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Volumn 7, Issue 2, 2013, Pages 91-99

Preparation of pro-oncogenic mutant forms V659E and V659Q of the transmembrane domain of receptor protein kinase ErbB2 for structural studies

Author keywords

NMR spectroscopy; receptor tyrosine kinases; recombinant protein; transmembrane domain

Indexed keywords

CARBON 13; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GLUTAMIC ACID; GLUTAMINE; HYBRID PROTEIN; NITROGEN 15; RECOMBINANT ENZYME; THIOREDOXIN; THROMBIN; VALINE;

EID: 84879393678     PISSN: 19907478     EISSN: 19907494     Source Type: Journal    
DOI: 10.1134/S1990747813010029     Document Type: Article
Times cited : (1)

References (27)
  • 1
    • 0035256698 scopus 로고    scopus 로고
    • Untangling the ErbB signalling network
    • 11252954 10.1038/35052073 1:CAS:528:DC%2BD3MXivVWnt7k%3D
    • Yarden Y., Sliwkowski M.X. 2001. Untangling the ErbB signalling network. Nat. Rev. Mol. Cell Biol. 2, 127-137.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 127-137
    • Yarden, Y.1    Sliwkowski, M.X.2
  • 2
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • 11057895 10.1016/S0092-8674(00)00114-8 1:CAS:528:DC%2BD3cXns1Cltrs%3D
    • Schlessinger J. 2000. Cell signaling by receptor tyrosine kinases. Cell. 103, 211-225.
    • (2000) Cell. , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 3
    • 0034464005 scopus 로고    scopus 로고
    • The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: The achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans
    • 10696568 10.1210/er.21.1.23 1:CAS:528:DC%2BD3cXhs12hurc%3D
    • Vajo Z., Francomano C.A., Wilkin D.J. 2000. The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: The achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans. Endocr. Rev. 21, 23-39.
    • (2000) Endocr. Rev. , vol.21 , pp. 23-39
    • Vajo, Z.1    Francomano, C.A.2    Wilkin, D.J.3
  • 4
    • 0032774475 scopus 로고    scopus 로고
    • Clinical spectrum of fibroblast growth factor receptor mutations
    • 10425034 10.1002/(SICI)1098-1004(1999)14:2<115: AID-HUMU3>3.0.CO;2- 2 1:CAS:528:DyaK1MXltlejtrY%3D
    • Passos-Bueno M.R., Wilcox W.R., Jabs E.W., Sertie A.L., Alonso L.G., Kitoh H. 1999. Clinical spectrum of fibroblast growth factor receptor mutations. Hum. Mutat. 14, 115-125.
    • (1999) Hum. Mutat. , vol.14 , pp. 115-125
    • Passos-Bueno, M.R.1    Wilcox, W.R.2    Jabs, E.W.3    Sertie, A.L.4    Alonso, L.G.5    Kitoh, H.6
  • 6
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • 12297041 10.1016/S0092-8674(02)00966-2 1:CAS:528:DC%2BD38XnsFKis7w%3D
    • Schlessinger J. 2002. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell. 110, 669-672.
    • (2002) Cell. , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 7
    • 55449102296 scopus 로고    scopus 로고
    • All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells
    • 18782861 10.1242/jcs.033399 1:CAS:528:DC%2BD1cXhtlGltrnN
    • Tao R.H., Maruyama I.N. 2008. All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells. J. Cell. Sci. 121, 3207-3217.
    • (2008) J. Cell. Sci. , vol.121 , pp. 3207-3217
    • Tao, R.H.1    Maruyama, I.N.2
  • 8
    • 0037429725 scopus 로고    scopus 로고
    • The ErbB receptors and their role in cancer progression
    • 12648469 10.1016/S0014-4827(02)00099-X 1:CAS:528:DC%2BD3sXitVylt7o%3D
    • Holbro T., Civenni G., Hynes N.E. 2003. The ErbB receptors and their role in cancer progression. Exp. Cell Res. 284, 99-110.
    • (2003) Exp. Cell Res. , vol.284 , pp. 99-110
    • Holbro, T.1    Civenni, G.2    Hynes, N.E.3
  • 9
    • 0033063774 scopus 로고    scopus 로고
    • The epidermal growth factor receptor and its inhibition in cancer therapy
    • 10454201 10.1016/S0163-7258(98)00045-X 1:CAS:528:DyaK1MXjvFOhtLw%3D
    • Woodburn J.R. 1999. The epidermal growth factor receptor and its inhibition in cancer therapy. Pharmacol. Ther. 82, 241-250.
    • (1999) Pharmacol. Ther. , vol.82 , pp. 241-250
    • Woodburn, J.R.1
  • 10
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • 10880430 10.1093/emboj/19.13.3159 1:CAS:528:DC%2BD3cXlt1ajtLY%3D
    • Olayioye M.A., Neve R.M., Lane H.A., Hynes N.E. 2000. The ErbB signaling network: Receptor heterodimerization in development and cancer. EMBO J. 19, 3159-3167.
    • (2000) EMBO J. , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 11
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • 2871941 10.1016/0092-8674(86)90779-8 1:CAS:528:DyaL28XksFGmtL8%3D
    • Bargmann C.I., Hung M.-C., Weinberg R.A. 1986. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell. 45, 649-657.
    • (1986) Cell. , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.-C.2    Weinberg, R.A.3
  • 12
    • 0034163421 scopus 로고    scopus 로고
    • Population-based, case-control study of HER2 genetic polymorphism and breast cancer risk
    • 10699071 10.1093/jnci/92.5.412 1:CAS:528:DC%2BD3cXhvFGhu70%3D
    • Xie D., Shu X.O., Deng Z., Wen W.Q., Creek K.E., Dai Q., Gao Y.T., Jin F., Zheng W. 2000. Population-based, case-control study of HER2 genetic polymorphism and breast cancer risk. J. Nat. Cancer Inst. 92, 412-417.
    • (2000) J. Nat. Cancer Inst. , vol.92 , pp. 412-417
    • Xie, D.1    Shu, X.O.2    Deng, Z.3    Wen, W.Q.4    Creek, K.E.5    Dai, Q.6    Gao, Y.T.7    Jin, F.8    Zheng, W.9
  • 14
    • 33847118661 scopus 로고    scopus 로고
    • A dimerization hierarchy in the transmembrane domains of the HER receptor family
    • 17253768 10.1021/bi061436f 1:CAS:528:DC%2BD2sXot1Wqsw%3D%3D
    • Duneau J.P., Vegh A.P., Sturgis J.N. A dimerization hierarchy in the transmembrane domains of the HER receptor family. 2007. Biochemistry. 46, 2010-2019.
    • (2007) Biochemistry. , vol.46 , pp. 2010-2019
    • Duneau, J.P.1    Vegh, A.P.2    Sturgis, J.N.3
  • 15
    • 33646889068 scopus 로고    scopus 로고
    • Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies
    • 16700535 10.1021/bi060609y 1:CAS:528:DC%2BD28XktVSksrs%3D
    • Li E., Hristova K. 2006. Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Biochemistry. 45, 6241-6251.
    • (2006) Biochemistry. , vol.45 , pp. 6241-6251
    • Li, E.1    Hristova, K.2
  • 16
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • 11741943 10.1074/jbc.M108681200 1:CAS:528:DC%2BD38XhsFeqt78%3D
    • Mendrola J.M., Berger M.B., King M.C., Lemmon M.A. 2002. The single transmembrane domains of ErbB receptors self-associate in cell membranes. J. Biol. Chem. 277, 4704-4712.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 17
    • 33846688205 scopus 로고    scopus 로고
    • Prediction and simulation of motion in pairs of transmembrane alpha-helices
    • 10.1093/bioinformatics/btl325
    • Enosh A., Fleishman S.J., Ben-Tal N., Halperin D. 2007. Prediction and simulation of motion in pairs of transmembrane alpha-helices. Bioinformatics. 23, 212-218.
    • (2007) Bioinformatics. , vol.23 , pp. 212-218
    • Enosh, A.1    Fleishman, S.J.2    Ben-Tal, N.3    Halperin, D.4
  • 18
    • 0037199467 scopus 로고    scopus 로고
    • Transmembrane interactions in the activation of the Neu receptor tyrosine kinase
    • 12135353 10.1021/bi012117l 1:CAS:528:DC%2BD38XkvFClsbw%3D
    • Smith S.O., Smith C., Shekar S., Peersen O., Ziliox M., Aimoto S. 2002. Transmembrane interactions in the activation of the Neu receptor tyrosine kinase. Biochemistry. 41, 9321-9332.
    • (2002) Biochemistry. , vol.41 , pp. 9321-9332
    • Smith, S.O.1    Smith, C.2    Shekar, S.3    Peersen, O.4    Ziliox, M.5    Aimoto, S.6
  • 19
    • 18744378545 scopus 로고    scopus 로고
    • A putative molecular-activation switch in the transmembrane domain of ErbB2
    • 12461170 10.1073/pnas.252640799 1:CAS:528:DC%2BD38Xps1egurk%3D
    • Fleishman S.J., Schlessinger J., Ben-Tal N. 2002. A putative molecular-activation switch in the transmembrane domain of ErbB2. Proc. Natl. Acad. Sci. USA. 99, 15937-15940.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 15937-15940
    • Fleishman, S.J.1    Schlessinger, J.2    Ben-Tal, N.3
  • 20
    • 43749091771 scopus 로고    scopus 로고
    • Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state
    • 18178548 10.1074/jbc.M709202200 1:CAS:528:DC%2BD1cXivFyjt7c%3D
    • Bocharov E.V., Mineev K.S., Volynsky P.E., Ermolyuk Ya.S., Tkach E.N., Sobol A.G., Chupin V.V., Kirpichnikov M.P., Efremov R.G., Arseniev A.S. 2008. Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state. J. Biol. Chem. 283, 6950-6956.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6950-6956
    • Bocharov, E.V.1    Mineev, K.S.2    Volynsky, P.E.3    Ermolyuk, Y.4    Tkach, E.N.5    Sobol, A.G.6    Chupin, V.V.7    Kirpichnikov, M.P.8    Efremov, R.G.9    Arseniev, A.S.10
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680-685.
    • (1970) Nature. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 77953810629 scopus 로고    scopus 로고
    • Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases
    • 20471394 10.1016/j.jmb.2010.05.016 1:CAS:528:DC%2BC3cXntlaju7o%3D
    • Mineev K.S., Bocharov E.V., Pustovalova Y.E., Bocharova O.V., Chupin V.V., Arseniev A.S. 2010. Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases. J. Mol. Biol. 400, 231-243.
    • (2010) J. Mol. Biol. , vol.400 , pp. 231-243
    • Mineev, K.S.1    Bocharov, E.V.2    Pustovalova, Y.E.3    Bocharova, O.V.4    Chupin, V.V.5    Arseniev, A.S.6
  • 25
    • 57649221018 scopus 로고    scopus 로고
    • Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1
    • 18728013 10.1074/jbc.M803089200 1:CAS:528:DC%2BD1cXht1GlsbvM
    • Bocharov E.V., Mayzel M.L., Volynsky P.E., Goncharuk M.V., Ermolyuk Ya.S., Schulga A.A., Artemenko E.O., Efremov R.G., Arseniev A.S. 2008. Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1. J. Biol. Chem. 283, 29385-29395.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29385-29395
    • Bocharov, E.V.1    Mayzel, M.L.2    Volynsky, P.E.3    Goncharuk, M.V.4    Ermolyuk, Y.5    Schulga, A.A.6    Artemenko, E.O.7    Efremov, R.G.8    Arseniev, A.S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.