메뉴 건너뛰기




Volumn 157, Issue 2, 2011, Pages 599-607

Structural resolution of the complex between a fungal polygalacturonase and a plant polygalacturonase-inhibiting protein by small-angle x-ray scattering

Author keywords

[No Author keywords available]

Indexed keywords

FUSARIUM PHYLLOPHILUM; PHASEOLUS VULGARIS;

EID: 80053585495     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.111.181057     Document Type: Article
Times cited : (39)

References (61)
  • 1
    • 35148827341 scopus 로고    scopus 로고
    • Elicitors, effectors, and R genes: The new paradigm and a lifetime supply of questions
    • Bent AF, Mackey D (2007) Elicitors, effectors, and R genes: the new paradigm and a lifetime supply of questions. Annu Rev Phytopathol 45: 399-436.
    • (2007) Annu Rev Phytopathol , vol.45 , pp. 399-436
    • Bent, A.F.1    Mackey, D.2
  • 2
    • 28044458515 scopus 로고    scopus 로고
    • Blackledge M(2005) A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering
    • Bernadó P, Blanchard L, Timmins P, Marion D, Ruigrok RWH, Blackledge M(2005) A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. Proc Natl Acad Sci USA 102: 17002-17007.
    • Proc Natl Acad Sci USA , vol.102 , pp. 17002-17007
    • Bernadó, P.1    Blanchard, L.2    Timmins, P.3    Marion, D.4    Ruigrok, R.W.H.5
  • 3
    • 66249135697 scopus 로고    scopus 로고
    • A renaissance of elicitors: Perception of microbeassociated molecular patterns and danger signals by pattern-recognition receptors
    • Boller T, Felix G (2009) A renaissance of elicitors: perception of microbeassociated molecular patterns and danger signals by pattern-recognition receptors. Annu Rev Plant Biol 60: 379-406.
    • (2009) Annu Rev Plant Biol , vol.60 , pp. 379-406
    • Boller, T.1    Felix, G.2
  • 4
    • 37349092304 scopus 로고    scopus 로고
    • Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonaseinhibiting proteins
    • Bonivento D, Pontiggia D, Di Matteo A, Fernandez-Recio J, Salvi G, Tsernoglou D, Cervone F, Lorenzo GD, Federici L (2008) Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonaseinhibiting proteins. Proteins 70: 294-299.
    • (2008) Proteins , vol.70 , pp. 294-299
    • Bonivento, D.1    Pontiggia, D.2    di Matteo, A.3    Fernandez-Recio, J.4    Salvi, G.5    Tsernoglou, D.6    Cervone, F.7    Lorenzo, G.D.8    Federici, L.9
  • 5
    • 77952690864 scopus 로고    scopus 로고
    • A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides
    • Brutus A, Sicilia F, Macone A, Cervone F, De Lorenzo G (2010) A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides. Proc Natl Acad Sci USA 107: 9452-9457.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9452-9457
    • Brutus, A.1    Sicilia, F.2    Macone, A.3    Cervone, F.4    de Lorenzo, G.5
  • 7
    • 0034705330 scopus 로고    scopus 로고
    • Reconstruction of protein form with x-ray solution scattering and a genetic algorithm
    • Chación P, Díaz JF, Morán F, Andreu JM (2000) Reconstruction of protein form with x-ray solution scattering and a genetic algorithm. J Mol Biol 299: 1289-1302.
    • (2000) J Mol Biol , vol.299 , pp. 1289-1302
    • Chación, P.1    Díaz, J.F.2    Morán, F.3    Andreu, J.M.4
  • 8
    • 4444320185 scopus 로고    scopus 로고
    • Characterization of the complex locus of bean encoding polygalacturonase-inhibiting proteins reveals subfunctionalization for defense against fungi and insects
    • D'Ovidio R, Raiola A, Capodicasa C, Devoto A, Pontiggia D, Roberti S, Galletti R, Conti E, O'Sullivan D, De Lorenzo G (2004) Characterization of the complex locus of bean encoding polygalacturonase-inhibiting proteins reveals subfunctionalization for defense against fungi and insects. Plant Physiol 135: 2424-2435.
    • (2004) Plant Physiol , vol.135 , pp. 2424-2435
    • D'ovidio, R.1    Raiola, A.2    Capodicasa, C.3    Devoto, A.4    Pontiggia, D.5    Roberti, S.6    Galletti, R.7    Conti, E.8    O'Sullivan, D.9    de Lorenzo, G.10
  • 9
    • 79957558889 scopus 로고    scopus 로고
    • Engineering plant resistance by constructing chimeric receptors that recognize damageassociated molecular patterns (DAMPs)
    • De Lorenzo G, Brutus A, Savatin DV, Sicilia F, Cervone F (2011) Engineering plant resistance by constructing chimeric receptors that recognize damageassociated molecular patterns (DAMPs). FEBS Lett 585: 1521-1528.
    • (2011) FEBS Lett , vol.585 , pp. 1521-1528
    • de Lorenzo, G.1    Brutus, A.2    Savatin, D.V.3    Sicilia, F.4    Cervone, F.5
  • 10
    • 0034789069 scopus 로고    scopus 로고
    • The role of polygalacturonase- inhibiting proteins (PGIPs) in defense against pathogenic fungi
    • De Lorenzo G, D'Ovidio R, Cervone F (2001) The role of polygalacturonase- inhibiting proteins (PGIPs) in defense against pathogenic fungi. Annu Rev Phytopathol 39: 313-335.
    • (2001) Annu Rev Phytopathol , vol.39 , pp. 313-335
    • de Lorenzo, G.1    D'ovidio, R.2    Cervone, F.3
  • 15
    • 34250621711 scopus 로고    scopus 로고
    • Resistance to Botrytis cinerea induced in Arabidopsis by elicitors is independent of salicylic acid, ethylene or jasmonate signaling but requires PHYTOALEXIN DEFICIENT3
    • Ferrari S, Galletti R, Denoux C, De Lorenzo G, Ausubel FM, Dewdney J (2007) Resistance to Botrytis cinerea induced in Arabidopsis by elicitors is independent of salicylic acid, ethylene or jasmonate signaling but requires PHYTOALEXIN DEFICIENT3. Plant Physiol 144: 367-379.
    • (2007) Plant Physiol , vol.144 , pp. 367-379
    • Ferrari, S.1    Galletti, R.2    Denoux, C.3    de Lorenzo, G.4    Ausubel, F.M.5    Dewdney, J.6
  • 16
    • 33746224382 scopus 로고    scopus 로고
    • Antisense expression of the Arabidopsis thaliana AtPGIP1 gene reduces polygalacturonase- inhibiting protein accumulation and enhances susceptibility to Botrytis cinerea
    • Ferrari S, Galletti R, Vairo D, Cervone F, De Lorenzo G (2006) Antisense expression of the Arabidopsis thaliana AtPGIP1 gene reduces polygalacturonase- inhibiting protein accumulation and enhances susceptibility to Botrytis cinerea. Mol Plant Microbe Interact 19: 931-936.
    • (2006) Mol Plant Microbe Interact , vol.19 , pp. 931-936
    • Ferrari, S.1    Galletti, R.2    Vairo, D.3    Cervone, F.4    de Lorenzo, G.5
  • 17
    • 0347925092 scopus 로고    scopus 로고
    • Tandemly duplicated Arabidopsis genes that encode polygalacturonase-inhibiting proteins are regulated coordinately by different signal transduction pathways in response to fungal infection
    • Ferrari S, Vairo D, Ausubel FM, Cervone F, De Lorenzo G (2003) Tandemly duplicated Arabidopsis genes that encode polygalacturonase-inhibiting proteins are regulated coordinately by different signal transduction pathways in response to fungal infection. Plant Cell 15: 93-106.
    • (2003) Plant Cell , vol.15 , pp. 93-106
    • Ferrari, S.1    Vairo, D.2    Ausubel, F.M.3    Cervone, F.4    de Lorenzo, G.5
  • 19
    • 77649338894 scopus 로고    scopus 로고
    • Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea
    • Galantini L, Leggio C, Konarev PV, Pavel NV (2010) Human serum albumin binding ibuprofen: a 3D description of the unfolding pathway in urea. Biophys Chem 147: 111-122.
    • (2010) Biophys Chem , vol.147 , pp. 111-122
    • Galantini, L.1    Leggio, C.2    Konarev, P.V.3    Pavel, N.V.4
  • 20
    • 57949110254 scopus 로고    scopus 로고
    • Human serum albumin unfolding: A small-angle X-ray scattering and light scattering study
    • Galantini L, Leggio C, Pavel NV (2008) Human serum albumin unfolding: a small-angle X-ray scattering and light scattering study. J Phys Chem B 112: 15460-15469.
    • (2008) J Phys Chem B , vol.112 , pp. 15460-15469
    • Galantini, L.1    Leggio, C.2    Pavel, N.V.3
  • 21
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • Glatter O (1977) A new method for the evaluation of small-angle scattering data. J Appl Cryst 10: 415-421.
    • (1977) J Appl Cryst , vol.10 , pp. 415-421
    • Glatter, O.1
  • 24
    • 0042820143 scopus 로고    scopus 로고
    • Further insights into calmodulin- myosin light chain kinase interaction from solution scattering and shape restoration
    • Heller WT, Krueger JK, Trewhella J (2003) Further insights into calmodulin- myosin light chain kinase interaction from solution scattering and shape restoration. Biochemistry 42: 10579-10588.
    • (2003) Biochemistry , vol.42 , pp. 10579-10588
    • Heller, W.T.1    Krueger, J.K.2    Trewhella, J.3
  • 25
    • 0035018083 scopus 로고    scopus 로고
    • Endopolygalacturonase is essential for citrus black rot caused by Alternaria citri but not brown spot caused by Alternaria alternata
    • Isshiki A, Akimitsu K, Yamamoto M, Yamamoto H (2001) Endopolygalacturonase is essential for citrus black rot caused by Alternaria citri but not brown spot caused by Alternaria alternata. Mol Plant Microbe Interact 14: 749-757.
    • (2001) Mol Plant Microbe Interact , vol.14 , pp. 749-757
    • Isshiki, A.1    Akimitsu, K.2    Yamamoto, M.3    Yamamoto, H.4
  • 27
    • 77950223101 scopus 로고    scopus 로고
    • Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls
    • Jacques DA, Trewhella J (2010) Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls. Protein Sci 19: 642-657.
    • (2010) Protein Sci , vol.19 , pp. 642-657
    • Jacques, D.A.1    Trewhella, J.2
  • 28
    • 38349147028 scopus 로고    scopus 로고
    • The expression of a bean PGIP in transgenic wheat confers increased resistance to the fungal pathogen Bipolaris sorokiniana
    • Janni M, Sella L, Favaron F, Blechl AE, De Lorenzo G, D'Ovidio R (2008) The expression of a bean PGIP in transgenic wheat confers increased resistance to the fungal pathogen Bipolaris sorokiniana. Mol Plant Microbe Interact 21: 171-177.
    • (2008) Mol Plant Microbe Interact , vol.21 , pp. 171-177
    • Janni, M.1    Sella, L.2    Favaron, F.3    Blechl, A.E.4    de Lorenzo, G.5    D'ovidio, R.6
  • 29
    • 33751501231 scopus 로고    scopus 로고
    • The grapevine polygalacturonase- inhibiting protein (VvPGIP1) reduces Botrytis cinerea susceptibility in transgenic tobacco and differentially inhibits fungal polygalacturonases
    • Joubert DA, Slaughter AR, Kemp G, Becker JV, Krooshof GH, Bergmann C, Benen J, Pretorius IS, Vivier MA (2006) The grapevine polygalacturonase- inhibiting protein (VvPGIP1) reduces Botrytis cinerea susceptibility in transgenic tobacco and differentially inhibits fungal polygalacturonases. Transgenic Res 15: 687-702.
    • (2006) Transgenic Res , vol.15 , pp. 687-702
    • Joubert, D.A.1    Slaughter, A.R.2    Kemp, G.3    Becker, J.V.4    Krooshof, G.H.5    Bergmann, C.6    Benen, J.7    Pretorius, I.S.8    Vivier, M.A.9
  • 30
    • 22544465583 scopus 로고    scopus 로고
    • Necrotizing activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris
    • Kars I, Krooshof GH, Wagemakers L, Joosten R, Benen JAE, van Kan JAL (2005) Necrotizing activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris. Plant J 43: 213-225.
    • (2005) Plant J , vol.43 , pp. 213-225
    • Kars, I.1    Krooshof, G.H.2    Wagemakers, L.3    Joosten, R.4    Benen, J.A.E.5    van Kan, J.A.L.6
  • 31
    • 0037072292 scopus 로고    scopus 로고
    • Use of amide exchange mass spectrometry to study conformational changes within the endopolygalacturonase II-homogalacturonan-polygalacturonase inhibiting protein system
    • King D, Bergmann C, Orlando R, Benen JA, Kester HC, Visser J (2002) Use of amide exchange mass spectrometry to study conformational changes within the endopolygalacturonase II-homogalacturonan-polygalacturonase inhibiting protein system. Biochemistry 41: 10225-10233.
    • (2002) Biochemistry , vol.41 , pp. 10225-10233
    • King, D.1    Bergmann, C.2    Orlando, R.3    Benen, J.A.4    Kester, H.C.5    Visser, J.6
  • 32
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch MH, Vachette P, Svergun DI (2003) Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q Rev Biophys 36: 147-227.
    • (2003) Q Rev Biophys , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 33
    • 0033179941 scopus 로고    scopus 로고
    • A leucine-rich repeat receptor-like protein kinase (LRPKm1) gene is induced in Malus x domestica by Venturia inaequalis infection and salicylic acid treatment
    • Komjanc M, Festi S, Rizzotti L, Cattivelli L, Cervone F, De Lorenzo G (1999) A leucine-rich repeat receptor-like protein kinase (LRPKm1) gene is induced in Malus x domestica by Venturia inaequalis infection and salicylic acid treatment. Plant Mol Biol 40: 945-957.
    • (1999) Plant Mol Biol , vol.40 , pp. 945-957
    • Komjanc, M.1    Festi, S.2    Rizzotti, L.3    Cattivelli, L.4    Cervone, F.5    de Lorenzo, G.6
  • 34
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and lowresolution structural models
    • Kozin MB, Svergun DI (2001) Automated matching of high- and lowresolution structural models. J Appl Cryst 34: 33-41.
    • (2001) J Appl Cryst , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 35
    • 0033522402 scopus 로고    scopus 로고
    • The specificity of polygalacturonaseinhibiting protein (PGIP): A single amino acid substitution in the solvent-exposed beta-strand/beta-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability
    • Leckie F, Mattei B, Capodicasa C, Hemmings A, Nuss L, Aracri B, De Lorenzo G, Cervone F (1999) The specificity of polygalacturonaseinhibiting protein (PGIP): a single amino acid substitution in the solvent-exposed beta-strand/beta-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability. EMBO J 18: 2352-2363.
    • (1999) EMBO J , vol.18 , pp. 2352-2363
    • Leckie, F.1    Mattei, B.2    Capodicasa, C.3    Hemmings, A.4    Nuss, L.5    Aracri, B.6    de Lorenzo, G.7    Cervone, F.8
  • 36
    • 70349132068 scopus 로고    scopus 로고
    • Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid
    • Leggio C, Galantini L, Konarev PV, Pavel NV (2009) Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid. J Phys Chem B 113: 12590-12602.
    • (2009) J Phys Chem B , vol.113 , pp. 12590-12602
    • Leggio, C.1    Galantini, L.2    Konarev, P.V.3    Pavel, N.V.4
  • 38
    • 34249894142 scopus 로고    scopus 로고
    • Small-angle x-ray scattering from RNA, proteins, and protein complexes
    • Lipfert J, Doniach S (2007) Small-angle x-ray scattering from RNA, proteins, and protein complexes. Annu Rev Biophys Biomol Struct 36: 307-327.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 307-327
    • Lipfert, J.1    Doniach, S.2
  • 39
    • 31744435195 scopus 로고    scopus 로고
    • Polygalacturonase inhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection
    • Manfredini C, Sicilia F, Ferrari S, Pontiggia D, Salvi G, Caprari C, Lorito M, De Lorenzo G (2005) Polygalacturonase inhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection. Physiol Mol Plant Pathol 67: 108-115.
    • (2005) Physiol Mol Plant Pathol , vol.67 , pp. 108-115
    • Manfredini, C.1    Sicilia, F.2    Ferrari, S.3    Pontiggia, D.4    Salvi, G.5    Caprari, C.6    Lorito, M.7    de Lorenzo, G.8
  • 41
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle x-ray solution scattering
    • Mertens HDT, Svergun DI (2010) Structural characterization of proteins and complexes using small-angle x-ray solution scattering. J Struct Biol 172: 128-141.
    • (2010) J Struct Biol , vol.172 , pp. 128-141
    • Mertens, H.D.T.1    Svergun, D.I.2
  • 42
  • 43
    • 74049136101 scopus 로고    scopus 로고
    • Three-dimensional model of human platelet integrin alphaIIb beta3 in solution obtained by small angle neutron scattering
    • Nogales A, García C, Pérez J, Callow P, Ezquerra TA, González-Rodrńguez J (2010) Three-dimensional model of human platelet integrin alphaIIb beta3 in solution obtained by small angle neutron scattering. J Biol Chem 285: 1023-1031.
    • (2010) J Biol Chem , vol.285 , pp. 1023-1031
    • Nogales, A.1    García, C.2    Pérez, J.3    Callow, P.4    Ezquerra, T.A.5    González-Rodrńguez, J.6
  • 44
    • 0034484513 scopus 로고    scopus 로고
    • SAXS experiments on absolute scale with Kratky systems using water as a secondary standard
    • Orthaber D, Bergmann A, Glatter O (2000) SAXS experiments on absolute scale with Kratky systems using water as a secondary standard. J Appl Cryst 33: 218-225.
    • (2000) J Appl Cryst , vol.33 , pp. 218-225
    • Orthaber, D.1    Bergmann, A.2    Glatter, O.3
  • 45
  • 46
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89: 1237-1250.
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 47
    • 77957221991 scopus 로고    scopus 로고
    • Structural characterization of protein-protein complexes by integrating computational docking with small-angle scattering data
    • Pons C, D'Abramo M, Svergun DI, Orozco M, Bernadó P, Fernández-Recio J (2010) Structural characterization of protein-protein complexes by integrating computational docking with small-angle scattering data. J Mol Biol 403: 217-230.
    • (2010) J Mol Biol , vol.403 , pp. 217-230
    • Pons, C.1    D'abramo, M.2    Svergun, D.I.3    Orozco, M.4    Bernadó, P.5    Fernández-Recio, J.6
  • 49
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam CD, Hammel M, Hura GL, Tainer JA (2007) X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q Rev Biophys 40: 191-285.
    • (2007) Q Rev Biophys , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 51
    • 0032497321 scopus 로고    scopus 로고
    • Protein denaturation: A small-angle x-ray scattering study of the ensemble of unfolded states of cytochrome c
    • Segel DJ, Fink AL, Hodgson KO, Doniach S (1998) Protein denaturation: a small-angle x-ray scattering study of the ensemble of unfolded states of cytochrome c. Biochemistry 37: 12443-12451.
    • (1998) Biochemistry , vol.37 , pp. 12443-12451
    • Segel, D.J.1    Fink, A.L.2    Hodgson, K.O.3    Doniach, S.4
  • 52
    • 32644461318 scopus 로고    scopus 로고
    • The polygalacturonase-inhibiting protein PGIP2 of Phaseolus vulgaris has evolved a mixed mode of inhibition of endopolygalacturonase PG1 of Botrytis cinerea
    • Sicilia F, Fernandez-Recio J, Caprari C, De Lorenzo G, Tsernoglou D, Cervone F, Federici L (2005) The polygalacturonase-inhibiting protein PGIP2 of Phaseolus vulgaris has evolved a mixed mode of inhibition of endopolygalacturonase PG1 of Botrytis cinerea. Plant Physiol 139: 1380-1388.
    • (2005) Plant Physiol , vol.139 , pp. 1380-1388
    • Sicilia, F.1    Fernandez-Recio, J.2    Caprari, C.3    de Lorenzo, G.4    Tsernoglou, D.5    Cervone, F.6    Federici, L.7
  • 54
    • 70350460190 scopus 로고    scopus 로고
    • Three aspartic acid residues of polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris are critical for inhibition of Fusarium phyllophilum PG
    • Spinelli F, Mariotti L, Mattei B, Salvi G, Cervone F, Caprari C (2009) Three aspartic acid residues of polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris are critical for inhibition of Fusarium phyllophilum PG. Plant Biol (Stuttg) 11: 738-743.
    • (2009) Plant Biol (Stuttg) , vol.11 , pp. 738-743
    • Spinelli, F.1    Mariotti, L.2    Mattei, B.3    Salvi, G.4    Cervone, F.5    Caprari, C.6
  • 55
    • 0000323953 scopus 로고
    • A new technique for the measurement of the absolute intensity of x-ray small angle scattering: The moving slit method
    • Stabinger H, Kratky O (1978) A new technique for the measurement of the absolute intensity of x-ray small angle scattering: the moving slit method. Makromol Chem 179: 1655-1659.
    • (1978) Makromol Chem , vol.179 , pp. 1655-1659
    • Stabinger, H.1    Kratky, O.2
  • 56
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules fromsolution scattering using simulated annealing
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules fromsolution scattering using simulated annealing. Biophys J 76: 2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 57
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun DI, Barberato C, Koch MH (1995) CRYSOL-a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Cryst 28: 768-773.
    • (1995) J Appl Cryst , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.3
  • 58
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from x-ray solution scattering. Biophys J 80: 2946-2953.
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 59
    • 69249155059 scopus 로고    scopus 로고
    • DC-SIGN neck domain is a pH-sensor controlling oligomerization: SAXS and hydrodynamic studies of extracellular domain
    • Tabarani G, Thépaut M, Stroebel D, Ebel C, Vivès C, Vachette P, Durand D, Fieschi F (2009) DC-SIGN neck domain is a pH-sensor controlling oligomerization: SAXS and hydrodynamic studies of extracellular domain. J Biol Chem 284: 21229-21240.
    • (2009) J Biol Chem , vol.284 , pp. 21229-21240
    • Tabarani, G.1    Thépaut, M.2    Stroebel, D.3    Ebel, C.4    Vivès, C.5    Vachette, P.6    Durand, D.7    Fieschi, F.8
  • 60
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst 36: 860-864.
    • (2003) J Appl Cryst , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 61
    • 23044488858 scopus 로고    scopus 로고
    • An endopolygalacturonase from Sclerotinia sclerotiorum induces calciummediated signaling and programmed cell death in soybean cells
    • Zuppini A, Navazio L, Sella L, Castiglioni C, Favaron F, Mariani P (2005) An endopolygalacturonase from Sclerotinia sclerotiorum induces calciummediated signaling and programmed cell death in soybean cells. Mol Plant Microbe Interact 18: 849-855.
    • (2005) Mol Plant Microbe Interact , vol.18 , pp. 849-855
    • Zuppini, A.1    Navazio, L.2    Sella, L.3    Castiglioni, C.4    Favaron, F.5    Mariani, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.