메뉴 건너뛰기




Volumn 472, Issue 2, 2015, Pages 157-167

Characterization of a sialate-O-acetylesterase (NanS) from the oral pathogen Tannerella forsythia that enhances sialic acid release by NanH, its cognate sialidase

Author keywords

Acetlyesterase; Bacteroidetes; Carbohydrate active enzyme; Glycans; Oral cavity; Sialic acid

Indexed keywords

ACETYLESTERASE; ERYTHROPOIETIN; MUCIN; NANH PROTEIN; SIALATEO O ACETYLESTERASE; SIALIC ACID; SIALIDASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; EPO PROTEIN, HUMAN; NEURAMINIC ACID DERIVATIVE; POLYSACCHARIDE; RECOMBINANT PROTEIN; SIALATE O-ACETYLESTERASE; SIALIC ACID DERIVATIVE; SIALOGLYCOPROTEIN; SIALOMUCIN;

EID: 84955495504     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150388     Document Type: Article
Times cited : (24)

References (47)
  • 4
    • 84863406922 scopus 로고    scopus 로고
    • Sialic acid, periodontal pathogens and Tannerella forsythia: Stick around and enjoy the feast! Mol
    • PubMed
    • Stafford, G., Roy, S., Honma, K. and Sharma, A. (2012) Sialic acid, periodontal pathogens and Tannerella forsythia : stick around and enjoy the feast! Mol. Oral Microbiol. 26, 11-22 PubMed
    • (2012) Oral Microbiol. , vol.26 , pp. 11-22
    • Stafford, G.1    Roy, S.2    Honma, K.3    Sharma, A.4
  • 5
    • 84896848081 scopus 로고    scopus 로고
    • Structural and functional characterization of NanU, a novel high-affinity sialic acid-inducible binding protein of oral and gut-dwelling bacteroidetes species
    • CrossRef PubMed
    • Phansopa, C., Roy, S., Rafferty, J.B., Douglas, C.W.I., Pandhal, J., Wright, P.C., Kelly, D.J. and Stafford, G.P. (2014) Structural and functional characterization of NanU, a novel high-affinity sialic acid-inducible binding protein of oral and gut-dwelling bacteroidetes species. Biochem. J. 458, 499-511 CrossRef PubMed
    • (2014) Biochem. J. , vol.458 , pp. 499-511
    • Phansopa, C.1    Roy, S.2    Rafferty, J.B.3    Douglas, C.W.I.4    Pandhal, J.5    Wright, P.C.6    Kelly, D.J.7    Stafford, G.P.8
  • 6
    • 77951053020 scopus 로고    scopus 로고
    • A novel sialic acid utilization and uptake system in the periodontal pathogen Tannerella forsythia
    • CrossRef PubMed
    • Roy, S., Douglas, C.W.I. and Stafford, G.P. (2010) A novel sialic acid utilization and uptake system in the periodontal pathogen Tannerella forsythia. J. Bacteriol. 192, 2285-2293 CrossRef PubMed
    • (2010) J. Bacteriol. , vol.192 , pp. 2285-2293
    • Roy, S.1    Douglas, C.W.I.2    Stafford, G.P.3
  • 7
    • 69949094849 scopus 로고    scopus 로고
    • Complex glycan catabolism by the human gut microbiota: The Bacteroidetes Sus-like paradigm
    • CrossRef PubMed
    • Martens, E.C., Koropatkin, N.M., Smith, T.J. and Gordon, J.I. (2009) Complex glycan catabolism by the human gut microbiota: the Bacteroidetes Sus-like paradigm. J. Biol. Chem. 284, 24673-24677 CrossRef PubMed
    • (2009) J. Biol. Chem. , vol.284 , pp. 24673-24677
    • Martens, E.C.1    Koropatkin, N.M.2    Smith, T.J.3    Gordon, J.I.4
  • 10
    • 0021112669 scopus 로고
    • A neuraminidase from Streptococcus sanguis that can release O-acetylated sialic acids
    • PubMed
    • Varki, A. and Diaz, S. (1983) A neuraminidase from Streptococcus sanguis that can release O-acetylated sialic acids. J. Biol. Chem. 258, 12465-12471 PubMed
    • (1983) J. Biol. Chem. , vol.258 , pp. 12465-12471
    • Varki, A.1    Diaz, S.2
  • 11
    • 0026619682 scopus 로고
    • Bacterial sialidases-roles in pathogenicity and nutrition
    • CrossRef PubMed
    • Corfield, T. (1992) Bacterial sialidases-roles in pathogenicity and nutrition. Glycobiology 2, 509-521 CrossRef PubMed
    • (1992) Glycobiology , vol.2 , pp. 509-521
    • Corfield, T.1
  • 12
    • 0026640768 scopus 로고
    • Mucin degradation in the human colon: Production of sialidase, sialate O-acetylesterase, N-acetylneuraminate lyase, arylesterase, and glycosulfatase activities by strains of fecal bacteria
    • PubMed
    • Corfield, A.P., Wagner, S.A., Clamp, J.R., Kriaris, M.S. and Hoskins, L.C. (1992) Mucin degradation in the human colon: production of sialidase, sialate O-acetylesterase, N-acetylneuraminate lyase, arylesterase, and glycosulfatase activities by strains of fecal bacteria. Infect. Immun. 60, 3971-3978 PubMed
    • (1992) Infect. Immun. , vol.60 , pp. 3971-3978
    • Corfield, A.P.1    Wagner, S.A.2    Clamp, J.R.3    Kriaris, M.S.4    Hoskins, L.C.5
  • 13
    • 0023002952 scopus 로고
    • Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells
    • PubMed
    • Rogers, G.N., Herrler, G., Paulson, J.C. and Klenk, H.D. (1986) Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J. Biol. Chem. 261, 5947-5951 PubMed
    • (1986) J. Biol. Chem. , vol.261 , pp. 5947-5951
    • Rogers, G.N.1    Herrler, G.2    Paulson, J.C.3    Klenk, H.D.4
  • 14
    • 84880852483 scopus 로고    scopus 로고
    • Sialic acid binding properties of soluble coronavirus spike (S1) proteins: Differences between infectious bronchitis virus and transmissible gastroenteritis virus
    • CrossRef PubMed
    • Shahwan, K., Hesse, M., Mork, A.-K., Herrler, G. and Winter, C. (2013) Sialic acid binding properties of soluble coronavirus spike (S1) proteins: differences between infectious bronchitis virus and transmissible gastroenteritis virus. Viruses 5, 1924-1933 CrossRef PubMed
    • (2013) Viruses , vol.5 , pp. 1924-1933
    • Shahwan, K.1    Hesse, M.2    Mork, A.-K.3    Herrler, G.4    Winter, C.5
  • 15
    • 0031899115 scopus 로고    scopus 로고
    • O-acetylation of sialic acids
    • CrossRef PubMed
    • Klein, A. and Roussel, P. (1998) O-acetylation of sialic acids. Biochimie 80, 49-57 CrossRef PubMed
    • (1998) Biochimie , vol.80 , pp. 49-57
    • Klein, A.1    Roussel, P.2
  • 16
    • 70349559578 scopus 로고    scopus 로고
    • Esterases and autoimmunity: The sialic acid acetylesterase pathway and the regulation of peripheral B cell tolerance
    • CrossRef PubMed
    • Pillai, S., Cariappa, A. and Pirnie, S.P. (2009) Esterases and autoimmunity: the sialic acid acetylesterase pathway and the regulation of peripheral B cell tolerance. Trends Immunol. 30, 488-493 CrossRef PubMed
    • (2009) Trends Immunol. , vol.30 , pp. 488-493
    • Pillai, S.1    Cariappa, A.2    Pirnie, S.P.3
  • 17
    • 0034046950 scopus 로고    scopus 로고
    • Identification and purification of cytolytic antibodies directed against O-acetylated sialic acid in childhood acute lymphoblastic leukemia
    • CrossRef PubMed
    • Pal, S., Chatterjee, M., Bhattacharya, D.K., Bandhyopadhyay, S. and Mandal, C. (2000) Identification and purification of cytolytic antibodies directed against O-acetylated sialic acid in childhood acute lymphoblastic leukemia. Glycobiology 10, 539-549 CrossRef PubMed
    • (2000) Glycobiology , vol.10 , pp. 539-549
    • Pal, S.1    Chatterjee, M.2    Bhattacharya, D.K.3    Bandhyopadhyay, S.4    Mandal, C.5
  • 18
    • 33845584445 scopus 로고    scopus 로고
    • O-acetylation of sialic acids is required for the survival of lymphoblasts in childhood acute lymphoblastic leukemia (ALL)
    • CrossRef PubMed
    • Ghosh, S., Bandyopadhyay, S., Mukherjee, K., Mallick, A., Pal, S., Mandal, C., Bhattacharya, D.K. and Mandal, C. (2007) O-acetylation of sialic acids is required for the survival of lymphoblasts in childhood acute lymphoblastic leukemia (ALL). Glycoconj. J. 24, 17-24 CrossRef PubMed
    • (2007) Glycoconj. J. , vol.24 , pp. 17-24
    • Ghosh, S.1    Bandyopadhyay, S.2    Mukherjee, K.3    Mallick, A.4    Pal, S.5    Mandal, C.6    Bhattacharya, D.K.7    Mandal, C.8
  • 19
    • 66149143854 scopus 로고    scopus 로고
    • An orthologue of bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia
    • CrossRef PubMed
    • Thompson, H., Homer, K.A., Rao, S., Booth, V. and Hosie, A.H.F. (2009) An orthologue of bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia. J. Bacteriol. 191, 3623-3628 CrossRef PubMed
    • (2009) J. Bacteriol. , vol.191 , pp. 3623-3628
    • Thompson, H.1    Homer, K.A.2    Rao, S.3    Booth, V.4    Hosie, A.H.F.5
  • 20
    • 79952924336 scopus 로고    scopus 로고
    • Erythropoietin produced in a human cell line (Dynepo) has significant differences in glycosylation compared with erythropoietins produced in CHO cell lines
    • CrossRef PubMed
    • Shahrokh, Z., Royle, L., Saldova, R., Bones, J., Abrahams, J.L., Artemenko, N.V., Flatman, S., Davies, M., Baycroft, A., Sehgal, S. et al. (2011) Erythropoietin produced in a human cell line (Dynepo) has significant differences in glycosylation compared with erythropoietins produced in CHO cell lines. Mol. Pharm. 8, 286-296 CrossRef PubMed
    • (2011) Mol. Pharm. , vol.8 , pp. 286-296
    • Shahrokh, Z.1    Royle, L.2    Saldova, R.3    Bones, J.4    Abrahams, J.L.5    Artemenko, N.V.6    Flatman, S.7    Davies, M.8    Baycroft, A.9    Sehgal, S.10
  • 22
    • 73049171244 scopus 로고
    • Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids
    • CrossRef PubMed
    • Aminoff, D. (1961) Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem. J. 81, 384-392 CrossRef PubMed
    • (1961) Biochem. J. , vol.81 , pp. 384-392
    • Aminoff, D.1
  • 23
    • 0030819594 scopus 로고    scopus 로고
    • Sialic acid measurement by a modified Aminoff method: A time-saving reduction in 2-thiobarbituric acid concentration
    • CrossRef PubMed
    • Romero, E.L., Pardo, M.F., Porro, S. and Alonso, S. (1997) Sialic acid measurement by a modified Aminoff method: a time-saving reduction in 2-thiobarbituric acid concentration. J. Biochem. Biophys. Methods 35, 129-134 CrossRef PubMed
    • (1997) J. Biochem. Biophys. Methods , vol.35 , pp. 129-134
    • Romero, E.L.1    Pardo, M.F.2    Porro, S.3    Alonso, S.4
  • 25
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • CrossRef PubMed
    • Bigge, J.C., Patel, T.P., Bruce, J.A., Goulding, P.N., Charles, S.M. and Parekh, R.B. (1995) Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem. 230, 229-238 CrossRef PubMed
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 26
    • 0036571275 scopus 로고    scopus 로고
    • An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins
    • CrossRef PubMed
    • Royle, L., Mattu, T.S., Hart, E., Langridge, J.I., Merry, A.H., Murphy, N., Harvey, D.J., Dwek, R.A. and Rudd, P.M. (2002) An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins. Anal. Biochem. 304, 70-90 CrossRef PubMed
    • (2002) Anal. Biochem. , vol.304 , pp. 70-90
    • Royle, L.1    Mattu, T.S.2    Hart, E.3    Langridge, J.I.4    Merry, A.H.5    Murphy, N.6    Harvey, D.J.7    Dwek, R.A.8    Rudd, P.M.9
  • 27
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • CrossRef PubMed
    • Corpet, F. (1988) Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16, 10881-10890 CrossRef PubMed
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 28
    • 78650912796 scopus 로고    scopus 로고
    • Role of Tannerella forsythia NanH sialidase in epithelial cell attachment
    • CrossRef PubMed
    • Honma, K., Mishima, E. and Sharma, A. (2011) Role of Tannerella forsythia NanH sialidase in epithelial cell attachment. Infect. Immun. 79, 393-401 CrossRef PubMed
    • (2011) Infect. Immun. , vol.79 , pp. 393-401
    • Honma, K.1    Mishima, E.2    Sharma, A.3
  • 29
    • 0034655985 scopus 로고    scopus 로고
    • Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases
    • CrossRef PubMed
    • Mølgaard, A., Kauppinen, S. and Larsen, S. (2000) Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Structure 8, 373-383 CrossRef PubMed
    • (2000) Structure , vol.8 , pp. 373-383
    • Mølgaard, A.1    Kauppinen, S.2    Larsen, S.3
  • 30
    • 79959372165 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of NanS (YjhS), a 9-O-Acetyl N-acetylneuraminic acid esterase from Escherichia coli O157:H7
    • CrossRef PubMed
    • Rangarajan, E.S., Ruane, K.M., Proteau, A., Schrag, J.D., Valladares, R., Gonzalez, C.F., Gilbert, M., Yakunin, A.F. and Cygler, M. (2011) Structural and enzymatic characterization of NanS (YjhS), a 9-O-Acetyl N-acetylneuraminic acid esterase from Escherichia coli O157:H7. Protein Sci. 20, 1208-1219 CrossRef PubMed
    • (2011) Protein Sci. , vol.20 , pp. 1208-1219
    • Rangarajan, E.S.1    Ruane, K.M.2    Proteau, A.3    Schrag, J.D.4    Valladares, R.5    Gonzalez, C.F.6    Gilbert, M.7    Yakunin, A.F.8    Cygler, M.9
  • 31
    • 0028850080 scopus 로고
    • The catalytic triad of the influenza C virus glycoprotein HEF esterase: Characterization by site-directed mutagenesis and functional analysis
    • CrossRef PubMed
    • Pleschka, S., Klenk, H.D. and Herrler, G. (1995) The catalytic triad of the influenza C virus glycoprotein HEF esterase: characterization by site-directed mutagenesis and functional analysis. J. Gen. Virol. 76, 2529-2537 CrossRef PubMed
    • (1995) J. Gen. Virol. , vol.76 , pp. 2529-2537
    • Pleschka, S.1    Klenk, H.D.2    Herrler, G.3
  • 32
    • 33645461049 scopus 로고    scopus 로고
    • Structure, function and evolution of the hemagglutinin-esterase proteins of corona-and toroviruses
    • CrossRef PubMed
    • De Groot, R.J. (2006) Structure, function and evolution of the hemagglutinin-esterase proteins of corona-and toroviruses. Glycoconj. J. 23, 59-72 CrossRef PubMed
    • (2006) Glycoconj. J. , vol.23 , pp. 59-72
    • De Groot, R.J.1
  • 33
    • 70350468849 scopus 로고    scopus 로고
    • YjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-acetylneuraminic acid
    • CrossRef PubMed
    • Steenbergen, S.M., Jirik, J.L. and Vimr, E.R. (2009) YjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-acetylneuraminic acid. J. Bacteriol. 191, 7134-7139 CrossRef PubMed
    • (2009) J. Bacteriol. , vol.191 , pp. 7134-7139
    • Steenbergen, S.M.1    Jirik, J.L.2    Vimr, E.R.3
  • 34
    • 0032406533 scopus 로고    scopus 로고
    • Identification of antibodies directed against O-acetylated sialic acids in visceral leishmaniasis: Its diagnostic and prognostic role
    • CrossRef PubMed
    • Chatterjee, M., Sharma, V., Mandal, C., Sundar, S. and Sen, S. (1998) Identification of antibodies directed against O-acetylated sialic acids in visceral leishmaniasis: its diagnostic and prognostic role. Glycoconj. J. 15, 1141-1147 CrossRef PubMed
    • (1998) Glycoconj. J. , vol.15 , pp. 1141-1147
    • Chatterjee, M.1    Sharma, V.2    Mandal, C.3    Sundar, S.4    Sen, S.5
  • 35
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological functions of sialic acids
    • CrossRef PubMed
    • Schauer, R. (1982) Chemistry, metabolism, and biological functions of sialic acids. Adv. Carbohydr. Chem. Biochem. 40, 131-234 CrossRef PubMed
    • (1982) Adv. Carbohydr. Chem. Biochem. , vol.40 , pp. 131-234
    • Schauer, R.1
  • 36
    • 0032158982 scopus 로고    scopus 로고
    • Gingival crevicular pH in experimental gingivitis and occlusal trauma in man
    • CrossRef PubMed
    • Kobayashi, K., Soeda, W. and Watanabe, T. (1998) Gingival crevicular pH in experimental gingivitis and occlusal trauma in man. J. Periodontol. 69, 1036-1043 CrossRef PubMed
    • (1998) J. Periodontol. , vol.69 , pp. 1036-1043
    • Kobayashi, K.1    Soeda, W.2    Watanabe, T.3
  • 37
    • 0026079094 scopus 로고
    • Activity of influenza C virus O-acetylesterase with O-acetyl-containing compounds
    • CrossRef PubMed
    • Garcia-Sastre, A., Villar, E., Manuguerra, J.C., Hannoun, C. and Cabezas, J.A. (1991) Activity of influenza C virus O-acetylesterase with O-acetyl-containing compounds. Biochem. J. 273, 435-441 CrossRef PubMed
    • (1991) Biochem. J. , vol.273 , pp. 435-441
    • Garcia-Sastre, A.1    Villar, E.2    Manuguerra, J.C.3    Hannoun, C.4    Cabezas, J.A.5
  • 38
    • 33645461049 scopus 로고    scopus 로고
    • Structure, function and evolution of the hemagglutinin-esterase proteins of corona-and toroviruses
    • CrossRef PubMed
    • De Groot, R.J. (2006) Structure, function and evolution of the hemagglutinin-esterase proteins of corona-and toroviruses. Glycoconj. J. 23, 59-72 CrossRef PubMed
    • (2006) Glycoconj. J. , vol.23 , pp. 59-72
    • De Groot, R.J.1
  • 39
    • 0036171471 scopus 로고    scopus 로고
    • The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: A proposal to reorganize group 2 coronaviridae
    • CrossRef PubMed
    • Wurzer, W.J., Obojes, K. and Vlasak, R. (2002) The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: a proposal to reorganize group 2 coronaviridae. J. Gen. Virol. 83, 395-402 CrossRef PubMed
    • (2002) J. Gen. Virol. , vol.83 , pp. 395-402
    • Wurzer, W.J.1    Obojes, K.2    Vlasak, R.3
  • 40
    • 0024807862 scopus 로고
    • O-Acetylation and de-O-acetylation of sialic acids. Purification, characterization, and properties of a glycosylated rat liver esterase specific for 9-o-acetylated sialic acids
    • PubMed
    • Higa, H.H., Manzi, A. and Varki, A. (1989) O-Acetylation and de-O-acetylation of sialic acids. purification, characterization, and properties of a glycosylated rat liver esterase specific for 9-O-acetylated sialic acids. J. Biol. Chem. 264, 19435-19442 PubMed
    • (1989) J. Biol. Chem. , vol.264 , pp. 19435-19442
    • Higa, H.H.1    Manzi, A.2    Varki, A.3
  • 42
    • 84891945296 scopus 로고    scopus 로고
    • Highly sialylated recombinant human erythropoietin production in large-scale perfusion bioreactor utilizing CHO-gmt4 (JW152) with restored GnT i function
    • CrossRef PubMed
    • Goh, J.S.Y., Liu, Y., Liu, H., Chan, K.F., Wan, C., Teo, G., Zhou, X., Xie, F., Zhang, P., Zhang, Y. and Song, Z. (2014) Highly sialylated recombinant human erythropoietin production in large-scale perfusion bioreactor utilizing CHO-gmt4 (JW152) with restored GnT I function. Biotechnol. J. 9, 100-109 CrossRef PubMed
    • (2014) Biotechnol. J. , vol.9 , pp. 100-109
    • Goh, J.S.Y.1    Liu, Y.2    Liu, H.3    Chan, K.F.4    Wan, C.5    Teo, G.6    Zhou, X.7    Xie, F.8    Zhang, P.9    Zhang, Y.10    Song, Z.11
  • 43
    • 84878205044 scopus 로고    scopus 로고
    • Mass spectrometric glycoform profiling of the innovator and biosimilar erythropoietin and darbepoetin by LC/ESI-MS
    • CrossRef PubMed
    • Harazono, A., Hashii, N., Kuribayashi, R., Nakazawa, S. and Kawasaki, N. (2013) Mass spectrometric glycoform profiling of the innovator and biosimilar erythropoietin and darbepoetin by LC/ESI-MS. J. Pharm. Biomed. Anal. 83, 65-74 CrossRef PubMed
    • (2013) J. Pharm. Biomed. Anal. , vol.83 , pp. 65-74
    • Harazono, A.1    Hashii, N.2    Kuribayashi, R.3    Nakazawa, S.4    Kawasaki, N.5
  • 44
    • 0026743923 scopus 로고
    • Increased influenza A virus sialidase activity with N-acetyl-9-O-acetylneuraminic acid-containing substrates resulting from influenza C virus O-acetylesterase action
    • CrossRef PubMed
    • Muñoz-Barroso, I., García-Sastre, A., Villar, E., Manuguerra, J.C., Hannoun, C. and Cabezas, J.A. (1992) Increased influenza A virus sialidase activity with N-acetyl-9-O-acetylneuraminic acid-containing substrates resulting from influenza C virus O-acetylesterase action. Virus Res. 25, 145-153 CrossRef PubMed
    • (1992) Virus Res. , vol.25 , pp. 145-153
    • Muñoz-Barroso, I.1    García-Sastre, A.2    Villar, E.3    Manuguerra, J.C.4    Hannoun, C.5    Cabezas, J.A.6
  • 45
    • 84894615309 scopus 로고    scopus 로고
    • The link between periodontal disease and rheumatoid arthritis: An updated review
    • CrossRef PubMed
    • Koziel, J., Mydel, P. and Potempa, J. (2014) The link between periodontal disease and rheumatoid arthritis: an updated review. Curr. Rheumatol. Rep. 16, 408 CrossRef PubMed
    • (2014) Curr. Rheumatol. Rep. , vol.16 , pp. 408
    • Koziel, J.1    Mydel, P.2    Potempa, J.3
  • 46
    • 84897944384 scopus 로고    scopus 로고
    • Protein-linked glycans in periodontal bacteria: Prevalence and role at the immune interface
    • CrossRef PubMed
    • Settem, R.P., Honma, K., Stafford, G.P. and Sharma, A. (2013) Protein-linked glycans in periodontal bacteria: prevalence and role at the immune interface. Front. Microbiol. 4, 310 CrossRef PubMed
    • (2013) Front. Microbiol. , vol.4 , pp. 310
    • Settem, R.P.1    Honma, K.2    Stafford, G.P.3    Sharma, A.4
  • 47
    • 0025937004 scopus 로고
    • Leukosialin, a major O-glycan-containing sialoglycoprotein defining leukocyte differentiation and malignancy
    • CrossRef PubMed
    • Fukuda, M. (1991) Leukosialin, a major O-glycan-containing sialoglycoprotein defining leukocyte differentiation and malignancy. Glycobiology 1, 347-356 CrossRef PubMed
    • (1991) Glycobiology , vol.1 , pp. 347-356
    • Fukuda, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.