메뉴 건너뛰기




Volumn 56, Issue 4, 2006, Pages 164-172

RET receptor signaling: Dysfunction in thyroid cancer and Hirschsprung's disease

Author keywords

Hirschsprung's disease; Medullary thyroid carcinoma; Multiple endocrine neoplasia type 2; Papillary thyroid carcinoma; RET tyrosine kinase

Indexed keywords

B RAF KINASE; ENDOTHELIN; GLIAL CELL LINE DERIVED NEUROTROPHIC FACTOR; PROTEIN RET; PROTEIN TYROSINE KINASE; RAS PROTEIN;

EID: 33645290520     PISSN: 13205463     EISSN: 14401827     Source Type: Journal    
DOI: 10.1111/j.1440-1827.2006.01942.x     Document Type: Review
Times cited : (69)

References (115)
  • 1
    • 0022330363 scopus 로고
    • Activation of a novel human transforming gene, ret, by DNA rearrangement
    • . .
    • Takahashi M Ritz J Cooper GM. Activation of a novel human transforming gene, ret, by DNA rearrangement. Cell 1985 42 581 8.
    • (1985) Cell , vol.42 , pp. 581-8
    • Takahashi, M.1    Ritz, J.2    Cooper, G.M.3
  • 2
    • 0023158426 scopus 로고
    • Ret transforming gene encodes a fusion protein homologous to tyrosine kinases
    • .
    • Takahashi M Cooper GM. ret transforming gene encodes a fusion protein homologous to tyrosine kinases. Mol Cell Biol 1987 7 1378 85.
    • (1987) Mol Cell Biol , vol.7 , pp. 1378-85
    • Takahashi, M.1    Cooper, G.M.2
  • 3
    • 0023875393 scopus 로고
    • Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5′ half of the ret transforming gene
    • .
    • Takahashi M Inaguma Y Hiai H Hirose F. Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5′ half of the ret transforming gene. Mol Cell Biol 1988 8 1853 6.
    • (1988) Mol Cell Biol , vol.8 , pp. 1853-6
    • Takahashi, M.1    Inaguma, Y.2    Hiai, H.3    Hirose, F.4
  • 4
    • 0024208663 scopus 로고
    • Cloning and expression of the ret proto-oncogene encoding a tyrosine kinase with two potential transmembrane domains
    • .
    • Takahashi M Buma Y Iwamoto T Inaguma Y Ikeda H Hiai H. Cloning and expression of the ret proto-oncogene encoding a tyrosine kinase with two potential transmembrane domains. Oncogene 1988 3 571 8.
    • (1988) Oncogene , vol.3 , pp. 571-8
    • Takahashi, M.1    Buma, Y.2    Iwamoto, T.3    Inaguma, Y.4    Ikeda, H.5    Hiai, H.6
  • 5
    • 0027407552 scopus 로고
    • CDNA cloning of mouse ret proto-oncogene and its sequence similarity to the cadherin superfamily
    • .
    • Iwamoto T Taniguchi M Asai N Ohkusu K Nakashima I Takahashi M. cDNA cloning of mouse ret proto-oncogene and its sequence similarity to the cadherin superfamily. Oncogene 1993 8 1087 91.
    • (1993) Oncogene , vol.8 , pp. 1087-91
    • Iwamoto, T.1    Taniguchi, M.2    Asai, N.3    Ohkusu, K.4    Nakashima, I.5    Takahashi, M.6
  • 6
    • 0027374562 scopus 로고
    • Expression of the c-ret proto-oncogene during mouse embryogenesis
    • .
    • Pachnis V Mankoo B Costantini F. Expression of the c-ret proto-oncogene during mouse embryogenesis. Development 1993 119 1005 17.
    • (1993) Development , vol.119 , pp. 1005-17
    • Pachnis, V.1    Mankoo, B.2    Costantini, F.3
  • 7
    • 0028896367 scopus 로고
    • Spatial and temporal expression of the ret proto-oncogene product in embryonic, infant and adult rat tissues
    • .
    • Tsuzuki T Takahashi M Asai N Iwashita T Matsuyama M Asai J. Spatial and temporal expression of the ret proto-oncogene product in embryonic, infant and adult rat tissues. Oncogene 1995 10 191 8.
    • (1995) Oncogene , vol.10 , pp. 191-8
    • Tsuzuki, T.1    Takahashi, M.2    Asai, N.3    Iwashita, T.4    Matsuyama, M.5    Asai, J.6
  • 8
    • 15844406351 scopus 로고    scopus 로고
    • Functional receptor for GDNF encoded by the c-ret proto-oncogene
    • .
    • Trupp M Arenas E Fainzilber M et al. Functional receptor for GDNF encoded by the c-ret proto-oncogene. Nature 1996 381 785 9.
    • (1996) Nature , vol.381 , pp. 785-9
    • Trupp, M.1    Arenas, E.2    Fainzilber, M.3
  • 9
    • 15844422453 scopus 로고    scopus 로고
    • GDNF signalling through the Ret receptor tyrosine kinase
    • .
    • Durbec P Marcos-Gutierrez CV Kilkenny C et al. GDNF signalling through the Ret receptor tyrosine kinase. Nature 1996 381 789 93.
    • (1996) Nature , vol.381 , pp. 789-93
    • Durbec, P.1    Marcos-Gutierrez, C.V.2    Kilkenny, C.3
  • 10
    • 15844365303 scopus 로고    scopus 로고
    • GDNF-induced activation of the Ret protein tyrosine kinase is mediated by GDNFR-α, a novel receptor for GDNF
    • .
    • Jing S Wen D Yu Y et al. GDNF-induced activation of the Ret protein tyrosine kinase is mediated by GDNFR-α, a novel receptor for GDNF. Cell 1996 85 1113 24.
    • (1996) Cell , vol.85 , pp. 1113-24
    • Jing, S.1    Wen, D.2    Yu, Y.3
  • 11
    • 15844418441 scopus 로고    scopus 로고
    • Characterization of a multicomponent receptor for GDNF
    • .
    • Treanor JJS Goodman L de Sauvage F et al. Characterization of a multicomponent receptor for GDNF. Nature 1996 382 80 83.
    • (1996) Nature , vol.382 , pp. 80-83
    • Treanor, J.J.S.1    Goodman, L.2    De Sauvage, F.3
  • 12
    • 16944365682 scopus 로고    scopus 로고
    • A GPI-linked protein that interacts with Ret to form a candidate neurturin receptor
    • .
    • Klein RD Sherman D Ho W-H et al. A GPI-linked protein that interacts with Ret to form a candidate neurturin receptor. Nature 1997 387 717 21.
    • (1997) Nature , vol.387 , pp. 717-21
    • Klein, R.D.1    Sherman, D.2    Ho, W.-H.3
  • 13
    • 0036581222 scopus 로고    scopus 로고
    • The GDNF family: Signaling, biological functions and therapeutic value
    • .
    • Airaksinen MS Saarma M. The GDNF family: Signaling, biological functions and therapeutic value. Nat Rev Neurosci 2002 3 383 94.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 383-94
    • Airaksinen, M.S.1    Saarma, M.2
  • 14
    • 0028174023 scopus 로고
    • Defects in the kidney and enteric nervous system of mice lacking the tyrosine kinase receptor Ret
    • .
    • Schuchardt A D'Agati V Larsson-Blomberg L Costantini F Pachnis V. Defects in the kidney and enteric nervous system of mice lacking the tyrosine kinase receptor Ret. Nature 1994 367 380 83.
    • (1994) Nature , vol.367 , pp. 380-83
    • Schuchardt, A.1    D'Agati, V.2    Larsson-Blomberg, L.3    Costantini, F.4    Pachnis, V.5
  • 16
    • 15844426332 scopus 로고    scopus 로고
    • Defects in enteric innervation and kidney development in mice lacking GDNF
    • .
    • Pichel JG Shen L Sheng HZ et al. Defects in enteric innervation and kidney development in mice lacking GDNF. Nature 1996 382 73 6.
    • (1996) Nature , vol.382 , pp. 73-6
    • Pichel, J.G.1    Shen, L.2    Sheng, H.Z.3
  • 17
    • 15844384629 scopus 로고    scopus 로고
    • Renal and neuronal abnormalities in mice lacking GDNF
    • .
    • Moore MW Klein RD Fariñas I et al. Renal and neuronal abnormalities in mice lacking GDNF. Nature 1996 382 76 9.
    • (1996) Nature , vol.382 , pp. 76-9
    • Moore, M.W.1    Klein, R.D.2    Fariñas, I.3
  • 18
    • 0032114122 scopus 로고    scopus 로고
    • GFRα1 is an essential receptor component for GDNF in the developing nervous system and kidney
    • .
    • Cacalano G Fariñas I Wang L-C et al. GFRα1 is an essential receptor component for GDNF in the developing nervous system and kidney. Neuron 1998 21 53 62.
    • (1998) Neuron , vol.21 , pp. 53-62
    • Cacalano, G.1    Fariñas, I.2    Wang, L.-C.3
  • 19
    • 0032129239 scopus 로고    scopus 로고
    • GFRα1-deficient mice have deficits in the enteric nervous system and kidneys
    • .
    • Enomoto H Araki T Jackman A et al. GFRα1-deficient mice have deficits in the enteric nervous system and kidneys. Neuron 1998 21 317 24.
    • (1998) Neuron , vol.21 , pp. 317-24
    • Enomoto, H.1    Araki, T.2    Jackman, A.3
  • 20
    • 0033083374 scopus 로고    scopus 로고
    • Gene targeting reveals a critical role for neurturin in the development and maintenance of enteric, sensory, and parasympathetic neurons
    • .
    • Heuckeroth RO Enomoto H Grider JR et al. Gene targeting reveals a critical role for neurturin in the development and maintenance of enteric, sensory, and parasympathetic neurons. Neuron 1999 22 253 63.
    • (1999) Neuron , vol.22 , pp. 253-63
    • Heuckeroth, R.O.1    Enomoto, H.2    Grider, J.R.3
  • 21
    • 0033083093 scopus 로고    scopus 로고
    • Retarded growth and deficits in the enteric and parasympathetic nervous system in mice lacking GFRα2, a functional neurturin receptor
    • .
    • Rossi J Luukko K Poteryaev D et al. Retarded growth and deficits in the enteric and parasympathetic nervous system in mice lacking GFRα2, a functional neurturin receptor. Neuron 1999 22 243 52.
    • (1999) Neuron , vol.22 , pp. 243-52
    • Rossi, J.1    Luukko, K.2    Poteryaev, D.3
  • 22
    • 0033172962 scopus 로고    scopus 로고
    • GFRα3, a component of the artemin receptor, is required for migration and survival of the superior cervical ganglion
    • .
    • Nishino J Mochida K Ohfuji Y et al. GFRα3, a component of the artemin receptor, is required for migration and survival of the superior cervical ganglion. Neuron 1999 23 725 36.
    • (1999) Neuron , vol.23 , pp. 725-36
    • Nishino, J.1    Mochida, K.2    Ohfuji, Y.3
  • 23
    • 0037047048 scopus 로고    scopus 로고
    • Effects of cerebral ischemia in mice deficient in Persephin
    • .
    • Tomac A Agulnick AD Haughey N et al. Effects of cerebral ischemia in mice deficient in Persephin. Proc Natl Acad Sci USA 2002 99 9521 6.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9521-6
    • Tomac, A.1    Agulnick, A.D.2    Haughey, N.3
  • 24
    • 0025022463 scopus 로고
    • PTC is a novel rearranged form of the ret proto-oncogene and is frequently detected in vivo in human thyroid papillary carcinomas
    • .
    • Grieco M Santoro M Berlingieri MT et al. PTC is a novel rearranged form of the ret proto-oncogene and is frequently detected in vivo in human thyroid papillary carcinomas. Cell 1990 60 557 63.
    • (1990) Cell , vol.60 , pp. 557-63
    • Grieco, M.1    Santoro, M.2    Berlingieri, M.T.3
  • 25
    • 0026763062 scopus 로고
    • Ret oncogene activation in human thyroid neoplasms is restricted to the papillary cancer subtype
    • .
    • Santoro M Carlomagno F Hay ID et al. Ret oncogene activation in human thyroid neoplasms is restricted to the papillary cancer subtype. J Clin Invest 1992 89 1517 22.
    • (1992) J Clin Invest , vol.89 , pp. 1517-22
    • Santoro, M.1    Carlomagno, F.2    Hay, I.D.3
  • 26
    • 0026686316 scopus 로고
    • Low frequency of rearrangements of the ret and trk proto-oncogenes in Japanese thyroid papillary carcinomas
    • .
    • Wajjwalku W Nakamura S Hasegawa Y et al. Low frequency of rearrangements of the ret and trk proto-oncogenes in Japanese thyroid papillary carcinomas. Jpn J Cancer Res 1992 83 671 5.
    • (1992) Jpn J Cancer Res , vol.83 , pp. 671-5
    • Wajjwalku, W.1    Nakamura, S.2    Hasegawa, Y.3
  • 27
    • 0028292310 scopus 로고
    • Activated RET oncogene in thyroid cancers of children from area contaminated by Chernobyl accident
    • .
    • Ito T Seyama T Iwamoto KS et al. Activated RET oncogene in thyroid cancers of children from area contaminated by Chernobyl accident. Lancet 1994 344 259.
    • (1994) Lancet , vol.344 , pp. 259
    • Ito, T.1    Seyama, T.2    Iwamoto, K.S.3
  • 28
    • 0028821932 scopus 로고
    • Oncogenic rearrangements of the RET proto-oncogene in papillary thyroid carcinomas from children exposed to the Chernobyl nuclear accident
    • .
    • Fugazzola L Pilotti S Pinchera A et al. Oncogenic rearrangements of the RET proto-oncogene in papillary thyroid carcinomas from children exposed to the Chernobyl nuclear accident. Cancer Res 1995 55 5617 20.
    • (1995) Cancer Res , vol.55 , pp. 5617-20
    • Fugazzola, L.1    Pilotti, S.2    Pinchera, A.3
  • 29
    • 6244280442 scopus 로고
    • High prevalence of RET rearrangement in thyroid tumors of children from Belarus after the Chernobyl reactor accident
    • .
    • Klugbauer S Lengfelder E Demidchik EP Rabes HM. High prevalence of RET rearrangement in thyroid tumors of children from Belarus after the Chernobyl reactor accident. Oncogene 1995 11 2459 67.
    • (1995) Oncogene , vol.11 , pp. 2459-67
    • Klugbauer, S.1    Lengfelder, E.2    Demidchik, E.P.3    Rabes, H.M.4
  • 30
    • 0034693757 scopus 로고    scopus 로고
    • The RET proto-oncogene in human cancers
    • .
    • Jhiang SM. The RET proto-oncogene in human cancers. Oncogene 2000 19 5590 97.
    • (2000) Oncogene , vol.19 , pp. 5590-97
    • Jhiang, S.M.1
  • 32
    • 30944445020 scopus 로고    scopus 로고
    • BRAF mediates RET/PTC-induced MAPK activation in thyroid cells: Functional support for requirement of the RET/PTC-RAS-BRAF pathway in papillary thyroid carcinogenesis
    • .
    • Mitsutake N Miyagishi M Mitsutake S et al. BRAF mediates RET/PTC-induced MAPK activation in thyroid cells: Functional support for requirement of the RET/PTC-RAS-BRAF pathway in papillary thyroid carcinogenesis. Endocrinology 2006 147 1014 19.
    • (2006) Endocrinology , vol.147 , pp. 1014-19
    • Mitsutake, N.1    Miyagishi, M.2    Mitsutake, S.3
  • 33
    • 20144387455 scopus 로고    scopus 로고
    • The RET/PTC-RAS-BRAF linear signaling cascade mediates the motile and mitogenic phenotype of thyroid cancer cells
    • .
    • Melillo RM Castellone MD Guarino V et al. The RET/PTC-RAS-BRAF linear signaling cascade mediates the motile and mitogenic phenotype of thyroid cancer cells. J Clin Invest 2005 115 1068 80.
    • (2005) J Clin Invest , vol.115 , pp. 1068-80
    • Melillo, R.M.1    Castellone, M.D.2    Guarino, V.3
  • 34
    • 0037379904 scopus 로고    scopus 로고
    • High prevalence of BRAF mutations in thyroid cancer: Genetic evidence for constitutive activation of the RET/PTC-RAS-BRAF signaling pathway in papillary thyroid carcinoma
    • .
    • Kimura ET Nikiforova MN Zhu Z Knauf JA Nikiforov YE Fagin JA. High prevalence of BRAF mutations in thyroid cancer: Genetic evidence for constitutive activation of the RET/PTC-RAS-BRAF signaling pathway in papillary thyroid carcinoma. Cancer Res 2003 63 1454 7.
    • (2003) Cancer Res , vol.63 , pp. 1454-7
    • Kimura, E.T.1    Nikiforova, M.N.2    Zhu, Z.3    Knauf, J.A.4    Nikiforov, Y.E.5    Fagin, J.A.6
  • 35
    • 2442568538 scopus 로고    scopus 로고
    • V599E mutation is the leading genetic event in adult sporadic papillary thyroid carcinomas
    • .
    • V599E mutation is the leading genetic event in adult sporadic papillary thyroid carcinomas. J Clin Endocrinol Metab 2004 89 2414 20.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 2414-20
    • Puxeddu, E.1    Moretti, S.2    Elisei, R.3
  • 36
    • 0041589377 scopus 로고    scopus 로고
    • High prevalence of BRAF gene mutation in papillary thyroid carcinomas and thyroid tumor cell lines
    • .
    • Xu X Quiros RM Gattuso P Ain KB Prinz RA. High prevalence of BRAF gene mutation in papillary thyroid carcinomas and thyroid tumor cell lines. Cancer Res 2003 63 4561 7.
    • (2003) Cancer Res , vol.63 , pp. 4561-7
    • Xu, X.1    Quiros, R.M.2    Gattuso, P.3    Ain, K.B.4    Prinz, R.A.5
  • 37
    • 21244457181 scopus 로고    scopus 로고
    • BRAF mutation in thyroid cancer
    • .
    • Xing M. BRAF mutation in thyroid cancer. Endocr Relat Cancer 2005 12 245 62.
    • (2005) Endocr Relat Cancer , vol.12 , pp. 245-62
    • Xing, M.1
  • 38
    • 85047691154 scopus 로고    scopus 로고
    • Oncogenic AKAP9-BRAF fusion is a novel mechanism of MAPK pathway activation in thyroid cancer
    • .
    • Ciampi R Knauf JA Kerler R et al. Oncogenic AKAP9-BRAF fusion is a novel mechanism of MAPK pathway activation in thyroid cancer. J Clin Invest 2005 115 94 101.
    • (2005) J Clin Invest , vol.115 , pp. 94-101
    • Ciampi, R.1    Knauf, J.A.2    Kerler, R.3
  • 39
    • 85047687680 scopus 로고    scopus 로고
    • Molecular profile and clinical-pathologic features of the follicular variant of papillary thyroid carcinoma: An unusually high prevalence of ras mutations
    • .
    • Zhu Z Gandhi M Nikiforova MN Fischer AH Nikiforov YE. Molecular profile and clinical-pathologic features of the follicular variant of papillary thyroid carcinoma: An unusually high prevalence of ras mutations. Am J Clin Pathol 2003 120 71 7.
    • (2003) Am J Clin Pathol , vol.120 , pp. 71-7
    • Zhu, Z.1    Gandhi, M.2    Nikiforova, M.N.3    Fischer, A.H.4    Nikiforov, Y.E.5
  • 40
    • 26844576749 scopus 로고    scopus 로고
    • Induction of a proinflammatory program in normal human thyrocytes by the RET/PTC1 oncogene
    • . 25 . 30
    • Borrello MG Alberti L Fischer A et al. Induction of a proinflammatory program in normal human thyrocytes by the RET/PTC1 oncogene. Proc Natl Acad Sic USA 2005 41 14 25 30.
    • (2005) Proc Natl Acad Sic USA , vol.41 , pp. 14
    • Borrello, M.G.1    Alberti, L.2    Fischer, A.3
  • 41
    • 21244505009 scopus 로고    scopus 로고
    • RET/PTC-induced gene expression in thyroid PCCL3 cells reveals early activation of genes involved in regulation of the immune response
    • .
    • Puxeddu E Knauf JA Sartor MA et al. RET/PTC-induced gene expression in thyroid PCCL3 cells reveals early activation of genes involved in regulation of the immune response. Endocr Relat Cancer 2005 12 319 34.
    • (2005) Endocr Relat Cancer , vol.12 , pp. 319-34
    • Puxeddu, E.1    Knauf, J.A.2    Sartor, M.A.3
  • 42
    • 0027231568 scopus 로고
    • Germ-line mutations of the RET proto-oncogene in multiple endocrine neoplasia type 2A
    • .
    • Mulligan LM Kwok JBJ Healey CS et al. Germ-line mutations of the RET proto-oncogene in multiple endocrine neoplasia type 2A. Nature 1993 363 458 60.
    • (1993) Nature , vol.363 , pp. 458-60
    • Mulligan, L.M.1    Kwok, J.B.J.2    Healey, C.S.3
  • 43
    • 0027303248 scopus 로고
    • Mutations in the RET protooncogene are associated with MEN 2A and FMTC
    • .
    • Donis-Keller H Dou S Chi D et al. Mutations in the RET protooncogene are associated with MEN 2A and FMTC. Hum Mol Genet 1993 2 851 6.
    • (1993) Hum Mol Genet , vol.2 , pp. 851-6
    • Donis-Keller, H.1    Dou, S.2    Chi, D.3
  • 44
    • 0028174024 scopus 로고
    • A mutation in the RET proto-oncogene associated with multiple endocrine neoplasia type 2B and sporadic medullary thyroid carcinoma
    • .
    • Hofstra RMW Landsvater RM Ceccherini I et al. A mutation in the RET proto-oncogene associated with multiple endocrine neoplasia type 2B and sporadic medullary thyroid carcinoma. Nature 1994 367 375 6.
    • (1994) Nature , vol.367 , pp. 375-6
    • Hofstra, R.M.W.1    Landsvater, R.M.2    Ceccherini, I.3
  • 45
    • 0027977002 scopus 로고
    • Single missense mutation in the tyrosine kinase catalytic domain of the RET protooncogene is associated with multiple endocrine neoplasia type 2B
    • .
    • Carlson KM Dou S Chi D et al. Single missense mutation in the tyrosine kinase catalytic domain of the RET protooncogene is associated with multiple endocrine neoplasia type 2B. Proc Natl Acad Sci USA 1994 91 1579 83.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1579-83
    • Carlson, K.M.1    Dou, S.2    Chi, D.3
  • 46
    • 0033045514 scopus 로고    scopus 로고
    • Two germline missense mutations at codons 804 and 806 of the RET proto-oncogene in the same allele in a patient with multiple endocrine neoplasia type 2B without codon 918 mutation
    • .
    • Miyauchi A Futami H Hai N et al. Two germline missense mutations at codons 804 and 806 of the RET proto-oncogene in the same allele in a patient with multiple endocrine neoplasia type 2B without codon 918 mutation. Jpn J Cancer Res 1999 90 1 5.
    • (1999) Jpn J Cancer Res , vol.90 , pp. 1-5
    • Miyauchi, A.1    Futami, H.2    Hai, N.3
  • 47
    • 0035158951 scopus 로고    scopus 로고
    • Novel germline RET mutation segregating with papillary thyroid carcinomas
    • .
    • Rey JM Brouillet JP Fonteneau-Allaire J et al. Novel germline RET mutation segregating with papillary thyroid carcinomas. Genes Chromosomes Cancer 2001 32 390 91.
    • (2001) Genes Chromosomes Cancer , vol.32 , pp. 390-91
    • Rey, J.M.1    Brouillet, J.P.2    Fonteneau-Allaire, J.3
  • 48
    • 3242769786 scopus 로고    scopus 로고
    • The oncogenic activity of RET point mutants for follicular thyroid cells may account for the occurrence of papillary thyroid carcinoma in patients affected by familial medullary thyroid carcinoma
    • .
    • Melillo RM Cirafici AM De Falco V et al. The oncogenic activity of RET point mutants for follicular thyroid cells may account for the occurrence of papillary thyroid carcinoma in patients affected by familial medullary thyroid carcinoma. Am J Pathol 2004 165 511 21.
    • (2004) Am J Pathol , vol.165 , pp. 511-21
    • Melillo, R.M.1    Cirafici, A.M.2    De Falco, V.3
  • 49
    • 0033917197 scopus 로고    scopus 로고
    • Variable expressivity of familial medullary thyroid carcinoma (FMTC) due to a RET V804M (GTG→ATG) mutation
    • .
    • Feldman GL Edmonds MW Ainsworth PJ et al. Variable expressivity of familial medullary thyroid carcinoma (FMTC) due to a RET V804M (GTG→ATG) mutation. Surgery 2000 28 93 8.
    • (2000) Surgery , vol.28 , pp. 93-8
    • Feldman, G.L.1    Edmonds, M.W.2    Ainsworth, P.J.3
  • 50
    • 0035992864 scopus 로고    scopus 로고
    • Papillary thyroid carcinoma in patients with RET proto-oncogene germline mutation
    • .
    • Brauckhoff M Gimm O Hinze R et al. Papillary thyroid carcinoma in patients with RET proto-oncogene germline mutation. Thyroid 2002 12 557 61.
    • (2002) Thyroid , vol.12 , pp. 557-61
    • Brauckhoff, M.1    Gimm, O.2    Hinze, R.3
  • 51
    • 0242351686 scopus 로고    scopus 로고
    • Concurrent lymph node metastases of medullary and papillary thyroid carcinoma in a case with RET oncogene germline mutation
    • .
    • Papi G Corrado S Pomponi MG Carapezzi C Cesinaro A LiVolsi VA. Concurrent lymph node metastases of medullary and papillary thyroid carcinoma in a case with RET oncogene germline mutation. Endocr Pathol 2003 14 269 76.
    • (2003) Endocr Pathol , vol.14 , pp. 269-76
    • Papi, G.1    Corrado, S.2    Pomponi, M.G.3    Carapezzi, C.4    Cesinaro, A.5    LiVolsi, V.A.6
  • 52
    • 0035114386 scopus 로고    scopus 로고
    • RET proto-oncogene mutation in a mixed medullary-follicular thyroid carcinoma
    • .
    • Orlandi F Ciefari E Caraci P et al. RET proto-oncogene mutation in a mixed medullary-follicular thyroid carcinoma. J Endocrinol Invest 2001 24 51 5.
    • (2001) J Endocrinol Invest , vol.24 , pp. 51-5
    • Orlandi, F.1    Ciefari, E.2    Caraci, P.3
  • 53
    • 0035811591 scopus 로고    scopus 로고
    • C-cell and thyroid epithelial tumours and altered follicular development in transgenic mice expressing the long isoform of MEN 2A RET
    • .
    • Reynolds L Jones K Winton DJ et al. C-cell and thyroid epithelial tumours and altered follicular development in transgenic mice expressing the long isoform of MEN 2A RET. Oncogene 2001 20 3986 94.
    • (2001) Oncogene , vol.20 , pp. 3986-94
    • Reynolds, L.1    Jones, K.2    Winton, D.J.3
  • 54
    • 0028838086 scopus 로고
    • Mechanism of activation of ret proto-oncogene by multiple endocrine neoplasia 2A mutation
    • .
    • Asai N Iwashita T Matsuyama M Takahashi M. Mechanism of activation of ret proto-oncogene by multiple endocrine neoplasia 2A mutation. Mol Cell Biol 1995 15 1613 19.
    • (1995) Mol Cell Biol , vol.15 , pp. 1613-19
    • Asai, N.1    Iwashita, T.2    Matsuyama, M.3    Takahashi, M.4
  • 55
    • 0028914683 scopus 로고
    • Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B
    • .
    • Santoro M Carlomagno F Romano A et al. Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B. Science 1995 267 381 3.
    • (1995) Science , vol.267 , pp. 381-3
    • Santoro, M.1    Carlomagno, F.2    Romano, A.3
  • 56
    • 13344286328 scopus 로고
    • RET activation by germline MEN2A and MEN2B mutations
    • .
    • Borrello MG Smith DP Pasini B et al. RET activation by germline MEN2A and MEN2B mutations. Oncogene 1995 11 2419 27.
    • (1995) Oncogene , vol.11 , pp. 2419-27
    • Borrello, M.G.1    Smith, D.P.2    Pasini, B.3
  • 57
    • 0030047832 scopus 로고    scopus 로고
    • Identification of tyrosine residues that are essential for transforming activity of the ret proto-oncogene with MEN2A or MEN2B mutation
    • .
    • Iwashita T Asai N Murakami H Takahashi M. Identification of tyrosine residues that are essential for transforming activity of the ret proto-oncogene with MEN2A or MEN2B mutation. Oncogene 1996 12 481 7.
    • (1996) Oncogene , vol.12 , pp. 481-7
    • Iwashita, T.1    Asai, N.2    Murakami, H.3    Takahashi, M.4
  • 58
    • 0028938721 scopus 로고
    • Catalytic specificity of protein-tyrosine kinase is critical for selective signalling
    • . III
    • Songyanag Z Carraway KL III Eck MJ et al. Catalytic specificity of protein-tyrosine kinase is critical for selective signalling. Nature 1995 373 536 9.
    • (1995) Nature , vol.373 , pp. 536-9
    • Songyanag, Z.1    Carraway, K.L.2    Eck, M.J.3
  • 59
    • 0033166442 scopus 로고    scopus 로고
    • Biological and biochemical properties of Ret with kinase domain mutations identified in multiple endocrine neoplasia type 2B and familial medullary thyroid carcinoma
    • .
    • Iwashita T Kato M Murakami H et al. Biological and biochemical properties of Ret with kinase domain mutations identified in multiple endocrine neoplasia type 2B and familial medullary thyroid carcinoma. Oncogene 1999 18 3919 22.
    • (1999) Oncogene , vol.18 , pp. 3919-22
    • Iwashita, T.1    Kato, M.2    Murakami, H.3
  • 60
    • 0029893933 scopus 로고    scopus 로고
    • A mutation at tyrosine 1062 in MEN2A-Ret and MEN2B-Ret impairs their transforming activity and association with Shc adaptor proteins
    • . 44 . 9
    • Asai N Murakami H Iwashita T Takahashi M. A mutation at tyrosine 1062 in MEN2A-Ret and MEN2B-Ret impairs their transforming activity and association with Shc adaptor proteins. J Biol Chem 1996 271 17 44 9.
    • (1996) J Biol Chem , vol.271 , pp. 17
    • Asai, N.1    Murakami, H.2    Iwashita, T.3    Takahashi, M.4
  • 61
    • 0034603172 scopus 로고    scopus 로고
    • Transforming ability of MEN2A-RET requires activation of the phosphatidylinositol 3-kinase/AKT signaling pathway
    • .
    • Segouffin-Cariou C Billaud M. Transforming ability of MEN2A-RET requires activation of the phosphatidylinositol 3-kinase/AKT signaling pathway. J Biol Chem 2000 275 3568 76.
    • (2000) J Biol Chem , vol.275 , pp. 3568-76
    • Segouffin-Cariou, C.1    Billaud, M.2
  • 62
    • 6044275784 scopus 로고    scopus 로고
    • Differential requirement of Tyr1062 multidocking site by RET isoforms to promote neural cell scattering and epithelial cell branching
    • .
    • Degl'Innocenti D Arighi E Popsueva A et al. Differential requirement of Tyr1062 multidocking site by RET isoforms to promote neural cell scattering and epithelial cell branching. Oncogene 2004 23 7297 309.
    • (2004) Oncogene , vol.23 , pp. 7297-309
    • Degl'Innocenti, D.1    Arighi, E.2    Popsueva, A.3
  • 63
    • 0034849573 scopus 로고    scopus 로고
    • The GDNF/RET signaling pathway and human diseases
    • .
    • Takahashi M. The GDNF/RET signaling pathway and human diseases. Cytokine Growth Factor Rev 2001 12 361 73.
    • (2001) Cytokine Growth Factor Rev , vol.12 , pp. 361-73
    • Takahashi, M.1
  • 65
    • 17744373695 scopus 로고    scopus 로고
    • The RET proto-oncogene: A molecular therapeutic target in thyroid cancer
    • .
    • Kodama Y Asai N Kawai K et al. The RET proto-oncogene: A molecular therapeutic target in thyroid cancer. Cancer Sci 2005 96 143 8.
    • (2005) Cancer Sci , vol.96 , pp. 143-8
    • Kodama, Y.1    Asai, N.2    Kawai, K.3
  • 66
    • 10344230447 scopus 로고    scopus 로고
    • The neuronal scaffold protein Shank3 mediates signaling and biological function of the receptor tyrosine kinase Ret in epithelial cells
    • .
    • Schuetz G Rosario M Grimm J Boeckers TM Gundelfinger ED Birchmeier W. The neuronal scaffold protein Shank3 mediates signaling and biological function of the receptor tyrosine kinase Ret in epithelial cells. J Cell Biol 2004 167 945 52.
    • (2004) J Cell Biol , vol.167 , pp. 945-52
    • Schuetz, G.1    Rosario, M.2    Grimm, J.3    Boeckers, T.M.4    Gundelfinger, E.D.5    Birchmeier, W.6
  • 67
    • 0034648718 scopus 로고    scopus 로고
    • Characterization of intracellular signals via tyrosine 1062 in RET activated by glial cell line-derived neurotrophic factor
    • .
    • Hayashi H Ichihara M Iwashita T et al. Characterization of intracellular signals via tyrosine 1062 in RET activated by glial cell line-derived neurotrophic factor. Oncogene 2000 19 4469 75.
    • (2000) Oncogene , vol.19 , pp. 4469-75
    • Hayashi, H.1    Ichihara, M.2    Iwashita, T.3
  • 68
    • 0034671913 scopus 로고    scopus 로고
    • Signaling complexes and protein-protein interactions involved in the activation of the Ras and phosphatidylinositol 3-kinase pathways by the c-Ret receptor tyrosine kinase
    • . 59 . 66
    • Besset V Scott RP Ibáñez CF. Signaling complexes and protein-protein interactions involved in the activation of the Ras and phosphatidylinositol 3-kinase pathways by the c-Ret receptor tyrosine kinase. J Biol Chem 2000 275 39 59 66.
    • (2000) J Biol Chem , vol.275 , pp. 39
    • Besset, V.1    Scott, R.P.2    Ibáñez, C.F.3
  • 69
    • 0034816526 scopus 로고    scopus 로고
    • Activation of BMK1 via tyrosine 1062 in RET by GDNF and MEN2A mutation
    • .
    • Hayashi Y Iwashita T Murakami H et al. Activation of BMK1 via tyrosine 1062 in RET by GDNF and MEN2A mutation. Biochem Biophys Res Commun 2001 281 682 9.
    • (2001) Biochem Biophys Res Commun , vol.281 , pp. 682-9
    • Hayashi, Y.1    Iwashita, T.2    Murakami, H.3
  • 71
    • 0033584474 scopus 로고    scopus 로고
    • Enhanced phosphatidylinositol 3-kinase activity and high phosphorylation state of its downstream signalling molecules mediated by Ret with the MEN 2B mutation
    • .
    • Murakami H Iwashita T Asai N et al. Enhanced phosphatidylinositol 3-kinase activity and high phosphorylation state of its downstream signalling molecules mediated by Ret with the MEN 2B mutation. Biochem Biophys Res Commun 1999 262 68 75.
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 68-75
    • Murakami, H.1    Iwashita, T.2    Asai, N.3
  • 72
    • 15144348923 scopus 로고    scopus 로고
    • Expression of multiple endocrine neoplasia 2B RET in neuroblastoma cells alters cell adhesion in vitro, enhances metastatic behavior in vivo, and activates Jun kinase
    • .
    • Marshall GM Peaston AE Hocker JE et al. Expression of multiple endocrine neoplasia 2B RET in neuroblastoma cells alters cell adhesion in vitro, enhances metastatic behavior in vivo, and activates Jun kinase. Cancer Res 1997 57 5399 405.
    • (1997) Cancer Res , vol.57 , pp. 5399-405
    • Marshall, G.M.1    Peaston, A.E.2    Hocker, J.E.3
  • 73
    • 3442876128 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase and extracellular signal-regulated kinase is required for glial cell line-derived neurotrophic factor-induced migration and invasion of pancreatic carcinoma cells
    • .
    • Viet C Genze F Menke A et al. Activation of phosphatidylinositol 3-kinase and extracellular signal-regulated kinase is required for glial cell line-derived neurotrophic factor-induced migration and invasion of pancreatic carcinoma cells. Cancer Res 2004 64 5291 300.
    • (2004) Cancer Res , vol.64 , pp. 5291-300
    • Viet, C.1    Genze, F.2    Menke, A.3
  • 74
    • 0035489468 scopus 로고    scopus 로고
    • PKB/AKT: Functional insights from genetic models
    • .
    • Scheid MP Woodgett JR. PKB/AKT: Functional insights from genetic models. Nat Rev Mol Cell Biol 2001 2 760 68.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 760-68
    • Scheid, M.P.1    Woodgett, J.R.2
  • 75
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase-Akt pathway in human cancer
    • .
    • Vianco I Sawyers CL. The phosphatidylinositol 3-kinase-Akt pathway in human cancer. Nat Rev Cancer 2002 2 489 501.
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vianco, I.1    Sawyers, C.L.2
  • 76
    • 24144496081 scopus 로고    scopus 로고
    • Akt/PKB regulates actin organization and cell motility via Girdin/APE
    • .
    • Enomoto A Murakami H Asai N et al. Akt/PKB regulates actin organization and cell motility via Girdin/APE. Dev Cell 2005 9 389 402.
    • (2005) Dev Cell , vol.9 , pp. 389-402
    • Enomoto, A.1    Murakami, H.2    Asai, N.3
  • 77
    • 0036314247 scopus 로고    scopus 로고
    • Characterization of gene expression induced by RET with MEN2A or MEN2B mutation
    • .
    • Watanabe T Ichihara M Hashimoto M et al. Characterization of gene expression induced by RET with MEN2A or MEN2B mutation. Am J Pathol 2002 161 249 56.
    • (2002) Am J Pathol , vol.161 , pp. 249-56
    • Watanabe, T.1    Ichihara, M.2    Hashimoto, M.3
  • 78
    • 2542622016 scopus 로고    scopus 로고
    • Expression profiles provide insights into early malignant potential and skeletal abnormalities in multiple endocrine neoplasia type 2B syndrome tumors
    • .
    • Jain S Watoson MA DeBenedetti MK Hiraki Y Moley JF Milbrandt J. Expression profiles provide insights into early malignant potential and skeletal abnormalities in multiple endocrine neoplasia type 2B syndrome tumors. Cancer Res 2004 64 3907 13.
    • (2004) Cancer Res , vol.64 , pp. 3907-13
    • Jain, S.1    Watoson, M.A.2    Debenedetti, M.K.3    Hiraki, Y.4    Moley, J.F.5    Milbrandt, J.6
  • 79
    • 0028120882 scopus 로고
    • Point mutations affecting the tyrosine kinase domain of the RET proto-oncogene in Hirschsprung's disease
    • .
    • Romeo G Ronchetto P Luo Y et al. Point mutations affecting the tyrosine kinase domain of the RET proto-oncogene in Hirschsprung's disease. Nature 1994 367 377 8.
    • (1994) Nature , vol.367 , pp. 377-8
    • Romeo, G.1    Ronchetto, P.2    Luo, Y.3
  • 80
    • 0027972513 scopus 로고
    • Mutations of the RET protooncogene in Hirschsprung's disease
    • .
    • Edery P Lyonnet S Mulligan LM et al. Mutations of the RET protooncogene in Hirschsprung's disease. Nature 1994 367 378 80.
    • (1994) Nature , vol.367 , pp. 378-80
    • Edery, P.1    Lyonnet, S.2    Mulligan, L.M.3
  • 81
    • 0030292383 scopus 로고    scopus 로고
    • Germline mutations in glial cell line-derived neurotrophic factor (GDNF) and RET in a Hirschsprung disease patient
    • .
    • Angrist M Bolk S Halushka M Lapchak PA Chakravarti A. Germline mutations in glial cell line-derived neurotrophic factor (GDNF) and RET in a Hirschsprung disease patient. Nat Genet 1996 14 341 4.
    • (1996) Nat Genet , vol.14 , pp. 341-4
    • Angrist, M.1    Bolk, S.2    Halushka, M.3    Lapchak, P.A.4    Chakravarti, A.5
  • 82
    • 16144368214 scopus 로고    scopus 로고
    • Germline mutations of the RET ligand GDNF are not sufficient to cause Hirschsprung disease
    • .
    • Salomon R Attie T Pelet A et al. Germline mutations of the RET ligand GDNF are not sufficient to cause Hirschsprung disease. Nat Genet 1996 14 345 7.
    • (1996) Nat Genet , vol.14 , pp. 345-7
    • Salomon, R.1    Attie, T.2    Pelet, A.3
  • 83
    • 0029822720 scopus 로고    scopus 로고
    • De novo mutation of GDNF, ligand for the RET/GDNFR-alpha receptor complex, in Hirschsprung disease
    • .
    • Ivanchuk SM Myers SM Eng C Mulligan LM. De novo mutation of GDNF, ligand for the RET/GDNFR-alpha receptor complex, in Hirschsprung disease. Hum Mol Genet 1996 5 2023 6.
    • (1996) Hum Mol Genet , vol.5 , pp. 2023-6
    • Ivanchuk, S.M.1    Myers, S.M.2    Eng, C.3    Mulligan, L.M.4
  • 84
    • 7344244286 scopus 로고    scopus 로고
    • Mutation of the RET ligand, neurturin, supports multigenic inheritance in Hirschsprung disease
    • .
    • Doray B Salomon R Amiel J et al. Mutation of the RET ligand, neurturin, supports multigenic inheritance in Hirschsprung disease. Hum Mol Genet 1998 9 1449 52.
    • (1998) Hum Mol Genet , vol.9 , pp. 1449-52
    • Doray, B.1    Salomon, R.2    Amiel, J.3
  • 85
    • 0028618372 scopus 로고
    • A missense mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease
    • .
    • Puffenberger EG Hosoda K Washington SS et al. A missense mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease. Cell 1994 79 1257 66.
    • (1994) Cell , vol.79 , pp. 1257-66
    • Puffenberger, E.G.1    Hosoda, K.2    Washington, S.S.3
  • 86
    • 0006457459 scopus 로고    scopus 로고
    • Mutation of the endothelin-3 gene in the Waardenburg-Hirschsprung disease (Shah-Waardenburg syndrome)
    • .
    • Edery P Attie T Amiel J et al. Mutation of the endothelin-3 gene in the Waardenburg-Hirschsprung disease (Shah-Waardenburg syndrome). Nat Genet 1996 12 442 4.
    • (1996) Nat Genet , vol.12 , pp. 442-4
    • Edery, P.1    Attie, T.2    Amiel, J.3
  • 87
    • 0009675716 scopus 로고    scopus 로고
    • A homozygous mutation in the endothelin-3 gene associated with a combined Waardenburg type 2 and Hirschsprung phenotype (Shah-Waardenburg syndrome)
    • .
    • Hofstra RM Osinga J Tan-Sindhunata G et al. A homozygous mutation in the endothelin-3 gene associated with a combined Waardenburg type 2 and Hirschsprung phenotype (Shah-Waardenburg syndrome). Nat Genet 1996 4 445 7.
    • (1996) Nat Genet , vol.4 , pp. 445-7
    • Hofstra, R.M.1    Osinga, J.2    Tan-Sindhunata, G.3
  • 88
    • 0033366516 scopus 로고    scopus 로고
    • A loss-of-function mutation in the endothelin-converting enzyme 1 (ECE-1) associated with Hirschsprung disease, cardiac defects, and autonomic dysfunction
    • .
    • Hofstra RMW Valdenaire O Arch E et al. A loss-of-function mutation in the endothelin-converting enzyme 1 (ECE-1) associated with Hirschsprung disease, cardiac defects, and autonomic dysfunction. Am J Hum Genet 1999 64 304 8.
    • (1999) Am J Hum Genet , vol.64 , pp. 304-8
    • Hofstra, R.M.W.1    Valdenaire, O.2    Arch, E.3
  • 89
    • 17344366171 scopus 로고    scopus 로고
    • SOX10 mutations in patients with Waardenburg-Hirschsprung disease
    • .
    • Pingault V Bondurand N Kuhlbrodt K et al. SOX10 mutations in patients with Waardenburg-Hirschsprung disease. Nat Genet 1998 18 171 3.
    • (1998) Nat Genet , vol.18 , pp. 171-3
    • Pingault, V.1    Bondurand, N.2    Kuhlbrodt, K.3
  • 90
    • 0035065576 scopus 로고    scopus 로고
    • Mutations in SIP1 encoding Smad interacting protein-1, cause a form of Hirschsprung disease
    • .
    • Wakamatsu N Yamada Y Yamada K et al. Mutations in SIP1 encoding Smad interacting protein-1, cause a form of Hirschsprung disease. Nat Genet 2001 27 369 70.
    • (2001) Nat Genet , vol.27 , pp. 369-70
    • Wakamatsu, N.1    Yamada, Y.2    Yamada, K.3
  • 91
    • 15844405218 scopus 로고    scopus 로고
    • Molecular heterogeneity of RET loss of function in Hirschsprung's disease
    • .
    • Carlomagno F De Vita G Berlingieri MT et al. Molecular heterogeneity of RET loss of function in Hirschsprung's disease. EMBO J 1996 15 2717 25.
    • (1996) EMBO J , vol.15 , pp. 2717-25
    • Carlomagno, F.1    De Vita, G.2    Berlingieri, M.T.3
  • 92
    • 0029798406 scopus 로고    scopus 로고
    • Mechanism of Ret dysfunction by Hirschsprung mutations affecting its extracellular domain
    • .
    • Iwashita T Murakami H Asai N Takahashi M. Mechanism of Ret dysfunction by Hirschsprung mutations affecting its extracellular domain. Hum Mol Genet 1996 5 1578 80.
    • (1996) Hum Mol Genet , vol.5 , pp. 1578-80
    • Iwashita, T.1    Murakami, H.2    Asai, N.3    Takahashi, M.4
  • 93
    • 0031843172 scopus 로고    scopus 로고
    • Mutations in the extracellular domain cause RET loss of function by a dominant negative mechanism
    • .
    • Cosma MP Cardone M Carlomagno F Colantuoni V. Mutations in the extracellular domain cause RET loss of function by a dominant negative mechanism. Mol Cell Biol 1998 18 3321 9.
    • (1998) Mol Cell Biol , vol.18 , pp. 3321-9
    • Cosma, M.P.1    Cardone, M.2    Carlomagno, F.3    Colantuoni, V.4
  • 94
    • 0030739287 scopus 로고    scopus 로고
    • Biological properties of Ret with cysteine mutations correlate with multiple endocrine neoplasia type 2A, familial medullary thyroid carcinoma, and Hirschsprung's disease phenotype
    • .
    • Ito S Iwashita T Asai N et al. Biological properties of Ret with cysteine mutations correlate with multiple endocrine neoplasia type 2A, familial medullary thyroid carcinoma, and Hirschsprung's disease phenotype. Cancer Res 1997 57 2870 72.
    • (1997) Cancer Res , vol.57 , pp. 2870-72
    • Ito, S.1    Iwashita, T.2    Asai, N.3
  • 95
    • 0032521177 scopus 로고    scopus 로고
    • Various mechanisms cause RET-mediated signaling defects in Hirschsprung's disease
    • .
    • Pelet A Geneste O Edery P et al. Various mechanisms cause RET-mediated signaling defects in Hirschsprung's disease. J Clin Invest 1998 101 1415 23.
    • (1998) J Clin Invest , vol.101 , pp. 1415-23
    • Pelet, A.1    Geneste, O.2    Edery, P.3
  • 96
    • 0032481129 scopus 로고    scopus 로고
    • Dual effect on the RET receptor of MEN 2 mutations affecting specific extracytoplasmic cysteines
    • .
    • Chappuis-Flament S Pasini A De Vita G et al. Dual effect on the RET receptor of MEN 2 mutations affecting specific extracytoplasmic cysteines. Oncogene 1998 17 2851 61.
    • (1998) Oncogene , vol.17 , pp. 2851-61
    • Chappuis-Flament, S.1    Pasini, A.2    De Vita, G.3
  • 97
    • 0033054334 scopus 로고    scopus 로고
    • Co-segregation of MEN2 and Hirschsprung's disease: The same mutation of RET with both gain and loss-of-function?
    • Takahashi M Iwashita T Santoro M Lyonnet S Leinor GM Billaud M. Co-segregation of MEN2 and Hirschsprung's disease: The same mutation of RET with both gain and loss-of-function? Hum Mutat 1999 13 331 6.
    • (1999) Hum Mutat , vol.13 , pp. 331-6
    • Takahashi, M.1    Iwashita, T.2    Santoro, M.3    Lyonnet, S.4    Leinor, G.M.5    Billaud, M.6
  • 98
    • 0029050368 scopus 로고
    • Loss of function effect of RET mutations causing Hirschsprung disease
    • .
    • Pasini B Borrello MG Greco A et al. Loss of function effect of RET mutations causing Hirschsprung disease. Nat Genet 1995 10 35 40.
    • (1995) Nat Genet , vol.10 , pp. 35-40
    • Pasini, B.1    Borrello, M.G.2    Greco, A.3
  • 99
    • 0034950648 scopus 로고    scopus 로고
    • Functional analysis of RET with Hirschsprung's mutations affecting the extracellular domain
    • .
    • Iwashita T Kurokawa K Qiao S et al. Functional analysis of RET with Hirschsprung's mutations affecting the extracellular domain. Gastroenterology 2001 121 24 33.
    • (2001) Gastroenterology , vol.121 , pp. 24-33
    • Iwashita, T.1    Kurokawa, K.2    Qiao, S.3
  • 100
    • 0032869135 scopus 로고    scopus 로고
    • Two distinct mutations of the RET receptor causing Hirschsprung's disease impair the binding of signalling effector to a multifunctional docking site
    • .
    • Geneste O Bidaud C De Vita G et al. Two distinct mutations of the RET receptor causing Hirschsprung's disease impair the binding of signalling effector to a multifunctional docking site. Hum Mol Genet 1999 8 1989 99.
    • (1999) Hum Mol Genet , vol.8 , pp. 1989-99
    • Geneste, O.1    Bidaud, C.2    De Vita, G.3
  • 101
    • 0033305444 scopus 로고    scopus 로고
    • The role of amino acids surrounding tyrosine 1062 in Ret in specific binding of the Shc phosphotyrosine binding domain
    • .
    • Ishiguro Y Iwashita T Murakami H et al. The role of amino acids surrounding tyrosine 1062 in Ret in specific binding of the Shc phosphotyrosine binding domain. Endocrinology 1999 140 3992 8.
    • (1999) Endocrinology , vol.140 , pp. 3992-8
    • Ishiguro, Y.1    Iwashita, T.2    Murakami, H.3
  • 102
    • 4444324911 scopus 로고    scopus 로고
    • A targeting mutation of tyrosine 1062 in Ret causes a marked decrease of enteric neurons and renal hypoplasia
    • .
    • Jijiwa M Fukuda T Kawai K et al. A targeting mutation of tyrosine 1062 in Ret causes a marked decrease of enteric neurons and renal hypoplasia. Mol Cell Biol 2004 24 8026 36.
    • (2004) Mol Cell Biol , vol.24 , pp. 8026-36
    • Jijiwa, M.1    Fukuda, T.2    Kawai, K.3
  • 103
    • 27144467717 scopus 로고    scopus 로고
    • Phosphotyrosine 1062 is critical for the in vivo activity of the Ret9 receptor tyrosine kinase isoform
    • .
    • Wong A Bogni S Kotka P et al. Phosphotyrosine 1062 is critical for the in vivo activity of the Ret9 receptor tyrosine kinase isoform. Mol Cell Biol 2005 25 9661 73.
    • (2005) Mol Cell Biol , vol.25 , pp. 9661-73
    • Wong, A.1    Bogni, S.2    Kotka, P.3
  • 104
    • 9444225531 scopus 로고    scopus 로고
    • Mice expressing a dominant-negative Ret mutation phenocopy human Hirschsprung disease and delineate a direct role of Ret in spermatogenesis
    • .
    • Jain S Naughton CK Yang M et al. Mice expressing a dominant-negative Ret mutation phenocopy human Hirschsprung disease and delineate a direct role of Ret in spermatogenesis. Development 2004 131 5503 13.
    • (2004) Development , vol.131 , pp. 5503-13
    • Jain, S.1    Naughton, C.K.2    Yang, M.3
  • 105
    • 17244383525 scopus 로고    scopus 로고
    • A common sex-dependent mutation in a RET enhancer underlies Hirschsprung disease risk
    • .
    • Emison ES McCallion AS Kashuk CS et al. A common sex-dependent mutation in a RET enhancer underlies Hirschsprung disease risk. Nature 2005 43 857 63.
    • (2005) Nature , vol.43 , pp. 857-63
    • Emison, E.S.1    McCallion, A.S.2    Kashuk, C.S.3
  • 106
    • 29644434290 scopus 로고    scopus 로고
    • Evaluation of the RET regulatory landscape reveals the biological relevance of a HSCR-implicated enhancer
    • .
    • Grice EA Rochelle ES Green ED Chakravatri A McCallion AS. Evaluation of the RET regulatory landscape reveals the biological relevance of a HSCR-implicated enhancer. Hum Mol Genet 2005 14 3837 45.
    • (2005) Hum Mol Genet , vol.14 , pp. 3837-45
    • Grice, E.A.1    Rochelle, E.S.2    Green, E.D.3    Chakravatri, A.4    McCallion, A.S.5
  • 107
    • 19944430369 scopus 로고    scopus 로고
    • TTF-1 and RET promoter SNPs: Regulation of RET transcription in Hirschsprung's disease
    • .
    • Garcia-Barcelo M Ganster RW Lui VC et al. TTF-1 and RET promoter SNPs: Regulation of RET transcription in Hirschsprung's disease. Hum Mol Genet 2005 14 191 204.
    • (2005) Hum Mol Genet , vol.14 , pp. 191-204
    • Garcia-Barcelo, M.1    Ganster, R.W.2    Lui, V.C.3
  • 108
    • 0034602646 scopus 로고    scopus 로고
    • A human model for multigenic inheritance: Phenotypic expression in Hirschsprung disease requires both the RET gene and a new 9q31 locus
    • .
    • Bolk S Pelet A Hofstra RMW et al. A human model for multigenic inheritance: Phenotypic expression in Hirschsprung disease requires both the RET gene and a new 9q31 locus. Proc Natl Acad Sci USA 2000 97 268 73.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 268-73
    • Bolk, S.1    Pelet, A.2    Hofstra, R.M.W.3
  • 109
    • 18544365991 scopus 로고    scopus 로고
    • Segregation at three loci explains familial and population risk in Hirschsprung disease
    • .
    • Gabriel AB Salomon R Pelet A et al. Segregation at three loci explains familial and population risk in Hirschsprung disease. Nat Genet 2002 31 89 93.
    • (2002) Nat Genet , vol.31 , pp. 89-93
    • Gabriel, A.B.1    Salomon, R.2    Pelet, A.3
  • 110
    • 0036788576 scopus 로고    scopus 로고
    • Genome-wide association study and mouse model identify interaction between RET and EDNRB pathways in Hirschsprung disease
    • .
    • Carrasquillo MM McCallion AS Puffenberger EG et al. Genome-wide association study and mouse model identify interaction between RET and EDNRB pathways in Hirschsprung disease. Nat Genet 2002 32 237 44.
    • (2002) Nat Genet , vol.32 , pp. 237-44
    • Carrasquillo, M.M.1    McCallion, A.S.2    Puffenberger, E.G.3
  • 111
    • 0037452581 scopus 로고    scopus 로고
    • Phenotype variation in two-locus mouse models of Hirschsprung disease: Tissue-specific interaction between Ret and Ednrb
    • .
    • McCallion AS Stames E Conlon RA Chakravarti A. Phenotype variation in two-locus mouse models of Hirschsprung disease: Tissue-specific interaction between Ret and Ednrb. Proc Natl Acad Sci USA 2003 100 1826 31.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1826-31
    • McCallion, A.S.1    Stames, E.2    Conlon, R.A.3    Chakravarti, A.4
  • 112
    • 0347194147 scopus 로고    scopus 로고
    • Enteric nervous system progenitors are coordinately controlled by the G protein-coupled receptor EDNRB and the receptor tyrosine kinase RET
    • .
    • Barlow A Graaff ED Pachnis V. Enteric nervous system progenitors are coordinately controlled by the G protein-coupled receptor EDNRB and the receptor tyrosine kinase RET. Neuron 2003 40 905 16.
    • (2003) Neuron , vol.40 , pp. 905-16
    • Barlow, A.1    Graaff, E.D.2    Pachnis, V.3
  • 113
    • 0037166286 scopus 로고    scopus 로고
    • Novel mechanism of regulation of Rac activity and lamellipodia formation by RET tyrosine kinase
    • . 14 . 21
    • Fukuda T Kiuchi K Takahashi M. Novel mechanism of regulation of Rac activity and lamellipodia formation by RET tyrosine kinase. J Biol Chem 2002 277 19 14 21.
    • (2002) J Biol Chem , vol.277 , pp. 19
    • Fukuda, T.1    Kiuchi, K.2    Takahashi, M.3
  • 114
    • 21644486401 scopus 로고    scopus 로고
    • Activation of c-Jun amino-terminal kinase by GDNF induces G2/M cell cycle delay linked with actin reorganization
    • .
    • Fukuda T Asai N Enomoto A Takahashi M. Activation of c-Jun amino-terminal kinase by GDNF induces G2/M cell cycle delay linked with actin reorganization. Genes Cells 2005 10 655 63.
    • (2005) Genes Cells , vol.10 , pp. 655-63
    • Fukuda, T.1    Asai, N.2    Enomoto, A.3    Takahashi, M.4
  • 115
    • 17944401554 scopus 로고    scopus 로고
    • Regulation of cell fate decision of undifferentiated spermatogonia by GDNF
    • .
    • Meng X Lindahl M Hyvönen ME et al. Regulation of cell fate decision of undifferentiated spermatogonia by GDNF. Science 2000 287 1489 93.
    • (2000) Science , vol.287 , pp. 1489-93
    • Meng, X.1    Lindahl, M.2    Hyvönen, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.