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Volumn 2013, Issue 2, 2013, Pages

Structural analysis of autoinhibition in the Ras-specific exchange factor RasGRP1

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; DIACYLGLYCEROL; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; PROTEIN RASGRP1; PROTEIN TYROSINE PHOSPHATASE; RAS PROTEIN; UNCLASSIFIED DRUG; CALCIUM; DNA BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RASGRP1 PROTEIN, HUMAN; RECOMBINANT PROTEIN;

EID: 84881045879     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.00813     Document Type: Article
Times cited : (67)

References (105)
  • 2
    • 84255195028 scopus 로고    scopus 로고
    • Regulating the regulator: Post-translational modification of RAS
    • doi: 10.1038/nrm3255
    • Ahearn IM, Haigis K, Bar-Sagi D, Philips MR. 2012. Regulating the regulator: post-translational modification of RAS. Nat Rev Mol Cell Biol 13:39-51. doi: 10.1038/nrm3255.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 39-51
    • Ahearn, I.M.1    Haigis, K.2    Bar-Sagi, D.3    Philips, M.R.4
  • 3
    • 0344773502 scopus 로고    scopus 로고
    • Fluorescence methods in the study of small GTP-binding proteins
    • doi: 10.1385/1-59259-281-3:045
    • Ahmadian MR, Wittinghofer A, Herrmann C. 2002. Fluorescence methods in the study of small GTP-binding proteins. Methods Mol Biol 189:45-63. doi: 10.1385/1-59259-281-3:045.
    • (2002) Methods Mol Biol , vol.189 , pp. 45-63
    • Ahmadian, M.R.1    Wittinghofer, A.2    Herrmann, C.3
  • 4
    • 9344264018 scopus 로고    scopus 로고
    • Activation of RasGRP3 by phosphorylation of Thr-133 is required for B cell receptor-mediated Ras activation
    • doi: 10.1073/pnas.0407468101
    • Aiba Y, Oh-hora M, Kiyonaka S, Kimura Y, Hijikata A, Mori Y, et al. 2004. Activation of RasGRP3 by phosphorylation of Thr-133 is required for B cell receptor-mediated Ras activation. Proc Natl Acad Sci USA 101:16612-7. doi: 10.1073/pnas.0407468101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16612-16617
    • Aiba, Y.1    Oh-Hora, M.2    Kiyonaka, S.3    Kimura, Y.4    Hijikata, A.5    Mori, Y.6
  • 6
    • 0033516487 scopus 로고    scopus 로고
    • Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases
    • doi: 10.1074/jbc.274.27.19329
    • Ames JB, Dizhoor AM, Ikura M, Palczewski K, Stryer L. 1999. Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases. J Biol Chem 274:19329-37. doi: 10.1074/jbc.274.27.19329.
    • (1999) J Biol Chem , vol.274 , pp. 19329-19337
    • Ames, J.B.1    Dizhoor, A.M.2    Ikura, M.3    Palczewski, K.4    Stryer, L.5
  • 7
    • 39049105983 scopus 로고    scopus 로고
    • Regulatory and structural EF-hand motifs of neuronal calcium sensor-1: Mg 2+ modulates Ca 2+ binding, Ca 2+ -induced conformational changes, and equilibrium unfolding transitions
    • doi: 10.1016/j.jmb.2007.12.033
    • Aravind P, Chandra K, Reddy PP, Jeromin A, Chary KV, Sharma Y. 2008. Regulatory and structural EF-hand motifs of neuronal calcium sensor-1: mg 2+ modulates Ca 2+ binding, Ca 2+ -induced conformational changes, and equilibrium unfolding transitions. J Mol Biol 376:1100-15. doi: 10.1016/j.jmb.2007.12.033.
    • (2008) J Mol Biol , vol.376 , pp. 1100-1115
    • Aravind, P.1    Chandra, K.2    Reddy, P.P.3    Jeromin, A.4    Chary, K.V.5    Sharma, Y.6
  • 8
    • 0027931640 scopus 로고
    • Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
    • doi: 10.1016/0092-8674(94)90271-2
    • Aronheim A, Engelberg D, Li N, al-Alawi N, Schlessinger J, Karin M. 1994. Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway. Cell 78:949-61. doi: 10.1016/0092-8674(94)90271-2.
    • (1994) Cell , vol.78 , pp. 949-961
    • Aronheim, A.1    Engelberg, D.2    Li, N.3    Al-Alawi, N.4    Schlessinger, J.5    Karin, M.6
  • 9
    • 34547739994 scopus 로고    scopus 로고
    • Regulation of RasGRP1 by B cell antigen receptor requires cooperativity between three domains controlling translocation to the plasma membrane
    • doi: 10.1091/mbc.E06-10-0932
    • Beaulieu N, Zahedi B, Goulding RE, Tazmini G, Anthony KV, Omeis SL, et al. 2007. Regulation of RasGRP1 by B cell antigen receptor requires cooperativity between three domains controlling translocation to the plasma membrane. Mol Biol Cell. 18:3156-68. doi: 10.1091/mbc.E06-10-0932.
    • (2007) Mol Biol Cell , vol.18 , pp. 3156-3168
    • Beaulieu, N.1    Zahedi, B.2    Goulding, R.E.3    Tazmini, G.4    Anthony, K.V.5    Omeis, S.L.6
  • 10
    • 33747831881 scopus 로고    scopus 로고
    • PREDITOR: A web server for predicting protein torsion angle restraints
    • doi: 10.1093/nar/gkl341
    • Berjanskii MV, Neal S, Wishart DS. 2006. PREDITOR: a web server for predicting protein torsion angle restraints. Nucleic Acids Res 34:W63-69. doi: 10.1093/nar/gkl341.
    • (2006) Nucleic Acids Res , vol.34
    • Berjanskii, M.V.1    Neal, S.2    Wishart, D.S.3
  • 11
    • 33847079676 scopus 로고    scopus 로고
    • Evaluating protein structures determined by structural genomics consortia
    • doi: 10.1002/prot.21165
    • Bhattacharya A, Tejero R, Montelione GT. 2007. Evaluating protein structures determined by structural genomics consortia. Proteins 66:778-95. doi: 10.1002/prot.21165.
    • (2007) Proteins , vol.66 , pp. 778-795
    • Bhattacharya, A.1    Tejero, R.2    Montelione, G.T.3
  • 12
    • 0032560850 scopus 로고    scopus 로고
    • The structural basis of the activation of Ras by Sos
    • doi: 10.1038/28548
    • Boriack-Sjodin PA, Margarit SM, Bar-Sagi D, Kuriyan J. 1998. The structural basis of the activation of Ras by Sos. Nature 394:337-43. doi: 10.1038/28548.
    • (1998) Nature , vol.394 , pp. 337-343
    • Boriack-Sjodin, P.A.1    Margarit, S.M.2    Bar-Sagi, D.3    Kuriyan, J.4
  • 13
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • doi: 10.1016/j.cell.2007.05.018
    • Bos JL, Rehmann H, Wittinghofer A. 2007. GEFs and GAPs: critical elements in the control of small G proteins. Cell 129:865-77. doi: 10.1016/j.cell.2007.05.018.
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 14
    • 33751102674 scopus 로고    scopus 로고
    • Regulation of ras signaling dynamics by Sos-mediated positive feedback
    • doi: 10.1016/j.cub.2006.09.033
    • Boykevisch S, Zhao C, Sondermann H, Philippidou P, Halegoua S, Kuriyan J, et al. 2006. Regulation of ras signaling dynamics by Sos-mediated positive feedback. Current biology 16:2173-9. doi: 10.1016/j.cub.2006.09.033.
    • (2006) Current Biology , vol.16 , pp. 2173-2179
    • Boykevisch, S.1    Zhao, C.2    Sondermann, H.3    Philippidou, P.4    Halegoua, S.5    Kuriyan, J.6
  • 15
    • 3042630992 scopus 로고    scopus 로고
    • PKCdelta associates with and is involved in the phosphorylation of RasGRP3 in response to phorbol esters
    • doi: 10.1124/mol.66.1.76
    • Brodie C, Steinhart R, Kazimirsky G, Rubinfeld H, Hyman T, Ayres JN, et al. 2004. PKCdelta associates with and is involved in the phosphorylation of RasGRP3 in response to phorbol esters. Mol Pharmacol 66:76-84. doi: 10.1124/mol.66.1.76.
    • (2004) Mol Pharmacol , vol.66 , pp. 76-84
    • Brodie, C.1    Steinhart, R.2    Kazimirsky, G.3    Rubinfeld, H.4    Hyman, T.5    Ayres, J.N.6
  • 16
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • doi: 10.1038/nprot.2007.406
    • Brunger AT. 2007. Version 1.2 of the crystallography and NMR system. Nat Protoc 2:2728-33. doi: 10.1038/nprot.2007.406.
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 17
    • 7044223022 scopus 로고    scopus 로고
    • Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin
    • doi: 10.1016/j.cell.2004.10.012
    • Canagarajah B, Leskow FC, Ho JY, Mischak H, Saidi LF, Kazanietz MG, et al. 2004. Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin. Cell 119:407-18. doi: 10.1016/j.cell.2004.10.012.
    • (2004) Cell , vol.119 , pp. 407-418
    • Canagarajah, B.1    Leskow, F.C.2    Ho, J.Y.3    Mischak, H.4    Saidi, L.F.5    Kazanietz, M.G.6
  • 18
    • 84874433733 scopus 로고    scopus 로고
    • Regulation of small GTPases by GEFs, GAPs, and GDIs
    • doi: 10.1152/physrev.00003.2012
    • Cherfils J, Zeghouf M. 2013. Regulation of small GTPases by GEFs, GAPs, and GDIs. Physiol Rev 93:269-309. doi: 10.1152/physrev.00003.2012.
    • (2013) Physiol Rev , vol.93 , pp. 269-309
    • Cherfils, J.1    Zeghouf, M.2
  • 19
    • 0032113480 scopus 로고    scopus 로고
    • A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
    • doi: 10.1006/jmre.1998.1419
    • Clore GM, Gronenborn AM, Bax A. 1998. A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J Magn Reson 133:216-21. doi: 10.1006/jmre.1998.1419.
    • (1998) J Magn Reson , vol.133 , pp. 216-221
    • Clore, G.M.1    Gronenborn, A.M.2    Bax, A.3
  • 20
    • 28244476478 scopus 로고    scopus 로고
    • RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling
    • Coughlin JJ, Stang SL, Dower NA, Stone JC. 2005. RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling. J Immunol 175:7179-84.
    • (2005) J Immunol , vol.175 , pp. 7179-7184
    • Coughlin, J.J.1    Stang, S.L.2    Dower, N.A.3    Stone, J.C.4
  • 21
    • 33845607123 scopus 로고    scopus 로고
    • Thymic selection threshold defined by compartmentalization of Ras/MAPK signalling
    • doi: 10.1038/nature05269
    • Daniels MA, Teixeiro E, Gill J, Hausmann B, Roubaty D, Holmberg K, et al. 2006. Thymic selection threshold defined by compartmentalization of Ras/MAPK signalling. Nature 444:724-9. doi: 10.1038/nature05269.
    • (2006) Nature , vol.444 , pp. 724-729
    • Daniels, M.A.1    Teixeiro, E.2    Gill, J.3    Hausmann, B.4    Roubaty, D.5    Holmberg, K.6
  • 22
    • 58249092059 scopus 로고    scopus 로고
    • Digital signaling and hysteresis characterize ras activation in lymphoid cells
    • doi: 10.1016/j.cell.2008.11.051
    • Das J, Ho M, Zikherman J, Govern C, Yang M, Weiss A, et al. 2009. Digital signaling and hysteresis characterize ras activation in lymphoid cells. Cell 136:337-51. doi: 10.1016/j.cell.2008.11.051.
    • (2009) Cell , vol.136 , pp. 337-351
    • Das, J.1    Ho, M.2    Zikherman, J.3    Govern, C.4    Yang, M.5    Weiss, A.6
  • 23
    • 0034604366 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor
    • doi: 10.1006/jmbi.2000.3895
    • Day CL, Alber T. 2000. Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor. J Mol Biol 301:147-56. doi: 10.1006/jmbi.2000.3895.
    • (2000) J Mol Biol , vol.301 , pp. 147-156
    • Day, C.L.1    Alber, T.2
  • 24
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • doi: 10.1007/BF00197809
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. 1995. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-93. doi: 10.1007/BF00197809.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 25
    • 67649981422 scopus 로고    scopus 로고
    • RasGRP1 transgenic mice develop cutaneous squamous cell carcinomas in response to skin wounding: Potential role of granulocyte colony-stimulating factor
    • doi: 10.2353/ajpath.2009.090036
    • Diez FR, Garrido AA, Sharma A, Luke CT, Stone JC, Dower NA, et al. 2009. RasGRP1 transgenic mice develop cutaneous squamous cell carcinomas in response to skin wounding: potential role of granulocyte colony-stimulating factor. Am J Pathol 175:392-9. doi: 10.2353/ajpath.2009.090036.
    • (2009) Am J Pathol , vol.175 , pp. 392-399
    • Diez, F.R.1    Garrido, A.A.2    Sharma, A.3    Luke, C.T.4    Stone, J.C.5    Dower, N.A.6
  • 26
    • 36249015526 scopus 로고    scopus 로고
    • Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors
    • doi: 10.1016/j.molcel.2007.09.017
    • DiNitto JP, Delprato A, Gabe Lee MT, Cronin TC, Huang S, Guilherme A, et al. 2007. Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors. Mol Cell 28:569-83. doi: 10.1016/j.molcel.2007.09.017.
    • (2007) Mol Cell , vol.28 , pp. 569-583
    • Dinitto, J.P.1    Delprato, A.2    Gabe, L.M.T.3    Cronin, T.C.4    Huang, S.5    Guilherme, A.6
  • 27
    • 0034303371 scopus 로고    scopus 로고
    • RasGRP is essential for mouse thymocyte differentiation and TCR signaling
    • doi: 10.1038/79766
    • Dower NA, Stang SL, Bottorff DA, Ebinu JO, Dickie P, Ostergaard HL, et al. 2000. RasGRP is essential for mouse thymocyte differentiation and TCR signaling. Nat Immunol 1:317-21. doi: 10.1038/79766.
    • (2000) Nat Immunol , vol.1 , pp. 317-321
    • Dower, N.A.1    Stang, S.L.2    Bottorff, D.A.3    Ebinu, J.O.4    Dickie, P.5    Ostergaard, H.L.6
  • 28
    • 0032524389 scopus 로고    scopus 로고
    • RasGRP, a Ras guanyl nucleotidereleasing protein with calcium- and diacylglycerol-binding motifs
    • doi: 10.1126/science.280.5366.1082
    • Ebinu JO, Bottorff DA, Chan EY, Stang SL, Dunn RJ, Stone JC. 1998. RasGRP, a Ras guanyl nucleotidereleasing protein with calcium- and diacylglycerol-binding motifs. Science 280:1082-6. doi: 10.1126/science.280.5366.1082.
    • (1998) Science , vol.280 , pp. 1082-1086
    • Ebinu, J.O.1    Bottorff, D.A.2    Chan, E.Y.3    Stang, S.L.4    Dunn, R.J.5    Stone, J.C.6
  • 30
    • 84874787934 scopus 로고    scopus 로고
    • Interaction domains of sos1/grb2 are finely tuned for cooperative control of embryonic stem cell fate
    • doi: 10.1016/j.cell.2013.01.056
    • Findlay GM, Smith MJ, Lanner F, Hsiung MS, Gish GD, Petsalaki E, et al. 2013. Interaction domains of sos1/grb2 are finely tuned for cooperative control of embryonic stem cell fate. Cell 152:1008-20. doi: 10.1016/j.cell.2013.01.056.
    • (2013) Cell , vol.152 , pp. 1008-1020
    • Findlay, G.M.1    Smith, M.J.2    Lanner, F.3    Hsiung, M.S.4    Gish, G.D.5    Petsalaki, E.6
  • 32
    • 84862231986 scopus 로고    scopus 로고
    • Regulation of RasGRP1 function in T cell development and activation by its unique tail domain
    • doi: 10.1371/journal.pone.0038796
    • Fuller DM, Zhu M, Song X, Ou-Yang CW, Sullivan SA, Stone JC, et al. 2012. Regulation of RasGRP1 function in T cell development and activation by its unique tail domain. PloS One 7:e38796. doi: 10.1371/journal.pone.0038796.
    • (2012) PloS One , vol.7
    • Fuller, D.M.1    Zhu, M.2    Song, X.3    Ou-Yang, C.W.4    Sullivan, S.A.5    Stone, J.C.6
  • 33
    • 34447130835 scopus 로고    scopus 로고
    • Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs
    • doi: 10.1042/BJ20070255
    • Gifford JL, Walsh MP, Vogel HJ. 2007. Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs. Biochem J 405:199-221. doi: 10.1042/BJ20070255.
    • (2007) Biochem J , vol.405 , pp. 199-221
    • Gifford, J.L.1    Walsh, M.P.2    Vogel, H.J.3
  • 34
    • 84872021840 scopus 로고    scopus 로고
    • RasGRP1, but not RasGRP3, is required for efficient thymic beta-selection and ERK activation downstream of CXCR4
    • doi: 10.1371/journal.pone.0053300
    • Golec DP, Dower NA, Stone JC, Baldwin TA. 2013. RasGRP1, but not RasGRP3, is required for efficient thymic beta-selection and ERK activation downstream of CXCR4. PloS One 8:e53300. doi: 10.1371/journal.pone.0053300.
    • (2013) PloS One , vol.8
    • Golec, D.P.1    Dower, N.A.2    Stone, J.C.3    Baldwin, T.A.4
  • 35
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization
    • doi: 10.1006/jmrb.1993.1019
    • Grzesiek S, Anglister J, Bax A. 1993. Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. J Magn Reson B 101:114-9. doi: 10.1006/jmrb.1993.1019.
    • (1993) J Magn Reson B , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 36
    • 2342558003 scopus 로고    scopus 로고
    • Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND
    • doi: 10.1023/A:1008391403193
    • Guntert P, Billeter M, Ohlenschlager O, Brown LR, Wuthrich K. 1998. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND. J Biomol NMR 12:543-8. doi: 10.1023/A:1008391403193.
    • (1998) J Biomol NMR , vol.12 , pp. 543-548
    • Guntert, P.1    Billeter, M.2    Ohlenschlager, O.3    Brown, L.R.4    Wuthrich, K.5
  • 38
    • 77649241353 scopus 로고    scopus 로고
    • Role of the histone domain in the autoinhibition and activation of the Ras activator Son of Sevenless
    • doi: 10.1073/pnas.0913915107
    • Gureasko J, Kuchment O, Makino DL, Sondermann H, Bar-Sagi D, Kuriyan J. 2010. Role of the histone domain in the autoinhibition and activation of the Ras activator Son of Sevenless. Proc Natl Acad Sci USA 107:3430-5. doi: 10.1073/pnas.0913915107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3430-3435
    • Gureasko, J.1    Kuchment, O.2    Makino, D.L.3    Sondermann, H.4    Bar-Sagi, D.5    Kuriyan, J.6
  • 39
    • 0035920116 scopus 로고    scopus 로고
    • Structure-based mutagenesis reveals distinct functions for Ras switch 1 and switch 2 in Sos-catalyzed guanine nucleotide exchange
    • doi: 10.1074/jbc.M101727200
    • Hall BE, Yang SS, Boriack-Sjodin PA, Kuriyan J, Bar-Sagi D. 2001. Structure-based mutagenesis reveals distinct functions for Ras switch 1 and switch 2 in Sos-catalyzed guanine nucleotide exchange. J Biol Chem 276:27629-37. doi: 10.1074/jbc.M101727200.
    • (2001) J Biol Chem , vol.276 , pp. 27629-27637
    • Hall, B.E.1    Yang, S.S.2    Boriack-Sjodin, P.A.3    Kuriyan, J.4    Bar-Sagi, D.5
  • 40
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • doi: 10.1038/4176
    • Hansen MR, Mueller L, Pardi A. 1998. Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions. Nat Struct Biol 5:1065-74. doi: 10.1038/4176.
    • (1998) Nat Struct Biol , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 41
    • 84875736558 scopus 로고    scopus 로고
    • Dysregulated RasGRP1 responds to cytokine receptor input in T cell leukemogenesis
    • doi: 10.1126/scisignal.2003848
    • Hartzell C, Ksionda O, Lemmens E, Coakley K, Yang M, Dail M, et al. 2013. Dysregulated RasGRP1 responds to cytokine receptor input in T cell leukemogenesis. Sci Signal 6:ra21. doi: 10.1126/scisignal.2003848.
    • (2013) Sci Signal , vol.6 , pp. 21
    • Hartzell, C.1    Ksionda, O.2    Lemmens, E.3    Coakley, K.4    Yang, M.5    Dail, M.6
  • 42
    • 0031050299 scopus 로고    scopus 로고
    • Taxonomy and function of C1 protein kinase C homology domains
    • doi: 10.1002/pro.5560060228
    • Hurley JH, Newton AC, Parker PJ, Blumberg PM, Nishizuka Y. 1997. Taxonomy and function of C1 protein kinase C homology domains. Protein Sci 6:477-80. doi: 10.1002/pro.5560060228.
    • (1997) Protein Sci , vol.6 , pp. 477-480
    • Hurley, J.H.1    Newton, A.C.2    Parker, P.J.3    Blumberg, P.M.4    Nishizuka, Y.5
  • 43
    • 0021948138 scopus 로고
    • Hydrogen bonding in the carboxyl-terminal half-fragment 78-148 of calmodulin as studied by two-dimensional nuclear magnetic resonance
    • doi: 10.1021/bi00337a002
    • Ikura M, Minowa O, Hikichi K. 1985. Hydrogen bonding in the carboxyl-terminal half-fragment 78-148 of calmodulin as studied by two-dimensional nuclear magnetic resonance. Biochemistry 24:4264-9. doi: 10.1021/bi00337a002.
    • (1985) Biochemistry , vol.24 , pp. 4264-4269
    • Ikura, M.1    Minowa, O.2    Hikichi, K.3
  • 45
    • 84859396347 scopus 로고    scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. 1990
    • doi: 10.1016/j.jmr.2011.09.004
    • Kay LE, Ikura M, Tschudin R, Bax A. 2011. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. 1990. J Magn Reson 213:423-41. doi: 10.1016/j.jmr.2011.09.004.
    • (2011) J Magn Reson , vol.213 , pp. 423-441
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 46
    • 17844375168 scopus 로고    scopus 로고
    • Deregulated expression of RasGRP1 initiates thymic lymphomagenesis independently of T-cell receptors
    • doi: 10.1038/sj.onc.1208334
    • Klinger MB, Guilbault B, Goulding RE, Kay RJ. 2005. Deregulated expression of RasGRP1 initiates thymic lymphomagenesis independently of T-cell receptors. Oncogene 24:2695-704. doi: 10.1038/sj.onc.1208334.
    • (2005) Oncogene , vol.24 , pp. 2695-2704
    • Klinger, M.B.1    Guilbault, B.2    Goulding, R.E.3    Kay, R.J.4
  • 47
    • 79961097285 scopus 로고    scopus 로고
    • Targeted Sos1 deletion reveals its critical role in early T-cell development
    • doi: 10.1073/pnas.1104295108
    • Kortum RL, Sommers CL, Alexander CP, Pinski JM, Li W, Grinberg A, et al. 2011. Targeted Sos1 deletion reveals its critical role in early T-cell development. Proc Natl Acad Sci USA 108:12407-12. doi: 10.1073/pnas.1104295108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 12407-12412
    • Kortum, R.L.1    Sommers, C.L.2    Alexander, C.P.3    Pinski, J.M.4    Li, W.5    Grinberg, A.6
  • 49
    • 33646029128 scopus 로고    scopus 로고
    • Fluorescent cell barcoding in flow cytometry allows high-throughput drug screening and signaling profiling
    • doi: 10.1038/nmeth872
    • Krutzik PO, Nolan GP. 2006. Fluorescent cell barcoding in flow cytometry allows high-throughput drug screening and signaling profiling. Nat Methods 3:361-8. doi: 10.1038/nmeth872.
    • (2006) Nat Methods , vol.3 , pp. 361-368
    • Krutzik, P.O.1    Nolan, G.P.2
  • 50
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • doi: 10.1007/BF00228148
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. 1996. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8:477-86. doi: 10.1007/BF00228148.
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 51
    • 70349273655 scopus 로고    scopus 로고
    • Response and resistance to MEK inhibition in leukaemias initiated by hyperactive Ras
    • doi: 10.1038/nature08279
    • Lauchle JO, Kim D, Le DT, Akagi K, Crone M, Krisman K, et al. 2009. Response and resistance to MEK inhibition in leukaemias initiated by hyperactive Ras. Nature 461:411-4. doi: 10.1038/nature08279.
    • (2009) Nature , vol.461 , pp. 411-414
    • Lauchle, J.O.1    Kim, D.2    Le, D.T.3    Akagi, K.4    Crone, M.5    Krisman, K.6
  • 52
    • 0042432047 scopus 로고    scopus 로고
    • Autoimmunity as the consequence of a spontaneous mutation in Rasgrp1
    • doi: 10.1016/S1074-7613(03)00209-7
    • Layer K, Lin G, Nencioni A, Hu W, Schmucker A, Antov AN, et al. 2003. Autoimmunity as the consequence of a spontaneous mutation in Rasgrp1. Immunity 19:243-55. doi: 10.1016/S1074-7613(03)00209-7.
    • (2003) Immunity , vol.19 , pp. 243-255
    • Layer, K.1    Lin, G.2    Nencioni, A.3    Hu, W.4    Schmucker, A.5    Antov, A.N.6
  • 54
    • 78650942010 scopus 로고    scopus 로고
    • Crystal structure and allosteric activation of protein kinase C betaII
    • doi: 10.1016/j.cell.2010.12.013
    • Leonard TA, Rozycki B, Saidi LF, Hummer G, Hurley JH. 2011. Crystal structure and allosteric activation of protein kinase C betaII. Cell 144:55-66. doi: 10.1016/j.cell.2010.12.013.
    • (2011) Cell , vol.144 , pp. 55-66
    • Leonard, T.A.1    Rozycki, B.2    Saidi, L.F.3    Hummer, G.4    Hurley, J.H.5
  • 55
    • 79955004049 scopus 로고    scopus 로고
    • STIM1, PKC-δ and RasGRP set a threshold for proapoptotic Erk signaling during B cell development
    • doi: 10.1038/ni.2016
    • Limnander A, Depeille P, Freedman TS, Liou J, Leitges M, Kurosaki T, et al. 2011. STIM1, PKC-δ and RasGRP set a threshold for proapoptotic Erk signaling during B cell development. Nat Immunol 12:425-33. doi: 10.1038/ni.2016.
    • (2011) Nat Immunol , vol.12 , pp. 425-433
    • Limnander, A.1    Depeille, P.2    Freedman, T.S.3    Liou, J.4    Leitges, M.5    Kurosaki, T.6
  • 56
    • 0034061660 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor RasGRP is a high-affinity target for diacylglycerol and phorbol esters
    • Lorenzo PS, Beheshti M, Pettit GR, Stone JC, Blumberg PM. 2000. The guanine nucleotide exchange factor RasGRP is a high-affinity target for diacylglycerol and phorbol esters. Mol Pharmacol 57:840-6.
    • (2000) Mol Pharmacol , vol.57 , pp. 840-846
    • Lorenzo, P.S.1    Beheshti, M.2    Pettit, G.R.3    Stone, J.C.4    Blumberg, P.M.5
  • 57
    • 35949004382 scopus 로고    scopus 로고
    • RasGRP1 overexpression in the epidermis of transgenic mice contributes to tumor progression during multistage skin carcinogenesis
    • doi: 10.1158/0008-5472.CAN-07-2375
    • Luke CT, Oki-Idouchi CE, Cline JM, Lorenzo PS. 2007. RasGRP1 overexpression in the epidermis of transgenic mice contributes to tumor progression during multistage skin carcinogenesis. Cancer Res 67:10190-7. doi: 10.1158/0008-5472.CAN-07-2375.
    • (2007) Cancer Res , vol.67 , pp. 10190-10197
    • Luke, C.T.1    Oki-Idouchi, C.E.2    Cline, J.M.3    Lorenzo, P.S.4
  • 58
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • doi: 10.1126/science.252.5009.1162
    • Lupas A, Van Dyke M, Stock J. 1991. Predicting coiled coils from protein sequences. Science 252:1162-4. doi: 10.1126/science.252.5009.1162.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    van Dyke, M.2    Stock, J.3
  • 59
    • 0344885558 scopus 로고    scopus 로고
    • Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS
    • doi: 10.1016/S0092-8674(03)00149-1
    • Margarit SM, Sondermann H, Hall BE, Nagar B, Hoelz A, Pirruccello M, et al. 2003. Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS. Cell 112:685-95. doi: 10.1016/S0092-8674(03)00149-1.
    • (2003) Cell , vol.112 , pp. 685-695
    • Margarit, S.M.1    Sondermann, H.2    Hall, B.E.3    Nagar, B.4    Hoelz, A.5    Pirruccello, M.6
  • 61
    • 0036729878 scopus 로고    scopus 로고
    • High-throughput retroviral tagging to identify components of specific signaling pathways in cancer
    • doi: 10.1038/ng950
    • Mikkers H, Allen J, Knipscheer P, Romeijn L, Hart A, Vink E, et al. 2002. High-throughput retroviral tagging to identify components of specific signaling pathways in cancer. Nat Genet 32:153-9. doi: 10.1038/ng950.
    • (2002) Nat Genet , vol.32 , pp. 153-159
    • Mikkers, H.1    Allen, J.2    Knipscheer, P.3    Romeijn, L.4    Hart, A.5    Vink, E.6
  • 62
    • 84860757215 scopus 로고    scopus 로고
    • Aberrant expression of RasGRP1 cooperates with gain-of-function NOTCH1 mutations in T-cell leukemogenesis
    • doi: 10.1038/leu.2011.328
    • Oki T, Kitaura J, Watanabe-Okochi N, Nishimura K, Maehara A, Uchida T, et al. 2012. Aberrant expression of RasGRP1 cooperates with gain-of-function NOTCH1 mutations in T-cell leukemogenesis. Leukemia 26:1038-45. doi: 10.1038/leu.2011.328.
    • (2012) Leukemia , vol.26 , pp. 1038-1045
    • Oki, T.1    Kitaura, J.2    Watanabe-Okochi, N.3    Nishimura, K.4    Maehara, A.5    Uchida, T.6
  • 63
    • 33846425744 scopus 로고    scopus 로고
    • Transgenic overexpression of RasGRP1 in mouse epidermis results in spontaneous tumors of the skin
    • doi: 10.1158/0008-5472.CAN-06-3080
    • Oki-Idouchi CE, Lorenzo PS. 2007. Transgenic overexpression of RasGRP1 in mouse epidermis results in spontaneous tumors of the skin. Cancer Res 67:276-80. doi: 10.1158/0008-5472.CAN-06-3080.
    • (2007) Cancer Res , vol.67 , pp. 276-280
    • Oki-Idouchi, C.E.1    Lorenzo, P.S.2
  • 64
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • doi: 10.1126/science.1948029
    • O'Shea EK, Klemm JD, Kim PS, Alber T. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539-44. doi: 10.1126/science.1948029.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 65
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • doi: 10.1006/jmre.1998.1361
    • Ottiger M, Delaglio F, Bax A. 1998. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson 131:373-8. doi: 10.1006/jmre.1998.1361.
    • (1998) J Magn Reson , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 66
    • 77953624215 scopus 로고    scopus 로고
    • MicroRNA-21 and microRNA-148a contribute to DNA hypomethylation in lupus CD4+ T cells by directly and indirectly targeting DNA methyltransferase 1
    • doi: 10.4049/jimmunol.0904060
    • Pan W, Zhu S, Yuan M, Cui H, Wang L, Luo X, et al. 2010. MicroRNA-21 and microRNA-148a contribute to DNA hypomethylation in lupus CD4+ T cells by directly and indirectly targeting DNA methyltransferase 1. J Immunol 184:6773-81. doi: 10.4049/jimmunol.0904060.
    • (2010) J Immunol , vol.184 , pp. 6773-6781
    • Pan, W.1    Zhu, S.2    Yuan, M.3    Cui, H.4    Wang, L.5    Luo, X.6
  • 67
    • 77952717195 scopus 로고    scopus 로고
    • Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity
    • doi: 10.1073/pnas.0912295107
    • Petri ET, Celic A, Kennedy SD, Ehrlich BE, Boggon TJ, Hodsdon ME. 2010. Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity. Proc Natl Acad Sci USA 107:9176-81. doi: 10.1073/pnas.0912295107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9176-9181
    • Petri, E.T.1    Celic, A.2    Kennedy, S.D.3    Ehrlich, B.E.4    Boggon, T.J.5    Hodsdon, M.E.6
  • 68
    • 80052311755 scopus 로고    scopus 로고
    • Genome-wide association analysis of autoantibody positivity in type 1 diabetes cases
    • doi: 10.1371/journal.pgen.1002216
    • Plagnol V, Howson JM, Smyth DJ, Walker N, Hafler JP, Wallace C, et al. 2011. Genome-wide association analysis of autoantibody positivity in type 1 diabetes cases. PLoS Genet 7:e1002216. doi: 10.1371/journal.pgen.1002216.
    • (2011) PLoS Genet , vol.7
    • Plagnol, V.1    Howson, J.M.2    Smyth, D.J.3    Walker, N.4    Hafler, J.P.5    Wallace, C.6
  • 69
    • 58249087468 scopus 로고    scopus 로고
    • Origin of the sharp boundary that discriminates positive and negative selection of thymocytes
    • doi: 10.1073/pnas.0805981105
    • Prasad A, Zikherman J, Das J, Roose JP, Weiss A, Chakraborty AK. 2009. Origin of the sharp boundary that discriminates positive and negative selection of thymocytes. Proc Natl Acad Sci USA 106:528-33. doi: 10.1073/pnas.0805981105.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 528-533
    • Prasad, A.1    Zikherman, J.2    Das, J.3    Roose, J.P.4    Weiss, A.5    Chakraborty, A.K.6
  • 71
    • 68049144942 scopus 로고    scopus 로고
    • Association of RASGRP1 with type 1 diabetes is revealed by combined follow-up of two genome-wide studies
    • doi: 10.1136/jmg.2009.067140
    • Qu HQ, Grant SF, Bradfield JP, Kim C, Frackelton E, Hakonarson H, et al. 2009. Association of RASGRP1 with type 1 diabetes is revealed by combined follow-up of two genome-wide studies. J Med Genet 46:553-4. doi: 10.1136/jmg.2009.067140.
    • (2009) J Med Genet , vol.46 , pp. 553-554
    • Qu, H.Q.1    Grant, S.F.2    Bradfield, J.P.3    Kim, C.4    Frackelton, E.5    Hakonarson, H.6
  • 72
    • 34547160398 scopus 로고    scopus 로고
    • Ras oncogenes and their downstream targets
    • doi: 10.1016/j.bbamcr.2007.01.012
    • Rajalingam K, Schreck R, Rapp UR, Albert S. 2007. Ras oncogenes and their downstream targets. Biochimica et biophysica acta 1773:1177-95. doi: 10.1016/j.bbamcr.2007.01.012.
    • (2007) Biochimica Et Biophysica Acta , vol.1773 , pp. 1177-1195
    • Rajalingam, K.1    Schreck, R.2    Rapp, U.R.3    Albert, S.4
  • 73
    • 31844447089 scopus 로고    scopus 로고
    • Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state
    • doi: 10.1038/nature04468
    • Rehmann H, Das J, Knipscheer P, Wittinghofer A, Bos JL. 2006. Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state. Nature 439:625-8. doi: 10.1038/nature04468.
    • (2006) Nature , vol.439 , pp. 625-628
    • Rehmann, H.1    Das, J.2    Knipscheer, P.3    Wittinghofer, A.4    Bos, J.L.5
  • 74
    • 51349150613 scopus 로고    scopus 로고
    • Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B
    • doi: 10.1038/nature07187
    • Rehmann H, Arias-Palomo E, Hadders MA, Schwede F, Llorca O, Bos JL. 2008. Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B. Nature 455:124-7. doi: 10.1038/nature07187.
    • (2008) Nature , vol.455 , pp. 124-127
    • Rehmann, H.1    Arias-Palomo, E.2    Hadders, M.A.3    Schwede, F.4    Llorca, O.5    Bos, J.L.6
  • 75
    • 0037163027 scopus 로고    scopus 로고
    • RasGRP4 is a novel Ras activator isolated from acute myeloid leukemia
    • doi: 10.1074/jbc.M111330200
    • Reuther GW, Lambert QT, Rebhun JF, Caligiuri MA, Quilliam LA, Der CJ. 2002. RasGRP4 is a novel Ras activator isolated from acute myeloid leukemia. J Biol Chem 277:30508-14. doi: 10.1074/jbc.M111330200.
    • (2002) J Biol Chem , vol.277 , pp. 30508-30514
    • Reuther, G.W.1    Lambert, Q.T.2    Rebhun, J.F.3    Caligiuri, M.A.4    Quilliam, L.A.5    Der, C.J.6
  • 77
    • 18944383647 scopus 로고    scopus 로고
    • A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells
    • doi: 10.1128/MCB.25.11.4426-4441.2005
    • Roose JP, Mollenauer M, Gupta VA, Stone J, Weiss A. 2005. A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells. Mol Cell Biol 25:4426-41. doi: 10.1128/MCB.25.11.4426-4441.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 4426-4441
    • Roose, J.P.1    Mollenauer, M.2    Gupta, V.A.3    Stone, J.4    Weiss, A.5
  • 78
    • 34147203741 scopus 로고    scopus 로고
    • Unusual interplay of two types of Ras activators, RasGRP and SOS, establishes sensitive and robust Ras activation in lymphocytes
    • doi: 10.1128/MCB.01882-06
    • Roose JP, Mollenauer M, Ho M, Kurosaki T, Weiss A. 2007. Unusual interplay of two types of Ras activators, RasGRP and SOS, establishes sensitive and robust Ras activation in lymphocytes. Mol Cell Biol 27:2732-45. doi: 10.1128/MCB.01882-06.
    • (2007) Mol Cell Biol , vol.27 , pp. 2732-2745
    • Roose, J.P.1    Mollenauer, M.2    Ho, M.3    Kurosaki, T.4    Weiss, A.5
  • 80
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • doi: 10.1007/s10858-009-9333-z
    • Shen Y, Delaglio F, Cornilescu G, Bax A. 2009. TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44:213-23. doi: 10.1007/s10858-009-9333-z.
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 81
    • 7044226349 scopus 로고    scopus 로고
    • Structural analysis of autoinhibition in the Ras activator Son of sevenless
    • doi: 10.1016/j.cell.2004.10.005
    • Sondermann H, Soisson SM, Boykevisch S, Yang SS, Bar-Sagi D, Kuriyan J. 2004. Structural analysis of autoinhibition in the Ras activator Son of sevenless. Cell 119:393-405. doi: 10.1016/j.cell.2004.10.005.
    • (2004) Cell , vol.119 , pp. 393-405
    • Sondermann, H.1    Soisson, S.M.2    Boykevisch, S.3    Yang, S.S.4    Bar-Sagi, D.5    Kuriyan, J.6
  • 82
    • 0042470456 scopus 로고    scopus 로고
    • Positive and negative selection of T cells
    • doi: 10.1146/annurev.immunol.21.120601.141107
    • Starr TK, Jameson SC, Hogquist KA. 2003. Positive and negative selection of T cells. Annu Rev Immunol 21:139-76. doi: 10.1146/annurev.immunol.21.120601.141107.
    • (2003) Annu Rev Immunol , vol.21 , pp. 139-176
    • Starr, T.K.1    Jameson, S.C.2    Hogquist, K.A.3
  • 83
    • 79960044081 scopus 로고    scopus 로고
    • Regulation and function of the RasGRP family of ras activators in blood cells
    • doi: 10.1177/1947601911408082
    • Stone JC. 2011. Regulation and function of the RasGRP family of ras activators in blood cells. Genes Cancer 2:320-34. doi: 10.1177/1947601911408082.
    • (2011) Genes Cancer , vol.2 , pp. 320-334
    • Stone, J.C.1
  • 84
    • 0036725051 scopus 로고    scopus 로고
    • New genes involved in cancer identified by retroviral tagging
    • doi: 10.1038/ng949
    • Suzuki T, Shen H, Akagi K, Morse HC, Malley JD, Naiman DQ, et al. 2002. New genes involved in cancer identified by retroviral tagging. Nat Genet 32:166-74. doi: 10.1038/ng949.
    • (2002) Nat Genet , vol.32 , pp. 166-174
    • Suzuki, T.1    Shen, H.2    Akagi, K.3    Morse, H.C.4    Malley, J.D.5    Naiman, D.Q.6
  • 86
    • 33845884026 scopus 로고    scopus 로고
    • Gain-of-function SOS1 mutations cause a distinctive form of Noonan syndrome
    • doi: 10.1038/ng1939
    • Tartaglia M, Pennacchio LA, Zhao C, Yadav KK, Fodale V, Sarkozy A, et al. 2007. Gain-of-function SOS1 mutations cause a distinctive form of Noonan syndrome. Nat Genet 39:75-9. doi: 10.1038/ng1939.
    • (2007) Nat Genet , vol.39 , pp. 75-79
    • Tartaglia, M.1    Pennacchio, L.A.2    Zhao, C.3    Yadav, K.K.4    Fodale, V.5    Sarkozy, A.6
  • 87
    • 60549101661 scopus 로고    scopus 로고
    • Membrane localization of RasGRP1 is controlled by an EF-hand, and by the GEF domain
    • doi: 10.1016/j.bbamcr.2008.12.019
    • Tazmini G, Beaulieu N, Woo A, Zahedi B, Goulding RE, Kay RJ. 2009. Membrane localization of RasGRP1 is controlled by an EF-hand, and by the GEF domain. Biochimica et biophysica acta 1793:447-61. doi: 10.1016/j.bbamcr.2008.12.019.
    • (2009) Biochimica Et Biophysica Acta , vol.1793 , pp. 447-461
    • Tazmini, G.1    Beaulieu, N.2    Woo, A.3    Zahedi, B.4    Goulding, R.E.5    Kay, R.J.6
  • 88
    • 0029589671 scopus 로고
    • Cytosolic calcium concentration in resting and stimulated endothelium of excised intact rat aorta
    • Usachev YM, Marchenko SM, Sage SO. 1995. Cytosolic calcium concentration in resting and stimulated endothelium of excised intact rat aorta. J Physiol 489:309-17.
    • (1995) J Physiol , vol.489 , pp. 309-317
    • Usachev, Y.M.1    Marchenko, S.M.2    Sage, S.O.3
  • 89
    • 0037047325 scopus 로고    scopus 로고
    • Structural independence of the two EF-hand domains of caltractin
    • doi: 10.1074/jbc.M112232200
    • Veeraraghavan S, Fagan PA, Hu H, Lee V, Harper JF, Huang B, et al. 2002. Structural independence of the two EF-hand domains of caltractin. J Biol Chem 277:28564-71. doi: 10.1074/jbc.M112232200.
    • (2002) J Biol Chem , vol.277 , pp. 28564-28571
    • Veeraraghavan, S.1    Fagan, P.A.2    Hu, H.3    Lee, V.4    Harper, J.F.5    Huang, B.6
  • 90
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • doi: 10.1126/science.1062023
    • Vetter IR, Wittinghofer A. 2001. The guanine nucleotide-binding switch in three dimensions. Science 294:1299-304. doi: 10.1126/science.1062023.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 91
    • 0029031112 scopus 로고
    • The Grb2 binding domain of mSos1 is not required for downstream signal transduction
    • doi: 10.1038/ng0795-294
    • Wang W, Fisher EM, Jia Q, Dunn JM, Porfiri E, Downward J, et al. 1995. The Grb2 binding domain of mSos1 is not required for downstream signal transduction. Nat Genet 10:294-300. doi: 10.1038/ng0795-294.
    • (1995) Nat Genet , vol.10 , pp. 294-300
    • Wang, W.1    Fisher, E.M.2    Jia, Q.3    Dunn, J.M.4    Porfiri, E.5    Downward, J.6
  • 93
    • 0029364052 scopus 로고
    • 1H, 13C and 15N chemical shift referencing in biomolecular NMR
    • doi: 10.1007/BF00211777
    • Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, et al. 1995. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135-40. doi: 10.1007/BF00211777.
    • (1995) J Biomol NMR , vol.6 , pp. 135-140
    • Wishart, D.S.1    Bigam, C.G.2    Yao, J.3    Abildgaard, F.4    Dyson, H.J.5    Oldfield, E.6
  • 94
    • 78049277177 scopus 로고    scopus 로고
    • RasGRP3 contributes to formation and maintenance of the prostate cancer phenotype
    • doi: 10.1158/0008-5472.CAN-09-4729
    • Yang D, Kedei N, Li L, Tao J, Velasquez JF, Michalowski AM, et al. 2010. RasGRP3 contributes to formation and maintenance of the prostate cancer phenotype. Cancer Res 70:7905-17. doi: 10.1158/0008-5472.CAN-09-4729.
    • (2010) Cancer Res , vol.70 , pp. 7905-7917
    • Yang, D.1    Kedei, N.2    Li, L.3    Tao, J.4    Velasquez, J.F.5    Michalowski, A.M.6
  • 95
    • 80755132201 scopus 로고    scopus 로고
    • RasGRP3, a Ras activator, contributes to signaling and the tumorigenic phenotype in human melanoma
    • doi: 10.1038/onc.2011.166
    • Yang D, Tao J, Li L, Kedei N, Toth ZE, Czap A, et al. 2011. RasGRP3, a Ras activator, contributes to signaling and the tumorigenic phenotype in human melanoma. Oncogene 30:4590-600. doi: 10.1038/onc.2011.166.
    • (2011) Oncogene , vol.30 , pp. 4590-4600
    • Yang, D.1    Tao, J.2    Li, L.3    Kedei, N.4    Toth, Z.E.5    Czap, A.6
  • 96
    • 0001349394 scopus 로고    scopus 로고
    • An HNCO-based pulse scheme for the measurement of 13Calpha-1Halpha one-bond dipolar couplings in 15N, 13C labeled proteins
    • doi: 10.1023/A:1008223017233
    • Yang D, Tolman JR, Goto NK, Kay LE. 1998. An HNCO-based pulse scheme for the measurement of 13Calpha-1Halpha one-bond dipolar couplings in 15N, 13C labeled proteins. J Biomol NMR 12:325-32. doi: 10.1023/A:1008223017233.
    • (1998) J Biomol NMR , vol.12 , pp. 325-332
    • Yang, D.1    Tolman, J.R.2    Goto, N.K.3    Kay, L.E.4
  • 97
    • 0004757060 scopus 로고    scopus 로고
    • San Francisco, University of California
    • Goddard TD, Kneller DG. SPARKY 3. San Francisco, University of California.
    • SPARKY , vol.3
    • Goddard, T.D.1    Kneller, D.G.2
  • 98
    • 0037613335 scopus 로고    scopus 로고
    • Rational design of a calcium-binding protein
    • doi: 10.1021/ja034724x
    • Yang W, Jones LM, Isley L, Ye Y, Lee HW, Wilkins A, et al. 2003. Rational design of a calcium-binding protein. J Am Chem Soc 125:6165-71. doi: 10.1021/ja034724x.
    • (2003) J Am Chem Soc , vol.125 , pp. 6165-6171
    • Yang, W.1    Jones, L.M.2    Isley, L.3    Ye, Y.4    Lee, H.W.5    Wilkins, A.6
  • 99
    • 0037067713 scopus 로고    scopus 로고
    • RasGRP4, a new mast cell-restricted Ras guanine nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs. Identification of defective variants of this signaling protein in asthma, mastocytosis, and mast cell leukemia patients and demonstration of the importance of RasGRP4 in mast cell development and function
    • doi: 10.1074/jbc.M202575200
    • Yang Y, Li L, Wong GW, Krilis SA, Madhusudhan MS, Sali A, et al. 2002. RasGRP4, a new mast cell-restricted Ras guanine nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs. Identification of defective variants of this signaling protein in asthma, mastocytosis, and mast cell leukemia patients and demonstration of the importance of RasGRP4 in mast cell development and function. J Biol Chem 277:25756-74. doi: 10.1074/jbc.M202575200.
    • (2002) J Biol Chem , vol.277 , pp. 25756-25774
    • Yang, Y.1    Li, L.2    Wong, G.W.3    Krilis, S.A.4    Madhusudhan, M.S.5    Sali, A.6
  • 100
    • 39749157996 scopus 로고    scopus 로고
    • Defective expression of Ras guanyl nucleotide-releasing protein 1 in a subset of patients with systemic lupus erythematosus
    • Yasuda S, Stevens RL, Terada T, Takeda M, Hashimoto T, Fukae J, et al. 2007. Defective expression of Ras guanyl nucleotide-releasing protein 1 in a subset of patients with systemic lupus erythematosus. J Immunol 179:4890-900.
    • (2007) J Immunol , vol.179 , pp. 4890-4900
    • Yasuda, S.1    Stevens, R.L.2    Terada, T.3    Takeda, M.4    Hashimoto, T.5    Fukae, J.6
  • 101
    • 79953326132 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulates plasma membrane targeting of the Ras-specific exchange factor RasGRP1
    • doi: 10.1074/jbc.M110.189605
    • Zahedi B, Goo HJ, Beaulieu N, Tazmini G, Kay RJ, Cornell RB, et al. 2011. Phosphoinositide 3-kinase regulates plasma membrane targeting of the Ras-specific exchange factor RasGRP1. J Biol Chem 286:12712-23. doi: 10.1074/jbc.M110.189605.
    • (2011) J Biol Chem , vol.286 , pp. 12712-12723
    • Zahedi, B.1    Goo, H.J.2    Beaulieu, N.3    Tazmini, G.4    Kay, R.J.5    Cornell, R.B.6
  • 102
    • 0028979464 scopus 로고
    • Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester
    • doi: 10.1016/0092-8674(95)90011-X
    • Zhang G, Kazanietz MG, Blumberg PM, Hurley JH. 1995. Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester. Cell 81:917-24. doi: 10.1016/0092-8674(95)90011-X.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 103
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • doi: 10.1038/nsb0995-758
    • Zhang M, Tanaka T, Ikura M. 1995. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Biol 2:758-67. doi: 10.1038/nsb0995-758.
    • (1995) Nat Struct Biol , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 104
    • 84863230420 scopus 로고    scopus 로고
    • The role of Ras guanine nucleotide releasing protein 4 in Fc epsilonRI-mediated signaling, mast cell function, and T cell development
    • doi: 10.1074/jbc.M111.320580
    • Zhu M, Fuller DM, Zhang W. 2012. The role of Ras guanine nucleotide releasing protein 4 in Fc epsilonRI-mediated signaling, mast cell function, and T cell development. J Biol Chem 287:8135-43. doi: 10.1074/jbc.M111.320580.
    • (2012) J Biol Chem , vol.287 , pp. 8135-8143
    • Zhu, M.1    Fuller, D.M.2    Zhang, W.3
  • 105
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • doi: 10.1021/ja0000908
    • Zweckstetter M, Bax A. 2000. Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J Am Chem Soc 122:3791-2. doi: 10.1021/ja0000908.
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2


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