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Volumn 343, Issue 1, 2004, Pages 1-28

STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer

Author keywords

AP ATPases; molecular evolution; multidomain proteins; P loop NTPases; signaling

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENYLATE CYCLASE; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; ENZYME; NEPHROCYSTIN 3; UNCLASSIFIED DRUG;

EID: 4644247731     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.023     Document Type: Article
Times cited : (367)

References (133)
  • 1
    • 0025996094 scopus 로고
    • Evidence for an ancestral core structure in nucleotide-binding proteins with the type a motif
    • E.J. Milner-White, J.R. Coggins, and I.A. Anton Evidence for an ancestral core structure in nucleotide-binding proteins with the type A motif J. Mol. Biol. 221 1991 751 754
    • (1991) J. Mol. Biol. , vol.221 , pp. 751-754
    • Milner-White, E.J.1    Coggins, J.R.2    Anton, I.A.3
  • 2
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • M. Saraste, P.R. Sibbald, and A. Wittinghofer The P-loop - a common motif in ATP- and GTP-binding proteins Trends Biochem. Sci. 15 1990 430 434
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 3
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • G.E. Schulz Binding of nucleotides by proteins Curr. Opin. Struct. Biol. 2 1992 61 67
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 4
    • 0033511228 scopus 로고    scopus 로고
    • Nucleoside triphosphate-binding proteins: Different scaffolds to achieve phosphoryl transfer
    • I.R. Vetter, and A. Wittinghofer Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer Quart. Rev. Biophys. 32 1999 1 56
    • (1999) Quart. Rev. Biophys. , vol.32 , pp. 1-56
    • Vetter, I.R.1    Wittinghofer, A.2
  • 5
    • 0033941641 scopus 로고    scopus 로고
    • Protein fold recognition using sequence profiles and its application in structural genomics
    • E.V. Koonin, Y.I. Wolf, and L. Aravind Protein fold recognition using sequence profiles and its application in structural genomics Advan. Protein Chem. 54 2000 245 275
    • (2000) Advan. Protein Chem. , vol.54 , pp. 245-275
    • Koonin, E.V.1    Wolf, Y.I.2    Aravind, L.3
  • 6
    • 0030023247 scopus 로고    scopus 로고
    • Determining divergence times of the major kingdoms of living organisms with a protein clock
    • R.F. Doolittle, D.-F. Feng, S. Tsang, G. Cho, and E. LIttle Determining divergence times of the major kingdoms of living organisms with a protein clock Science 271 1996 470 477
    • (1996) Science , vol.271 , pp. 470-477
    • Doolittle, R.F.1    Feng, D.-F.2    Tsang, S.3    Cho, G.4    Little, E.5
  • 7
    • 0030309433 scopus 로고    scopus 로고
    • Constraints on protein evolution and the age of the eubacteria/eukaryote split
    • M.M. Miyamoto, and W.M. Fitch Constraints on protein evolution and the age of the eubacteria/eukaryote split Syst. Biol. 45 1996 568 575
    • (1996) Syst. Biol. , vol.45 , pp. 568-575
    • Miyamoto, M.M.1    Fitch, W.M.2
  • 8
    • 0036529621 scopus 로고    scopus 로고
    • Comparative genomics and evolution of proteins involved in RNA metabolism
    • V. Anantharaman, E.V. Koonin, and L. Aravind Comparative genomics and evolution of proteins involved in RNA metabolism Nucl. Acids Res. 30 2002 1427 1464
    • (2002) Nucl. Acids Res. , vol.30 , pp. 1427-1464
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 9
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • D.D. Leipe, Y.I. Wolf, E.V. Koonin, and L. Aravind Classification and evolution of P-loop GTPases and related ATPases J. Mol. Biol. 317 2002 41 72
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 10
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • A.G. Murzin, S.E. Brenner, T. Hubbard, and C. Chothia SCOP: a structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247 1995 536 540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 11
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • J.E. Walker, M. Saraste, M.J. Runswick, and N.J. Gay Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold EMBO J. 1 1982 945 951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 12
    • 0024462161 scopus 로고
    • Viral proteins containing the purine NTP-binding sequence pattern
    • A.E. Gorbalenya, and E.V. Koonin Viral proteins containing the purine NTP-binding sequence pattern Nucl. Acids Res. 17 1989 8413 8440
    • (1989) Nucl. Acids Res. , vol.17 , pp. 8413-8440
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 13
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • D.D. Leipe, E.V. Koonin, and L. Aravind Evolution and classification of P-loop kinases and related proteins J. Mol. Biol. 333 2003 781 815
    • (2003) J. Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 14
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • A.F. Neuwald, L. Aravind, J.L. Spouge, and E.V. Koonin AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes Genome Res. 9 1999 27 43
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 15
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • L.M. Iyer, D.D. Leipe, E.V. Koonin, and L. Aravind Evolutionary history and higher order classification of AAA+ ATPases J. Struct. Biol. 146 2004 11 31
    • (2004) J. Struct. Biol. , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 16
    • 4644335054 scopus 로고    scopus 로고
    • A novel family of P-loop NTPases with an unusual phyletic distribution and transmembrane segments inserted within the NTPase domain
    • L. Aravind, L. Iyer, D. Leipe, and E. Koonin A novel family of P-loop NTPases with an unusual phyletic distribution and transmembrane segments inserted within the NTPase domain Genome Biol. 5 2004 R30.1 R30.10
    • (2004) Genome Biol. , vol.5
    • Aravind, L.1    Iyer, L.2    Leipe, D.3    Koonin, E.4
  • 18
    • 0032568168 scopus 로고    scopus 로고
    • The NB-ARC domain: A novel signalling motif shared by plant resistance gene products and regulators of cell death in animals
    • E.A. van der Biezen, and J.D. Jones The NB-ARC domain: a novel signalling motif shared by plant resistance gene products and regulators of cell death in animals Curr. Biol. 8 1998 R226 R227
    • (1998) Curr. Biol. , vol.8
    • Van Der Biezen, E.A.1    Jones, J.D.2
  • 19
    • 0008824942 scopus 로고    scopus 로고
    • The domains of death: Evolution of the apoptosis machinery
    • L. Aravind, V.M. Dixit, and E.V. Koonin The domains of death: evolution of the apoptosis machinery Trends Biochem Sci. 24 1999 47 53
    • (1999) Trends Biochem Sci. , vol.24 , pp. 47-53
    • Aravind, L.1    Dixit, V.M.2    Koonin, E.V.3
  • 20
    • 0034194079 scopus 로고    scopus 로고
    • The NACHT family - A new group of predicted NTPases implicated in apoptosis and MHC transcription activation
    • E.V. Koonin, and L. Aravind The NACHT family - a new group of predicted NTPases implicated in apoptosis and MHC transcription activation Trends Biochem Sci. 25 2000 223 224
    • (2000) Trends Biochem Sci. , vol.25 , pp. 223-224
    • Koonin, E.V.1    Aravind, L.2
  • 21
    • 0036316720 scopus 로고    scopus 로고
    • Origin and evolution of eukaryotic apoptosis: The bacterial connection
    • E.V. Koonin, and L. Aravind Origin and evolution of eukaryotic apoptosis: the bacterial connection Cell Death Differ. 9 2002 394 404
    • (2002) Cell Death Differ. , vol.9 , pp. 394-404
    • Koonin, E.V.1    Aravind, L.2
  • 22
    • 0031046171 scopus 로고    scopus 로고
    • Evidence for a family of archaeal ATPases
    • E.V. Koonin Evidence for a family of archaeal ATPases Science 275 1997 1489 1490
    • (1997) Science , vol.275 , pp. 1489-1490
    • Koonin, E.V.1
  • 23
    • 0032766490 scopus 로고    scopus 로고
    • Comparative genomics of the Archaea (Euryarchaeota): Evolution of conserved protein families, the stable core, and the variable shell
    • K.S. Makarova, L. Aravind, M.Y. Galperin, N.V. Grishin, R.L. Tatusov, Y.I. Wolf, and E.V. Koonin Comparative genomics of the Archaea (Euryarchaeota): evolution of conserved protein families, the stable core, and the variable shell Genome Res. 9 1999 608 628
    • (1999) Genome Res. , vol.9 , pp. 608-628
    • Makarova, K.S.1    Aravind, L.2    Galperin, M.Y.3    Grishin, N.V.4    Tatusov, R.L.5    Wolf, Y.I.6    Koonin, E.V.7
  • 24
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • R.M. Story, and T.A. Steitz Structure of the recA protein-ADP complex Nature 355 1992 374 376
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 25
    • 0033582802 scopus 로고    scopus 로고
    • On the in vivo function of the RecA ATPase
    • M.J. Campbell, and R.W. Davis On the in vivo function of the RecA ATPase J. Mol. Biol. 286 1999 437 445
    • (1999) J. Mol. Biol. , vol.286 , pp. 437-445
    • Campbell, M.J.1    Davis, R.W.2
  • 27
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • L.W. Hung, I.X. Wang, K. Nikaido, P.Q. Liu, G.F. Ames, and S.H. Kim Crystal structure of the ATP-binding subunit of an ABC transporter Nature 396 1998 703 707
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 28
    • 0032807099 scopus 로고    scopus 로고
    • The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells
    • U. Herbig, C.A. Marlar, and E. Fanning The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells Mol. Biol. Cell 10 1999 2631 2645
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2631-2645
    • Herbig, U.1    Marlar, C.A.2    Fanning, E.3
  • 29
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • M.R. Sawaya, S. Guo, S. Tabor, C.C. Richardson, and T. Ellenberger Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7 Cell 99 1999 167 177
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 30
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • A.E. Gorbalenya, and E.V. Koonin Helicases: amino acid sequence comparisons and structure-function relationships Curr. Opin. Struct. Biol. 3 1993 419 429
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 31
    • 0033485460 scopus 로고    scopus 로고
    • DNA-binding proteins and evolution of transcription regulation in the archaea
    • L. Aravind, and E.V. Koonin DNA-binding proteins and evolution of transcription regulation in the archaea Nucl. Acids Res. 27 1999 4658 4670
    • (1999) Nucl. Acids Res. , vol.27 , pp. 4658-4670
    • Aravind, L.1    Koonin, E.V.2
  • 32
    • 0035839553 scopus 로고    scopus 로고
    • Roles of glucitol in the GutR-mediated transcription activation process in Bacillus subtilis: Glucitol induces GutR to change its conformation and to bind ATP
    • K.K. Poon, J.C. Chu, and S.L. Wong Roles of glucitol in the GutR-mediated transcription activation process in Bacillus subtilis: glucitol induces GutR to change its conformation and to bind ATP J. Biol. Chem. 276 2001 29819 29825
    • (2001) J. Biol. Chem. , vol.276 , pp. 29819-29825
    • Poon, K.K.1    Chu, J.C.2    Wong, S.L.3
  • 33
    • 0035179356 scopus 로고    scopus 로고
    • Crystal structure of transcription factor MalT domain III: A novel helix repeat fold implicated in regulated oligomerization
    • C. Steegborn, O. Danot, R. Huber, and T. Clausen Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization Structure (Camb) 9 2001 1051 1060
    • (2001) Structure (Camb) , vol.9 , pp. 1051-1060
    • Steegborn, C.1    Danot, O.2    Huber, R.3    Clausen, T.4
  • 34
    • 0032504224 scopus 로고    scopus 로고
    • The death inhibitory molecules CED-9 and CED-4L use a common mechanism to inhibit the CED-3 death protease
    • D. Chaudhary, K. O'Rourke, A.M. Chinnaiyan, and V.M. Dixit The death inhibitory molecules CED-9 and CED-4L use a common mechanism to inhibit the CED-3 death protease J. Biol. Chem. 273 1998 17708 17712
    • (1998) J. Biol. Chem. , vol.273 , pp. 17708-17712
    • Chaudhary, D.1    O'Rourke, K.2    Chinnaiyan, A.M.3    Dixit, V.M.4
  • 35
    • 0033580926 scopus 로고    scopus 로고
    • Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation
    • A. Saleh, S.M. Srinivasula, S. Acharya, R. Fishel, and E.S. Alnemri Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation J. Biol. Chem. 274 1999 17941 17945
    • (1999) J. Biol. Chem. , vol.274 , pp. 17941-17945
    • Saleh, A.1    Srinivasula, S.M.2    Acharya, S.3    Fishel, R.4    Alnemri, E.S.5
  • 36
    • 0036899079 scopus 로고    scopus 로고
    • Apoptosomes: Engines for caspase activation
    • J.M. Adams, and S. Cory Apoptosomes: engines for caspase activation Curr. Opin. Cell Biol. 14 2002 715 720
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 715-720
    • Adams, J.M.1    Cory, S.2
  • 37
    • 0034484977 scopus 로고    scopus 로고
    • Hypersensitive response-related death
    • M.C. Heath Hypersensitive response-related death Plant Mol. Biol. 44 2000 321 334
    • (2000) Plant Mol. Biol. , vol.44 , pp. 321-334
    • Heath, M.C.1
  • 38
    • 0034476823 scopus 로고    scopus 로고
    • Regulators of cell death in disease resistance
    • K. Shirasu, and P. Schulze-Lefert Regulators of cell death in disease resistance Plant Mol. Biol. 44 2000 371 385
    • (2000) Plant Mol. Biol. , vol.44 , pp. 371-385
    • Shirasu, K.1    Schulze-Lefert, P.2
  • 39
    • 0027931646 scopus 로고
    • The product of the tobacco mosaic virus resistance gene N: Similarity to toll and the interleukin-1 receptor
    • S. Whitham, S.P. Dinesh-Kumar, D. Choi, R. Hehl, C. Corr, and B. Baker The product of the tobacco mosaic virus resistance gene N: similarity to toll and the interleukin-1 receptor Cell 78 1994 1101 1115
    • (1994) Cell , vol.78 , pp. 1101-1115
    • Whitham, S.1    Dinesh-Kumar, S.P.2    Choi, D.3    Hehl, R.4    Corr, C.5    Baker, B.6
  • 41
    • 0037138361 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate-binding FYVE finger
    • H. Stenmark, R. Aasland, and P.C. Driscoll The phosphatidylinositol 3-phosphate-binding FYVE finger FEBS Letters 513 2002 77 84
    • (2002) FEBS Letters , vol.513 , pp. 77-84
    • Stenmark, H.1    Aasland, R.2    Driscoll, P.C.3
  • 42
    • 0035964259 scopus 로고    scopus 로고
    • CAMP acts as a second messenger in pollen tube growth and reorientation
    • A. Moutinho, P.J. Hussey, A.J. Trewavas, and R. Malho cAMP acts as a second messenger in pollen tube growth and reorientation Proc. Natl Acad. Sci. USA 98 2001 10481 10486
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10481-10486
    • Moutinho, A.1    Hussey, P.J.2    Trewavas, A.J.3    Malho, R.4
  • 43
    • 0025250635 scopus 로고
    • Primary structure of AfsR, a global regulatory protein for secondary metabolite formation in Streptomyces coelicolor A3(2)
    • S. Horinouchi, M. Kito, M. Nishiyama, K. Furuya, S.K. Hong, K. Miyake, and T. Beppu Primary structure of AfsR, a global regulatory protein for secondary metabolite formation in Streptomyces coelicolor A3(2) Gene 95 1990 49 56
    • (1990) Gene , vol.95 , pp. 49-56
    • Horinouchi, S.1    Kito, M.2    Nishiyama, M.3    Furuya, K.4    Hong, S.K.5    Miyake, K.6    Beppu, T.7
  • 44
    • 0036040203 scopus 로고    scopus 로고
    • Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces
    • T. Umeyama, P.C. Lee, and S. Horinouchi Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces Appl. Microbiol. Biotechnol. 59 2002 419 425
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 419-425
    • Umeyama, T.1    Lee, P.C.2    Horinouchi, S.3
  • 45
    • 0028364160 scopus 로고
    • Glucitol induction in Bacillus subtilis is mediated by a regulatory factor, GutR
    • R. Ye, S.N. Rehemtulla, and S.L. Wong Glucitol induction in Bacillus subtilis is mediated by a regulatory factor, GutR J. Bacteriol. 176 1994 3321 3327
    • (1994) J. Bacteriol. , vol.176 , pp. 3321-3327
    • Ye, R.1    Rehemtulla, S.N.2    Wong, S.L.3
  • 46
    • 0033231602 scopus 로고    scopus 로고
    • Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily
    • B.C. Meyers, A.W. Dickerman, R.W. Michelmore, S. Sivaramakrishnan, B.W. Sobral, and N.D. Young Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily Plant J. 20 1999 317 332
    • (1999) Plant J. , vol.20 , pp. 317-332
    • Meyers, B.C.1    Dickerman, A.W.2    Michelmore, R.W.3    Sivaramakrishnan, S.4    Sobral, B.W.5    Young, N.D.6
  • 47
    • 0033167213 scopus 로고    scopus 로고
    • Chemical induction of disease resistance in rice is correlated with the expression of a gene encoding a nucleotide binding site and leucine-rich repeats
    • K. Sakamoto, Y. Tada, Y. Yokozeki, H. Akagi, N. Hayashi, T. Fujimura, and N. Ichikawa Chemical induction of disease resistance in rice is correlated with the expression of a gene encoding a nucleotide binding site and leucine-rich repeats Plant Mol. Biol. 40 1999 847 855
    • (1999) Plant Mol. Biol. , vol.40 , pp. 847-855
    • Sakamoto, K.1    Tada, Y.2    Yokozeki, Y.3    Akagi, H.4    Hayashi, N.5    Fujimura, T.6    Ichikawa, N.7
  • 48
    • 0031469143 scopus 로고    scopus 로고
    • Novel disease resistance specificities result from sequence exchange between tandemly repeated genes at the Cf-4/9 locus of tomato
    • M. Parniske, K.E. Hammond-Kosack, C. Golstein, C.M. Thomas, D.A. Jones, and K. Harrison Novel disease resistance specificities result from sequence exchange between tandemly repeated genes at the Cf-4/9 locus of tomato Cell 91 1997 821 832
    • (1997) Cell , vol.91 , pp. 821-832
    • Parniske, M.1    Hammond-Kosack, K.E.2    Golstein, C.3    Thomas, C.M.4    Jones, D.A.5    Harrison, K.6
  • 49
    • 0031412063 scopus 로고    scopus 로고
    • Characterization of the tomato Cf-4 gene for resistance to Cladosporium fulvum identifies sequences that determine recognitional specificity in Cf-4 and Cf-9
    • C.M. Thomas, D.A. Jones, M. Parniske, K. Harrison, P.J. Balint-Kurti, K. Hatzixanthis, and J.D. Jones Characterization of the tomato Cf-4 gene for resistance to Cladosporium fulvum identifies sequences that determine recognitional specificity in Cf-4 and Cf-9 Plant Cell 9 1997 2209 2224
    • (1997) Plant Cell , vol.9 , pp. 2209-2224
    • Thomas, C.M.1    Jones, D.A.2    Parniske, M.3    Harrison, K.4    Balint-Kurti, P.J.5    Hatzixanthis, K.6    Jones, J.D.7
  • 50
    • 0035108614 scopus 로고    scopus 로고
    • Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax
    • P.N. Dodds, G.J. Lawrence, and J.G. Ellis Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax Plant Cell 13 2001 163 178
    • (2001) Plant Cell , vol.13 , pp. 163-178
    • Dodds, P.N.1    Lawrence, G.J.2    Ellis, J.G.3
  • 51
    • 0027241482 scopus 로고
    • Monophyletic origin of the metazoa: An evolutionary link with fungi
    • P.O. Wainright, G. Hinkle, M.L. Sogin, and S.K. Stickel Monophyletic origin of the metazoa: an evolutionary link with fungi Science 260 1993 340 342
    • (1993) Science , vol.260 , pp. 340-342
    • Wainright, P.O.1    Hinkle, G.2    Sogin, M.L.3    Stickel, S.K.4
  • 53
    • 0030691980 scopus 로고    scopus 로고
    • Reactivity in vegetative incompatibility of the HET-E protein of the fungus Podospora anserina is dependent on GTP-binding activity and a WD40 repeated domain
    • E. Espagne, P. Balhadere, J. Begueret, and B. Turcq Reactivity in vegetative incompatibility of the HET-E protein of the fungus Podospora anserina is dependent on GTP-binding activity and a WD40 repeated domain Mol. Gen. Genet. 256 1997 620 627
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 620-627
    • Espagne, E.1    Balhadere, P.2    Begueret, J.3    Turcq, B.4
  • 54
    • 0033610093 scopus 로고    scopus 로고
    • GTP binding by class II transactivator: Role in nuclear import
    • J.A. Harton, D.E. Cressman, K.C. Chin, C.J. Der, and J.P. Ting GTP binding by class II transactivator: role in nuclear import Science 285 1999 1402 1405
    • (1999) Science , vol.285 , pp. 1402-1405
    • Harton, J.A.1    Cressman, D.E.2    Chin, K.C.3    Der, C.J.4    Ting, J.P.5
  • 55
    • 0037108346 scopus 로고    scopus 로고
    • Cutting edge: CATERPILLER: A large family of mammalian genes containing CARD, pyrin, nucleotide-binding, and leucine-rich repeat domains
    • J.A. Harton, M.W. Linhoff, J. Zhang, and J.P. Ting Cutting edge: CATERPILLER: a large family of mammalian genes containing CARD, pyrin, nucleotide-binding, and leucine-rich repeat domains J. Immunol. 169 2002 4088 4093
    • (2002) J. Immunol. , vol.169 , pp. 4088-4093
    • Harton, J.A.1    Linhoff, M.W.2    Zhang, J.3    Ting, J.P.4
  • 56
    • 0042093746 scopus 로고    scopus 로고
    • Mutations in a novel gene, NPHP3, cause adolescent nephronophthisis, tapeto-retinal degeneration and hepatic fibrosis
    • H. Olbrich, M. Fliegauf, J. Hoefele, A. Kispert, E. Otto, and A. Volz Mutations in a novel gene, NPHP3, cause adolescent nephronophthisis, tapeto-retinal degeneration and hepatic fibrosis Nature Genet. 34 2003 455 459
    • (2003) Nature Genet. , vol.34 , pp. 455-459
    • Olbrich, H.1    Fliegauf, M.2    Hoefele, J.3    Kispert, A.4    Otto, E.5    Volz, A.6
  • 58
    • 1842524194 scopus 로고    scopus 로고
    • Worms taste bitter: ASH neurons, QUI-1, GPA-3 and ODR-3 mediate quinine avoidance in Caenorhabditis elegans
    • M.A. Hilliard, C. Bergamasco, S. Arbucci, R.H. Plasterk, and P. Bazzicalupo Worms taste bitter: ASH neurons, QUI-1, GPA-3 and ODR-3 mediate quinine avoidance in Caenorhabditis elegans EMBO J. 23 2004 1101 1111
    • (2004) EMBO J. , vol.23 , pp. 1101-1111
    • Hilliard, M.A.1    Bergamasco, C.2    Arbucci, S.3    Plasterk, R.H.4    Bazzicalupo, P.5
  • 59
    • 0029093235 scopus 로고
    • A gene responsible for vegetative incompatibility in the fungus Podospora anserina encodes a protein with a GTP-binding motif and G beta homologous domain
    • S. Saupe, B. Turcq, and J. Begueret A gene responsible for vegetative incompatibility in the fungus Podospora anserina encodes a protein with a GTP-binding motif and G beta homologous domain Gene 162 1995 135 139
    • (1995) Gene , vol.162 , pp. 135-139
    • Saupe, S.1    Turcq, B.2    Begueret, J.3
  • 60
    • 0036262783 scopus 로고    scopus 로고
    • HET-E and HET-D belong to a new subfamily of WD40 proteins involved in vegetative incompatibility specificity in the fungus Podospora anserina
    • E. Espagne, P. Balhadere, M.L. Penin, C. Barreau, and B. Turcq HET-E and HET-D belong to a new subfamily of WD40 proteins involved in vegetative incompatibility specificity in the fungus Podospora anserina Genetics 161 2002 71 81
    • (2002) Genetics , vol.161 , pp. 71-81
    • Espagne, E.1    Balhadere, P.2    Penin, M.L.3    Barreau, C.4    Turcq, B.5
  • 61
    • 0035697161 scopus 로고    scopus 로고
    • Rolling pebbles (rols) is required in Drosophila muscle precursors for recruitment of myoblasts for fusion
    • A. Rau, D. Buttgereit, A. Holz, R. Fetter, S.K. Doberstein, and A. Paululat rolling pebbles (rols) is required in Drosophila muscle precursors for recruitment of myoblasts for fusion Development 128 2001 5061 5073
    • (2001) Development , vol.128 , pp. 5061-5073
    • Rau, A.1    Buttgereit, D.2    Holz, A.3    Fetter, R.4    Doberstein, S.K.5    Paululat, A.6
  • 62
    • 0035515528 scopus 로고    scopus 로고
    • Drosophila rolling pebbles: A multidomain protein required for myoblast fusion that recruits D-Titin in response to the myoblast attractant Dumbfounded
    • S.D. Menon, and W. Chia Drosophila rolling pebbles: a multidomain protein required for myoblast fusion that recruits D-Titin in response to the myoblast attractant Dumbfounded Dev. Cell 1 2001 691 703
    • (2001) Dev. Cell , vol.1 , pp. 691-703
    • Menon, S.D.1    Chia, W.2
  • 65
    • 0037844844 scopus 로고    scopus 로고
    • Kinetic properties of "soluble" adenylyl cyclase. Synergism between calcium and bicarbonate
    • T.N. Litvin, M. Kamenetsky, A. Zarifyan, J. Buck, and L.R. Levin Kinetic properties of "soluble" adenylyl cyclase. Synergism between calcium and bicarbonate J. Biol. Chem. 278 2003 15922 15926
    • (2003) J. Biol. Chem. , vol.278 , pp. 15922-15926
    • Litvin, T.N.1    Kamenetsky, M.2    Zarifyan, A.3    Buck, J.4    Levin, L.R.5
  • 66
    • 0035881479 scopus 로고    scopus 로고
    • The Dictyostelium homologue of mammalian soluble adenylyl cyclase encodes a guanylyl cyclase
    • J. Roelofs, M. Meima, P. Schaap, and P.J. Van Haastert The Dictyostelium homologue of mammalian soluble adenylyl cyclase encodes a guanylyl cyclase EMBO J. 20 2001 4341 4348
    • (2001) EMBO J. , vol.20 , pp. 4341-4348
    • Roelofs, J.1    Meima, M.2    Schaap, P.3    Van Haastert, P.J.4
  • 67
    • 0035963319 scopus 로고    scopus 로고
    • Genes lost during evolution
    • J. Roelofs, and P.J. Van Haastert Genes lost during evolution Nature 411 2001 1013 1014
    • (2001) Nature , vol.411 , pp. 1013-1014
    • Roelofs, J.1    Van Haastert, P.J.2
  • 68
    • 0036900083 scopus 로고    scopus 로고
    • Deducing the origin of soluble adenylyl cyclase, a gene lost in multiple lineages
    • J. Roelofs, and P.J. Van Haastert Deducing the origin of soluble adenylyl cyclase, a gene lost in multiple lineages Mol. Biol. Evol. 19 2002 2239 2246
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 2239-2246
    • Roelofs, J.1    Van Haastert, P.J.2
  • 69
    • 0033145727 scopus 로고    scopus 로고
    • A subfamily of MalT-related ATPdependent regulators in the LuxR family
    • A. De Schrijver, and R. De Mot A subfamily of MalT-related ATPdependent regulators in the LuxR family Microbiology 145 1999 1287 1288
    • (1999) Microbiology , vol.145 , pp. 1287-1288
    • De Schrijver, A.1    De Mot, R.2
  • 70
    • 0042705655 scopus 로고    scopus 로고
    • The Streptomyces coelicolor A3(2) lipAR operon encodes an extracellular lipase and a new type of transcriptional regulator
    • F. Valdez, G. Gonzalez-Ceron, H.M. Kieser, and L. Servin-Gonzalez The Streptomyces coelicolor A3(2) lipAR operon encodes an extracellular lipase and a new type of transcriptional regulator Microbiology 145 1999 2365 2374
    • (1999) Microbiology , vol.145 , pp. 2365-2374
    • Valdez, F.1    Gonzalez-Ceron, G.2    Kieser, H.M.3    Servin-Gonzalez, L.4
  • 71
    • 0034047123 scopus 로고    scopus 로고
    • Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455: Analysis of the gene cluster and deduction of the biosynthetic pathway
    • T. Brautaset, O.N. Sekurova, H. Sletta, T.E. Ellingsen, A.R. StrLm, S. Valla, and S.B. Zotchev Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455: analysis of the gene cluster and deduction of the biosynthetic pathway Chem. Biol. 7 2000 395 403
    • (2000) Chem. Biol. , vol.7 , pp. 395-403
    • Brautaset, T.1    Sekurova, O.N.2    Sletta, H.3    Ellingsen, T.E.4    Strlm, A.R.5    Valla, S.6    Zotchev, S.B.7
  • 72
    • 0035031304 scopus 로고    scopus 로고
    • Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae
    • D.J. Wilson, Y. Xue, K.A. Reynolds, and D.H. Sherman Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae J. Bacteriol. 183 2001 3468 3475
    • (2001) J. Bacteriol. , vol.183 , pp. 3468-3475
    • Wilson, D.J.1    Xue, Y.2    Reynolds, K.A.3    Sherman, D.H.4
  • 73
    • 0037469308 scopus 로고    scopus 로고
    • Cloning and characterization of a gene cluster for geldanamycin production in Streptomyces hygroscopicus NRRL 3602
    • A. Rascher, Z. Hu, N. Viswanathan, A. Schirmer, R. Reid, and W.C. Nierman Cloning and characterization of a gene cluster for geldanamycin production in Streptomyces hygroscopicus NRRL 3602 FEMS Microbiol. Letters 218 2003 223 230
    • (2003) FEMS Microbiol. Letters , vol.218 , pp. 223-230
    • Rascher, A.1    Hu, Z.2    Viswanathan, N.3    Schirmer, A.4    Reid, R.5    Nierman, W.C.6
  • 74
    • 0030986983 scopus 로고    scopus 로고
    • Characterization of the genes encoding a receptor-like histidine kinase and a cognate response regulator from a biphenyl/polychlorobiphenyl-degrading bacterium, Rhodococcus sp. strain M5
    • D. Labbe, J. Garnon, and P.C. Lau Characterization of the genes encoding a receptor-like histidine kinase and a cognate response regulator from a biphenyl/polychlorobiphenyl-degrading bacterium, Rhodococcus sp. strain M5 J. Bacteriol. 179 1997 2772 2776
    • (1997) J. Bacteriol. , vol.179 , pp. 2772-2776
    • Labbe, D.1    Garnon, J.2    Lau, P.C.3
  • 75
    • 0023712288 scopus 로고
    • Alkane utilization in Pseudomonas oleovorans. Structure and function of the regulatory locus alkR
    • G. Eggink, H. Engel, W.G. Meijer, J. Otten, J. Kingma, and B. Witholt Alkane utilization in Pseudomonas oleovorans. Structure and function of the regulatory locus alkR J. Biol. Chem. 263 1988 13400 13405
    • (1988) J. Biol. Chem. , vol.263 , pp. 13400-13405
    • Eggink, G.1    Engel, H.2    Meijer, W.G.3    Otten, J.4    Kingma, J.5    Witholt, B.6
  • 77
    • 0034283843 scopus 로고    scopus 로고
    • Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network
    • W. Boos, and A. Bohm Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network Trends Genet. 16 2000 404 409
    • (2000) Trends Genet. , vol.16 , pp. 404-409
    • Boos, W.1    Bohm, A.2
  • 78
    • 0035895198 scopus 로고    scopus 로고
    • A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator family
    • O. Danot A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator family Proc. Natl Acad. Sci. USA 98 2001 435 440
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 435-440
    • Danot, O.1
  • 79
    • 0037053363 scopus 로고    scopus 로고
    • The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon
    • N. Joly, O. Danot, A. Schlegel, W. Boos, and E. Richet The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon J. Biol. Chem. 277 2002 16606 16613
    • (2002) J. Biol. Chem. , vol.277 , pp. 16606-16613
    • Joly, N.1    Danot, O.2    Schlegel, A.3    Boos, W.4    Richet, E.5
  • 80
    • 0033585068 scopus 로고    scopus 로고
    • Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP
    • V. Schreiber, and E. Richet Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP J. Biol. Chem. 274 1999 33220 33226
    • (1999) J. Biol. Chem. , vol.274 , pp. 33220-33226
    • Schreiber, V.1    Richet, E.2
  • 81
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta′ subunit of the clamp-loader complex of E. coli DNA polymerase III
    • B. Guenther, R. Onrust, A. Sali, M. O'Donnell, and J. Kuriyan Crystal structure of the delta′ subunit of the clamp-loader complex of E. coli DNA polymerase III Cell 91 1997 335 345
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 82
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • R.C. Yu, P.I. Hanson, R. Jahn, and A.T. Brunger Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP Nature Struct. Biol. 5 1998 803 811
    • (1998) Nature Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 83
    • 0033081408 scopus 로고    scopus 로고
    • The hexamerization domain of N-ethylmaleimidesensitive factor: Structural clues to chaperone function
    • A.F. Neuwald The hexamerization domain of N-ethylmaleimidesensitive factor: structural clues to chaperone function Struct. Fold. Des. 7 1999 R19 R23
    • (1999) Struct. Fold. Des. , vol.7
    • Neuwald, A.F.1
  • 85
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: Implications for origin recognition and checkpoint control
    • J. Liu, C.L. Smith, D. DeRyckere, K. DeAngelis, G.S. Martin, and J.M. Berger Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control Mol. Cell 6 2000 637 648
    • (2000) Mol. Cell , vol.6 , pp. 637-648
    • Liu, J.1    Smith, C.L.2    Deryckere, D.3    Deangelis, K.4    Martin, G.S.5    Berger, J.M.6
  • 86
    • 0035800571 scopus 로고    scopus 로고
    • Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase
    • M.N. Fodje, A. Hansson, M. Hansson, J.G. Olsen, S. Gough, R.D. Willows, and S. Al-Karadaghi Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase J. Mol. Biol. 311 2001 111 122
    • (2001) J. Mol. Biol. , vol.311 , pp. 111-122
    • Fodje, M.N.1    Hansson, A.2    Hansson, M.3    Olsen, J.G.4    Gough, S.5    Willows, R.D.6    Al-Karadaghi, S.7
  • 87
    • 0035852703 scopus 로고    scopus 로고
    • Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8
    • K. Yamada, N. Kunishima, K. Mayanagi, T. Ohnishi, T. Nishino, and H. Iwasaki Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8 Proc. Natl Acad. Sci. USA 98 2001 1442 1447
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1442-1447
    • Yamada, K.1    Kunishima, N.2    Mayanagi, K.3    Ohnishi, T.4    Nishino, T.5    Iwasaki, H.6
  • 88
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • F. Guo, M.R. Maurizi, L. Esser, and D. Xia Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease J. Biol. Chem. 277 2002 46743 46752
    • (2002) J. Biol. Chem. , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 89
    • 0036054289 scopus 로고    scopus 로고
    • The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 resolution
    • S. Krzywda, A.M. Brzozowski, C. Verma, K. Karata, T. Ogura, and A.J. Wilkinson The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 resolution Structure (Camb) 10 2002 1073 1083
    • (2002) Structure (Camb) , vol.10 , pp. 1073-1083
    • Krzywda, S.1    Brzozowski, A.M.2    Verma, C.3    Karata, K.4    Ogura, T.5    Wilkinson, A.J.6
  • 90
    • 0034664813 scopus 로고    scopus 로고
    • SURVEY and SUMMARY: Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories
    • L. Aravind, K.S. Makarova, and E.V. Koonin SURVEY AND SUMMARY: holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories Nucl. Acids Res. 28 2000 3417 3432
    • (2000) Nucl. Acids Res. , vol.28 , pp. 3417-3432
    • Aravind, L.1    Makarova, K.S.2    Koonin, E.V.3
  • 91
    • 0029914954 scopus 로고    scopus 로고
    • Linkage of genes essential for synthesis of a polysaccharide capsule in Sphingomonas strain S88
    • M. Yamazaki, L. Thorne, M. Mikolajczak, R.W. Armentrout, and T.J. Pollock Linkage of genes essential for synthesis of a polysaccharide capsule in Sphingomonas strain S88 J. Bacteriol. 178 1996 2676 2687
    • (1996) J. Bacteriol. , vol.178 , pp. 2676-2687
    • Yamazaki, M.1    Thorne, L.2    Mikolajczak, M.3    Armentrout, R.W.4    Pollock, T.J.5
  • 92
    • 0022617696 scopus 로고
    • The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon
    • S.T. Cole, and O. Raibaud The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon Gene 42 1986 201 208
    • (1986) Gene , vol.42 , pp. 201-208
    • Cole, S.T.1    Raibaud, O.2
  • 93
    • 0031046574 scopus 로고    scopus 로고
    • Identification and characterization of acoK, a regulatory gene of the Klebsiella pneumoniae acoABCD operon
    • H.L. Peng, Y.H. Yang, W.L. Deng, and H.Y. Chang Identification and characterization of acoK, a regulatory gene of the Klebsiella pneumoniae acoABCD operon J. Bacteriol. 179 1997 1497 1504
    • (1997) J. Bacteriol. , vol.179 , pp. 1497-1504
    • Peng, H.L.1    Yang, Y.H.2    Deng, W.L.3    Chang, H.Y.4
  • 94
    • 0141703301 scopus 로고    scopus 로고
    • Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa
    • B.S. Jaiswal, and M. Conti Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa Proc. Natl Acad. Sci. USA 100 2003 10676 10681
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10676-10681
    • Jaiswal, B.S.1    Conti, M.2
  • 96
    • 0029819318 scopus 로고    scopus 로고
    • The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny
    • S.L. Baldauf, J.D. Palmer, and W.F. Doolittle The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny Proc. Natl Acad. Sci. USA 93 1996 7749 7754
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7749-7754
    • Baldauf, S.L.1    Palmer, J.D.2    Doolittle, W.F.3
  • 97
    • 0031769997 scopus 로고    scopus 로고
    • Evolutionary anomalies among the aminoacyl-tRNA synthetases
    • R.F. Doolittle, and J. Handy Evolutionary anomalies among the aminoacyl-tRNA synthetases Curr. Opin. Genet. Dev. 8 1998 630 636
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 630-636
    • Doolittle, R.F.1    Handy, J.2
  • 98
    • 0033975419 scopus 로고    scopus 로고
    • The bacterial replicative helicase DnaB evolved from a RecA duplication
    • D.D. Leipe, L. Aravind, N.V. Grishin, and E.V. Koonin The bacterial replicative helicase DnaB evolved from a RecA duplication Genome Res. 10 2000 5 16
    • (2000) Genome Res. , vol.10 , pp. 5-16
    • Leipe, D.D.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 99
    • 0036066765 scopus 로고    scopus 로고
    • The role of lineage-specific gene family expansion in the evolution of eukaryotes
    • O. Lespinet, Y.I. Wolf, E.V. Koonin, and L. Aravind The role of lineage-specific gene family expansion in the evolution of eukaryotes Genome Res. 12 2002 1048 1059
    • (2002) Genome Res. , vol.12 , pp. 1048-1059
    • Lespinet, O.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 100
    • 0343352530 scopus 로고    scopus 로고
    • Divergent evolution of plant NBS-LRR resistance gene homologues in dicot and cereal genomes
    • Q. Pan, J. Wendel, and R. Fluhr Divergent evolution of plant NBS-LRR resistance gene homologues in dicot and cereal genomes J. Mol. Evol. 50 2000 203 213
    • (2000) J. Mol. Evol. , vol.50 , pp. 203-213
    • Pan, Q.1    Wendel, J.2    Fluhr, R.3
  • 101
    • 0036916368 scopus 로고    scopus 로고
    • Diversity in nucleotide binding site-leucine-rich repeat genes in cereals
    • J. Bai, L.A. Pennill, J. Ning, S.W. Lee, J. Ramalingam, and C.A. Webb Diversity in nucleotide binding site-leucine-rich repeat genes in cereals Genome Res. 12 2002 1871 1884
    • (2002) Genome Res. , vol.12 , pp. 1871-1884
    • Bai, J.1    Pennill, L.A.2    Ning, J.3    Lee, S.W.4    Ramalingam, J.5    Webb, C.A.6
  • 102
    • 0035895540 scopus 로고    scopus 로고
    • Apoptotic molecular machinery: Vastly increased complexity in vertebrates revealed by genome comparisons
    • L. Aravind, V.M. Dixit, and E.V. Koonin Apoptotic molecular machinery: vastly increased complexity in vertebrates revealed by genome comparisons Science 291 2001 1279 1284
    • (2001) Science , vol.291 , pp. 1279-1284
    • Aravind, L.1    Dixit, V.M.2    Koonin, E.V.3
  • 104
    • 0036032981 scopus 로고    scopus 로고
    • Domain analysis of transcriptional regulators bearing PTS regulatory domains
    • D.B. Greenberg, J. Stulke, and M.H. Saier Jr Domain analysis of transcriptional regulators bearing PTS regulatory domains Res. Microbiol. 153 2002 519 526
    • (2002) Res. Microbiol. , vol.153 , pp. 519-526
    • Greenberg, D.B.1    Stulke, J.2    Saier Jr., M.H.3
  • 105
    • 0242354978 scopus 로고    scopus 로고
    • Evolutionary connections between bacterial and eukaryotic signaling systems: A genomic perspective
    • L. Aravind, V. Anantharaman, and L.M. Iyer Evolutionary connections between bacterial and eukaryotic signaling systems: a genomic perspective Curr. Opin. Microbiol. 6 2003 490 497
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 490-497
    • Aravind, L.1    Anantharaman, V.2    Iyer, L.M.3
  • 106
    • 0032404453 scopus 로고    scopus 로고
    • You are what you eat: A gene transfer ratchet could account for bacterial genes in eukaryotic nuclear genomes
    • W.F. Doolittle You are what you eat: a gene transfer ratchet could account for bacterial genes in eukaryotic nuclear genomes Trends Genet. 14 1998 307 311
    • (1998) Trends Genet. , vol.14 , pp. 307-311
    • Doolittle, W.F.1
  • 107
    • 0348044549 scopus 로고    scopus 로고
    • Genome trees constructed using five different approaches suggest new major bacterial clades
    • Y.I. Wolf, I.B. Rogozin, N.V. Grishin, R.L. Tatusov, and E.V. Koonin Genome trees constructed using five different approaches suggest new major bacterial clades BMC Evol. Biol. 1 2001 8
    • (2001) BMC Evol. Biol. , vol.1 , pp. 8
    • Wolf, Y.I.1    Rogozin, I.B.2    Grishin, N.V.3    Tatusov, R.L.4    Koonin, E.V.5
  • 108
    • 2942576138 scopus 로고    scopus 로고
    • Evolution of bacterial RNA polymerase: Implications for large-scale bacterial phylogeny, domain accretion, and horizontal gene transfer
    • L.M. Iyer, E.V. Koonin, and LA Evolution of bacterial RNA polymerase: implications for large-scale bacterial phylogeny, domain accretion, and horizontal gene transfer Gene 335 2004 73 88
    • (2004) Gene , vol.335 , pp. 73-88
    • Iyer, L.M.1    Koonin, E.V.2
  • 109
    • 18644379392 scopus 로고    scopus 로고
    • Crystal structure of the RuvA-RuvB complex: A structural basis for the Holliday junction migrating motor machinery
    • K. Yamada, T. Miyata, D. Tsuchiya, T. Oyama, Y. Fujiwara, and T. Ohnishi Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery Mol. Cell 10 2002 671 681
    • (2002) Mol. Cell , vol.10 , pp. 671-681
    • Yamada, K.1    Miyata, T.2    Tsuchiya, D.3    Oyama, T.4    Fujiwara, Y.5    Ohnishi, T.6
  • 110
    • 0032202153 scopus 로고    scopus 로고
    • Three genes of the Arabidopsis RPP1 complex resistance locus recognize distinct Peronospora parasitica avirulence determinants
    • M.A. Botella, J.E. Parker, L.N. Frost, P.D. Bittner-Eddy, J.L. Beynon, and M.J. Daniels Three genes of the Arabidopsis RPP1 complex resistance locus recognize distinct Peronospora parasitica avirulence determinants Plant Cell 10 1998 1847 1860
    • (1998) Plant Cell , vol.10 , pp. 1847-1860
    • Botella, M.A.1    Parker, J.E.2    Frost, L.N.3    Bittner-Eddy, P.D.4    Beynon, J.L.5    Daniels, M.J.6
  • 114
    • 0033591330 scopus 로고    scopus 로고
    • Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB
    • N. Inohara, T. Koseki, L. del Peso, Y. Hu, C. Yee, and S. Chen Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB J. Biol. Chem. 274 1999 14560 14567
    • (1999) J. Biol. Chem. , vol.274 , pp. 14560-14567
    • Inohara, N.1    Koseki, T.2    Del Peso, L.3    Hu, Y.4    Yee, C.5    Chen, S.6
  • 115
    • 0035050491 scopus 로고    scopus 로고
    • Two distinct domains within CIITA mediate selfassociation: Involvement of the GTP-binding and leucine-rich repeat domains
    • M.W. Linhoff, J.A. Harton, D.E. Cressman, B.K. Martin, and J.P. Ting Two distinct domains within CIITA mediate selfassociation: involvement of the GTP-binding and leucine-rich repeat domains Mol. Cell. Biol. 21 2001 3001 3011
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3001-3011
    • Linhoff, M.W.1    Harton, J.A.2    Cressman, D.E.3    Martin, B.K.4    Ting, J.P.5
  • 116
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • D. Acehan, X. Jiang, D.G. Morgan, J.E. Heuser, X. Wang, and C.W. Akey Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation Mol. Cell 9 2002 423 432
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 118
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases
    • S.F. Altschul, and E.V. Koonin Iterated profile searches with PSI-BLAST - a tool for discovery in protein databases Trends Biochem. Sci. 23 1998 444 447
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 120
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • C. Notredame, D.G. Higgins, and J. Heringa T-Coffee: a novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302 2000 205 217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 121
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • G.J. Barton ALSCRIPT: a tool to format multiple sequence alignments Protein Eng. 6 1993 37 40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 122
    • 0030788541 scopus 로고    scopus 로고
    • Extracting protein alignment models from the sequence database
    • A.F. Neuwald, J.S. Liu, D.J. Lipman, and C.E. Lawrence Extracting protein alignment models from the sequence database Nucl. Acids Res. 25 1997 1665 1677
    • (1997) Nucl. Acids Res. , vol.25 , pp. 1665-1677
    • Neuwald, A.F.1    Liu, J.S.2    Lipman, D.J.3    Lawrence, C.E.4
  • 123
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • J.A. Cuff, and G.J. Barton Application of multiple sequence alignment profiles to improve protein secondary structure prediction Proteins: Struct. Funct. Genet. 40 2000 502 511
    • (2000) Proteins: Struct. Funct. Genet. , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 124
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • B. Rost PHD: predicting one-dimensional protein structure by profile-based neural networks Methods Enzymol. 266 1996 525 539
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 128
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • D.T. Jones, W.R. Taylor, and J.M. Thornton The rapid generation of mutation data matrices from protein sequences Comput. Appl. Biosci. 8 1992 275 282
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 129
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • S. Kumar, K. Tamura, I.B. Jakobsen, and M. Nei MEGA2: molecular evolutionary genetics analysis software Bioinformatics 17 2001 1244 1245
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 131
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • R.D. Page TreeView: an application to display phylogenetic trees on personal computers Comput. Appl. Biosci. 12 1996 357 358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 132
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains archaea, bacteria, and eucarya
    • C.R. Woese, O. Kandler, and M.L. Wheelis Towards a natural system of organisms: proposal for the domains archaea, bacteria, and eucarya Proc. Natl Acad. Sci. USA 87 1990 4576 4579
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 133
    • 2942733563 scopus 로고    scopus 로고
    • New knowledge from old: In silico discovery of novel protein domains in Streptomyces coelicolor
    • C. Yeats, S. Bentley, and A. Bateman New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor BMC Microbiol. 3 2003 3
    • (2003) BMC Microbiol. , vol.3 , pp. 3
    • Yeats, C.1    Bentley, S.2    Bateman, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.