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Volumn 15, Issue 1, 2014, Pages 104-121

Longin and GAF Domains: Structural Evolution and Adaptation to the Subcellular Trafficking Machinery

Author keywords

Architecture; Evolution; Fold; GAF; Last Eukaryotic Common Ancestor; Longin; PAS; Permutation; Protein domain; Subcellular trafficking; Topology

Indexed keywords

CGMP SPECIFIC PHOSPHODIESTERASE ADENYLYL CYCLASE AND FHIA; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; SULFAMETHOXYPYRIDAZINE; UNCLASSIFIED DRUG;

EID: 84889597180     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12124     Document Type: Article
Times cited : (38)

References (87)
  • 1
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino JS, Glick BS. The mechanisms of vesicle budding and fusion. Cell 2004;116:153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 2
    • 34948835726 scopus 로고    scopus 로고
    • Evolution of the eukaryotic membrane-trafficking system: origin, tempo and mode
    • Dacks JB, Field MC. Evolution of the eukaryotic membrane-trafficking system: origin, tempo and mode. J Cell Sci 2007;120(Pt 17):2977-2985.
    • (2007) J Cell Sci , vol.120 , Issue.PART 17 , pp. 2977-2985
    • Dacks, J.B.1    Field, M.C.2
  • 3
    • 77957348884 scopus 로고    scopus 로고
    • Rab protein evolution and the history of the eukaryotic endomembrane system
    • Brighouse A, Dacks JB, Field MC. Rab protein evolution and the history of the eukaryotic endomembrane system. Cell Mol Life Sci 2010;67:3449-3465.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3449-3465
    • Brighouse, A.1    Dacks, J.B.2    Field, M.C.3
  • 4
    • 49749133839 scopus 로고    scopus 로고
    • SNAREing the basis of multicellularity: consequences of protein family expansion during evolution
    • Kloepper TH, Kienle CN, Fasshauer D. SNAREing the basis of multicellularity: consequences of protein family expansion during evolution. Mol Biol Evol 2008;25:2055-2068.
    • (2008) Mol Biol Evol , vol.25 , pp. 2055-2068
    • Kloepper, T.H.1    Kienle, C.N.2    Fasshauer, D.3
  • 5
    • 57149118232 scopus 로고    scopus 로고
    • Structural evidence for common ancestry of the nuclear pore complex and vesicle coats
    • Brohawn SG, Leksa NC, Spear ED, Rajashankar KR, Schwartz TU. Structural evidence for common ancestry of the nuclear pore complex and vesicle coats. Science 2008;322:1369-1373.
    • (2008) Science , vol.322 , pp. 1369-1373
    • Brohawn, S.G.1    Leksa, N.C.2    Spear, E.D.3    Rajashankar, K.R.4    Schwartz, T.U.5
  • 6
    • 61349170303 scopus 로고    scopus 로고
    • First and last ancestors: reconstructing evolution of the endomembrane system with ESCRTs, vesicle coat proteins, and nuclear pore complexes
    • Field MC, Dacks JB. First and last ancestors: reconstructing evolution of the endomembrane system with ESCRTs, vesicle coat proteins, and nuclear pore complexes. Curr Opin Cell Biol 2009;21:4-13.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 4-13
    • Field, M.C.1    Dacks, J.B.2
  • 7
    • 59449093322 scopus 로고    scopus 로고
    • Repeated secondary loss of adaptin complex genes in the Apicomplexa
    • Nevin WD, Dacks JB. Repeated secondary loss of adaptin complex genes in the Apicomplexa. Parasitol Int 2009;58:86-94.
    • (2009) Parasitol Int , vol.58 , pp. 86-94
    • Nevin, W.D.1    Dacks, J.B.2
  • 8
    • 78650101853 scopus 로고    scopus 로고
    • Patterns and processes in the evolution of the eukaryotic endomembrane system
    • Elias M. Patterns and processes in the evolution of the eukaryotic endomembrane system. Mol Membr Biol 2010;27:469-489.
    • (2010) Mol Membr Biol , vol.27 , pp. 469-489
    • Elias, M.1
  • 9
    • 38649092668 scopus 로고    scopus 로고
    • Phylogeny of endocytic components yields insight into the process of nonendosymbiotic organelle evolution
    • Dacks JB, Poon PP, Field MC. Phylogeny of endocytic components yields insight into the process of nonendosymbiotic organelle evolution. Proc Natl Acad Sci USA 2008;105:588-593.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 588-593
    • Dacks, J.B.1    Poon, P.P.2    Field, M.C.3
  • 11
    • 78649395975 scopus 로고    scopus 로고
    • Evolution. Intermediate steps
    • Devos DP, Reynaud EG. Evolution. Intermediate steps. Science 2010;330:1187-1188.
    • (2010) Science , vol.330 , pp. 1187-1188
    • Devos, D.P.1    Reynaud, E.G.2
  • 12
    • 34249282745 scopus 로고    scopus 로고
    • Homologs of eukaryotic Ras superfamily proteins in prokaryotes and their novel phylogenetic correlation with their eukaryotic analogs
    • Dong JH, Wen JF, Tian HF. Homologs of eukaryotic Ras superfamily proteins in prokaryotes and their novel phylogenetic correlation with their eukaryotic analogs. Gene 2007;396:116-124.
    • (2007) Gene , vol.396 , pp. 116-124
    • Dong, J.H.1    Wen, J.F.2    Tian, H.F.3
  • 13
    • 0035900653 scopus 로고    scopus 로고
    • Reconstructing/ deconstructing the earliest eukaryotes: how comparative genomics can help
    • Dacks JB, Doolittle WF. Reconstructing/ deconstructing the earliest eukaryotes: how comparative genomics can help. Cell 2001;107:419-425.
    • (2001) Cell , vol.107 , pp. 419-425
    • Dacks, J.B.1    Doolittle, W.F.2
  • 15
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: grappling with SNARE and SM proteins
    • Südhof TC, Rothman JE. Membrane fusion: grappling with SNARE and SM proteins. Science 2009;323:474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 17
    • 0035958644 scopus 로고    scopus 로고
    • An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p
    • Tochio H, Tsui MM, Banfield DK, Zhang M. An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p. Science 2001;293:698-702.
    • (2001) Science , vol.293 , pp. 698-702
    • Tochio, H.1    Tsui, M.M.2    Banfield, D.K.3    Zhang, M.4
  • 19
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. Molecular architecture and functional model of the endocytic AP2 complex. Cell 2002;109:523-535.
    • (2002) Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 20
    • 0037147148 scopus 로고    scopus 로고
    • Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda
    • Jang SB, Kim YG, Cho YS, Suh PG, Kim KH, Oh BH. Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda. J Biol Chem 2002;277:49863-49869.
    • (2002) J Biol Chem , vol.277 , pp. 49863-49869
    • Jang, S.B.1    Kim, Y.G.2    Cho, Y.S.3    Suh, P.G.4    Kim, K.H.5    Oh, B.H.6
  • 21
    • 0037459447 scopus 로고    scopus 로고
    • Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor
    • Schwartz T, Blobel G. Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor. Cell 2003;112:793-803.
    • (2003) Cell , vol.112 , pp. 793-803
    • Schwartz, T.1    Blobel, G.2
  • 24
    • 33646461205 scopus 로고    scopus 로고
    • The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains
    • Schlenker O, Hendricks A, Sinning I, Wild K. The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains. J Biol Chem 2006;281:8898-8906.
    • (2006) J Biol Chem , vol.281 , pp. 8898-8906
    • Schlenker, O.1    Hendricks, A.2    Sinning, I.3    Wild, K.4
  • 25
    • 33751109759 scopus 로고    scopus 로고
    • Longin-like folds identified in CHiPS and DUF254 proteins: vesicle trafficking complexes conserved in eukaryotic evolution
    • Kinch LN, Grishin NV. Longin-like folds identified in CHiPS and DUF254 proteins: vesicle trafficking complexes conserved in eukaryotic evolution. Protein Sci 2006;15:2669-2674.
    • (2006) Protein Sci , vol.15 , pp. 2669-2674
    • Kinch, L.N.1    Grishin, N.V.2
  • 26
    • 70749093076 scopus 로고    scopus 로고
    • Comparative analysis of plant genomes allows the definition of the ''Phytolongins'': a novel non-SNARE longin domain protein family
    • Vedovato M, Rossi V, Dacks JB, Filippini F. Comparative analysis of plant genomes allows the definition of the ''Phytolongins'': a novel non-SNARE longin domain protein family. BMC Genomics 2009;10:510.
    • (2009) BMC Genomics , vol.10 , pp. 510
    • Vedovato, M.1    Rossi, V.2    Dacks, J.B.3    Filippini, F.4
  • 27
    • 60149108669 scopus 로고    scopus 로고
    • Solution structure of human zeta-COP: direct evidences for structural similarity between COP I and clathrin-adaptor coats
    • Yu W, Lin J, Jin C, Xia B. Solution structure of human zeta-COP: direct evidences for structural similarity between COP I and clathrin-adaptor coats. J Mol Biol 2009;386:903-912.
    • (2009) J Mol Biol , vol.386 , pp. 903-912
    • Yu, W.1    Lin, J.2    Jin, C.3    Xia, B.4
  • 28
    • 79954614556 scopus 로고    scopus 로고
    • DENN domain proteins: regulators of Rab GTPases
    • Marat AL, Dokainish H, McPherson PS. DENN domain proteins: regulators of Rab GTPases. J Biol Chem 2011;286:13791-13800.
    • (2011) J Biol Chem , vol.286 , pp. 13791-13800
    • Marat, A.L.1    Dokainish, H.2    McPherson, P.S.3
  • 29
    • 81755163615 scopus 로고    scopus 로고
    • Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate
    • Wu X, Bradley MJ, Cai Y, Kümmel D, De La Cruz EM, Barr FA, Reinisch KM. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proc Natl Acad Sci USA 2011;108:18672-18677.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18672-18677
    • Wu, X.1    Bradley, M.J.2    Cai, Y.3    Kümmel, D.4    De La Cruz, E.M.5    Barr, F.A.6    Reinisch, K.M.7
  • 30
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain: a ubiquitous signaling motif and a new class of cyclic GMP receptor
    • Ho YS, Burden LM, Hurley JH. Structure of the GAF domain: a ubiquitous signaling motif and a new class of cyclic GMP receptor. EMBO J 2000;19:5288-5299.
    • (2000) EMBO J , vol.19 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 31
    • 1642554150 scopus 로고    scopus 로고
    • GAF domains: two-billion-year-old molecular switches that bind cyclic nucleotides
    • Martinez SE, Beavo JA, Hol WG. GAF domains: two-billion-year-old molecular switches that bind cyclic nucleotides. Mol Interv 2002;2:317-323.
    • (2002) Mol Interv , vol.2 , pp. 317-323
    • Martinez, S.E.1    Beavo, J.A.2    Hol, W.G.3
  • 32
    • 58149187899 scopus 로고    scopus 로고
    • The CATH classification revisited--architectures reviewed and new ways to characterize structural divergence in superfamilies
    • Cuff AL, Sillitoe I, Lewis T, Redfern OC, Garratt R, Thornton J, Orengo CA. The CATH classification revisited--architectures reviewed and new ways to characterize structural divergence in superfamilies. Nucleic Acids Res 2009;37(Database issue):D310-314.
    • (2009) Nucleic Acids Res , vol.37 , Issue.DATABASE ISSUE
    • Cuff, A.L.1    Sillitoe, I.2    Lewis, T.3    Redfern, O.C.4    Garratt, R.5    Thornton, J.6    Orengo, C.A.7
  • 33
    • 77953172923 scopus 로고    scopus 로고
    • Early origin of genes encoding subunits of biogenesis of lysosome-related organelles complex-1, -2 and -3
    • Cheli VT, Dell'Angelica EC. Early origin of genes encoding subunits of biogenesis of lysosome-related organelles complex-1, -2 and -3. Traffic 2010;11:579-586.
    • (2010) Traffic , vol.11 , pp. 579-586
    • Cheli, V.T.1    Dell'Angelica, E.C.2
  • 36
    • 84856289301 scopus 로고    scopus 로고
    • Eukaryotic systematics: a user's guide for cell biologists and parasitologists
    • Walker G, Dorrell RG, Schlacht A, Dacks JB. Eukaryotic systematics: a user's guide for cell biologists and parasitologists. Parasitology 2011;138:1638-1663.
    • (2011) Parasitology , vol.138 , pp. 1638-1663
    • Walker, G.1    Dorrell, R.G.2    Schlacht, A.3    Dacks, J.B.4
  • 39
    • 84859945474 scopus 로고    scopus 로고
    • The evolutionary history of haptophytes and cryptophytes: phylogenomic evidence for separate origins
    • Burki F, Okamoto N, Pombert JF, Keeling PJ. The evolutionary history of haptophytes and cryptophytes: phylogenomic evidence for separate origins. Proc Biol Sci 2012;279:2246-2254.
    • (2012) Proc Biol Sci , vol.279 , pp. 2246-2254
    • Burki, F.1    Okamoto, N.2    Pombert, J.F.3    Keeling, P.J.4
  • 40
    • 57749191527 scopus 로고    scopus 로고
    • Crystal structure of human synbindin reveals two conformations of longin domain
    • Fan S, Wei Z, Xu H, Gong W. Crystal structure of human synbindin reveals two conformations of longin domain. Biochem Biophys Res Commun 2009;378:338-343.
    • (2009) Biochem Biophys Res Commun , vol.378 , pp. 338-343
    • Fan, S.1    Wei, Z.2    Xu, H.3    Gong, W.4
  • 42
    • 33847648364 scopus 로고    scopus 로고
    • Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins
    • Koumandou VL, Dacks JB, Coulson RM, Field MC. Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins. BMC Evol Biol 2007;7:29.
    • (2007) BMC Evol Biol , vol.7 , pp. 29
    • Koumandou, V.L.1    Dacks, J.B.2    Coulson, R.M.3    Field, M.C.4
  • 43
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • Poteryaev D, Datta S, Ackema K, Zerial M, Spang A. Identification of the switch in early-to-late endosome transition. Cell 2010;141:497-508.
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1    Datta, S.2    Ackema, K.3    Zerial, M.4    Spang, A.5
  • 45
    • 84869491973 scopus 로고    scopus 로고
    • BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor
    • Gerondopoulos A, Langemeyer L, Liang JR, Linford A, Barr FA. BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor. Curr Biol 2012;22:2135-2139.
    • (2012) Curr Biol , vol.22 , pp. 2135-2139
    • Gerondopoulos, A.1    Langemeyer, L.2    Liang, J.R.3    Linford, A.4    Barr, F.A.5
  • 47
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenström P. Dali server: conservation mapping in 3D. Nucleic Acids Res 2010;38(Web Server issue):W545-549.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Holm, L.1    Rosenström, P.2
  • 48
    • 80053291460 scopus 로고    scopus 로고
    • Ligand-binding PAS domains in a genomic, cellular, and structural context
    • Henry JT, Crosson S. Ligand-binding PAS domains in a genomic, cellular, and structural context. Annu Rev Microbiol 2011;65:261-286.
    • (2011) Annu Rev Microbiol , vol.65 , pp. 261-286
    • Henry, J.T.1    Crosson, S.2
  • 49
    • 78649675368 scopus 로고    scopus 로고
    • Conformation changes, N-terminal involvement and cGMP signal relay in phosphodiesterase-5 GAF domain
    • Wang H, Robinson H, Ke H. Conformation changes, N-terminal involvement and cGMP signal relay in phosphodiesterase-5 GAF domain. J Biol Chem 2010;285:38149-38156.
    • (2010) J Biol Chem , vol.285 , pp. 38149-38156
    • Wang, H.1    Robinson, H.2    Ke, H.3
  • 50
    • 33847383702 scopus 로고    scopus 로고
    • Changes in purine specificity in tandem GAF chimeras from cyanobacterial cyaB1 adenylate cyclase and rat phosphodiesterase 2
    • Linder JU, Bruder S, Schultz A, Schultz JE. Changes in purine specificity in tandem GAF chimeras from cyanobacterial cyaB1 adenylate cyclase and rat phosphodiesterase 2. FEBS J 2007;274:1514-1523.
    • (2007) FEBS J , vol.274 , pp. 1514-1523
    • Linder, J.U.1    Bruder, S.2    Schultz, A.3    Schultz, J.E.4
  • 51
    • 70549106122 scopus 로고    scopus 로고
    • How depolymerization can promote polymerization: the case of actin and profilin
    • Yarmola EG, Bubb MR. How depolymerization can promote polymerization: the case of actin and profilin. Bioessays 2009;31:1150-1160.
    • (2009) Bioessays , vol.31 , pp. 1150-1160
    • Yarmola, E.G.1    Bubb, M.R.2
  • 52
    • 2542432265 scopus 로고    scopus 로고
    • The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling
    • Lunin VV, Munger C, Wagner J, Ye Z, Cygler M, Sacher M. The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling. J Biol Chem 2004;279:23422-23430.
    • (2004) J Biol Chem , vol.279 , pp. 23422-23430
    • Lunin, V.V.1    Munger, C.2    Wagner, J.3    Ye, Z.4    Cygler, M.5    Sacher, M.6
  • 53
    • 77954568867 scopus 로고    scopus 로고
    • The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly
    • Hall J, Song Y, Karplus PA, Barbar E. The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly. J Biol Chem 2010;285:22566-22575.
    • (2010) J Biol Chem , vol.285 , pp. 22566-22575
    • Hall, J.1    Song, Y.2    Karplus, P.A.3    Barbar, E.4
  • 54
    • 84855612321 scopus 로고    scopus 로고
    • Unique properties of eukaryote-type actin and profilin horizontally transferred to cyanobacteria
    • Guljamow A, Delissen F, Baumann O, Thünemann AF, Dittmann E. Unique properties of eukaryote-type actin and profilin horizontally transferred to cyanobacteria. PLoS One 2012;7:e29926.
    • (2012) PLoS One , vol.7
    • Guljamow, A.1    Delissen, F.2    Baumann, O.3    Thünemann, A.F.4    Dittmann, E.5
  • 55
    • 0034597558 scopus 로고    scopus 로고
    • Dynein light chains of the Roadblock/LC7 group belong to an ancient protein superfamily implicated in NTPase regulation
    • Koonin EV, Aravind L. Dynein light chains of the Roadblock/LC7 group belong to an ancient protein superfamily implicated in NTPase regulation. Curr Biol 2000;10:R774-776.
    • (2000) Curr Biol , vol.10
    • Koonin, E.V.1    Aravind, L.2
  • 58
    • 28144455335 scopus 로고    scopus 로고
    • Solution structure of isoform 1 of Roadblock/LC7: a light chain in the dynein complex
    • Song J, Tyler RC, Lee MS, Tyler EM, Markley JL. Solution structure of isoform 1 of Roadblock/LC7: a light chain in the dynein complex. J Mol Biol 2005;354:1043-1051.
    • (2005) J Mol Biol , vol.354 , pp. 1043-1051
    • Song, J.1    Tyler, R.C.2    Lee, M.S.3    Tyler, E.M.4    Markley, J.L.5
  • 59
    • 5044252143 scopus 로고    scopus 로고
    • An ear-core interaction regulates the recruitment of the AP-3 complex to membranes
    • Lefrançois S, Janvier K, Boehm M, Ooi CE, Bonifacino JS. An ear-core interaction regulates the recruitment of the AP-3 complex to membranes. Dev Cell 2004;7:619-625.
    • (2004) Dev Cell , vol.7 , pp. 619-625
    • Lefrançois, S.1    Janvier, K.2    Boehm, M.3    Ooi, C.E.4    Bonifacino, J.S.5
  • 65
    • 84865492819 scopus 로고    scopus 로고
    • Crystal structure of the Gtr1p(GTP)-Gtr2p(GDP) protein complex reveals large structural rearrangements triggered by GTP-to-GDP conversion
    • Jeong JH, Lee KH, Kim YM, Kim DH, Oh BH, Kim YG. Crystal structure of the Gtr1p(GTP)-Gtr2p(GDP) protein complex reveals large structural rearrangements triggered by GTP-to-GDP conversion. J Biol Chem 2012;287:29648-29653.
    • (2012) J Biol Chem , vol.287 , pp. 29648-29653
    • Jeong, J.H.1    Lee, K.H.2    Kim, Y.M.3    Kim, D.H.4    Oh, B.H.5    Kim, Y.G.6
  • 67
    • 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, Bonifacino JS, Hurley JH. Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. Cell 2013;152:755-767.
    • (2013) Cell , vol.152 , pp. 755-767
    • Ren, X.1    Farías, G.G.2    Canagarajah, B.J.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 68
    • 84856760126 scopus 로고    scopus 로고
    • A structure-based mechanism for Arf1-dependent recruitment of coatomer to membranes
    • Yu X, Breitman M, Goldberg J. A structure-based mechanism for Arf1-dependent recruitment of coatomer to membranes. Cell 2012;148:530-542.
    • (2012) Cell , vol.148 , pp. 530-542
    • Yu, X.1    Breitman, M.2    Goldberg, J.3
  • 69
    • 77956740779 scopus 로고    scopus 로고
    • Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals
    • Kogan K, Spear ED, Kaiser CA, Fass D. Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals. J Mol Biol 2010;402:388-398.
    • (2010) J Mol Biol , vol.402 , pp. 388-398
    • Kogan, K.1    Spear, E.D.2    Kaiser, C.A.3    Fass, D.4
  • 70
    • 84866431363 scopus 로고    scopus 로고
    • Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1
    • Bar-Peled L, Schweitzer LD, Zoncu R, Sabatini DM. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell 2012;150:1196-1208.
    • (2012) Cell , vol.150 , pp. 1196-1208
    • Bar-Peled, L.1    Schweitzer, L.D.2    Zoncu, R.3    Sabatini, D.M.4
  • 72
    • 77955015657 scopus 로고    scopus 로고
    • A Bacterial Ras-Like Small GTP-Binding Protein and Its Cognate GAP Establish a Dynamic Spatial Polarity Axis to Control Directed Motility
    • Zhang Y, Franco M, Ducret A, Mignot T. A Bacterial Ras-Like Small GTP-Binding Protein and Its Cognate GAP Establish a Dynamic Spatial Polarity Axis to Control Directed Motility. PLoS Biol 2010;8:e1000430.
    • (2010) PLoS Biol , vol.8
    • Zhang, Y.1    Franco, M.2    Ducret, A.3    Mignot, T.4
  • 73
    • 84876431000 scopus 로고    scopus 로고
    • Discovery of new Longin and Roadblock domains that for platforms for small GTPases in Ragulator and TRAPP-II
    • Levine TP, Daniels RD, Wong LH, Gatta AT, Gerondopoulos A, Barr FA. Discovery of new Longin and Roadblock domains that for platforms for small GTPases in Ragulator and TRAPP-II. Small GTPases 2013;4:62-69.
    • (2013) Small GTPases , vol.4 , pp. 62-69
    • Levine, T.P.1    Daniels, R.D.2    Wong, L.H.3    Gatta, A.T.4    Gerondopoulos, A.5    Barr, F.A.6
  • 74
    • 34247579058 scopus 로고    scopus 로고
    • The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope
    • Mancias JD, Goldberg J. The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope. Mol Cell 2007;26:403-414.
    • (2007) Mol Cell , vol.26 , pp. 403-414
    • Mancias, J.D.1    Goldberg, J.2
  • 76
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP
    • Ferron F, Rebowski G, Lee SH, Dominguez R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J 2007;26:4597-4606.
    • (2007) EMBO J , vol.26 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 77
    • 33947589440 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation within the MKK1-ERK2 complex by MP1 and the MP1*P14 heterodimer
    • Brahma A, Dalby KN. Regulation of protein phosphorylation within the MKK1-ERK2 complex by MP1 and the MP1*P14 heterodimer. Arch Biochem Biophys 2007;460:85-91.
    • (2007) Arch Biochem Biophys , vol.460 , pp. 85-91
    • Brahma, A.1    Dalby, K.N.2
  • 78
    • 62049084764 scopus 로고    scopus 로고
    • The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes
    • Nada S, Hondo A, Kasai A, Koike M, Saito K, Uchiyama Y, Okada M. The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes. EMBO J 2009;28:477-489.
    • (2009) EMBO J , vol.28 , pp. 477-489
    • Nada, S.1    Hondo, A.2    Kasai, A.3    Koike, M.4    Saito, K.5    Uchiyama, Y.6    Okada, M.7
  • 79
    • 11144288242 scopus 로고    scopus 로고
    • Molecular evolution of PAS domain-containing proteins of filamentous cyanobacteria through domain shuffling and domain duplication
    • Narikawa R, Okamoto S, Ikeuchi M, Ohmori M. Molecular evolution of PAS domain-containing proteins of filamentous cyanobacteria through domain shuffling and domain duplication. DNA Res 2004;11:69-81.
    • (2004) DNA Res , vol.11 , pp. 69-81
    • Narikawa, R.1    Okamoto, S.2    Ikeuchi, M.3    Ohmori, M.4
  • 80
    • 1842427563 scopus 로고    scopus 로고
    • The extended left-handed helix: a simple nucleic acid binding-motif
    • Hicks JM, Hsu VL. The extended left-handed helix: a simple nucleic acid binding-motif. Proteins 2004;55:330-338.
    • (2004) Proteins , vol.55 , pp. 330-338
    • Hicks, J.M.1    Hsu, V.L.2
  • 81
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: interactive sequence similarity searching
    • Finn RD, Clements J, Eddy SR. HMMER web server: interactive sequence similarity searching. Nucleic Acids Res 2011;39(web server issue):w29-37.
    • (2011) Nucleic Acids Res , vol.39 , Issue.WEB SERVER ISSUE
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 82
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding J, Biegert A, Lupas AN. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 2005;33(web server issue):w244-248.
    • (2005) Nucleic Acids Res , vol.33 , Issue.WEB SERVER ISSUE
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 83
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: selection of best-fit models of protein evolution
    • Abscal F, Posada D. ProtTest: selection of best-fit models of protein evolution. Bioinformatics 2005;21:2104-2105.
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abscal, F.1    Posada, D.2
  • 84
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ. Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 2009;4:363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 85
    • 38849092210 scopus 로고    scopus 로고
    • A note on difficult structure alignment problems
    • Sippl MJ, Wiederstein M. A note on difficult structure alignment problems. Bioinformatics 2008;24:426-427.
    • (2008) Bioinformatics , vol.24 , pp. 426-427
    • Sippl, M.J.1    Wiederstein, M.2
  • 86
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007;372:774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 87
    • 78651235334 scopus 로고    scopus 로고
    • Computer-aided drug design platform using PyMOL
    • Lill MA, Danielson ML. Computer-aided drug design platform using PyMOL. J Comput Aided Mol Des 2011;25:13-19.
    • (2011) J Comput Aided Mol Des , vol.25 , pp. 13-19
    • Lill, M.A.1    Danielson, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.