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Volumn 6, Issue , 2007, Pages

Evidence for glycosylation on a DNA-binding protein of Salmonella enterica

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA METHYLGALACTOPYRANOSIDE; BACTERIAL PROTEIN; CARBOHYDRATE; CARBOHYDRATE DERIVATIVE; DNA BINDING PROTEIN; DPS PROTEIN; GLUCOSE; JACALIN; LECTIN; MANNOSE; MONOSACCHARIDE; OLIGOSACCHARIDE; PYRANOSIDE; UNCLASSIFIED DRUG;

EID: 34247512597     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-6-11     Document Type: Article
Times cited : (11)

References (52)
  • 1
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almirón M Link AJ Furlong D Kolter R A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli Gen Develop 1992 6 2646-2654
    • (1992) Gen Develop , vol.6 , pp. 2646-2654
    • Almirón, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 2
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • 179379 9260963
    • Martinez A Kolter R Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps J Bacteriol 1997 179 5188-5194 179379 9260963
    • (1997) J Bacteriol , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 3
    • 4344703928 scopus 로고    scopus 로고
    • Biocrystallization: A last-resort strategy in bacteria
    • Frenkiel-krispin D Minsky A Biocrystallization: A last-resort strategy in bacteria ASM News 2002 68 277-283
    • (2002) ASM News , vol.68 , pp. 277-283
    • Frenkiel-krispin, D.1    Minsky, A.2
  • 4
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • 10.1038/nsb0498-294 9546221
    • Grant RA Filman DJ Filkel SE Kolter R Hogle JM The crystal structure of Dps, a ferritin homolog that binds and protects DNA Nat Struct Biol 1998 5 294-303 10.1038/nsb0498-294 9546221
    • (1998) Nat Struct Biol , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Filkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 5
    • 0038291700 scopus 로고    scopus 로고
    • The multi-layered structure of Dps with a novel di-nuclear ferroxidase center
    • 10.1016/S0022-2836(03)00466-2 12767829
    • Ren B Tibbelin G Kajino T Asami O Ladenstein R The multi-layered structure of Dps with a novel di-nuclear ferroxidase center J Mol Biol 2003 329 467-77 10.1016/S0022-2836(03)00466-2 12767829
    • (2003) J Mol Biol , vol.329 , pp. 467-477
    • Ren, B.1    Tibbelin, G.2    Kajino, T.3    Asami, O.4    Ladenstein, R.5
  • 6
    • 0028861959 scopus 로고
    • Bacillus subtilis MrgA is a Dps (PexB) homologue: Evidence for metalloregulation of an oxidative-stress gene
    • 10.1111/j.1365-2958.1995.mmi_18020295.x 8709848
    • Chen L Helmann JD Bacillus subtilis MrgA is a Dps (PexB) homologue: evidence for metalloregulation of an oxidative-stress gene Mol Microbiol 1995 18 295-300 10.1111/j.1365-2958.1995.mmi_18020295.x 8709848
    • (1995) Mol Microbiol , vol.18 , pp. 295-300
    • Chen, L.1    Helmann, J.D.2
  • 7
    • 0029067783 scopus 로고
    • Purification and characterization of a Synechococcus sp. strain PCC 7942 polypeptide structurally similar to the stress-induced Dps/PexB protein of Escherichia coli
    • 7794101
    • Pena MM Burkhart W Bullerjahn GS Purification and characterization of a Synechococcus sp. strain PCC 7942 polypeptide structurally similar to the stress-induced Dps/PexB protein of Escherichia coli Arch Microbiol 1995 163 337-344 7794101
    • (1995) Arch Microbiol , vol.163 , pp. 337-344
    • Pena, M.M.1    Burkhart, W.2    Bullerjahn, G.S.3
  • 8
    • 0030825124 scopus 로고    scopus 로고
    • Glycoproteins in prokaryotes
    • 10.1007/s002030050484 9382700
    • Moens S Vanderleyden J Glycoproteins in prokaryotes Arch Microbiol 1997 168 169-175 10.1007/s002030050484 9382700
    • (1997) Arch Microbiol , vol.168 , pp. 169-175
    • Moens, S.1    Vanderleyden, J.2
  • 9
    • 0026740469 scopus 로고
    • Structure of the glycan chain from the surface layer glycoprotein of Clostridium thermohydrosulfuricum L77-66
    • 1320936
    • Altman E Brisson J-R Gagné SM Kolbe J Messner P Sleytr UB Structure of the glycan chain from the surface layer glycoprotein of Clostridium thermohydrosulfuricum L77-66 Biochim Biophys Acta 1992 1117 71-77 1320936
    • (1992) Biochim Biophys Acta , vol.1117 , pp. 71-77
    • Altman, E.1    Brisson, J.-R.2    Gagné, S.M.3    Kolbe, J.4    Messner, P.5    Sleytr, U.B.6
  • 10
    • 0028986366 scopus 로고
    • Imilarity of "core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins
    • 176864 7721708
    • Messner P Christian R Neuninger C Schulz G imilarity of "core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins J Bacteriol 1995 177 2188 2193 176864 7721708
    • (1995) J Bacteriol , vol.177 , pp. 2188-2193
    • Messner, P.1    Christian, R.2    Neuninger, C.3    Schulz, G.4
  • 11
    • 0026594002 scopus 로고
    • Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70
    • 205844 1551844
    • Messner P Christian R Kolbe J Schulz G Sleytr UB Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70 J Bacteriol 1992 174 2236-2240 205844 1551844
    • (1992) J Bacteriol , vol.174 , pp. 2236-2240
    • Messner, P.1    Christian, R.2    Kolbe, J.3    Schulz, G.4    Sleytr, U.B.5
  • 13
    • 0030918282 scopus 로고    scopus 로고
    • Post-translational modifications of meningococcal pili. Identification of common substituents: Glycans and α-glycerophosphate - A review
    • 10.1016/S0378-1119(97)00082-6 9224884
    • Virji M Post-translational modifications of meningococcal pili. Identification of common substituents: Glycans and α-glycerophosphate - a review Gene 1997 192 141-147 10.1016/ S0378-1119(97)00082-6 9224884
    • (1997) Gene , vol.192 , pp. 141-147
    • Virji, M.1
  • 14
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • 10.1146/annurev.bi.58.070189.001133 2673008
    • Lechner J Wieland F Structure and biosynthesis of prokaryotic glycoproteins Annu Rev Biochem 1989 58 173-194 10.1146/ annurev.bi.58.070189.001133 2673008
    • (1989) Annu Rev Biochem , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 15
    • 0025974948 scopus 로고
    • Improvement of bacterial β-glucanase thermostability by glycosylation
    • Olsen O Thomsen KK Improvement of bacterial β-glucanase thermostability by glycosylation J Gen Microbiol 1991 137 579-585
    • (1991) J Gen Microbiol , vol.137 , pp. 579-585
    • Olsen, O.1    Thomsen, K.K.2
  • 16
    • 0030455618 scopus 로고    scopus 로고
    • An N -linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells
    • 507748 8981929
    • Kuo C Takahashi N Swanson AF Ozeki Y Hakomori S An N -linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells J Clin Invest 1996 98 2813-2818 507748 8981929
    • (1996) J Clin Invest , vol.98 , pp. 2813-2818
    • Kuo, C.1    Takahashi, N.2    Swanson, A.F.3    Ozeki, Y.4    Hakomori, S.5
  • 17
    • 0025952051 scopus 로고
    • Formation of bacterial membrane ice-nucleating lipoglycoprotein complexes
    • 208989 1917877
    • Kozloff LM Turner MF Arellano F Formation of bacterial membrane ice-nucleating lipoglycoprotein complexes J Bacteriol 1991 173 6528-6536 208989 1917877
    • (1991) J Bacteriol , vol.173 , pp. 6528-6536
    • Kozloff, L.M.1    Turner, M.F.2    Arellano, F.3
  • 18
    • 0027121321 scopus 로고
    • The sialylation of gonococcal lipopolysaccharide by host factors: A major impact on pathogenicity
    • 10.1111/j.1574-6968.1992.tb05717.x
    • Smith H Cole JA Parsons NJ The sialylation of gonococcal lipopolysaccharide by host factors: A major impact on pathogenicity FEMS Microbiol Lett 1992 100 287-292 10.1111/j.1574-6968.1992.tb05717.x
    • (1992) FEMS Microbiol Lett , vol.100 , pp. 287-292
    • Smith, H.1    Cole, J.A.2    Parsons, N.J.3
  • 19
    • 0023442206 scopus 로고
    • The glycoprotein toxin of Bacillus thuringiensis subsp. Israelensis indicates a lectin-like receptor in the larval mosquito gut
    • 204167 2827571
    • Muthukumar G Nickerson KW The glycoprotein toxin of Bacillus thuringiensis subsp. Israelensis indicates a lectin-like receptor in the larval mosquito gut Appl Environ Microbiol 1987 53 2650-2655 204167 2827571
    • (1987) Appl Environ Microbiol , vol.53 , pp. 2650-2655
    • Muthukumar, G.1    Nickerson, K.W.2
  • 20
    • 0037387036 scopus 로고    scopus 로고
    • Bacterial glycoproteins: Functions, biosynthesis and applications
    • 10.1002/pmic.200390052 12687605
    • Upreti RK Kumar M Shankar V Bacterial glycoproteins: Functions, biosynthesis and applications Proteomics 2003 3 363-379 10.1002/ pmic.200390052 12687605
    • (2003) Proteomics , vol.3 , pp. 363-379
    • Upreti, R.K.1    Kumar, M.2    Shankar, V.3
  • 24
    • 0023002029 scopus 로고
    • Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen [beta-D-Gal(1-3)D-GalNAc]
    • 3745164
    • Sastry MV Banarjee P Patanjali SR Swamy MJ Swarnalatha GV Surolia A Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen [beta-D-Gal(1-3)D-GalNAc] J Biol Chem 1986 261 11726-11733 3745164
    • (1986) J Biol Chem , vol.261 , pp. 11726-11733
    • Sastry, M.V.1    Banarjee, P.2    Patanjali, S.R.3    Swamy, M.J.4    Swarnalatha, G.V.5    Surolia, A.6
  • 26
    • 14244258308 scopus 로고    scopus 로고
    • Structural basis for the energetics of jacalin-sugar interactions: Promiscuity versus specificity
    • 10.1016/j.jmb.2005.01.015 15733927
    • Arockia-Jeyaprakash A Jayashree G Mahanta SK Swaminathan CP Sekar K Surolia A Vijayan M Structural basis for the energetics of jacalin-sugar interactions: Promiscuity versus specificity J Mol Biol 2005 347 181 188 10.1016/j.jmb.2005.01.015 15733927
    • (2005) J Mol Biol , vol.347 , pp. 181-188
    • Arockia-Jeyaprakash, A.1    Jayashree, G.2    Mahanta, S.K.3    Swaminathan, C.P.4    Sekar, K.5    Surolia, A.6    Vijayan, M.7
  • 27
    • 0028200484 scopus 로고
    • The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase
    • 10.1111/j.1365-2958.1994.tb00421.x 7984106
    • Altuvia S Almirón M Huisman G Kolter R Storz G The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase Mol Microbiol 1994 13 265-272 10.1111/j.1365-2958.1994.tb00421.x 7984106
    • (1994) Mol Microbiol , vol.13 , pp. 265-272
    • Altuvia, S.1    Almirón, M.2    Huisman, G.3    Kolter, R.4    Storz, G.5
  • 28
    • 0842326209 scopus 로고    scopus 로고
    • The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium Oxidative Stress Resistance and Virulence
    • 321587 10.1128/IAI.72.2.1155-1158.2004
    • Halsey TA Vazquez-Torres A Gravdahl DJ Fang FC Libby SJ The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium Oxidative Stress Resistance and Virulence Infect Immun 2004 72 1155-1158 321587 14742565 10.1128/IAI.72.2.1155-1158.2004
    • (2004) Infect Immun , vol.72 , pp. 1155-1158
    • Halsey, T.A.1    Vazquez-Torres, A.2    Gravdahl, D.J.3    Fang, F.C.4    Libby, S.J.5
  • 29
    • 0024962069 scopus 로고
    • Further characterization and immunochemical studies on the carbohydrate specificity of Jackfruit (Artocarpus integrifolia)
    • 2722839
    • Ahmed H Chatterjee BP Further characterization and immunochemical studies on the carbohydrate specificity of Jackfruit (Artocarpus integrifolia) J Biol Chem 1989 264 9365-9372 2722839
    • (1989) J Biol Chem , vol.264 , pp. 9365-9372
    • Ahmed, H.1    Chatterjee, B.P.2
  • 30
    • 0034939563 scopus 로고    scopus 로고
    • Glycosylation with heptose residues mediated by the aah gene product is essencial for adherence of the AIDA-I adhesion
    • 10.1046/j.1365-2958.2001.02487.x 11442838
    • Benz I Schimidt MA Glycosylation with heptose residues mediated by the aah gene product is essencial for adherence of the AIDA-I adhesion Mol Microbiol 2001 40 1403-1413 10.1046/j.1365-2958.2001.02487.x 11442838
    • (2001) Mol Microbiol , vol.40 , pp. 1403-1413
    • Benz, I.1    Schimidt, M.A.2
  • 31
    • 2442732620 scopus 로고    scopus 로고
    • Structural determination of a 5-acetamido-3,5,7,9-tetradeoxy-7-(3-hydroxybutyramido) -L-glycero-L-manno-nonulosonic acid-containing homopolysaccharide isolated from Sinorhizobium fredii HH103
    • 1220493 10477263 10.1042/0264-6021:3420527
    • Gil-Serrano AM Rodriguez-Carvajal MA Tejero-Mateo P Espartero JL Menendez M Corzo J Ruiz-Sainz JE BuendiA-Claveria AM Structural determination of a 5-acetamido-3,5,7,9-tetradeoxy-7-(3-hydroxybutyramido) -L-glycero-L-manno-nonulosonic acid-containing homopolysaccharide isolated from Sinorhizobium fredii HH103 Biochem J 1999 342 527-535 1220493 10477263 10.1042/0264-6021:3420527
    • (1999) Biochem J , vol.342 , pp. 527-535
    • Gil-Serrano, A.M.1    Rodriguez-Carvajal, M.A.2    Tejero-Mateo, P.3    Espartero, J.L.4    Menendez, M.5    Corzo, J.6    Ruiz-Sainz, J.E.7    BuendiA-Claveria, A.M.8
  • 32
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • 10.1046/j.1365-2958.2003.03527.x 12791140
    • Schirm M Soo EC Aubry AJ Austin J Thibault P Logan SM Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori Mol Microbiol 2003 48 1579-1592 10.1046/ j.1365-2958.2003.03527.x 12791140
    • (2003) Mol Microbiol , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5    Logan, S.M.6
  • 33
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin
    • 10.1074/jbc.M104529200 11461915
    • Thibault P Logan SM Kelly JF Brisson JR Ewing CP Trust TJ Guerry P Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin J Biol Chem 2001 276 34862-34870 10.1074/ jbc.M104529200 11461915
    • (2001) J Biol Chem , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.R.4    Ewing, C.P.5    Trust, T.J.6    Guerry, P.7
  • 34
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • 528800 15534364 10.1093/nar/gkh915
    • Ceci P Cellai S Falvo E Rivetti C Rossi GL Chiancone E DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus Nucl Acids Res 2004 32 5935-5944 528800 15534364 10.1093/nar/gkh915
    • (2004) Nucl Acids Res , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 35
    • 34247516723 scopus 로고    scopus 로고
    • http://www.cbs.dtu.dk/services/NetOGlyc/
  • 36
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • 10.1074/jbc.M403773200 15138254
    • Zachara NE O'Donnell N Cheung WD Mercer JJ Marth JD Hart GW Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells J Biol Chem 2004 279 30133-30142 10.1074/jbc.M403773200 15138254
    • (2004) J Biol Chem , vol.279 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6
  • 38
    • 0037432341 scopus 로고    scopus 로고
    • Dynamic nuclear and cytoplasmicglycosylation: Enzymes of O-GlcNAc cycling
    • 10.1021/bi020685a
    • Iyer SP Hart GW Dynamic nuclear and cytoplasmicglycosylation: Enzymes of O-GlcNAc cycling Biochem 2003 42 2493-2499 10.1021/bi020685a
    • (2003) Biochem , vol.42 , pp. 2493-2499
    • Iyer, S.P.1    Hart, G.W.2
  • 40
    • 0033168858 scopus 로고    scopus 로고
    • DNA protection by stress-induced biocrystallization
    • 10.1038/21918 10403254
    • Wolf SG Frenkiel D Arad T Finkel SE Kolter R Minsky A DNA protection by stress-induced biocrystallization Nature 1999 400 83 -85 10.1038/21918 10403254
    • (1999) Nature , vol.400 , pp. 83-85
    • Wolf, S.G.1    Frenkiel, D.2    Arad, T.3    Finkel, S.E.4    Kolter, R.5    Minsky, A.6
  • 41
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • 103771 10515926
    • Ali Azam T Iwata A Nishimura A Ueda S Ishihama A Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid J Bacteriol 1999 181 6361-6370 103771 10515926
    • (1999) J Bacteriol , vol.181 , pp. 6361-6370
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 42
    • 0141566368 scopus 로고    scopus 로고
    • Dynamic control of Dpsprotein levels by ClpXP and ClpAP proteases in Escherichia coli
    • 10.1046/j.1365-2958.2003.03644.x 12950924
    • Stephani K Weichart D Hengge R Dynamic control of Dpsprotein levels by ClpXP and ClpAP proteases in Escherichia coli Mol Microbiol 2003 49 1605-1614 10.1046/j.1365-2958.2003.03644.x 12950924
    • (2003) Mol Microbiol , vol.49 , pp. 1605-1614
    • Stephani, K.1    Weichart, D.2    Hengge, R.3
  • 43
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • 10.1002/elps.1150080203
    • Blum H Beier H Gross HJ Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels Electrophoresis 1987 8 93-99 10.1002/ elps.1150080203
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 44
    • 0020055346 scopus 로고
    • A sensitive silver stain for detecting lipopolisaccharides in polyacrilamide gels
    • 10.1016/0003-2697(82)90673-X 6176137
    • Tsai C-H Frasch CE A sensitive silver stain for detecting lipopolisaccharides in polyacrilamide gels Anal Biochem 1982 119 115-119 10.1016/0003-2697(82)90673-X 6176137
    • (1982) Anal Biochem , vol.119 , pp. 115-119
    • Tsai, C.-H.1    Frasch, C.E.2
  • 45
    • 0032079528 scopus 로고    scopus 로고
    • Improving the recovery of lysine in automated protein sequencing
    • 10.1006/abio.1998.2565 9570839
    • Fontes W Cunha RB Sousa MV Morhy L Improving the recovery of lysine in automated protein sequencing Anal Biochem 1998 258-259 267 10.1006/ abio.1998.2565 9570839
    • (1998) Anal Biochem , vol.258 , pp. 259-267
    • Fontes, W.1    Cunha, R.B.2    Sousa, M.V.3    Morhy, L.4
  • 46
    • 0023953283 scopus 로고
    • Direct protein microsequencing from Immobilon-P Transfer Membrane
    • 3273181
    • LeGendre N Matsudaira P Direct protein microsequencing from Immobilon-P Transfer Membrane Biotechniques 1988 6 154-159 3273181
    • (1988) Biotechniques , vol.6 , pp. 154-159
    • LeGendre, N.1    Matsudaira, P.2
  • 47
    • 0032521310 scopus 로고    scopus 로고
    • Mass spectrometric determination of the sites of O-glycan attachment with low picomolar sensitivity
    • 10.1006/abio.1997.2548 9514784
    • Rademaker GJ Pergantis SA Blok-Tip L Langridge JI Kleen A Thomas-Oates JE Mass spectrometric determination of the sites of O-glycan attachment with low picomolar sensitivity Anal Biochem 1998 257 149-160 10.1006/ abio.1997.2548 9514784
    • (1998) Anal Biochem , vol.257 , pp. 149-160
    • Rademaker, G.J.1    Pergantis, S.A.2    Blok-Tip, L.3    Langridge, J.I.4    Kleen, A.5    Thomas-Oates, J.E.6
  • 48
    • 0033532728 scopus 로고    scopus 로고
    • Structural and thermodynamic studies of KM+, a D-mannosebinding lectin from Artocarpus integrifolia seeds
    • 10.1016/S0301-4622(99)00035-6 17030315
    • Silva-Lucca RA Tabak M Nascimento OR Roque-Barreira MC Beltramini LM Structural and thermodynamic studies of KM+, a D-mannosebinding lectin from Artocarpus integrifolia seeds Biophys Chem 1999 79-81 93 10.1016/ S0301-4622(99)00035-6 17030315
    • (1999) Biophys Chem , vol.79 , pp. 81-93
    • Silva-Lucca, R.A.1    Tabak, M.2    Nascimento, O.R.3    Roque-Barreira, M.C.4    Beltramini, L.M.5
  • 50
    • 0034492764 scopus 로고    scopus 로고
    • Neutrophil migration and aggregation induced by euphorbin, a lectin from the latex of Euphorbia milii, var. milii
    • 10.1007/s000110050654 11211926
    • Dias-Baruffi M Sakamoto M Rossetto S Vozari-Hampe MM Roque-Barreira MC Neutrophil migration and aggregation induced by euphorbin, a lectin from the latex of Euphorbia milii, var. milii Inflamm Res 2000 49 732-736 10.1007/s000110050654 11211926
    • (2000) Inflamm Res , vol.49 , pp. 732-736
    • Dias-Baruffi, M.1    Sakamoto, M.2    Rossetto, S.3    Vozari-Hampe, M.M.4    Roque-Barreira, M.C.5
  • 51
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites
    • 10.1093/glycob/cwh151
    • Julenius K Mølgaard A Gupta R Brunak S Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites Glycobiol 2005 15 153-164 10.1093/glycob/cwh151
    • (2005) Glycobiol , vol.15 , pp. 153-164
    • Julenius, K.1    Mølgaard, A.2    Gupta, R.3    Brunak, S.4
  • 52
    • 0002677062 scopus 로고
    • GPI-membrane anchors: Isolation and analysis
    • Oxford University Press, New York, NY Fukuda M, Kobata A
    • Ferguson MAJ GPI-membrane anchors: Isolation and analysis Glycobiology: a practical approach Oxford University Press, New York, NY Fukuda M, Kobata A 1993 349-383
    • (1993) Glycobiology: A Practical Approach , pp. 349-383
    • Ferguson, M.A.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.