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Volumn 31, Issue 6, 2011, Pages 387-394

Receptor tyrosine kinases: From biology to pathology

Author keywords

Disease; human; ligand; mutation; RTK

Indexed keywords

EPHRIN RECEPTOR; EPHRIN RECEPTOR A2; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; FIBROBLAST GROWTH FACTOR RECEPTOR 1; FIBROBLAST GROWTH FACTOR RECEPTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR 3; FIBROBLAST GROWTH FACTOR RECEPTOR 4; INSULIN RECEPTOR; MUSCLE SPECIFIC RECEPTOR TYROSINE KINASE; NERVE GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR ALPHA RECEPTOR; PLATELET DERIVED GROWTH FACTOR BETA RECEPTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE; RECEPTOR TYROSINE KINASE LIKE ORPHAN RECEPTOR; SCATTER FACTOR RECEPTOR; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG; VASCULOTROPIN RECEPTOR;

EID: 80955158149     PISSN: 10799893     EISSN: 15324281     Source Type: Journal    
DOI: 10.3109/10799893.2011.625425     Document Type: Review
Times cited : (40)

References (48)
  • 1
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2000, 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 2
    • 13244292544 scopus 로고
    • Modular exchange principles in proteins
    • Patthy L. Modular exchange principles in proteins. Curr Opin Struct Biol 1991, 1, 351-361. (Pubitemid 121002540)
    • (1991) Current Opinion in Structural Biology , vol.1 , Issue.3 , pp. 351-361
    • Patthy, L.1
  • 3
  • 5
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin CH. Dimerization of cell surface receptors in signal transduction. Cell 1995, 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 6
    • 0036668277 scopus 로고    scopus 로고
    • Eph family functions from an evolutionary perspective
    • DOI 10.1016/S0959-437X(02)00316-7
    • Drescher U. Eph family functions from an evolutionary perspective. Curr Opin Genet Dev 2002, 12, 397-402. (Pubitemid 34722917)
    • (2002) Current Opinion in Genetics and Development , vol.12 , Issue.4 , pp. 397-402
    • Drescher, U.1
  • 8
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010, 141, 1117-1134.
    • (2009) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 9
    • 78349232462 scopus 로고    scopus 로고
    • Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases
    • Bae JH, Schlessinger J. Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases. Mol Cells 2010, 29, 443-448.
    • (2009) Mol. Cells , vol.29 , pp. 443-448
    • Bae, J.H.1    Schlessinger, J.2
  • 10
    • 79551632876 scopus 로고    scopus 로고
    • Protein kinase signaling networks in cancer
    • Brognard J, Hunter T. Protein kinase signaling networks in cancer. Curr Opin Genet Dev 2011, 21, 4-11.
    • (2011) Curr. Opin. Genet. Dev. , vol.21 , pp. 4-11
    • Brognard, J.1    Hunter, T.2
  • 11
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • DOI 10.1038/35077225
    • Blume-Jensen P, Hunter T. Oncogenic kinase signalling. Nature 2001, 411, 355-365. (Pubitemid 32467045)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 12
    • 33646889068 scopus 로고    scopus 로고
    • Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies
    • DOI 10.1021/bi060609y
    • Li E, Hristova K. Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Biochemistry 2006, 45, 6241-6251. (Pubitemid 43787791)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6241-6251
    • Li, E.1    Hristova, K.2
  • 14
    • 0034213931 scopus 로고    scopus 로고
    • RTK mutations and human syndromes - When good receptors turn bad
    • DOI 10.1016/S0168-9525(00)02021-7, PII S0168952500020217
    • Robertson SC, Tynan JA, Donoghue DJ. RTK mutations and human syndromes when good receptors turn bad. Trends Genet 2000, 16, 265-271. (Pubitemid 30332143)
    • (2000) Trends in Genetics , vol.16 , Issue.6 , pp. 265-271
    • Robertson, S.C.1    Tynan, J.A.2    Donoghue, D.J.3
  • 15
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye MA, Neve RM, Lane HA, Hynes NE. The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J 2000, 19, 3159-3167. (Pubitemid 30428195)
    • (2000) EMBO Journal , vol.19 , Issue.13 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 17
    • 17844390172 scopus 로고    scopus 로고
    • Epidermal growth factor receptor mutations small-molecule kinase inhibitors and non-small-cell lung cancer: Current knowledge and future directions
    • Pao W, Miller VA. Epidermal growth factor receptor mutations, small-molecule kinase inhibitors, and non-small-cell lung cancer: current knowledge and future directions. J Clin Oncol 2005, 23, 2556-2568.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 2556-2568
    • Pao, W.1    Miller, V.A.2
  • 19
    • 17844402791 scopus 로고    scopus 로고
    • Bad bones absent smell selfish testes: The pleiotropic consequences of human FGF receptor mutations
    • Wilikie AO. Bad bones, absent smell, selfish testes: the pleiotropic consequences of human FGF receptor mutations. Cytokine Growth Factor Rev 2005, 16, 187-203.
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 187-203
    • Wilikie, A.O.1
  • 21
    • 33744948332 scopus 로고    scopus 로고
    • Clinical and functional characteristics of the human Arg59Ter insulin-like growth factor I receptor (IGF1R) mutation: Implications for a gene dosage effect of the human IGF1R
    • DOI 10.1210/jc.2005-2146
    • Raile K, Klammt J, Schneider A, Keller A, Laue S, Smith R, Pfäffle R, Kratzsch J, Keller E, Kiess W. Clinical and functional characteristics of the human Arg59Ter insulin-like growth factor i receptor (IGF1R) mutation: implications for a gene dosage effect of the human IGF1R. J Clin Endocrinol Metab 2006, 91, 2264-2271. (Pubitemid 43855016)
    • (2006) Journal of Clinical Endocrinology and Metabolism , vol.91 , Issue.6 , pp. 2264-2271
    • Raile, K.1    Klammt, J.2    Schneider, A.3    Keller, A.4    Laue, S.5    Smith, R.6    Pfaffle, R.7    Kratzsch, J.8    Keller, E.9    Kiess, W.10
  • 22
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. The protein kinase complement of the human genome. Science 2002, 298, 1912-1934. (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 23
    • 77649114060 scopus 로고    scopus 로고
    • Eph receptors and ephrins in cancer: Bidirectional signalling and beyond
    • Pasquale EB. Eph receptors and ephrins in cancer: bidirectional signalling and beyond. Nat Rev Cancer 2010, 10, 165-180.
    • (2009) Nat. Rev. Cancer , vol.10 , pp. 165-180
    • Pasquale, E.B.1
  • 26
    • 0027275594 scopus 로고
    • C-FMS point mutations in acute myeloid leukemia: Fact or fiction?
    • Springall F, O'Mara S, Shounan Y, Todd A, Ford D, Iland H. c-fms point mutations in acute myeloid leukemia: fact or fiction? Leukemia 1993, 7, 978-985. (Pubitemid 23230976)
    • (1993) Leukemia , vol.7 , Issue.7 , pp. 978-985
    • Springall, F.1    O'Mara, S.2    Shounan, Y.3    Todd, A.4    Ford, D.5    Iland, H.6
  • 27
    • 70649111388 scopus 로고    scopus 로고
    • Pharmacogenomics in acute myeloid leukemia
    • Roumier C, Cheok MH. Pharmacogenomics in acute myeloid leukemia. Pharmacogenomics 2009, 10, 1839-1851.
    • (2009) Pharmacogenomics , vol.10 , pp. 1839-1851
    • Roumier, C.1    Cheok, M.H.2
  • 28
    • 34447628353 scopus 로고    scopus 로고
    • Molecular mechanisms of lymphatic vascular development
    • DOI 10.1007/s00018-007-7040-z
    • Mäkinen T, Norrmén C, Petrova TV. Molecular mechanisms of lymphatic vascular development. Cell Mol Life Sci 2007, 64, 1915-1929. (Pubitemid 47094431)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.15 , pp. 1915-1929
    • Makinen, T.1    Norrmen, C.2    Petrova, T.V.3
  • 31
    • 35148848262 scopus 로고    scopus 로고
    • Comparative integromics on non-canonical WNT or planar cell polarity signaling molecules: Transcriptional mechanism of PTK7 in colorectal cancer and that of SEMA6A in undifferentiated ES cells
    • Katoh M, Katoh M. Comparative integromics on non-canonical WNT or planar cell polarity signaling molecules: transcriptional mechanism of PTK7 in colorectal cancer and that of SEMA6A in undifferentiated ES cells. Int J Mol Med 2007, 20, 405-409.
    • (2007) Int. J. Mol. Med. , vol.20 , pp. 405-409
    • Katoh, M.1    Katoh, M.2
  • 32
    • 0028115022 scopus 로고
    • Neurotrophin signal transduction by the Trk receptor
    • DOI 10.1002/neu.480251108
    • Kaplan DR, Stephens RM. Neurotrophin signal transduction by the Trk receptor. J Neurobiol 1994, 25, 1404-1417. (Pubitemid 24325065)
    • (1994) Journal of Neurobiology , vol.25 , Issue.11 , pp. 1404-1417
    • Kaplan, D.R.1    Stephens, R.M.2
  • 33
    • 79959569898 scopus 로고    scopus 로고
    • A short in-frame deletion in NRTK1 tyrosine kinase domain caused by a novel splice site mutation in a patient with congenital insensivity to pain with anhidrosis
    • Sarasola Rodriguez JA, Garrote E, Aristegui J, Garcia-Barcina MJE. A short in-frame deletion in NRTK1 tyrosine kinase domain caused by a novel splice site mutation in a patient with congenital insensivity to pain with anhidrosis. BMC Med Genet 2011, 12, 86.
    • (2011) BMC Med. Genet. , vol.12 , pp. 86
    • Sarasola Rodriguez, J.A.1    Garrote, E.2    Aristegui, J.3    Garcia-Barcina, M.J.E.4
  • 34
    • 79551540928 scopus 로고    scopus 로고
    • Protein S blocks the extrinsic apoptotic cascade in tissue plasminogen activator/N-methyl D-aspartatetreated neurons via Tyro3-Akt-FKHRL1 signaling pathway
    • Guo H, Barrett TM, Zhong Z, Fernández JA, Griffin JH, Freeman RS, Zlokovic BV. Protein S blocks the extrinsic apoptotic cascade in tissue plasminogen activator/N-methyl D-aspartatetreated neurons via Tyro3-Akt-FKHRL1 signaling pathway. Mol Neurodegener 2011, 6, 13.
    • (2011) Mol. Neurodegener. , vol.6 , pp. 13
    • Guo, H.1    Barrett, T.M.2    Zhong, Z.3    Fernández, J.A.4    Griffin, J.H.5    Freeman, R.S.6    Zlokovic, B.V.7
  • 35
    • 79951470770 scopus 로고    scopus 로고
    • The novel receptor tyrosine kinase Axl is constitutively active in B-cell chronic lymphocytic leukemia and acts as a docking site of nonreceptor kinases: Implications for therapy
    • Ghosh AK, Secreto C, Boysen J, Sassoon T, Shanafelt TD, Mukhopadhyay D, Kay NE. The novel receptor tyrosine kinase Axl is constitutively active in B-cell chronic lymphocytic leukemia and acts as a docking site of nonreceptor kinases: implications for therapy. Blood 2011, 117, 1928-1937.
    • (2011) Blood , vol.117 , pp. 1928-1937
    • Ghosh, A.K.1    Secreto, C.2    Boysen, J.3    Sassoon, T.4    Shanafelt, T.D.5    Mukhopadhyay, D.6    Kay, N.E.7
  • 38
    • 0033994339 scopus 로고    scopus 로고
    • Identification and regulation of receptor tyrosine kinases Rse and Mer and their ligand Gas6 in testicular somatic cells
    • Chan MC, Mather JP, McCray G, Lee WM. Identification and regulation of receptor tyrosine kinases Rse and Mer and their ligand Gas6 in testicular somatic cells. J Androl 2000, 21, 291-302. (Pubitemid 30123711)
    • (2000) Journal of Andrology , vol.21 , Issue.2 , pp. 291-302
    • Chan, M.C.W.1    Mather, J.P.2    McCray, G.3    Lee, W.M.4
  • 39
    • 0034914238 scopus 로고    scopus 로고
    • Novel patterns of gene expression in pituitary adenomas identified by complementary deoxyribonucleic acid microarrays and quantitative reverse transcription-polymerase chain reaction
    • DOI 10.1210/jc.86.7.3097
    • Evans CO, Young AN, Brown MR, Brat DJ, Parks JS, Neish AS, Oyesiku NM. Novel patterns of gene expression in pituitary adenomas identified by complementary deoxyribonucleic acid microarrays and quantitative reverse transcription-polymerase chain reaction. J Clin Endocrinol Metab 2001, 86, 3097-3107. (Pubitemid 32673472)
    • (2001) Journal of Clinical Endocrinology and Metabolism , vol.86 , Issue.7 , pp. 3097-3107
    • Evans, C.-O.1    Young, A.N.2    Brown, M.R.3    Brat, D.J.4    Parks, J.S.5    Neish, A.S.6    Oyesiku, N.M.7
  • 41
    • 0036213857 scopus 로고    scopus 로고
    • Identification of Gas6, a putative ligand for Sky and Axl receptor tyrosine kinases, as a novel neurotrophic factor for hippocampal neurons
    • DOI 10.1002/jnr.10211
    • Funakoshi H, Yonemasu T, Nakano T, Matumoto K, Nakamura T. Identification of Gas6, a putative ligand for Sky and Axl receptor tyrosine kinases, as a novel neurotrophic factor for hippocampal neurons. J Neurosci Res 2002, 68, 150-160. (Pubitemid 34275008)
    • (2002) Journal of Neuroscience Research , vol.68 , Issue.2 , pp. 150-160
    • Funakoshi, H.1    Yonemasu, T.2    Nakano, T.3    Matumoto, K.4    Nakamura, T.5
  • 42
    • 77951499651 scopus 로고    scopus 로고
    • How do angiopoietins Tie in with vascular endothelial growth factors
    • Saharinen P, Bry M, Alitalo K. How do angiopoietins Tie in with vascular endothelial growth factors? Curr Opin Hematol 2010, 17, 198-205.
    • (2009) Curr. Opin. Hematol. , vol.17 , pp. 198-205
    • Saharinen, P.1    Bry, M.2    Alitalo, K.3
  • 44


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