메뉴 건너뛰기




Volumn 5, Issue 6, 2010, Pages

The minimal autoinhibited unit of the guanine nucleotide exchange factor intersectin

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; INTERSECTIN; INTERSECTIN 1L; PROTEIN CDC42; PROTEIN SH3; UNCLASSIFIED DRUG; GUANINE NUCLEOTIDE EXCHANGE FACTOR; INTERSECTIN 1; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 77955291246     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0011291     Document Type: Article
Times cited : (21)

References (67)
  • 1
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: Turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman KL, Der CJ, Sondek J (2005) GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat Rev Mol Cell Biol 6: 167-180.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 2
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe AB, Hall A (2005) Rho GTPases: biochemistry and biology. Annu Rev Cell Dev Biol 21: 247-269.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 3
    • 0037138364 scopus 로고    scopus 로고
    • Signaling to the Rho GTPases: Networking with the DH domain
    • Hoffman GR, Cerione RA (2002) Signaling to the Rho GTPases: networking with the DH domain. FEBS Lett 513: 85-91.
    • (2002) FEBS Lett , vol.513 , pp. 85-91
    • Hoffman, G.R.1    Cerione, R.A.2
  • 4
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L, D'Souza-Schorey C (1997) Rho GTPases and signaling networks. Genes Dev 11: 2295-2322.
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • van Aelst, L.1    D'souza-Schorey, C.2
  • 6
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
    • Worthylake DK, Rossman KL, Sondek J (2000) Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature 408: 682-688.
    • (2000) Nature , vol.408 , pp. 682-688
    • Worthylake, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 7
    • 0036263915 scopus 로고    scopus 로고
    • Structural basis for the selective activation of Rho GTPases by Dbl exchange factors
    • Snyder JT, Worthylake DK, Rossman KL, Betts L, Pruitt WM, et al. (2002) Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat Struct Biol 9: 468-475.
    • (2002) Nat Struct Biol , vol.9 , pp. 468-475
    • Snyder, J.T.1    Worthylake, D.K.2    Rossman, K.L.3    Betts, L.4    Pruitt, W.M.5
  • 8
    • 0037086652 scopus 로고    scopus 로고
    • A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange
    • Rossman KL, Worthylake DK, Snyder JT, Siderovski DP, Campbell SL, et al. (2002) A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange. Embo J 21: 1315-1326.
    • (2002) Embo J , vol.21 , pp. 1315-1326
    • Rossman, K.L.1    Worthylake, D.K.2    Snyder, J.T.3    Siderovski, D.P.4    Campbell, S.L.5
  • 9
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop AL, Hall A (2000) Rho GTPases and their effector proteins. Biochem J 348 Pt 2: 241-255.
    • (2000) Biochem J 348 Pt , vol.2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 11
    • 0025758833 scopus 로고
    • A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr
    • Ron D, Zannini M, Lewis M, Wickner RB, Hunt LT, et al. (1991) A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr. New Biol 3: 372-379.
    • (1991) New Biol , vol.3 , pp. 372-379
    • Ron, D.1    Zannini, M.2    Lewis, M.3    Wickner, R.B.4    Hunt, L.T.5
  • 12
    • 0027958423 scopus 로고
    • Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product
    • Hart MJ, Eva A, Zangrilli D, Aaronson SA, Evans T, et al. (1994) Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J Biol Chem 269: 62-65.
    • (1994) J Biol Chem , vol.269 , pp. 62-65
    • Hart, M.J.1    Eva, A.2    Zangrilli, D.3    Aaronson, S.A.4    Evans, T.5
  • 13
    • 0034269240 scopus 로고    scopus 로고
    • Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation
    • Aghazadeh B, Lowry WE, Huang XY, Rosen MK (2000) Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation. Cell 102: 625-633.
    • (2000) Cell , vol.102 , pp. 625-633
    • Aghazadeh, B.1    Lowry, W.E.2    Huang, X.Y.3    Rosen, M.K.4
  • 14
    • 0032538295 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio
    • Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, et al. (1998) NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio. Cell 95: 269-277.
    • (1998) Cell , vol.95 , pp. 269-277
    • Liu, X.1    Wang, H.2    Eberstadt, M.3    Schnuchel, A.4    Olejniczak, E.T.5
  • 15
    • 0033179296 scopus 로고    scopus 로고
    • GEFs: Structural basis for their activation of small GTP-binding proteins
    • Cherfils J, Chardin P (1999) GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem Sci 24: 306-311.
    • (1999) Trends Biochem Sci , vol.24 , pp. 306-311
    • Cherfils, J.1    Chardin, P.2
  • 17
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB (1995) Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83: 1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 18
    • 0035824624 scopus 로고    scopus 로고
    • Quantitative analysis of the effect of phosphoinositide interactions on the function of Dbl family proteins
    • Snyder JT, Rossman KL, Baumeister MA, Pruitt WM, Siderovski DP, et al. (2001) Quantitative analysis of the effect of phosphoinositide interactions on the function of Dbl family proteins. J Biol Chem 276: 45868-45875.
    • (2001) J Biol Chem , vol.276 , pp. 45868-45875
    • Snyder, J.T.1    Rossman, K.L.2    Baumeister, M.A.3    Pruitt, W.M.4    Siderovski, D.P.5
  • 19
    • 0037986310 scopus 로고    scopus 로고
    • Loss of phosphatidylinositol 3-phosphate binding by the C-terminal Tiam-1 pleckstrin homology domain prevents in vivo Rac1 activation without affecting membrane targeting
    • Baumeister MA, Martinu L, Rossman KL, Sondek J, Lemmon MA, et al. (2003) Loss of phosphatidylinositol 3-phosphate binding by the C-terminal Tiam-1 pleckstrin homology domain prevents in vivo Rac1 activation without affecting membrane targeting. J Biol Chem 278: 11457-11464.
    • (2003) J Biol Chem , vol.278 , pp. 11457-11464
    • Baumeister, M.A.1    Martinu, L.2    Rossman, K.L.3    Sondek, J.4    Lemmon, M.A.5
  • 20
    • 0030723206 scopus 로고    scopus 로고
    • Targeting of Tiam1 to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain
    • Stam JC, Sander EE, Michiels F, van Leeuwen FN, Kain HE, et al. (1997) Targeting of Tiam1 to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain. J Biol Chem 272: 28447-28454.
    • (1997) J Biol Chem , vol.272 , pp. 28447-28454
    • Stam, J.C.1    Sander, E.E.2    Michiels, F.3    van Leeuwen, F.N.4    Kain, H.E.5
  • 21
    • 0032584210 scopus 로고    scopus 로고
    • The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution
    • Liu Y, Hart PJ, Schlunegger MP, Eisenberg D (1998) The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution. Proc Natl Acad Sci U S A 95: 3437-3442.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 3437-3442
    • Liu, Y.1    Hart, P.J.2    Schlunegger, M.P.3    Eisenberg, D.4
  • 22
    • 0033777135 scopus 로고    scopus 로고
    • Bacterial expressed DH and DH/PH domains
    • Rossman KL, Campbell SL (2000) Bacterial expressed DH and DH/PH domains. Methods Enzymol 325: 25-38.
    • (2000) Methods Enzymol , vol.325 , pp. 25-38
    • Rossman, K.L.1    Campbell, S.L.2
  • 23
    • 8744317101 scopus 로고    scopus 로고
    • Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor
    • Kristelly R, Gao G, Tesmer JJ (2004) Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor. J Biol Chem 279: 47352-47362.
    • (2004) J Biol Chem , vol.279 , pp. 47352-47362
    • Kristelly, R.1    Gao, G.2    Tesmer, J.J.3
  • 24
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han J, Luby-Phelps K, Das B, Shu X, Xia Y, et al. (1998) Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 279: 558-560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3    Shu, X.4    Xia, Y.5
  • 25
    • 0034685772 scopus 로고    scopus 로고
    • Control of intramolecular interactions between the pleckstrin homology and Dbl homology domains of Vav and Sos1 regulates Rac binding
    • Das B, Shu X, Day GJ, Han J, Krishna UM, et al. (2000) Control of intramolecular interactions between the pleckstrin homology and Dbl homology domains of Vav and Sos1 regulates Rac binding. J Biol Chem 275: 15074-15081.
    • (2000) J Biol Chem , vol.275 , pp. 15074-15081
    • Das, B.1    Shu, X.2    Day, G.J.3    Han, J.4    Krishna, U.M.5
  • 26
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos
    • Nimnual AS, Yatsula BA, Bar-Sagi D (1998) Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos. Science 279: 560-563.
    • (1998) Science , vol.279 , pp. 560-563
    • Nimnual, A.S.1    Yatsula, B.A.2    Bar-Sagi, D.3
  • 27
    • 7044226349 scopus 로고    scopus 로고
    • Structural analysis of autoinhibition in the Ras activator Son of sevenless
    • Sondermann H, Soisson SM, Boykevisch S, Yang SS, Bar-Sagi D, et al. (2004) Structural analysis of autoinhibition in the Ras activator Son of sevenless. Cell 119: 393-405.
    • (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
  • 29
  • 30
    • 0032930549 scopus 로고    scopus 로고
    • Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting
    • Sterpetti P, Hack AA, Bashar MP, Park B, Cheng SD, et al. (1999) Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting. Mol Cell Biol 19: 1334-1345.
    • (1999) Mol Cell Biol , vol.19 , pp. 1334-1345
    • Sterpetti, P.1    Hack, A.A.2    Bashar, M.P.3    Park, B.4    Cheng, S.D.5
  • 31
    • 0032563187 scopus 로고    scopus 로고
    • Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin
    • Roos J, Kelly RB (1998) Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin. J Biol Chem 273: 19108-19119.
    • (1998) J Biol Chem , vol.273 , pp. 19108-19119
    • Roos, J.1    Kelly, R.B.2
  • 32
    • 74549174000 scopus 로고    scopus 로고
    • Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1
    • Yu B, Martins IR, Li P, Amarasinghe GK, Umetani J, et al. (2010) Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1. Cell 140: 246-256.
    • (2010) Cell , vol.140 , pp. 246-256
    • Yu, B.1    Martins, I.R.2    Li, P.3    Amarasinghe, G.K.4    Umetani, J.5
  • 33
    • 0032983521 scopus 로고    scopus 로고
    • Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells
    • Hussain NK, Yamabhai M, Ramjaun AR, Guy AM, Baranes D, et al. (1999) Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells. J Biol Chem 274: 15671-15677.
    • (1999) J Biol Chem , vol.274 , pp. 15671-15677
    • Hussain, N.K.1    Yamabhai, M.2    Ramjaun, A.R.3    Guy, A.M.4    Baranes, D.5
  • 34
    • 0035980247 scopus 로고    scopus 로고
    • The human intersectin genes and their spliced variants are differentially expressed
    • Pucharcos C, Casas C, Nadal M, Estivill X, de la Luna S (2001) The human intersectin genes and their spliced variants are differentially expressed. Biochim Biophys Acta 1521: 1-11.
    • (2001) Biochim Biophys Acta , vol.1521 , pp. 1-11
    • Pucharcos, C.1    Casas, C.2    Nadal, M.3    Estivill, X.4    de la Luna, S.5
  • 35
    • 0032211687 scopus 로고    scopus 로고
    • Two isoforms of a human intersectin (ITSN) protein are produced by brain-specific alternative splicing in a stop codon
    • Guipponi M, Scott HS, Chen H, Schebesta A, Rossier C, et al. (1998) Two isoforms of a human intersectin (ITSN) protein are produced by brain-specific alternative splicing in a stop codon. Genomics 53: 369-376.
    • (1998) Genomics , vol.53 , pp. 369-376
    • Guipponi, M.1    Scott, H.S.2    Chen, H.3    Schebesta, A.4    Rossier, C.5
  • 36
    • 0033106167 scopus 로고    scopus 로고
    • The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
    • Sengar AS, Wang W, Bishay J, Cohen S, Egan SE (1999) The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15. Embo J 18: 1159-1171.
    • (1999) Embo J , vol.18 , pp. 1159-1171
    • Sengar, A.S.1    Wang, W.2    Bishay, J.3    Cohen, S.4    Egan, S.E.5
  • 37
    • 0036633295 scopus 로고    scopus 로고
    • The endocytic machinery at an interface with the actin cytoskeleton: A dynamic, hip intersection
    • McPherson PS (2002) The endocytic machinery at an interface with the actin cytoskeleton: a dynamic, hip intersection. Trends Cell Biol 12: 312-315.
    • (2002) Trends Cell Biol , vol.12 , pp. 312-315
    • McPherson, P.S.1
  • 38
    • 0033147449 scopus 로고    scopus 로고
    • SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation
    • Simpson F, Hussain NK, Qualmann B, Kelly RB, Kay BK, et al. (1999) SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation. Nat Cell Biol 1: 119-124.
    • (1999) Nat Cell Biol , vol.1 , pp. 119-124
    • Simpson, F.1    Hussain, N.K.2    Qualmann, B.3    Kelly, R.B.4    Kay, B.K.5
  • 39
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki H, Miura K, Takenawa T (1996) N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. Embo J 15: 5326-5335.
    • (1996) Embo J , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 40
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki H, Sasaki T, Takai Y, Takenawa T (1998) Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391: 93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 41
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R, Ma L, Miki H, Lopez M, Kirchhausen T, et al. (1999) The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97: 221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5
  • 42
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda KE, Scott JA, Mullins RD, Lim WA (2000) Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290: 801-806.
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 43
    • 0034795425 scopus 로고    scopus 로고
    • Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP
    • Hussain NK, Jenna S, Glogauer M, Quinn CC, Wasiak S, et al. (2001) Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP. Nat Cell Biol 3: 927-932.
    • (2001) Nat Cell Biol , vol.3 , pp. 927-932
    • Hussain, N.K.1    Jenna, S.2    Glogauer, M.3    Quinn, C.C.4    Wasiak, S.5
  • 44
    • 0035473453 scopus 로고    scopus 로고
    • Mitogenesis and endocytosis: What's at the INTERSECTIoN?
    • O'Bryan JP, Mohney RP, Oldham CE (2001) Mitogenesis and endocytosis: What's at the INTERSECTIoN? Oncogene 20: 6300-6308.
    • (2001) Oncogene , vol.20 , pp. 6300-6308
    • O'Bryan, J.P.1    Mohney, R.P.2    Oldham, C.E.3
  • 45
    • 0036468381 scopus 로고    scopus 로고
    • Coupling actin dynamics and membrane dynamics during endocytosis
    • Schafer DA (2002) Coupling actin dynamics and membrane dynamics during endocytosis. Curr Opin Cell Biol 14: 76-81.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 76-81
    • Schafer, D.A.1
  • 46
    • 0034614930 scopus 로고    scopus 로고
    • Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP
    • Taunton J, Rowning BA, Coughlin ML, Wu M, Moon RT, et al. (2000) Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP. J Cell Biol 148: 519-530.
    • (2000) J Cell Biol , vol.148 , pp. 519-530
    • Taunton, J.1    Rowning, B.A.2    Coughlin, M.L.3    Wu, M.4    Moon, R.T.5
  • 47
    • 0038032733 scopus 로고    scopus 로고
    • Intersectin 1L guanine nucleotide exchange activity is regulated by adjacent src homology 3 domains that are also involved in endocytosis
    • Zamanian JL, Kelly RB (2003) Intersectin 1L guanine nucleotide exchange activity is regulated by adjacent src homology 3 domains that are also involved in endocytosis. Mol Biol Cell 14: 1624-1637.
    • (2003) Mol Biol Cell , vol.14 , pp. 1624-1637
    • Zamanian, J.L.1    Kelly, R.B.2
  • 48
    • 0037044785 scopus 로고    scopus 로고
    • XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC
    • Arthur WT, Ellerbroek SM, Der CJ, Burridge K, Wennerberg K (2002) XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC. J Biol Chem 277: 42964-42972.
    • (2002) J Biol Chem , vol.277 , pp. 42964-42972
    • Arthur, W.T.1    Ellerbroek, S.M.2    Der, C.J.3    Burridge, K.4    Wennerberg, K.5
  • 49
    • 0345411694 scopus 로고    scopus 로고
    • Rho-specific binding and guanine nucleotide exchange catalysis by KIAA0380, a dbl family member
    • Rumenapp U, Blomquist A, Schworer G, Schablowski H, Psoma A, et al. (1999) Rho-specific binding and guanine nucleotide exchange catalysis by KIAA0380, a dbl family member. FEBS Lett 459: 313-318.
    • (1999) FEBS Lett , vol.459 , pp. 313-318
    • Rumenapp, U.1    Blomquist, A.2    Schworer, G.3    Schablowski, H.4    Psoma, A.5
  • 50
    • 0037155727 scopus 로고    scopus 로고
    • P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac
    • Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, et al. (2002) P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell 108: 809-821.
    • (2002) Cell , vol.108 , pp. 809-821
    • Welch, H.C.1    Coadwell, W.J.2    Ellson, C.D.3    Ferguson, G.J.4    Andrews, S.R.5
  • 51
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim WA, Richards FM, Fox RO (1994) Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372: 375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 52
    • 48449084095 scopus 로고    scopus 로고
    • RAPIDO: A web server for the alignment of protein structures in the presence of conformational changes
    • Mosca R, Schneider TR (2008) RAPIDO: a web server for the alignment of protein structures in the presence of conformational changes. Nucleic Acids Res 36: W42-46.
    • (2008) Nucleic Acids Res , vol.36
    • Mosca, R.1    Schneider, T.R.2
  • 53
    • 0035173480 scopus 로고    scopus 로고
    • Oligomerization of DH domain is essential for Dbl-induced transformation
    • Zhu K, Debreceni B, Bi F, Zheng Y (2001) Oligomerization of DH domain is essential for Dbl-induced transformation. Mol Cell Biol 21: 425-437.
    • (2001) Mol Cell Biol , vol.21 , pp. 425-437
    • Zhu, K.1    Debreceni, B.2    Bi, F.3    Zheng, Y.4
  • 54
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • Lim WA (2002) The modular logic of signaling proteins: building allosteric switches from simple binding domains. Curr Opin Struct Biol 12: 61-68.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 55
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F, Moarefi I, Kuriyan J (1997) Crystal structure of the Src family tyrosine kinase Hck. Nature 385: 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 56
    • 34249894454 scopus 로고    scopus 로고
    • Rewiring cellular morphology pathways with synthetic guanine nucleotide exchange factors
    • Yeh BJ, Rutigliano RJ, Deb A, Bar-Sagi D, Lim WA (2007) Rewiring cellular morphology pathways with synthetic guanine nucleotide exchange factors. Nature 447: 596-600.
    • (2007) Nature , vol.447 , pp. 596-600
    • Yeh, B.J.1    Rutigliano, R.J.2    Deb, A.3    Bar-Sagi, D.4    Lim, W.A.5
  • 57
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi I, LaFevre-Bernt M, Sicheri F, Huse M, Lee CH, et al. (1997) Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385: 650-653.
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1    Lafevre-Bernt, M.2    Sicheri, F.3    Huse, M.4    Lee, C.H.5
  • 58
    • 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 MT, Cronin TC, Huang S, et al. (2007) Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors. Mol Cell 28: 569-583.
    • (2007) Mol Cell , vol.28 , pp. 569-583
    • Dinitto, J.P.1    Delprato, A.2    Gabe Lee, M.T.3    Cronin, T.C.4    Huang, S.5
  • 59
    • 17644370061 scopus 로고    scopus 로고
    • Leucine zipper-mediated homo-oligomerization regulates the Rho-GEF activity of AKAP-Lbc
    • Baisamy L, Jurisch N, Diviani D (2005) Leucine zipper-mediated homo-oligomerization regulates the Rho-GEF activity of AKAP-Lbc. J Biol Chem 280: 15405-15412.
    • (2005) J Biol Chem , vol.280 , pp. 15405-15412
    • Baisamy, L.1    Jurisch, N.2    Diviani, D.3
  • 60
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology 276: 307-326.
    • (1997) Methods In Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 61
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63: 32-41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 62
  • 63
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2: 2728-2733.
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 65
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 66
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 67
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson ML, Correia JJ, Yphantis DA, Halvorson HR (1981) Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys J 36: 575-588.
    • (1981) Biophys J , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.