메뉴 건너뛰기




Volumn 50, Issue 2, 2015, Pages 85-133

Structures of Ras superfamily effector complexes: What have we learnt in two decades?

Author keywords

Arf; GTPase; Rab; Ran; Ras; Rho; Small G protein

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 6; ARF PROTEIN; BINDING PROTEIN; EXPORTIN 5; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; MOLECULAR MOTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C; PLECKSTRIN; PLEXIN; PROTEIN CDC42; PROTEIN SERINE THREONINE KINASE; RAB PROTEIN; RAN PROTEIN; RAS PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RHO FACTOR; MONOMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; MULTIPROTEIN COMPLEX; PROTEIN BINDING;

EID: 84928822477     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2014.999191     Document Type: Review
Times cited : (65)

References (156)
  • 1
    • 0033609388 scopus 로고    scopus 로고
    • Structure of cdc42 in complex with the gtpase-binding domain of the 'wiskott-Aldrich syndrome'' protein
    • Abdul-Manan N, Aghazadeh B, Liu GA, et al. (1999). Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome'' protein. Nature 399: 379-83
    • (1999) Nature , vol.399 , pp. 379-383
    • Abdul-Manan, N.1    Aghazadeh, B.2    Liu, G.A.3
  • 2
    • 84859897794 scopus 로고    scopus 로고
    • Regulation of reactive oxygen species generation in cell signaling
    • Bae YS, Oh H, Rhee SG, Yoo YD. (2011). Regulation of reactive oxygen species generation in cell signaling. Mol Cells 32: 491-509
    • (2011) Mol Cells , vol.32 , pp. 491-509
    • Bae, Y.S.1    Oh, H.2    Rhee, S.G.3    Yoo, Y.D.4
  • 3
    • 59449085591 scopus 로고    scopus 로고
    • The structure of binder of arl2 (bart) reveals a novel g protein binding domain: Implications for function
    • Bailey LK, Campbell LJ, Evetts KA, et al. (2009). The structure of binder of Arl2 (BART) reveals a novel G protein binding domain: implications for function. J Biol Chem 284: 992-9
    • (2009) J Biol Chem , vol.284 , pp. 992-999
    • Bailey, L.K.1    Campbell, L.J.2    Evetts, K.A.3
  • 4
    • 84912126924 scopus 로고    scopus 로고
    • Adp-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin a1 polypeptide
    • Banerjee T, Taylor M, Jobling MG, et al. (2014). ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. Mol Microbiol 94: 898-912
    • (2014) Mol Microbiol , vol.94 , pp. 898-912
    • Banerjee, T.1    Taylor, M.2    Jobling, M.G.3
  • 5
    • 0033580833 scopus 로고    scopus 로고
    • Effector recognition by the small gtp-binding proteins ras and ral
    • Bauer B, Mirey G, Vetter IR, et al. (1999). Effector recognition by the small GTP-binding proteins Ras and Ral. J Biol Chem 274: 17763-70
    • (1999) J Biol Chem , vol.274 , pp. 17763-17770
    • Bauer, B.1    Mirey, G.2    Vetter, I.R.3
  • 6
    • 80052339290 scopus 로고    scopus 로고
    • A dual binding mode for rhogtpases in plexin signalling
    • Bell CH, Aricescu AR, Jones EY, Siebold C. (2011). A dual binding mode for RhoGTPases in plexin signalling. PLoS Biol 9: e1001134
    • (2011) PLoS Biol , vol.9 , pp. e1001134
    • Bell, C.H.1    Aricescu, A.R.2    Jones, E.Y.3    Siebold, C.4
  • 8
    • 84868524550 scopus 로고    scopus 로고
    • Entamoeba histolyticarho1 regulates actin polymerization through a divergent, diaphanousrelated formin
    • Bosch DE, Yang B, Siderovski DP. (2012). Entamoeba histolyticaRho1 regulates actin polymerization through a divergent, diaphanousrelated formin. Biochemistry 51: 8791-801
    • (2012) Biochemistry , vol.51 , pp. 8791-8801
    • Bosch, D.E.1    Yang, B.2    Siderovski, D.P.3
  • 9
    • 32444445745 scopus 로고    scopus 로고
    • Structural and mechanistic insights into ras association domains of phospholipase c epsilon
    • Bunney TD, Harris R, Gandarillas NL, et al. (2006). Structural and mechanistic insights into ras association domains of phospholipase C epsilon. Mol Cell 21: 495-507
    • (2006) Mol Cell , vol.21 , pp. 495-507
    • Bunney, T.D.1    Harris, R.2    Gandarillas, N.L.3
  • 10
    • 64749102105 scopus 로고    scopus 로고
    • Structural insights into formationof an active signaling complex between rac and phospholipase c gamma 2
    • Bunney TD, Opaleye O, Roe SM, et al. (2009). Structural insights into formationof an active signaling complex between Rac and phospholipase C Gamma 2. Mol Cell 34: 223-33
    • (2009) Mol Cell , vol.34 , pp. 223-233
    • Bunney, T.D.1    Opaleye, O.2    Roe, S.M.3
  • 11
    • 38749150383 scopus 로고    scopus 로고
    • Rab and arl gtpase family members cooperate in the localization of the golgin gcc185
    • Burguete AS, Fenn TD, Brunger AT, Pfeffer SR. (2008). Rab and Arl GTPase family members cooperate in the localization of the Golgin GCC185. Cell 132: 286-98
    • (2008) Cell , vol.132 , pp. 286-298
    • Burguete, A.S.1    Fenn, T.D.2    Brunger, A.T.3    Pfeffer, S.R.4
  • 12
    • 84856492497 scopus 로고    scopus 로고
    • The gdi-like solubilizing factor pde [delta] sustains the spatial organization and signalling of ras family proteins
    • Chandra A, Grecco HE, Pisupati V, et al. (2012). The GDI-like solubilizing factor PDE [delta] sustains the spatial organization and signalling of Ras family proteins. Nat Cell Biol 14: 148-58
    • (2012) Nat Cell Biol , vol.14 , pp. 148-158
    • Chandra, A.1    Grecco, H.E.2    Pisupati, V.3
  • 13
    • 53049100324 scopus 로고    scopus 로고
    • Elucidation of Rab27 recruitment by its effectors: Structure of Rab27Abound to Exophilin4/.Slp2-A
    • Chavas LMG, Ihara K, Kawasaki M, et al. (2008). Elucidation of Rab27 recruitment by its effectors: structure of Rab27Abound to Exophilin4/.Slp2-A. Structure 16: 1468-77
    • (2008) Structure , vol.16 , pp. 1468-1477
    • Chavas, L.M.G.1    Ihara, K.2    Kawasaki, M.3
  • 14
    • 84861212650 scopus 로고    scopus 로고
    • Structural insights into a unique legionella pneumophila effector lida recognizing both gdp and gtp bound rab1 in their active state
    • Cheng W, Yin K, Lu D, et al. (2012). Structural insights into a unique Legionella pneumophila effector LidA recognizing both GDP and GTP bound Rab1 in their active state. PLoS Pathog 8: e1002528
    • (2012) PLoS Pathog , vol.8 , pp. e1002528
    • Cheng, W.1    Yin, K.2    Lu, D.3
  • 15
    • 84874433733 scopus 로고    scopus 로고
    • Regulation of small gtpases by gefs, gaps, and gdis
    • Cherfils J, Zeghouf M. (2013). Regulation of small GTPases by GEFs, GAPs, and GDIs. Physiol Rev 93: 269-309
    • (2013) Physiol Rev , vol.93 , pp. 269-309
    • Cherfils, J.1    Zeghouf, M.2
  • 16
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-beta 2-ran center dot gppnhp
    • Chook Y, Blobel G. (1999). Structure of the nuclear transport complex karyopherin-beta 2-Ran center dot GppNHp. Nature 399: 230-7
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.1    Blobel, G.2
  • 17
    • 0037343940 scopus 로고    scopus 로고
    • The structure of the gga1-gat domain reveals the molecular basis for arf binding and membrane association of ggas
    • Collins BM, Watson PJ, Owen DJ. (2003). The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs. Dev Cell 4: 321-32
    • (2003) Dev Cell , vol.4 , pp. 321-332
    • Collins, B.M.1    Watson, P.J.2    Owen, D.J.3
  • 18
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook A, Bono F, Jinek M, Conti E. (2007). Structural biology of nucleocytoplasmic transport. Annu Rev Biochem 76: 647-71
    • (2007) Annu Rev Biochem , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 19
    • 20844458749 scopus 로고    scopus 로고
    • The structure of the nuclear export receptor cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding
    • Cook A, Fernandez E, Lindner D, et al. (2005). The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Mol Cell 18: 355-67
    • (2005) Mol Cell , vol.18 , pp. 355-367
    • Cook, A.1    Fernandez, E.2    Lindner, D.3
  • 20
    • 69949094998 scopus 로고    scopus 로고
    • Structures of the trna export factor in the nuclear and cytosolic states
    • Cook AG, Fukuhara N, Jinek M, Conti E. (2009). Structures of the tRNA export factor in the nuclear and cytosolic states. Nature 461: 60-5
    • (2009) Nature , vol.461 , pp. 60-65
    • Cook, A.G.1    Fukuhara, N.2    Jinek, M.3    Conti, E.4
  • 21
    • 1942487871 scopus 로고    scopus 로고
    • Cholera toxin: A paradigm for multifunctional engagement of cellular mechanisms (review
    • De Haan L, Hirst TR. (2004). Cholera toxin: a paradigm for multifunctional engagement of cellular mechanisms (Review). Mol Membr Biol 21: 77-92
    • (2004) Mol Membr Biol , vol.21 , pp. 77-92
    • De Haan, L.1    Hirst, T.R.2
  • 22
    • 0023857409 scopus 로고
    • Three-dimensional structure of an oncogene protein: Catalytic domain of human c-h-ras p21
    • de Vos AM, Tong L, Milburn MV, et al. (1988). Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. Science 239: 888-93
    • (1988) Science , vol.239 , pp. 888-893
    • De Vos, A.M.1    Tong, L.2    Milburn, M.V.3
  • 23
    • 68249161191 scopus 로고    scopus 로고
    • Structural and functional studies of the ras-Associating and pleckstrin-homology domains of grb10 and grb14
    • Depetris RS, Wu J, Hubbard SR. (2009). Structural and functional studies of the Ras-Associating and pleckstrin-homology domains of Grb10 and Grb14. Nat Struct Mol Biol 16: 833-9
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 833-839
    • Depetris, R.S.1    Wu, J.2    Hubbard, S.R.3
  • 24
    • 36249015526 scopus 로고    scopus 로고
    • Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent grp1 family arf gtpase exchange factors
    • DiNitto JP, Delprato A, Gabe Lee M-T, et al. (2007). Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors. Mol Cell 28: 569-83
    • (2007) Mol Cell , vol.28 , pp. 569-583
    • Dinitto, J.P.1    Delprato, A.2    Gabe Lee, M.-T.3
  • 25
    • 17344369066 scopus 로고    scopus 로고
    • Golgi-localized gap for cdc42 functions downstream of arf1 to control arp2/3 complex and f-Actin dynamics
    • Dubois T, Paléotti O, Mironovaa, et al. (2005). Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-Actin dynamics. Nat Cell Biol 7: 353-64
    • (2005) Nat Cell Biol , vol.7 , pp. 353-364
    • Dubois, T.1    Paléotti, O.2    Mironova, A.3
  • 26
    • 1342304087 scopus 로고    scopus 로고
    • Structural insights into the interaction of rocki with the switch regions of rhoa
    • Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR. (2004). Structural insights into the interaction of ROCKI with the switch regions of RhoA. J Biol Chem 279: 7098-104
    • (2004) J Biol Chem , vol.279 , pp. 7098-7104
    • Dvorsky, R.1    Blumenstein, L.2    Vetter, I.R.3    Ahmadian, M.R.4
  • 27
    • 33750437407 scopus 로고    scopus 로고
    • Structural basis for rab11-mediated recruitment of fip3 to recycling endosomes
    • eathiraj S, Mishra A, Prekeris R, Lambright DG. (2006). Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes. J Mol Biol 364: 121-35
    • (2006) J Mol Biol , vol.364 , pp. 121-135
    • Eathiraj, S.1    Mishra, A.2    Prekeris, R.3    Lambright, D.G.4
  • 28
    • 22944444569 scopus 로고    scopus 로고
    • Structural basis of family-wide rab gtpase recognition by rabenosyn-5
    • eathiraj S, Pan X, Ritacco C, Lambright DG. (2005). Structural basis of family-wide Rab GTPase recognition by rabenosyn-5. Nature 436: 415-19
    • (2005) Nature , vol.436 , pp. 415-419
    • Eathiraj, S.1    Pan, X.2    Ritacco, C.3    Lambright, D.G.4
  • 29
    • 0029041347 scopus 로고
    • Solution structure of the ras-binding domain of c-raf-1 and identification of its ras interaction surface
    • emerson SD, Madison V, Palermo R, et al. (1995). Solution structure of the Ras-binding domain of C-Raf-1 and identification of its Ras interaction surface. Biochemistry 34: 6911-18
    • (1995) Biochemistry , vol.34 , pp. 6911-6918
    • Emerson, S.D.1    Madison, V.2    Palermo, R.3
  • 30
    • 0028241777 scopus 로고
    • Chemical shift assignments and folding topology of the ras-binding domain of human raf-1 as determined by heteronuclear three-dimensional nmr spectroscopy
    • emerson SD, Waugh DS, Scheffler JE, et al. (1994). Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy. Biochemistry 33: 7745-52
    • (1994) Biochemistry , vol.33 , pp. 7745-7752
    • Emerson, S.D.1    Waugh, D.S.2    Scheffler, J.E.3
  • 31
    • 77955480325 scopus 로고    scopus 로고
    • The ralb-rlip76 complex reveals a novel mode of ral-effector interaction
    • Fenwick RB, Campbell LJ, Rajasekar K, et al. (2010). The RalB-RLIP76 complex reveals a novel mode of ral-effector interaction. Structure 18: 985-95
    • (2010) Structure , vol.18 , pp. 985-995
    • Fenwick, R.B.1    Campbell, L.J.2    Rajasekar, K.3
  • 32
    • 64349107039 scopus 로고    scopus 로고
    • Solution structure and dynamics of the small gtpase ralb in its active conformation: Significance for effector protein binding
    • Fenwick RB, Prasannan S, Campbell LJ, et al. (2009). Solution structure and dynamics of the small GTPase RalB in its active conformation: significance for effector protein binding. Biochemistry 48: 2192-206
    • (2009) Biochemistry , vol.48 , pp. 2192-2206
    • Fenwick, R.B.1    Prasannan, S.2    Campbell, L.J.3
  • 33
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried H, Kutay U. (2003). Nucleocytoplasmic transport: taking an inventory. Cell Mol Life Sci 60: 1659-88
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 34
    • 0038602702 scopus 로고    scopus 로고
    • Structural basis of the interaction between rala and sec5, a subunit of the sec6/8 complex
    • Fukai S, Matern HT, Jagath JR, et al. (2003). Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex. EMBO J 22: 3267-78
    • (2003) EMBO J , vol.22 , pp. 3267-3278
    • Fukai, S.1    Matern, H.T.2    Jagath, J.R.3
  • 35
    • 0037416217 scopus 로고    scopus 로고
    • Structure of cdc42 in a complex with the gtpase-binding domain of the cell polarity protein, par6
    • Garrard S, Capaldo C, Gao L, et al. (2003). Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6. EMBO J 22: 1125-33
    • (2003) EMBO J , vol.22 , pp. 1125-1133
    • Garrard, S.1    Capaldo, C.2    Gao, L.3
  • 36
    • 84882433525 scopus 로고    scopus 로고
    • The structure of the ternary complex of krev interaction trapped 1 (krit1) bound to both the rap1 gtpase and the heart of glass (heg1) cytoplasmic tail
    • Gingras AR, Puzon-Mclaughlin W, Ginsberg MH. (2013). The structure of the ternary complex of Krev Interaction Trapped 1 (KRIT1) bound to both the Rap1 GTPase and the Heart of Glass (HEG1) cytoplasmic tail. J Biol Chem 288: 23639-49
    • (2013) J Biol Chem , vol.288 , pp. 23639-23649
    • Gingras, A.R.1    Puzon-Mclaughlin, W.2    Ginsberg, M.H.3
  • 37
    • 35548936992 scopus 로고    scopus 로고
    • Krit-1/ccm1 is a rap1 effector that regulates endothelial cell junctions
    • Glading A, Han J, Stockton RA, Ginsberg MH. (2007). KRIT-1/CCM1 is a Rap1 effector that regulates endothelial cell junctions. J Cell Biol 179: 247-54
    • (2007) J Cell Biol , vol.179 , pp. 247-254
    • Glading, A.1    Han, J.2    Stockton, R.A.3    Ginsberg, M.H.4
  • 38
    • 0029864175 scopus 로고    scopus 로고
    • Equilibrium and kinetic measurements reveal rapidly reversible binding of ras to raf
    • Gorman C, Skinner R, Skelly J, et al. (1996). Equilibrium and kinetic measurements reveal rapidly reversible binding of ras to raf. J Biol Chem 271: 6713-19
    • (1996) J Biol Chem , vol.271 , pp. 6713-6719
    • Gorman, C.1    Skinner, R.2    Skelly, J.3
  • 39
    • 84875467016 scopus 로고    scopus 로고
    • Structural basis for the nuclear export activity of importin13
    • Grünwald M, Lazzaretti D, Bono F. (2013). Structural basis for the nuclear export activity of Importin13. EMBO J 32: 899-913
    • (2013) EMBO J , vol.32 , pp. 899-913
    • Grünwald, M.1    Lazzaretti, D.2    Bono, F.3
  • 40
    • 80052230265 scopus 로고    scopus 로고
    • Ran-dependent nuclear export mediators: A structural perspective
    • Güttler T, Görlich D. (2011). Ran-dependent nuclear export mediators: a structural perspective. EMBO J 30 3457-74
    • (2011) EMBO J , vol.30 , pp. 3457-3474
    • Güttler, T.1    Görlich, D.2
  • 41
    • 79952737559 scopus 로고    scopus 로고
    • Importin b-Type nuclear transport receptors have distinct binding affinities for ran-gtp
    • hahn S, Schlenstedt G. (2011). Importin b-Type nuclear transport receptors have distinct binding affinities for Ran-GTP. Biochem Biophys Res Commun 406: 383-8
    • (2011) Biochem Biophys Res Commun , vol.406 , pp. 383-388
    • Hahn, S.1    Schlenstedt, G.2
  • 42
    • 0036565668 scopus 로고    scopus 로고
    • The complex of arl2-gtp and pde delta: From structure to function
    • hanzal-Bayer M, Renault L, Roversi P, et al. (2002). The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J 21: 2095-106
    • (2002) EMBO J , vol.21 , pp. 2095-2106
    • Hanzal-Bayer, M.1    Renault, L.2    Roversi, P.3
  • 43
    • 84862268931 scopus 로고    scopus 로고
    • Exorcising the exocyst complex
    • heider MR, Munson M. (2012). Exorcising the exocyst complex. Traffic 13: 898-907
    • (2012) Traffic , vol.13 , pp. 898-907
    • Heider, M.R.1    Munson, M.2
  • 44
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the ras family gtp-binding proteins h-ras, rap1a, and r-ras with the putative effector molecules raf kinase and ral-guanine nucleotide exchange factor
    • herrmann CA, Horn G, Spaargaren M, Wittinghofer A. (1996). Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J Biol Chem 271: 6794-800
    • (1996) J Biol Chem , vol.271 , pp. 6794-6800
    • Herrmann, C.A.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 45
    • 84902081498 scopus 로고    scopus 로고
    • Varp is recruitedon to endosomes by direct interaction with retromer, where together they function in export to the cell surface
    • hesketh GG, Perez-Dorado I, Jackson LR, et al. (2014). VARP Is recruiteDon to endosomes by direct interaction with Retromer, where together they function in export to the cell surface. Dev Cell 29: 591-606
    • (2014) Dev Cell , vol.29 , pp. 591-606
    • Hesketh, G.G.1    Perez-Dorado, I.2    Jackson, L.R.3
  • 46
    • 0034603198 scopus 로고    scopus 로고
    • Structure of the rho family gtp-binding protein cdc42 in complex with the multifunctional regulator rhogdi
    • hoffman GR, Nassar N, Cerione RA. (2000). Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell 100: 345-56
    • (2000) Cell , vol.100 , pp. 345-356
    • Hoffman, G.R.1    Nassar, N.2    Cerione, R.A.3
  • 47
    • 84867848485 scopus 로고    scopus 로고
    • Plexin structures are coming: Opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions
    • hota PK, Buck M. (2012). Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions. Cell Mol Life Sci 69: 3765-805
    • (2012) Cell Mol Life Sci , vol.69 , pp. 3765-3805
    • Hota, P.K.1    Buck, M.2
  • 48
    • 79955000748 scopus 로고    scopus 로고
    • A structural basis for lowe syndrome caused by mutations in the rab-binding domain of ocrl1
    • hou X, Hagemann N, Schoebel S, et al. (2011). A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1. EMBO J 30: 1659-70
    • (2011) EMBO J , vol.30 , pp. 1659-1670
    • Hou, X.1    Hagemann, N.2    Schoebel, S.3
  • 49
    • 0031778630 scopus 로고    scopus 로고
    • Structural basis for the interaction of ras with ralgds
    • huang L, Hofer F, Martin GS, Kim SH. (1998). Structural basis for the interaction of Ras with RalGDS. Nat Struct Biol 5: 422-6
    • (1998) Nat Struct Biol , vol.5 , pp. 422-426
    • Huang, L.1    Hofer, F.2    Martin, G.S.3    Kim, S.H.4
  • 50
    • 79953683448 scopus 로고    scopus 로고
    • Mutational analysis reveals a single binding interface between rhoa and its effector, prk1
    • hutchinson CL, Lowe PN, McLaughlin SH, et al. (2011). Mutational analysis reveals a single binding interface between RhoA and its effector, PRK1. Biochemistry 50: 2860-9
    • (2011) Biochemistry , vol.50 , pp. 2860-2869
    • Hutchinson, C.L.1    Lowe, P.N.2    McLaughlin, S.H.3
  • 51
    • 84887572710 scopus 로고    scopus 로고
    • Differential binding of rhoa, rhob, and rhoc to protein kinase c-related kinase (prk) isoforms prk1, prk2, and prk3: Prks have the highest affinity for rhob
    • hutchinson CL, Lowe PN, McLaughlin SH, et al. (2013). Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB. Biochemistry 52: 7999-8011
    • (2013) Biochemistry , vol.52 , pp. 7999-8011
    • Hutchinson, C.L.1    Lowe, P.N.2    McLaughlin, S.H.3
  • 52
    • 70349205397 scopus 로고    scopus 로고
    • The structural basis of arf effector specificity: The crystal structure of arf6 in a complex with jip4
    • Isabet T, Montagnac G, Regazzoni K, et al. (2009). The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4. EMBO J 28: 2835-45
    • (2009) EMBO J , vol.28 , pp. 2835-2845
    • Isabet, T.1    Montagnac, G.2    Regazzoni, K.3
  • 53
    • 81355127367 scopus 로고    scopus 로고
    • Arl2-gtp and arl3-gtp regulate a gdi-like transport system for farnesylated cargo
    • Ismail SA, Chen Y-X, Rusinova A, et al. (2011). Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. Nat Chem Biol 7: 942-9
    • (2011) Nat Chem Biol , vol.7 , pp. 942-949
    • Ismail, S.A.1    Chen, Y.-X.2    Rusinova, A.3
  • 54
    • 77953884976 scopus 로고    scopus 로고
    • A large-scale conformational change couples membrane recruitment to cargo binding in the ap2 clathrin adaptor complex
    • Jackson LP, Kelly BT, McCoy AJ, et al. (2010). A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. Cell 141: 1220-9
    • (2010) Cell , vol.141 , pp. 1220-1229
    • Jackson, L.P.1    Kelly, B.T.2    McCoy, A.J.3
  • 55
    • 84865305431 scopus 로고    scopus 로고
    • Structures and mechanisms of vesicle coat components and multisubunit tethering complexes
    • Jackson LP, Kümmel D, Reinisch KM, Owen DJ. (2012). Structures and mechanisms of vesicle coat components and multisubunit tethering complexes. Curr Opin Cell Biol 24: 475-83
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 475-483
    • Jackson, L.P.1    Kümmel, D.2    Reinisch, K.M.3    Owen, D.J.4
  • 56
    • 0036223236 scopus 로고    scopus 로고
    • P21-Activated kinases: Three more join the pak
    • Jaffer ZM, Chernoff J. (2002). p21-Activated kinases: three more join the Pak. Int J Biochem Cell Biol 34: 713-7
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 713-717
    • Jaffer, Z.M.1    Chernoff, J.2
  • 57
    • 33746846072 scopus 로고    scopus 로고
    • Crystal structure of rab11 in complex with rab11 familyinteracting protein 2
    • Jagoe WN, Lindsay AJ, Read RJ, et al. (2006). Crystal structure of Rab11 in complex with Rab11 familYinteracting protein 2. Structure 14: 1273-83
    • (2006) Structure , vol.14 , pp. 1273-1283
    • Jagoe, W.N.1    Lindsay, A.J.2    Read, R.J.3
  • 58
    • 33845367647 scopus 로고    scopus 로고
    • Crystal structure of rac1 bound to its effector phospholipase c-beta 2
    • Jezyk M, Snyder J, Gershberg S, et al. (2006). Crystal structure of Rac1 bound to its effector phospholipase C-beta 2. Nat Struct Mol Biol 13: 1135-40
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 1135-1140
    • Jezyk, M.1    Snyder, J.2    Gershberg, S.3
  • 59
    • 21844443829 scopus 로고    scopus 로고
    • Exo84 and sec5 are competitive regulatory sec6/8 effectors to the rala gtpase
    • Jin R, Junutula JR, Matern HT, et al. (2005). Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase. EMBO J 24: 2064-74
    • (2005) EMBO J , vol.24 , pp. 2064-2074
    • Jin, R.1    Junutula, J.R.2    Matern, H.T.3
  • 60
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein par6 links par3 and atypical protein kinase c to cdc42
    • Joberty G, Petersen C, Gao L, Macara I. (2000). The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol 2: 531-9
    • (2000) Nat Cell Biol , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    MacAra, I.4
  • 61
    • 84897996949 scopus 로고    scopus 로고
    • Mechanism of irsp53 inhibition and combinatorial activation by cdc42 and downstream effectors
    • Kast DJ, Yang C, Disanza A, et al. (2014). Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nat Struct Mol Biol 21: 413-22
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 413-422
    • Kast, D.J.1    Yang, C.2    Disanza, A.3
  • 63
    • 84881414181 scopus 로고    scopus 로고
    • Structural biology of arf and rab gtpases' effector recruitment and specificity
    • Khan AR, Ménétrey J. (2013). Structural biology of Arf and Rab GTPases' effector recruitment and specificity. Struct/Fold Des 21: 1284-97
    • (2013) Struct/Fold des , vol.21 , pp. 1284-1297
    • Khan, A.R.1    Ménétrey, J.2
  • 64
    • 53049099181 scopus 로고    scopus 로고
    • Structural basis for the exclusive specificity of slac2-A/melanophilin for the rab27 gtpases
    • Kukimoto-Niino M, Sakamoto A, Kanno E, et al. (2008). Structural basis for the exclusive specificity of Slac2-A/melanophilin for the Rab27 GTPases. Structure 16: 1478-90
    • (2008) Structure , vol.16 , pp. 1478-1490
    • Kukimoto-Niino, M.1    Sakamoto, A.2    Kanno, E.3
  • 65
    • 84885353097 scopus 로고    scopus 로고
    • Structural and functional analysis of fip2 binding to the endosome-localised rab25 gtpase
    • Lall P, Horgan CP, Oda S, et al. (2013). Structural and functional analysis of FIP2 binding to the endosome-localised Rab25 GTPase. Biochim Biophys Acta 1834: 267990
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 267990
    • Lall, P.1    Horgan, C.P.2    Oda, S.3
  • 66
    • 58049213341 scopus 로고    scopus 로고
    • Specificity of interactions between mdia isoforms and rho proteins
    • Lammers M, Meyer S, Kuhlmann D, Wittinghofer A. (2008). Specificity of interactions between mDia isoforms and Rho proteins. J Biol Chem 283: 35236-46
    • (2008) J Biol Chem , vol.283 , pp. 35236-35246
    • Lammers, M.1    Meyer, S.2    Kuhlmann, D.3    Wittinghofer, A.4
  • 67
    • 0033635228 scopus 로고    scopus 로고
    • Structure of the tpr domain of p67phox in complex with rac.gtp
    • Lapouge K, Smith SJ, Walker PA, et al. (2000). Structure of the TPR domain of p67phox in complex with Rac.GTP. Mol Cell 6: 899-907
    • (2000) Mol Cell , vol.6 , pp. 899-907
    • Lapouge, K.1    Smith, S.J.2    Walker, P.A.3
  • 68
    • 0034602964 scopus 로고    scopus 로고
    • The fyve domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and rab5 binding critical role of this dual interaction for endosomal localization
    • Lawe DC, Patki V, Heller-Harrison R, et al. (2000). The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding critical role of this dual interaction for endosomal localization. J Biol Chem 275: 3699-705
    • (2000) J Biol Chem , vol.275 , pp. 3699-3705
    • Lawe, D.C.1    Patki, V.2    Heller-Harrison, R.3
  • 69
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by rangtp
    • Lee SJ, Matsuura Y, Liu SM, Stewart M. (2005). Structural basis for nuclear import complex dissociation by RanGTP. Nature 435: 693-6
    • (2005) Nature , vol.435 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 70
    • 0034604338 scopus 로고    scopus 로고
    • Structure of pak1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei M, Lu W, Meng W, et al. (2000). Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102: 387-97
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3
  • 71
    • 84862690469 scopus 로고    scopus 로고
    • Structural basis for the small g-protein-effector interaction of ras-related protein 1 (rap1) and the adaptor protein krev interaction trapped 1 (krit1
    • Li X, Zhang R, Draheim KM, et al. (2012). Structural basis for the small G-protein-effector interaction of Ras-related protein 1 (Rap1) and the adaptor protein Krev interaction trapped 1 (KRIT1). J Biol Chem 287: 22317-27
    • (2012) J Biol Chem , vol.287 , pp. 22317-22327
    • Li, X.1    Zhang, R.2    Draheim, K.M.3
  • 72
    • 0033532074 scopus 로고    scopus 로고
    • Thermodynamic and kinetic characterization of the interaction between the ras binding domain of af6 and members of the ras subfamily
    • Linnemann T, Geyer M, Jaitner B, et al. (1999). Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. J Biol Chem 274: 13556-62
    • (1999) J Biol Chem , vol.274 , pp. 13556-13562
    • Linnemann, T.1    Geyer, M.2    Jaitner, B.3
  • 73
    • 0037040885 scopus 로고    scopus 로고
    • The activation of ralgds can be achieved independently of its Ras binding domain. Implications of an activation mechanism in Ras effector specificity and signal distribution
    • Linnemann T, Kiel C, Herter P, Herrmann CA. (2002). The activation of RalGDS can be achieved independently of its Ras binding domain. Implications of an activation mechanism in Ras effector specificity and signal distribution. J Biol Chem 277: 7831-7
    • (2002) J Biol Chem , vol.277 , pp. 7831-7837
    • Linnemann, T.1    Kiel, C.2    Herter, P.3    Herrmann, C.A.4
  • 74
    • 0141856316 scopus 로고    scopus 로고
    • Interaction of arl1-gtp with grip domains recruits autoantigens golgin-97 and golgin-245/p230 onto the golgi
    • Lu L, Hong W. (2003). Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi. Mol Biol Cell 14: 3767-81
    • (2003) Mol Biol Cell , vol.14 , pp. 3767-3781
    • Lu, L.1    Hong, W.2
  • 75
    • 33748522337 scopus 로고    scopus 로고
    • Multilayer interactions determine the golgi localization of grip golgins
    • Lu L, Tai G, Wu M, et al. (2006). Multilayer interactions determine the Golgi localization of GRIP Golgins. Traffic 7: 1399-407
    • (2006) Traffic , vol.7 , pp. 1399-1407
    • Lu, L.1    Tai, G.2    Wu, M.3
  • 76
    • 0033231561 scopus 로고    scopus 로고
    • The structural basis of rho effector recognition revealed by the crystal structure of human rhoa complexed with the effector domain of pkn/prk1
    • Maesaki R, Ihara K, Shimizu T, et al. (1999). The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Mol Cell 4: 793-803
    • (1999) Mol Cell , vol.4 , pp. 793-803
    • Maesaki, R.1    Ihara, K.2    Shimizu, T.3
  • 77
    • 84861846404 scopus 로고    scopus 로고
    • Structural basis for arf6-mklp1 complex formation on the flemming body responsible for cytokinesis
    • Makyio H, Ohgi M, Takei T, et al. (2012). Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis. EMBO J 31: 2590-603
    • (2012) EMBO J , vol.31 , pp. 2590-2603
    • Makyio, H.1    Ohgi, M.2    Takei, T.3
  • 78
    • 84883352081 scopus 로고    scopus 로고
    • Structural basis for membrane recruitment and allosteric activation of cytohesin family arf gtpase exchange factors
    • Malaby AW, van den Berg B, Lambright DG. (2013). Structural basis for membrane recruitment and allosteric activation of cytohesin family Arf GTPase exchange factors. Proc Natl Acad Sci USA 110: 14213-18
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 14213-14218
    • Malaby, A.W.1    Van Den Berg, B.2    Lambright, D.G.3
  • 79
    • 0344885558 scopus 로고    scopus 로고
    • Structural evidence for feedback activation by ras-gtp of the ras-specific nucleotide exchange factor sos
    • Margarit S, Sondermann H, Hall BE, et al. (2003). Structural evidence for feedback activation by Ras-GTP of the Ras-specific nucleotide exchange factor SOS. Cell 112: 685-95
    • (2003) Cell , vol.112 , pp. 685-695
    • Margarit, S.1    Sondermann, H.2    Hall, B.E.3
  • 80
    • 11144257756 scopus 로고    scopus 로고
    • Structural basis for the assembly of a nuclear export complex
    • Matsuura Y, Stewart M. (2004). Structural basis for the assembly of a nuclear export complex. Nature 432: 872-7
    • (2004) Nature , vol.432 , pp. 872-877
    • Matsuura, Y.1    Stewart, M.2
  • 81
    • 3142523461 scopus 로고    scopus 로고
    • Cop and clathrin-coated vesicle budding: Different pathways, common approaches
    • Mcmahon HT, Mills IG. (2004). COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr Opin Cell Biol 16: 379-91
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 379-391
    • McMahon, H.T.1    Mills, I.G.2
  • 82
    • 34247244814 scopus 로고    scopus 로고
    • Structural basis for arf1-mediated recruitment of arhgap21 to golgi membranes
    • Ménétrey J, Perderiset M, Cicolari J, et al. (2007). Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes. EMBO J 26: 1953-62
    • (2007) EMBO J , vol.26 , pp. 1953-1962
    • Ménétrey, J.1    Perderiset, M.2    Cicolari, J.3
  • 83
    • 0034619847 scopus 로고    scopus 로고
    • Irsp53 is an essential intermediate between rac and wave in the regulation of membrane ruffling
    • Miki H, Yamaguchi H, Suetsugu S, Takenawa T. (2000). IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 408: 732-5
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 84
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn MV, Tong L, Devos AM, et al. (1990). Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 247: 939-45
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    Devos, A.M.3
  • 85
    • 77954649564 scopus 로고    scopus 로고
    • Structural basis for rab gtpase recognition and endosome tethering by the c2h2 zinc finger of early endosomal autoantigen 1 (eea1
    • Mishra A, Eathiraj S, Corvera S, Lambright DG. (2010). Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of Early Endosomal Autoantigen 1 (EEA1). Proc Natl Acad Sci 107: 10866-71
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 10866-10871
    • Mishra, A.1    Eathiraj, S.2    Corvera, S.3    Lambright, D.G.4
  • 87
    • 38349089896 scopus 로고    scopus 로고
    • The rac1 polybasic region is required for interaction with its effector prk1
    • Modha R, Campbell LJ, Nietlispach D, et al. (2008). The Rac1 polybasic region is required for interaction with its effector PRK1. J Biol Chem 283: 1492-500
    • (2008) J Biol Chem , vol.283 , pp. 1492-1500
    • Modha, R.1    Campbell, L.J.2    Nietlispach, D.3
  • 88
    • 66249108600 scopus 로고    scopus 로고
    • Crystal structure of the nuclear export receptor crm1 in complex with snurportin1 and rangtp
    • Monecke T, Guttler T, Neumann P, et al. (2009). Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP. Science 324: 1087-91
    • (2009) Science , vol.324 , pp. 1087-1091
    • Monecke, T.1    Guttler, T.2    Neumann, P.3
  • 89
    • 0034018304 scopus 로고    scopus 로고
    • Structure of cdc42 bound to the gtpase binding domain of pak
    • Morreale A, Venkatesan M, MotThR, et al. (2000). Structure of Cdc42 bound to the GTPase binding domain of PAK. Nat Struct Biol 7: 384-8
    • (2000) Nat Struct Biol , vol.7 , pp. 384-388
    • Morreale, A.1    Venkatesan, M.2    Motth, R.3
  • 90
    • 0037699926 scopus 로고    scopus 로고
    • Structure of the gtpase-binding domain of sec5 and elucidation of its ral binding site
    • MotThR, Nietlispach D, Hopkins LJ, et al. (2003). Structure of the GTPase-binding domain of Sec5 and elucidation of its Ral binding site. J Biol Chem 278: 17053-9
    • (2003) J Biol Chem , vol.278 , pp. 17053-17059
    • Motth, R.1    Nietlispach, D.2    Hopkins, L.J.3
  • 91
    • 0033609335 scopus 로고    scopus 로고
    • Structure of the small g protein cdc42 bound to the gtpase-binding domain of ack
    • MotThR, Owen D, Nietlispach D, et al. (1999). Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK. Nature 399: 384-8
    • (1999) Nature , vol.399 , pp. 384-388
    • Motth, R.1    Owen, D.2    Nietlispach, D.3
  • 92
    • 40049103757 scopus 로고    scopus 로고
    • Bart is essential for nuclear retention of stat3
    • Muromoto R, Sekine Y, Imoto S, et al. (2008). BART is essential for nuclear retention of STAT3. Int Immunol 20: 395-403
    • (2008) Int Immunol , vol.20 , pp. 395-403
    • Muromoto, R.1    Sekine, Y.2    Imoto, S.3
  • 93
    • 84864083155 scopus 로고    scopus 로고
    • Structural basis for membrane binding specificity of the bin/amphiphysin/rvs (bar) domain of arfaptin-2 determined by arl1 gtpase
    • Nakamura K, Man Z, Xie Y, et al. (2012). Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase. J Biol Chem 287: 25478-89
    • (2012) J Biol Chem , vol.287 , pp. 25478-25489
    • Nakamura, K.1    Man, Z.2    Xie, Y.3
  • 94
    • 0029107760 scopus 로고
    • The 4a crystal structure of the ras-binding domain of the serine/threonine kinase c-raf1 in complex with rapla and a gtp analogue
    • Nassar N, Horn G, Herrmann CA, et al. (1995). The 4A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogue. Nature 375: 554-60
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.A.3
  • 95
    • 0029745645 scopus 로고    scopus 로고
    • Ras/rap effector specificity determined by charge reversal
    • Nassar N, Horn G, Herrmann CA, et al. (1996). Ras/Rap effector specificity determined by charge reversal. Nat Struct Biol 3: 723-9
    • (1996) Nat Struct Biol , vol.3 , pp. 723-729
    • Nassar, N.1    Horn, G.2    Herrmann, C.A.3
  • 96
    • 70849093653 scopus 로고    scopus 로고
    • A high-resolution structure of the pre-microrna nuclear export machinery
    • Okada C, Yamashita E, Lee SJ, et al. (2009). A high-resolution structure of the pre-microRNA nuclear export machinery. Science 326: 1275-9
    • (2009) Science , vol.326 , pp. 1275-1279
    • Okada, C.1    Yamashita, E.2    Lee, S.J.3
  • 97
    • 1842487379 scopus 로고    scopus 로고
    • Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism
    • O'Neal CJ, Amaya EI, Jobling MG, et al. (2004). Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. Biochemistry 43: 3772-82
    • (2004) Biochemistry , vol.43 , pp. 3772-3782
    • O'neal, C.J.1    Amaya, E.I.2    Jobling, M.G.3
  • 98
    • 23644438026 scopus 로고    scopus 로고
    • Structural basis for the activation of cholera toxin by human arf6-gtp
    • O'Neal CJ, Jobling MG, Holmes RK, Hol W. (2005). Structural basis for the activation of cholera toxin by human ARF6-GTP. Science 309: 1093-6
    • (2005) Science , vol.309 , pp. 1093-1096
    • O'neal, C.J.1    Jobling, M.G.2    Holmes, R.K.3    Hol, W.4
  • 99
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of Rabphilin-3A
    • Ostermeier C, Brunger A. (1999). Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of Rabphilin-3A. Cell 96: 363-74
    • (1999) Cell , vol.96 , pp. 363-374
    • Ostermeier, C.1    Brunger, A.2
  • 100
    • 0348010318 scopus 로고    scopus 로고
    • Molecular dissection of the interaction between the small g proteins rac1 and rhoa and protein kinase c-related kinase 1 (prk1
    • Owen D, Lowe P, Nietlispach D, et al. (2003). Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1). J Biol Chem 278: 50578-87
    • (2003) J Biol Chem , vol.278 , pp. 50578-50587
    • Owen, D.1    Lowe, P.2    Nietlispach, D.3
  • 101
    • 0034673107 scopus 로고    scopus 로고
    • Residues in cdc42 that specify binding to individual crib effector proteins
    • Owen D, MotThR, Laue E, Lowe P. (2000). Residues in Cdc42 that specify binding to individual CRIB effector proteins. Biochemistry 39: 1243-50
    • (2000) Biochemistry , vol.39 , pp. 1243-1250
    • Owen, D.1    Motth, R.2    Laue, E.3    Lowe, P.4
  • 102
    • 0033635157 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase g
    • Pacold ME, Suire S, Perisic O, et al. (2000). Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase g. Cell 103: 931-44
    • (2000) Cell , vol.103 , pp. 931-944
    • Pacold, M.E.1    Suire, S.2    Perisic, O.3
  • 103
    • 0024463212 scopus 로고
    • Structure of the guaninenucleotide-binding domain of the ha-ras oncogene product p21 in the triphosphate conformation
    • Pai E, Kabsch W, Krengel U, et al. (1989). Structure of the guaninenucleotide-binding domain of the Ha-Ras oncogene product P21 in the triphosphate conformation. Nature 341: 209-14
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.1    Kabsch, W.2    Krengel, U.3
  • 104
    • 0025310575 scopus 로고
    • Refined crystalstructure of the triphosphate conformation of h-ras p21 at 1.35 a resolution-implications for the mechanism of gtp hydrolysis
    • Pai EF, Krengel U, Petsko GA, et al. (1990). Refined crystalstructure of the triphosphate conformation of H-Ras P21 at 1.35 a resolution-implications for the mechanism of Gtp hydrolysis. EMBO J 9: 2351-9
    • (1990) EMBO J , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3
  • 105
    • 0242266897 scopus 로고    scopus 로고
    • Structural basis for arl1-dependent targeting of homodimeric grip domains to the golgi apparatus
    • Panic B, Perisic O, Veprintsev DB, et al. (2003). Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus. Mol Cell 12: 863-74
    • (2003) Mol Cell , vol.12 , pp. 863-874
    • Panic, B.1    Perisic, O.2    Veprintsev, D.B.3
  • 106
    • 84859501836 scopus 로고    scopus 로고
    • Inositol 5-phosphatases: Insights from the lowe syndrome protein ocrl
    • Pirruccello M, de Camilli P. (2012). Inositol 5-phosphatases: insights from the Lowe syndrome protein OCRL. Trends Biochem Sci 37: 134-43
    • (2012) Trends Biochem Sci , vol.37 , pp. 134-143
    • Pirruccello, M.1    De Camilli, P.2
  • 107
    • 77954762892 scopus 로고    scopus 로고
    • The small gtpase arl2 is required for cytokinesis in trypanosomabrucei
    • Price HP, Peltan A, Stark M, Smith DF. (2010). The small GTPase ARL2 is required for cytokinesis in TrypanosomAbrucei. Mol Biochem Parasitol 173: 123-31
    • (2010) Mol Biochem Parasitol , vol.173 , pp. 123-131
    • Price, H.P.1    Peltan, A.2    Stark, M.3    Smith, D.F.4
  • 108
    • 84890825644 scopus 로고    scopus 로고
    • Structural basis of myosin v rab gtpase-dependent cargo recognition
    • Pylypenko O, Attanda W, Gauquelin C, et al. (2013). Structural basis of myosin V Rab GTPase-dependent cargo recognition. Proc Natl Acad Sci USA 110: 20443-8
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 20443-20448
    • Pylypenko, O.1    Attanda, W.2    Gauquelin, C.3
  • 109
    • 84881510335 scopus 로고    scopus 로고
    • Structural basis for the interaction of the adaptor protein Grb14 with activated Ras W
    • Qamra R, Hubbard SR. (2013). Structural basis for the interaction of the adaptor protein Grb14 with activated Ras W. Xu, ed. PLoS One 8: e72473
    • (2013) Xu, Ed. PLoS One , vol.8 , pp. e72473
    • Qamra, R.1    Hubbard, S.R.2
  • 110
    • 0031460029 scopus 로고    scopus 로고
    • Pdz domain proteins: Scaffolds for signaling complexes
    • Ranganathan R, Ross EM. (1997). PDZ domain proteins: scaffolds for signaling complexes. Curr Biol 7: R770-3
    • (1997) Curr Biol 7: R770-3
    • Ranganathan, R.1    Ross, E.M.2
  • 111
    • 58149181482 scopus 로고    scopus 로고
    • Structural basis for recruitment of rab6-interacting protein 1 to golgi via a run domain
    • Recacha R, Boulet A, Jollivet F, et al. (2009). Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain. Struct/Fold Des 17: 21-30
    • (2009) Struct/Fold des , vol.17 , pp. 21-30
    • Recacha, R.1    Boulet, A.2    Jollivet, F.3
  • 112
    • 84874033425 scopus 로고    scopus 로고
    • Structural basis for recruitment and activation of the ap-1 clathrin adaptor complex by arf1
    • Ren X, Farías GG, Canagarajah BJ, et al. (2013). Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. Cell 152: 755-67
    • (2013) Cell , vol.152 , pp. 755-767
    • Ren, X.1    Farías, G.G.2    Canagarajah, B.J.3
  • 113
    • 0030911052 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-oh kinase in cell transformation and control of the actin cytoskeleton by ras
    • Rodriguez-Viciana P, Warne PH, Khwaja A, et al. (1997). Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras. Cell 89: 457-67
    • (1997) Cell , vol.89 , pp. 457-467
    • Rodriguez-Viciana, P.1    Warne, P.H.2    Khwaja, A.3
  • 114
    • 84859967413 scopus 로고    scopus 로고
    • The ras protein superfamily: Evolutionary tree and role of conserved amino acids
    • Rojas AM, Fuentes G, Rausell A, Valencia A. (2012). The Ras protein superfamily: evolutionary tree and role of conserved amino acids. J Cell Biol 196: 189-201
    • (2012) J Cell Biol , vol.196 , pp. 189-201
    • Rojas, A.M.1    Fuentes, G.2    Rausell, A.3    Valencia, A.4
  • 115
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between rho and mammalian dia
    • Rose R, Weyand M, Lammers M, et al. (2005). Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435: 513-18
    • (2005) Nature , vol.435 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3
  • 116
    • 0032473351 scopus 로고    scopus 로고
    • Rhoa effector mutants reveal distincteffector pathways for cytoskeletal reorganization, srf activation and transformation
    • Sahai E, Alberts AS, Treisman R. (1998). RhoA effector mutants reveal distincteffector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J 17: 1350-61
    • (1998) EMBO J , vol.17 , pp. 1350-1361
    • Sahai, E.1    Alberts, A.S.2    Treisman, R.3
  • 117
    • 84870799578 scopus 로고    scopus 로고
    • The binding of varp to vamp7 traps vamp7 in a closed, fusogenicallyinactive conformation
    • Schaefer IB, Hesketh GG, Bright NA, et al. (2012). The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenicallYinactive conformation. Nat Struct Mol Biol 19: 1300-9
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1300-1309
    • Schaefer, I.B.1    Hesketh, G.G.2    Bright, N.A.3
  • 118
    • 0035184435 scopus 로고    scopus 로고
    • The ras-byr2rbd complex: Structural basis for ras effector recognition in yeast
    • Scheffzek K, Grunewald P, Wohlgemuth S, et al. (2001). The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast. Struct/Fold Des 9: 1043-50
    • (2001) Struct/Fold des , vol.9 , pp. 1043-1050
    • Scheffzek, K.1    Grunewald, P.2    Wohlgemuth, S.3
  • 119
    • 84864607612 scopus 로고    scopus 로고
    • Pleckstrin homology (ph) like domains -versatile modules in protein-protein interaction platforms
    • Scheffzek K, Welti S. (2012). Pleckstrin homology (PH) like domains -versatile modules in protein-protein interaction platforms. FEBS Lett 586: 2662-73
    • (2012) FEBS Lett , vol.586 , pp. 2662-2673
    • Scheffzek, K.1    Welti, S.2
  • 121
    • 0036156441 scopus 로고    scopus 로고
    • Arl2 and bartenter mitochondria and bind the adenine nucleotide transporter
    • Sharer JD, Shern JF, Van Valkenburgh H, et al. (2002). ARL2 and BARTenter mitochondria and bind the adenine nucleotide transporter. Mol Biol Cell 13: 71-83
    • (2002) Mol Biol Cell , vol.13 , pp. 71-83
    • Sharer, J.D.1    Shern, J.F.2    Van Valkenburgh, H.3
  • 122
    • 0037407395 scopus 로고    scopus 로고
    • Molecular mechanism of membrane recruitment of ggaby arf in lysosomal protein transport
    • Shiba T, Kawasaki M, Takatsu H, et al. (2003). Molecular mechanism of membrane recruitment of GGAby ARF in lysosomal protein transport. Nat Struct Biol 10: 386-93
    • (2003) Nat Struct Biol , vol.10 , pp. 386-393
    • Shiba, T.1    Kawasaki, M.2    Takatsu, H.3
  • 123
    • 33750365184 scopus 로고    scopus 로고
    • Structural basis for rab11-dependent membrane recruitment of a family of rab11-interacting protein 3 (fip3)/arfophilin-1
    • Shiba T, Koga H, Shin H-W, et al. (2006). Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1. Proc Natl Acad Sci USA 103: 15416-21
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15416-15421
    • Shiba, T.1    Koga, H.2    Shin, H.-W.3
  • 124
    • 84875608683 scopus 로고    scopus 로고
    • Seminars in cell & developmental biology
    • Siebold C, Jones EY. (2013). Seminars in cell & developmental biology. Semin Cell Dev Biol 24: 139-45
    • (2013) Semin Cell Dev Biol , vol.24 , pp. 139-145
    • Siebold, C.1    Jones, E.Y.2
  • 125
    • 0038756655 scopus 로고    scopus 로고
    • The pleckstrin homology domain of phospholipase c-2 as an effector site for rac
    • Snyder JT, Singer AU, Wing MR, et al. (2003). The Pleckstrin homology domain of phospholipase C-2 as an effector site for Rac. J Biol Chem 278: 21099-104
    • (2003) J Biol Chem , vol.278 , pp. 21099-21104
    • Snyder, J.T.1    Singer, A.U.2    Wing, M.R.3
  • 126
    • 84878935417 scopus 로고    scopus 로고
    • Arf gtpase regulation through cascade mechanisms and positive feedback loops
    • Stalder D, Antonny B. (2013). Arf GTPase regulation through cascade mechanisms and positive feedback loops. FEBS Lett 587: 2028-35
    • (2013) FEBS Lett , vol.587 , pp. 2028-2035
    • Stalder, D.1    Antonny, B.2
  • 127
    • 47949124438 scopus 로고    scopus 로고
    • Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II
    • Stieglitz B, Bee C, Schwarz D, et al. (2008). Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II. EMBO J 27: 1995-2005
    • (2008) EMBO J , vol.27 , pp. 1995-2005
    • Stieglitz, B.1    Bee, C.2    Schwarz, D.3
  • 128
    • 0037446843 scopus 로고    scopus 로고
    • Structure of the gat domain of human gga1: A syntaxin amino-Terminal domain fold in an endosomal trafficking adaptor
    • Suer S, Misra S, Saidi LF, Hurley JH. (2003). Structure of the GAT domain of human GGA1: a syntaxin amino-Terminal domain fold in an endosomal trafficking adaptor. Proc Natl Acad Sci USA 100: 4451-6
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4451-4456
    • Suer, S.1    Misra, S.2    Saidi, L.F.3    Hurley, J.H.4
  • 129
    • 0032491205 scopus 로고    scopus 로고
    • Transient kinetic studies on the interaction of ras and the ras-binding domain of c-raf-1 reveal rapid equilibration of the complex
    • Sydor J, Engelhard M, Wittinghofer A, et al. (1998). Transient kinetic studies on the interaction of ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex. Biochemistry 37: 14292-9
    • (1998) Biochemistry , vol.37 , pp. 14292-14299
    • Sydor, J.1    Engelhard, M.2    Wittinghofer, A.3
  • 131
    • 0035837426 scopus 로고    scopus 로고
    • The structural basis of arfaptin-mediated cross-Talk between rac and arf signalling pathways
    • Tarricone C, Xiao B, Justin N, et al. (2001). The structural basis of Arfaptin-mediated cross-Talk between Rac and Arf signalling pathways. Nature 411: 215-19
    • (2001) Nature , vol.411 , pp. 215-219
    • Tarricone, C.1    Xiao, B.2    Justin, N.3
  • 132
    • 37549021146 scopus 로고    scopus 로고
    • Binding of rac1, rnd1, and rhod to a novel rho gtpase interaction motif destabilizes dimerization of the plexin-b1 effector domain
    • Tong Y, Chugha P, Hota PK, et al. (2007). Binding of Rac1, Rnd1, and RhoD to a Novel Rho GTPase interaction motif destabilizes dimerization of the Plexin-B1 effector domain. J Biol Chem 282: 37215-24
    • (2007) J Biol Chem , vol.282 , pp. 37215-37224
    • Tong, Y.1    Chugha, P.2    Hota, P.K.3
  • 133
    • 72149087958 scopus 로고    scopus 로고
    • Structure and function of the intracellular region of the plexin-b1 transmembrane receptor
    • Tong Y, Hota PK, Penachioni JY, et al. (2009). Structure and function of the intracellular region of the Plexin-B1 transmembrane receptor. J Biol Chem 284: 35962-72
    • (2009) J Biol Chem , vol.284 , pp. 35962-35972
    • Tong, Y.1    Hota, P.K.2    Penachioni, J.Y.3
  • 134
    • 0032898066 scopus 로고    scopus 로고
    • Structural and biochemical analysis of ras-effector signaling via ralgds
    • Vetter I, Linnemann T, Wohlgemuth S, et al. (1999a). Structural and biochemical analysis of Ras-effector signaling via RalGDS. FEBS Lett 451: 175-80
    • (1999) FEBS Lett , vol.451 , pp. 175-180
    • Vetter, I.1    Linnemann, T.2    Wohlgemuth, S.3
  • 135
    • 0035834388 scopus 로고    scopus 로고
    • Signal transduction-The guanine nucleotide-binding switch in three dimensions
    • Vetter I, Wittinghofer A. (2001). Signal transduction-The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.1    Wittinghofer, A.2
  • 136
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the ranimportin beta interaction at 5 angstrom resolution
    • Vetter IR, Arndt A, Kutay U, et al. (1999b). Structural view of the Ranimportin beta interaction at 5 angstrom resolution. Cell 97: 635-46
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3
  • 137
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a ranbinding domain complexed with ran bound to a gtp analogue: Implications for nuclear transport
    • Vetter IR, Nowak C, Nishimoto T, et al. (1999c). Structure of a Ranbinding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature 398: 39-46
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3
  • 138
    • 0027250250 scopus 로고
    • Mammalian ras interacts directly with the serine/threonine kinase raf
    • Vojtek AB, Hollenberg SM, Cooper JA. (1993). Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205-14
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 139
    • 57649210150 scopus 로고    scopus 로고
    • Rac regulates its effector phospholipase c 2 through interaction with a split pleckstrin homology domain
    • Walliser C, Retlich M, Harris R, et al. (2008). Rac regulates its effector phospholipase C 2 through interaction with a split Pleckstrin homology domain. J Biol Chem 283: 30351-62
    • (2008) J Biol Chem , vol.283 , pp. 30351-30362
    • Walliser, C.1    Retlich, M.2    Harris, R.3
  • 140
    • 79960432633 scopus 로고    scopus 로고
    • Structural basis of rnd1 binding to plexin rho gtpase binding domains (rbds
    • Wang H, Hota PK, Tong Y, et al. (2011). Structural basis of Rnd1 binding to Plexin Rho GTPase Binding Domains (RBDs). J Biol Chem 286: 26093-106
    • (2011) J Biol Chem , vol.286 , pp. 26093-26106
    • Wang, H.1    Hota, P.K.2    Tong, Y.3
  • 141
    • 84856070985 scopus 로고    scopus 로고
    • Plexins are gtpaseactivating proteins for rap and are activated byinduced dimerization
    • 5: ra6
    • Wang Y, He H, Srivastava N, et al. (2012). Plexins are GTPaseactivating proteins for Rap and are activated bYinduced dimerization. Sci Signal 5: ra6
    • (2012) Sci Signal
    • Wang, Y.1    He, H.2    Srivastava, N.3
  • 142
    • 33744962988 scopus 로고    scopus 로고
    • Molecular dissection of rab11 binding from coiled-coil formation in the rab11-fip2 c-Terminal domain
    • Wei J, Fain S, Harrison C, et al. (2006). Molecular dissection of Rab11 binding from coiled-coil formation in the Rab11-FIP2 C-Terminal domain. Biochemistry 45: 6826-34
    • (2006) Biochemistry , vol.45 , pp. 6826-6834
    • Wei, J.1    Fain, S.2    Harrison, C.3
  • 143
    • 0028948382 scopus 로고
    • Multiple ras functions can contribute to mammalian cell transformation
    • White MA. (1995). Multiple ras functions can contribute to mammalian cell transformation. Cell 80: 533-41
    • (1995) Cell , vol.80 , pp. 533-541
    • White, M.A.1
  • 144
    • 0842269776 scopus 로고    scopus 로고
    • Structural basis for recruitment of grip domain golgin-245 by small gtpase arl1
    • Wu M, Lu L, Hong W, Song H. (2004). Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1. Nat Struct Mol Biol 11: 86-94
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 86-94
    • Wu, M.1    Lu, L.2    Hong, W.3    Song, H.4
  • 145
    • 18444381428 scopus 로고    scopus 로고
    • Structural basis for recruitment of rilp by small gtpase rab7
    • Wu MS, Wang TL, Loh E, et al. (2005). Structural basis for recruitment of RILP by small GTPase Rab7. EMBO J 24: 1491-501
    • (2005) EMBO J , vol.24 , pp. 1491-1501
    • Wu, M.S.1    Wang, T.L.2    Loh, E.3
  • 146
    • 84869146656 scopus 로고    scopus 로고
    • Rap1-interacting adapter molecule (riam) associates with the plasma membrane via a proximity detector
    • Wynne JP, Wu J, Su W, et al. (2012). Rap1-interacting adapter molecule (RIAM) associates with the plasma membrane via a proximity detector. J Cell Biol 199: 317-30
    • (2012) J Cell Biol , vol.199 , pp. 317-330
    • Wynne, J.P.1    Wu, J.2    Su, W.3
  • 147
    • 76349093365 scopus 로고    scopus 로고
    • Structural basis for the rho-And phosphoinositide-dependent localization of the exocyst subunit sec3
    • Yamashita M, Kurokawa K, Sato Y, et al. (2010). Structural basis for the Rho-And phosphoinositide-dependent localization of the exocyst subunit Sec3. Nat Struct Mol Biol 17: 180-6
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 180-186
    • Yamashita, M.1    Kurokawa, K.2    Sato, Y.3
  • 148
    • 84856760126 scopus 로고    scopus 로고
    • A structure-based mechanism for arf1-dependent recruitment of coatomer to membranes
    • Yu X, Breitman M, Goldberg J. (2012). A structure-based mechanism for Arf1-dependent recruitment of coatomer to membranes. Cell 148: 530-42
    • (2012) Cell , vol.148 , pp. 530-542
    • Yu, X.1    Breitman, M.2    Goldberg, J.3
  • 149
    • 84899677046 scopus 로고    scopus 로고
    • The structure of rap1 in complex with riam reveals specificity determinants and recruitment mechanism
    • Zhang H, Chang Y-C, Brennan ML, (2014a). The structure of Rap1 in complex with RIAM reveals specificity determinants and recruitment mechanism. J Mol Cell Biol 6: 128-39
    • (2014) J Mol Cell Biol , vol.6 , pp. 128-139
    • Zhang, H.1    Chang, Y.-C.2    Brennan, M.L.3    Wu, J.4
  • 150
    • 0029161099 scopus 로고
    • The threedimensional crystal structure of cholera toxin
    • Zhang RG, Scott DL, Westbrook ML, et al. (1995). The threedimensional crystal structure of cholera toxin. J Mol Biol 251: 563-73
    • (1995) J Mol Biol , vol.251 , pp. 563-573
    • Zhang, R.G.1    Scott, D.L.2    Westbrook, M.L.3
  • 151
    • 64049104591 scopus 로고    scopus 로고
    • Crystal structure of the arl2-gtp-bart complex reveals a novel recognition and binding mode of small gtpase with effector
    • Zhang T, Li S, Zhang Y, et al. (2009). Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector. Struct/Fold Des 17: 602-10
    • (2009) Struct/Fold des , vol.17 , pp. 602-610
    • Zhang, T.1    Li, S.2    Zhang, Y.3
  • 152
    • 33645729581 scopus 로고    scopus 로고
    • Varp is a rab21 guanine nucleotide exchange factor and regulates endosome dynamics
    • Zhang X, He X, Fu X-Y, Chang Z. (2006). Varp is a Rab21 guanine nucleotide exchange factor and regulates endosome dynamics. J Cell Sci 119: 1053-62
    • (2006) J Cell Sci , vol.119 , pp. 1053-1062
    • Zhang, X.1    He, X.2    Fu, X.-Y.3    Chang, Z.4
  • 154
    • 0031948850 scopus 로고    scopus 로고
    • A conserved negative regulatory region in alpha pak: Inhibition of pak kinases reveals their morphological roles downstream of cdc42 and rac1
    • Zhao Z, Manser E, Chen X, et al. (1998). A conserved negative regulatory region in alpha PAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1. Mol Cell Biol 18: 2153-63
    • (1998) Mol Cell Biol , vol.18 , pp. 2153-2163
    • Zhao, Z.1    Manser, E.2    Chen, X.3
  • 155
    • 0038010644 scopus 로고    scopus 로고
    • Crystal structure of the human gga1 gat domain
    • Zhu G, Zhai P, He X, et al. (2003). Crystal structure of the human GGA1 GAT domain. Biochemistry 42: 6392-9
    • (2003) Biochemistry , vol.42 , pp. 6392-6399
    • Zhu, G.1    Zhai, P.2    He, X.3
  • 156
    • 4744369353 scopus 로고    scopus 로고
    • Structural basis of rab5-rabaptin5 interaction in endocytosis
    • Zhu G, Zhai P, Liu J, et al. (2004). Structural basis of Rab5-Rabaptin5 interaction in endocytosis. Nat Struct Mol Biol 11: 975-83
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 975-983
    • Zhu, G.1    Zhai, P.2    Liu, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.