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Volumn 140, Issue 4, 2006, Pages 1233-1245

Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; HYDROLYSIS; MUTAGENS;

EID: 33745478448     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.105.073510     Document Type: Article
Times cited : (239)

References (77)
  • 1
    • 0242626505 scopus 로고    scopus 로고
    • Structural localization of disease-associated sequence variations in the NACHT and LRR domains of PYPAF1 and NOD2
    • Albrecht M, Domingues FS, Schreiber S, Lengauer T (2003a) Structural localization of disease-associated sequence variations in the NACHT and LRR domains of PYPAF1 and NOD2. FEES Lett 554: 520-528
    • (2003) FEES Lett , vol.554 , pp. 520-528
    • Albrecht, M.1    Domingues, F.S.2    Schreiber, S.3    Lengauer, T.4
  • 2
    • 0344033717 scopus 로고    scopus 로고
    • Disease-associated variants in PYPAF1 and NOD2 result in similar alterations of conserved sequence
    • Albrecht M, Lengauer T, Schreiber S (2003b) Disease-associated variants in PYPAF1 and NOD2 result in similar alterations of conserved sequence. Bioinformatics 19: 2171-2175
    • (2003) Bioinformatics , vol.19 , pp. 2171-2175
    • Albrecht, M.1    Lengauer, T.2    Schreiber, S.3
  • 3
    • 28444488986 scopus 로고    scopus 로고
    • Update on the domain architectures of NLRs and R proteins
    • Albrecht M, Takken FLW (2006) Update on the domain architectures of NLRs and R proteins. Biochem Biophys Res Commun 339: 459-462
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 459-462
    • Albrecht, M.1    Takken, F.L.W.2
  • 4
    • 0031127301 scopus 로고    scopus 로고
    • Inactivation of the flax rust resistance gene M associated with loss of a repeated unit within the leucine-rich repeat coding region
    • Anderson PA, Lawrence GJ, Morrish BC, Ayliffe MA, Finnegan EJ, Ellis JG (1997) Inactivation of the flax rust resistance gene M associated with loss of a repeated unit within the leucine-rich repeat coding region. Plant Cell 9: 641-651
    • (1997) Plant Cell , vol.9 , pp. 641-651
    • Anderson, P.A.1    Lawrence, G.J.2    Morrish, B.C.3    Ayliffe, M.A.4    Finnegan, E.J.5    Ellis, J.G.6
  • 7
    • 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
    • Aravind L, Iyer LM, Leipe DD, Koonin EV (2004) A novel family of P-loop NTPases with an unusual phyletic distribution and transmembrane segments inserted within the NTPase domain. Genome Biol 5: R30
    • (2004) Genome Biol , vol.5
    • Aravind, L.1    Iyer, L.M.2    Leipe, D.D.3    Koonin, E.V.4
  • 10
    • 3042762926 scopus 로고    scopus 로고
    • Plant disease resistance protein signaling: NBS-LRR proteins and their partners
    • Belkhadir Y, Subramaniam R, Dangl JL (2004) Plant disease resistance protein signaling: NBS-LRR proteins and their partners. Curr Opin Plant Biol 7: 391-399
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 391-399
    • Belkhadir, Y.1    Subramaniam, R.2    Dangl, J.L.3
  • 11
    • 0036775380 scopus 로고    scopus 로고
    • Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato
    • Bendahmane A, Farnham G, Moffett P, Baulcombe DC (2002) Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato. Plant J 32: 195-204
    • (2002) Plant J , vol.32 , pp. 195-204
    • Bendahmane, A.1    Farnham, G.2    Moffett, P.3    Baulcombe, D.C.4
  • 12
    • 20444426395 scopus 로고    scopus 로고
    • RAR1 positively controls steady state levels of barley MLA resistance proteins and enables sufficient MLA6 accumulation for effective resistance
    • Bieri S, Mauch S, Shen QH, Peart J, Devoto A, Casais C, Ceron F, Schulze S, Steinbiss HH, Shirasu K, et al (2004) RAR1 positively controls steady state levels of barley MLA resistance proteins and enables sufficient MLA6 accumulation for effective resistance. Plant Cell 16: 3480-3495
    • (2004) Plant Cell , vol.16 , pp. 3480-3495
    • Bieri, S.1    Mauch, S.2    Shen, Q.H.3    Peart, J.4    Devoto, A.5    Casais, C.6    Ceron, F.7    Schulze, S.8    Steinbiss, H.H.9    Shirasu, K.10
  • 15
    • 0041827164 scopus 로고    scopus 로고
    • Nods, Nalps and Naip: Intracellular regulators of bacterial-induced inflammation
    • Chamaillard M, Girardin SE, Viala J, Philpott DJ (2003) Nods, Nalps and Naip: intracellular regulators of bacterial-induced inflammation. Cell Microbiol 5: 581-592
    • (2003) Cell Microbiol , vol.5 , pp. 581-592
    • Chamaillard, M.1    Girardin, S.E.2    Viala, J.3    Philpott, D.J.4
  • 16
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl JL, Jones JDG (2001) Plant pathogens and integrated defence responses to infection. Nature 411: 826-833
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.G.2
  • 18
    • 0034687842 scopus 로고    scopus 로고
    • Structure-function analysis of the tobacco mosaic virus resistance gene N
    • Dinesh-Kumar SP, Tham WH, Baker BJ (2000) Structure-function analysis of the tobacco mosaic virus resistance gene N. Proc Natl Acad Sci USA 97: 14789-14794
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14789-14794
    • Dinesh-Kumar, S.P.1    Tham, W.H.2    Baker, B.J.3
  • 19
    • 2542452727 scopus 로고    scopus 로고
    • Cryopyrin-induced interleukin 1beta secretion in monocytic cells: Enhanced activity of disease-associated mutants and requirement for ASC
    • Dowds TA, Masumoto J, Zhu L, Inohara N, Nunez G (2004) Cryopyrin-induced interleukin 1beta secretion in monocytic cells: enhanced activity of disease-associated mutants and requirement for ASC. J Biol Chem 279: 21924-21928
    • (2004) J Biol Chem , vol.279 , pp. 21924-21928
    • Dowds, T.A.1    Masumoto, J.2    Zhu, L.3    Inohara, N.4    Nunez, G.5
  • 20
    • 0033946441 scopus 로고    scopus 로고
    • Structure, function and evolution of plant disease resistance genes
    • Ellis J, Dodds P, Pryor T (2000) Structure, function and evolution of plant disease resistance genes. Curr Opin Plant Biol 3: 278-284
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 278-284
    • Ellis, J.1    Dodds, P.2    Pryor, T.3
  • 21
    • 0034307755 scopus 로고    scopus 로고
    • Interplay of signaling pathways in plant disease resistance
    • Feys BJ, Parker JE (2000) Interplay of signaling pathways in plant disease resistance. Trends Genet 16: 449-455
    • (2000) Trends Genet , vol.16 , pp. 449-455
    • Feys, B.J.1    Parker, J.E.2
  • 22
    • 0030464460 scopus 로고    scopus 로고
    • SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny
    • Galtier N, Gouy M, Gautier C (1996) SEAVIEW and PHYLO_WIN: two graphic tools for sequence alignment and molecular phylogeny. Comput Appl Biosci 12: 543-548
    • (1996) Comput Appl Biosci , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2    Gautier, C.3
  • 24
    • 0041620404 scopus 로고    scopus 로고
    • Detection of reliable and unexpected protein fold predictions using 3D-Jury
    • Ginalski K, Rychlewski L (2003) Detection of reliable and unexpected protein fold predictions using 3D-Jury. Nucleic Acids Res 31: 3291-3292
    • (2003) Nucleic Acids Res , vol.31 , pp. 3291-3292
    • Ginalski, K.1    Rychlewski, L.2
  • 25
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P, Robert X, Courcelle E (2003) ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 31: 3320-3323
    • (2003) Nucleic Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 27
    • 0032807099 scopus 로고    scopus 로고
    • The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells
    • Herbig U, Marlar CA, Fanning E (1999) The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells. Mol Biol Cell 10: 2631-2645
    • (1999) Mol Biol Cell , vol.10 , pp. 2631-2645
    • Herbig, U.1    Marlar, C.A.2    Fanning, E.3
  • 28
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R, Krummel B, Saiki RK (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res 16: 7351-7367
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 29
    • 19544374693 scopus 로고    scopus 로고
    • Autoactive alleles of the flax L6 rust resistance gene induce non-race-specific rust resistance associated with the hypersensitive response
    • Howles P, Lawrence G, Finnegan J, McFadden H, Ayliffe M, Dodds P, Ellis J (2005) Autoactive alleles of the flax L6 rust resistance gene induce non-race-specific rust resistance associated with the hypersensitive response. Mol Plant Microbe Interact 18: 570-582
    • (2005) Mol Plant Microbe Interact , vol.18 , pp. 570-582
    • Howles, P.1    Lawrence, G.2    Finnegan, J.3    McFadden, H.4    Ayliffe, M.5    Dodds, P.6    Ellis, J.7
  • 30
    • 0033823537 scopus 로고    scopus 로고
    • Evidence for a role of the N terminus and leucine-rich repeat region of the Mi gene product in regulation of localized cell death
    • Hwang CF, Bhakta AV, Truesdell GM, Pudlo WM, Williamson VM (2000) Evidence for a role of the N terminus and leucine-rich repeat region of the Mi gene product in regulation of localized cell death. Plant Cell 12: 1319-1329
    • (2000) Plant Cell , vol.12 , pp. 1319-1329
    • Hwang, C.F.1    Bhakta, A.V.2    Truesdell, G.M.3    Pudlo, W.M.4    Williamson, V.M.5
  • 31
    • 0038806568 scopus 로고    scopus 로고
    • Leucine-rich repeat-mediated intramolecular interactions in nematode recognition and cell death signaling by the tomato resistance protein Mi
    • Hwang CF, Williamson VM (2003) Leucine-rich repeat-mediated intramolecular interactions in nematode recognition and cell death signaling by the tomato resistance protein Mi. Plant J 34: 585-593
    • (2003) Plant J , vol.34 , pp. 585-593
    • Hwang, C.F.1    Williamson, V.M.2
  • 32
    • 0038624558 scopus 로고    scopus 로고
    • NODs: Intracellular proteins involved in inflammation and apoptosis
    • Inohara N, Nunez G (2003) NODs: intracellular proteins involved in inflammation and apoptosis. Nature Rev lmmunol 3: 371-382
    • (2003) Nature Rev Lmmunol , vol.3 , pp. 371-382
    • Inohara, N.1    Nunez, G.2
  • 33
    • 0036696447 scopus 로고    scopus 로고
    • NPK1, an MEKK1-like mitogen-activated protein kinase kinase kinase, regulates innate immunity and development in plants
    • Jin H, Axtell MJ, Dahlbeck D, Ekwenna O, Zhang S, Staskawicz B, Baker B (2002) NPK1, an MEKK1-like mitogen-activated protein kinase kinase kinase, regulates innate immunity and development in plants. Dev Cell 3: 291-297
    • (2002) Dev Cell , vol.3 , pp. 291-297
    • Jin, H.1    Axtell, M.J.2    Dahlbeck, D.3    Ekwenna, O.4    Zhang, S.5    Staskawicz, B.6    Baker, B.7
  • 34
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 27644505459 scopus 로고    scopus 로고
    • Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on APAF-1
    • Kim H-E, Du F, Fang M, Wang X (2005) Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on APAF-1. Proc Natl Acad Sci USA 102: 17545-17550
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17545-17550
    • Kim, H.-E.1    Du, F.2    Fang, M.3    Wang, X.4
  • 36
    • 2442435683 scopus 로고    scopus 로고
    • A novel cost of R gene resistance in the presence of disease
    • Korves T (2004) A novel cost of R gene resistance in the presence of disease. Am Nat 163: 489-504
    • (2004) Am Nat , vol.163 , pp. 489-504
    • Korves, T.1
  • 37
    • 0029347064 scopus 로고
    • The 16 gene for flax rust resistance is related to the Arabidopsis bacterial resistance gene RPS2 and the tobacco viral resistance gene N
    • Lawrence GJ, Finnegan EJ, Ayliffe MA, Ellis JG (1995) The 16 gene for flax rust resistance is related to the Arabidopsis bacterial resistance gene RPS2 and the tobacco viral resistance gene N. Plant Cell 7: 1195-1206
    • (1995) Plant Cell , vol.7 , pp. 1195-1206
    • Lawrence, G.J.1    Finnegan, E.J.2    Ayliffe, M.A.3    Ellis, J.G.4
  • 38
    • 4644247731 scopus 로고    scopus 로고
    • 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
    • Leipe DD, Koonin EV, Aravind L (2004) 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. J Mol Biol 343: 1-28
    • (2004) J Mol Biol , vol.343 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 39
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: Implications for origin recognition and checkpoint control
    • Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM (2000) Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol Cell 6: 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
  • 40
    • 0142057020 scopus 로고    scopus 로고
    • Understanding the functions of plant disease resistance proteins
    • Martin GB, Bogdanove AJ, Sessa G (2003) Understanding the functions of plant disease resistance proteins. Annu Rev Plant Biol 54: 23-61
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 23-61
    • Martin, G.B.1    Bogdanove, A.J.2    Sessa, G.3
  • 41
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT (2000) The PSIPRED protein structure prediction server. Bioinformatics 16: 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 42
    • 33745455354 scopus 로고    scopus 로고
    • Elicitor-mediated oligomerization of the tobacco N disease resistance protein
    • Mestre P, Baulcombe DC (2006) Elicitor-mediated oligomerization of the tobacco N disease resistance protein. Plant Cell 18: 491-501
    • (2006) Plant Cell , vol.18 , pp. 491-501
    • Mestre, P.1    Baulcombe, D.C.2
  • 43
    • 0033231602 scopus 로고    scopus 로고
    • Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily
    • Meyers BC, Dickerman AW, Michelmore RW, Sivaramakrishnan S, Sobral BW, Young ND (1999) Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily. Plant J 20: 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
  • 45
    • 0036793439 scopus 로고    scopus 로고
    • TIR-X and TIR-NBS proteins: Two new families related to disease resistance TIR-NBS-LRR proteins encoded in Arabidopsis and other plant genomes
    • Meyers BC, Morgante M, Michelmore RW (2002) TIR-X and TIR-NBS proteins: two new families related to disease resistance TIR-NBS-LRR proteins encoded in Arabidopsis and other plant genomes. Plant J 32: 77-92
    • (2002) Plant J , vol.32 , pp. 77-92
    • Meyers, B.C.1    Morgante, M.2    Michelmore, R.W.3
  • 46
    • 0037009437 scopus 로고    scopus 로고
    • Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death
    • Moffett P, Farnham G, Peart J, Baulcombe DC (2002) Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death. EMBO J 21: 4511-4519
    • (2002) EMBO J , vol.21 , pp. 4511-4519
    • Moffett, P.1    Farnham, G.2    Peart, J.3    Baulcombe, D.C.4
  • 47
    • 0034738029 scopus 로고    scopus 로고
    • F(0)F(1)-ATP synthase: General structural features of ATP-engine and a problem on free energy transduction
    • Muneyuki E, Noji H, Amano T, Masaike T, Yoshida M (2000) F(0)F(1)-ATP synthase: general structural features of ATP-engine and a problem on free energy transduction. Biochim Biophys Acta 1458: 467-481
    • (2000) Biochim Biophys Acta , vol.1458 , pp. 467-481
    • Muneyuki, E.1    Noji, H.2    Amano, T.3    Masaike, T.4    Yoshida, M.5
  • 49
    • 0344875519 scopus 로고    scopus 로고
    • The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA
    • Orelle C, Dalmas O, Gros P, Di Pietro A, Jault JM (2003) The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA. J Biol Chem 278: 47002-47008
    • (2003) J Biol Chem , vol.278 , pp. 47002-47008
    • Orelle, C.1    Dalmas, O.2    Gros, P.3    Di Pietro, A.4    Jault, J.M.5
  • 50
    • 0030612658 scopus 로고    scopus 로고
    • The I2C family from the wilt disease resistance locus 12 belongs to the nucleotide binding, leucine-rich repeat superfamily of plant resistance genes
    • Ori N, Eshed Y, Paran I, Presting G, Aviv D, Tanksley S, Zamir D, Fluhr R (1997) The I2C family from the wilt disease resistance locus 12 belongs to the nucleotide binding, leucine-rich repeat superfamily of plant resistance genes. Plant Cell 9: 521-532
    • (1997) Plant Cell , vol.9 , pp. 521-532
    • Ori, N.1    Eshed, Y.2    Paran, I.3    Presting, G.4    Aviv, D.5    Tanksley, S.6    Zamir, D.7    Fluhr, R.8
  • 51
    • 0028265262 scopus 로고
    • Comparison of extraction procedures for high-performance liquid chromatographic determination of cellular deoxynucleotides
    • Palmer S, Cox S (1994) Comparison of extraction procedures for high-performance liquid chromatographic determination of cellular deoxynucleotides. J Chromatogr A 667: 316-321
    • (1994) J Chromatogr A , vol.667 , pp. 316-321
    • Palmer, S.1    Cox, S.2
  • 52
    • 0034014008 scopus 로고    scopus 로고
    • Comparative genetics of nucleotide binding site-leucine rich repeat resistance gene homologues in the genomes of two dicotyledons: Tomato and Arabidopsis
    • Pan Q, Liu YS, Budai Hadrian O, Sela M, Carmel Goren L, Zamir D, Fluhr R (2000a) Comparative genetics of nucleotide binding site-leucine rich repeat resistance gene homologues in the genomes of two dicotyledons: tomato and Arabidopsis. Genetics 155: 309-322
    • (2000) Genetics , vol.155 , pp. 309-322
    • Pan, Q.1    Liu, Y.S.2    Budai Hadrian, O.3    Sela, M.4    Carmel Goren, L.5    Zamir, D.6    Fluhr, R.7
  • 53
    • 0343352530 scopus 로고    scopus 로고
    • Divergent evolution of plant NBS-LRR resistance gene homologues in dicot and cereal genomes
    • Pan Q, Wendel J, Fluhr R (2000b) Divergent evolution of plant NBS-LRR resistance gene homologues in dicot and cereal genomes. J Mol Evol 50: 203-213
    • (2000) J Mol Evol , vol.50 , pp. 203-213
    • Pan, Q.1    Wendel, J.2    Fluhr, R.3
  • 56
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • Poirot O, O'Toole E, Notredame C (2003) Tcoffee@igs: a web server for computing, evaluating and combining multiple sequence alignments. Nucleic Acids Res 31: 3503-3506
    • (2003) Nucleic Acids Res , vol.31 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 57
    • 26844478455 scopus 로고    scopus 로고
    • The nematode death machine in 3D
    • Pop C, Salvesen GC (2005) The nematode death machine in 3D. Cell 123: 192-193
    • (2005) Cell , vol.123 , pp. 192-193
    • Pop, C.1    Salvesen, G.C.2
  • 58
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl SJ, Li W, Chao Y, Schwarzenbacher R, Shi Y (2005) Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434: 926-933
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 59
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez R, Chinea G, Lopez N, Pons T, Vriend G (1998) Homology modeling, model and software evaluation: three related resources. Bioinformatics 14: 523-528
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 61
    • 0025048136 scopus 로고
    • The P-loop-A common motif in ATP- and GTP-binding proteins
    • Saraste M, Sibbald PR, Wittinghofer A (1990) The P-loop-a common motif in ATP- and GTP-binding proteins. Trends Biochem Sci 15: 430-434
    • (1990) Trends Biochem Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 62
    • 0037085010 scopus 로고    scopus 로고
    • The molecular mechanism of ATP synthesis by F1F0-ATP synthase
    • Senior AE, Nadanaciva S, Weber J (2002) The molecular mechanism of ATP synthesis by F1F0-ATP synthase. Biochim Biophys Acta 1553: 188-211
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 188-211
    • Senior, A.E.1    Nadanaciva, S.2    Weber, J.3
  • 63
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov IN, Bourne PE (1998) Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng 11: 739-747
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 65
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang SR (1997) G protein mechanisms: insights from structural analysis. Annu Rev Biochem 66: 639-678
    • (1997) Annu Rev Biochem , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 68
    • 0034489715 scopus 로고    scopus 로고
    • Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2
    • Tao Y, Yuan F, Leister RT, Ausubel FM, Katagiri F (2000) Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2. Plant Cell 12: 2541-2554
    • (2000) Plant Cell , vol.12 , pp. 2541-2554
    • Tao, Y.1    Yuan, F.2    Leister, R.T.3    Ausubel, F.M.4    Katagiri, F.5
  • 69
    • 0036009775 scopus 로고    scopus 로고
    • Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein
    • Tornero P, Chao RA, Luthin WN, Goff SA, Dangl JL (2002a) Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein. Plant Cell 14: 435-450
    • (2002) Plant Cell , vol.14 , pp. 435-450
    • Tornero, P.1    Chao, R.A.2    Luthin, W.N.3    Goff, S.A.4    Dangl, J.L.5
  • 70
    • 0036016434 scopus 로고    scopus 로고
    • RAR1 and NDR1 contribute quantitatively to disease resistance in Arabidopsis, and their relative contributions are dependent on the R gene assayed
    • Tornero P, Merritt P, Sadanandom A, Shirasu K, Innes RW, Dangl JL (2002b) RAR1 and NDR1 contribute quantitatively to disease resistance in Arabidopsis, and their relative contributions are dependent on the R gene assayed. Plant Cell 14: 1005-1015
    • (2002) Plant Cell , vol.14 , pp. 1005-1015
    • Tornero, P.1    Merritt, P.2    Sadanandom, A.3    Shirasu, K.4    Innes, R.W.5    Dangl, J.L.6
  • 71
    • 0028279385 scopus 로고
    • The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites
    • Traut TW (1994) The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites. Eur J Biochem 222: 9-19
    • (1994) Eur J Biochem , vol.222 , pp. 9-19
    • Traut, T.W.1
  • 72
    • 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
    • van der Biezen EA, Jones JDG (1998) The NB-ARC domain: a novel signalling motif shared by plant resistance gene products and regulators of cell death in animals. Curr Biol 8: R226-R227
    • (1998) Curr Biol , vol.8
    • Van Der Biezen, E.A.1    Jones, J.D.G.2
  • 73
    • 0034063376 scopus 로고    scopus 로고
    • Agro-infiltration is a versatile tool that facilitates comparative analyses of Avr9/Cf-9-induced and Avr4/Cf-4-induced necrosis
    • Van der Hoorn RAL, Laurent F, Roth R, De Wit PJGM (2000) Agro-infiltration is a versatile tool that facilitates comparative analyses of Avr9/Cf-9-induced and Avr4/Cf-4-induced necrosis. Mol Plant Microbe Interact 13: 439-446
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 439-446
    • Van Der Hoorn, R.A.L.1    Laurent, F.2    Roth, R.3    De Wit, P.4
  • 74
    • 0033511228 scopus 로고    scopus 로고
    • Nucleoside triphosphate-binding proteins: Different scaffolds to achieve phosphoryl transfer
    • Vetter IR, Wittinghofer A (1999) Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer. Q Rev Biophys 32: 1-56
    • (1999) Q Rev Biophys , vol.32 , pp. 1-56
    • Vetter, I.R.1    Wittinghofer, A.2
  • 75
    • 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
    • Walker JE, Saraste M, Runswick MJ, Gay NJ (1982) 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: 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
  • 76
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, et al (2005) Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437: 831-837
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1    Chai, J.2    Lee, E.S.3    Gu, L.4    Liu, Q.5    He, J.6    Wu, J.W.7    Kokel, D.8    Li, H.9    Hao, Q.10


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