry. 270 (49): 29189—93. PMID 7493946. doi:10.1074/jbc.270.49.29189.
Kotani K, Wilden P, Pillay TS (1998). „SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase”. The Biochemical Journal. 335 ( Pt 1) (1): 103—9. PMC 1219757 . PMID 9742218. doi:10.1042/bj3350103.
Nelms K, O'Neill TJ, Li S, Hubbard SR, Gustafson TA, Paul WE (1999). „Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain”. Mammalian Genome. 10 (12): 1160—7. PMID 10594240. doi:10.1007/s003359901183.