Unified Theory of Bacterial Sialometabolism: How and Why Bacteria Metabolize Host Sialic Acids

Mucin dynamics and enteric pathogens

McGuckin, M. A., Lindén, S. K., Sutton, P., & Florin, T. H. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2538 · Cited by 1,428 · see citing works

Chemical Diversity in the Sialic Acids and Related α-Keto Acids: An Evolutionary Perspective

Angata, T., & Varki, A. P. (2002) · Chemical Reviews · doi:10.1021/cr000407m · Cited by 1,232 · see citing works

Mucosal Glycan Foraging Enhances Fitness and Transmission of a Saccharolytic Human Gut Bacterial Symbiont

Martens, E. C., Chiang, H. C., & Gordon, J. I. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.09.007 · Cited by 919 · see citing works

Diversity of Microbial Sialic Acid Metabolism

Vimr, E. R., Kalivoda, K. A., Deszo, E. L., & Steenbergen, S. M. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.1.132-153.2004 · Cited by 580 · see citing works

Composition and functional role of the mucus layers in the intestine

Johansson, M., Ambort, D., Pelaseyed, T., Schutte, A. H., Gustafsson, J. K., Ermund, A., Subramani, D. B., Holmén‐Larsson, J., Thomsson, K. A., Bergström, J. H., et al. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0822-3 · Cited by 559 · see citing works

Carbon nutrition of Escherichia coli in the mouse intestine

Chang, D., Smalley, D. J., Tucker, D. L., Leatham, M. P., Norris, W. E., Stevenson, S. J., Anderson, A. B., Grissom, J. E., Laux, D. C., Cohen, P. S., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307888101 · Cited by 513 · see citing works

Complete genome sequence of the marine planctomycete Pirellula sp. strain 1

Glöckner, F. O., Kube, M., Bauer, M., Teeling, H., Lombardot, T., Ludwig, W., Gade, D., Beck, A., Borzym, K., Heitmann, K., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1431443100 · Cited by 482 · see citing works

Structural diversity and specific distribution of O-glycans in normal human mucins along the intestinal tract

Masselot, C. R., Capon, C., Coddeville, B., & Michalski, J. (2004) · Biochemical Journal · doi:10.1042/bj20040605 · Cited by 388 · see citing works

Comparison of Carbon Nutrition for Pathogenic and Commensal <i>Escherichia coli</i> Strains in the Mouse Intestine

Fabich, A. J., Jones, S. A., Chowdhury, F. Z., Cernosek, A., Anderson, A., Smalley, D., McHargue, J. W., Hightower, G. A., Smith, J. T., Autieri, S. M., et al. (2008) · Infection and Immunity · doi:10.1128/iai.01386-07 · Cited by 380 · see citing works

A metagenomic insight into our gut's microbiome

Lepage, P., Leclerc, M., Joossens, M., Mondot, S., Blottière, H. M., Raes, J., Ehrlich, S. D., & Dore, J. M. (2012) · Gut · doi:10.1136/gutjnl-2011-301805 · Cited by 371 · see citing works

Fitness of Escherichia coli during Urinary Tract Infection Requires Gluconeogenesis and the TCA Cycle

Alteri, C. J., Smith, S. N., & Mobley, H. L. T. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000448 · Cited by 310 · see citing works

Temporal gene‐expression in Escherichia coli K‐12 biofilms

Domka, J., Lee, J., Bansal, T., & Wood, T. K. (2006) · Environmental Microbiology · doi:10.1111/j.1462-2920.2006.01143.x · Cited by 302 · see citing works

Experimental and Computational Assessment of Conditionally Essential Genes inEscherichia coli

Joyce, A. R., Reed, J. L., White, A., Edwards, R. A., Osterman, A. L., Baba, T., Mori, H., Lesely, S. A., Palsson, B. Ø., & Agarwalla, S. (2006) · Journal of Bacteriology · doi:10.1128/jb.00740-06 · Cited by 266 · see citing works

To sialylate, or not to sialylate: that is the question

Vimr, E. R., & Lichtensteiger, C. A. (2002) · Trends in Microbiology · doi:10.1016/s0966-842x(02)02361-2 · Cited by 238 · see citing works

Sweet-talk: role of host glycosylation in bacterial pathogenesis of the gastrointestinal tract

Moran, A. P., Gupta, A., & Joshi, L. (2011) · Gut · doi:10.1136/gut.2010.212704 · Cited by 235 · see citing works

Evidence of Regio-specific Glycosylation in Human Intestinal Mucins

Masselot, C. R., Capon, C., Maes, E., Rousset, M., Zweibaum, A., Zanetta, J., & Michalski, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302529200 · Cited by 232 · see citing works

Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase.

Crennell, S. J., Garman, E. F., Laver, W. G., Vimr, E. R., & Taylor, G. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.21.9852 · Cited by 228 · see citing works

Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae

King, S. J., Hippe, K. R., & Weiser, J. N. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04984.x · Cited by 224 · see citing works

Identification of an inducible catabolic system for sialic acids (nan) in Escherichia coli

Vimr, E. R., & Troy, F. A. (1985) · Journal of Bacteriology · doi:10.1128/jb.164.2.845-853.1985 · Cited by 218 · see citing works

Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production

Soong, G. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27920 · Cited by 214 · see citing works

Convergent Pathways for Utilization of the Amino Sugars N -Acetylglucosamine, N -Acetylmannosamine, and N -Acetylneuraminic Acid by Escherichia coli

PLUMBRIDGE, J. A., & Vimr, E. R. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.1.47-54.1999 · Cited by 207 · see citing works

Host sialoglycans and bacterial sialidases: a mucosal perspective

Lewis, A. L., & Lewis, W. G. (2012) · Cellular Microbiology · doi:10.1111/j.1462-5822.2012.01807.x · Cited by 206 · see citing works

Insights into the evolution of sialic acid catabolism among bacteria

Almagro‐Moreno, S., & Boyd, E. F. (2009) · BMC Evolutionary Biology · doi:10.1186/1471-2148-9-118 · Cited by 205 · see citing works

Host-derived sialic acid is incorporated into Haemophilus influenzae lipopolysaccharide and is a major virulence factor in experimental otitis media

Bouchet, V., Hood, D. W., Li, J., Brisson, J., Randle, G. A., Martin, A., Li, Z., Goldstein, R., Schweda, E. K. H., Pelton, S. I., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1432026100 · Cited by 204 · see citing works

Sialic Acid Catabolism Confers a Competitive Advantage to Pathogenic Vibrio cholerae in the Mouse Intestine

Almagro‐Moreno, S., & Boyd, E. F. (2009) · Infection and Immunity · doi:10.1128/iai.00279-09 · Cited by 191 · see citing works

Analysis of Pools of Targeted Salmonella Deletion Mutants Identifies Novel Genes Affecting Fitness during Competitive Infection in Mice

Santiviago, C. A., Reynolds, M., Porwollik, S., Choi, S.-H., Long, F., Andrews‐Polymenis, H. L., & McClelland, M. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000477 · Cited by 189 · see citing works

The sialidase superfamily and its spread by horizontal gene transfer

Roggentin, P., Schauer, R., Hoyer, L. L., & Vimr, E. R. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01221.x · Cited by 176 · see citing works

Sialic acid recognition by Vibrio cholerae neuraminidase

Moustafa, I., Connaris, H., Taylor, M., Zaitsev, V., Wilson, J. C., Kiefel, M. J., von Itzstein, M., & Taylor, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404965200 · Cited by 165 · see citing works

The NanA Neuraminidase of Streptococcus pneumoniae Is Involved in Biofilm Formation

Parker, D., Soong, G., Planet, P. J., Brower, J., Ratner, A. J., & Prince, A. S. (2009) · Infection and Immunity · doi:10.1128/iai.00228-09 · Cited by 165 · see citing works

Selective growth of mucolytic bacteria including Clostridium perfringens in a neonatal piglet model of total parenteral nutrition,,

Deplancke, B., Vidal, O., Ganessunker, D., Donovan, S. M., Mackie, R. I., & Gaskins, H. R. (2002) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/76.5.1117 · Cited by 155 · see citing works

Sialic Acid: A Preventable Signal for Pneumococcal Biofilm Formation, Colonization, and Invasion of the Host

Trappetti, C., Kadioglu, A., Carter, M., Hayre, J. K., Iannelli, F., Pozzi, G., Andrew, P. W., & Oggioni, M. R. (2009) · The Journal of Infectious Diseases · doi:10.1086/598483 · Cited by 152 · see citing works

glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein

Pellicer, M. T., Badı́a, J., Aguilar, J., & Baldomà, L. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.7.2051-2059.1996 · Cited by 148 · see citing works

Growth of Streptococcus pneumoniae on Human Glycoconjugates Is Dependent upon the Sequential Activity of Bacterial Exoglycosidases

Burnaugh, A. M., Frantz, L., & King, S. J. (2007) · Journal of Bacteriology · doi:10.1128/jb.01251-07 · Cited by 146 · see citing works

Regulation of sialic acid metabolism in Escherichia coli: role of N-acylneuraminate pyruvate-lyase

Vimr, E. R., & Troy, F. A. (1985) · Journal of Bacteriology · doi:10.1128/jb.164.2.854-860.1985 · Cited by 142 · see citing works

Role of Sialic Acid and Complex Carbohydrate Biosynthesis in Biofilm Formation by Nontypeable Haemophilus influenzae in the Chinchilla Middle Ear

Jurcisek, J. A., Greiner, L. L., Watanabe, H., Zaleski, A., Apicella, M. A., & Bakaletz, L. O. (2005) · Infection and Immunity · doi:10.1128/iai.73.6.3210-3218.2005 · Cited by 140 · see citing works

Innovations in host and microbial sialic acid biosynthesis revealed by phylogenomic prediction of nonulosonic acid structure

Lewis, A. L., Desa, N., Hansen, E. E., Knirel, Y. A., Gordon, J. I., Gagneux, P., Nizet, V., & Varki, A. P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902431106 · Cited by 138 · see citing works

Sialylation of Lipooligosaccharides Promotes Biofilm Formation by Nontypeable Haemophilus influenzae

Swords, W. E., Moore, M. L., Godzicki, L., Bukofzer, G. T., Mitten, M. J., & VonCannon, J. L. (2003) · Infection and Immunity · doi:10.1128/iai.72.1.106-113.2004 · Cited by 137 · see citing works

Purification and Properties of Cloned Salmonella typhimurium LT2 Sialidase with Virus-Typical Kinetic Preference for Sialyl α2→3 Linkages1

Hoyer, L. L., Roggentin, P., Schauer, R., & Vimr, E. R. (1991) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a123603 · Cited by 116 · see citing works

Three Streptococcus pneumoniae Sialidases: Three Different Products

Xu, G., Kiefel, M. J., Wilson, J. C., Andrew, P. W., Oggioni, M. R., & Taylor, G. L. (2011) · Journal of the American Chemical Society · doi:10.1021/ja110733q · Cited by 115 · see citing works

Sialic acid is an essential moiety of mucin as a hydroxyl radical scavenger

Ogasawara, Y., Namai, T., Yoshino, F., Lee, M., & Ishii, K. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.062 · Cited by 114 · see citing works

Phase variable desialylation of host proteins that bind to Streptococcus pneumoniae in vivo and protect the airway

King, S. J., Hippe, K. R., Gould, J. M., Bae, D., Peterson, S. N., Cline, R. T., Fasching, C. E., Janoff, E. N., & Weiser, J. N. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04252.x · Cited by 113 · see citing works

The roles of enteric bacterial sialidase, sialateO-acetyl esterase and glycosulfatase in the degradation of human colonic mucin

Corfield, A. P., WAGNER, S. A., O'Donnell, L. J. D., Durdey, P., Mountford, R. A., & Clamp, J. R. (1993) · Glycoconjugate Journal · doi:10.1007/bf00731190 · Cited by 112 · see citing works

Dissemination and Systemic Colonization of Uropathogenic Escherichia coli in a Murine Model of Bacteremia

Smith, S. N., Hagan, E. C., Lane, M. C., & Mobley, H. L. T. (2010) · mBio · doi:10.1128/mbio.00262-10 · Cited by 110 · see citing works

Nontypeable Haemophilus influenzae Strain 2019 Produces a Biofilm Containing N -Acetylneuraminic Acid That May Mimic Sialylated O-Linked Glycans

Greiner, L. L., Watanabe, H., Phillips, N. J., Shao, J., Morgan, A., Zaleski, A., Gibson, B. W., & Apicella, M. A. (2004) · Infection and Immunity · doi:10.1128/iai.72.7.4249-4260.2004 · Cited by 109 · see citing works

Sialic acid metabolism's dual function in Haemophilus influenzae

Vimr, E. R., Lichtensteiger, C. A., & Steenbergen, S. M. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01925.x · Cited by 107 · see citing works

Cloning, sequencing and distribution of the Salmonella typhimurlum LT2 siaiidase gene, nanH, provides evidence for interspecies gene transfer

Hoyer, L. L., Hamilton, A. C., Steenbergen, S. M., & Vimr, E. R. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb01538.x · Cited by 102 · see citing works

Regulation of Sialic Acid Catabolism by the DNA Binding Protein NanR in Escherichia coli

Kalivoda, K. A., Steenbergen, S. M., Vimr, E. R., & PLUMBRIDGE, J. A. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.16.4806-4815.2003 · Cited by 86 · see citing works

Sialic Acid ( N -Acetyl Neuraminic Acid) Utilization by Bacteroides fragilis Requires a Novel N -Acetyl Mannosamine Epimerase

Brigham, C. J., Caughlan, R. E., Gallegos, R., Dallas, M. M., Godoy, V. G., & Malamy, M. H. (2009) · Journal of Bacteriology · doi:10.1128/jb.00811-08 · Cited by 80 · see citing works

Sialic Acid Metabolism and Systemic Pasteurellosis

Steenbergen, S. M., Lichtensteiger, C. A., Caughlan, R. E., Garfinkle, J., Fuller, T. E., & Vimr, E. R. (2005) · Infection and Immunity · doi:10.1128/iai.73.3.1284-1294.2005 · Cited by 78 · see citing works

The ability to utilize mucin affects the regulation of virulence gene expression inStreptococcus pneumoniae

Yeşilkaya, H., Manco, S., Kadioglu, A., Terra, V. S., & Andrew, P. W. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.01003.x · Cited by 75 · see citing works

Derived structure of the putative sialic acid transporter from Escherichia coli predicts a novel sugar permease domain

Martinez, J., Steenbergen, S. M., & Vimr, E. R. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.20.6005-6010.1995 · Cited by 72 · see citing works

A role for Bacteroides fragilis neuraminidase in bacterial growth in two model systems

Godoy, V. G., Dallas, M. M., Russo, T. A., & Malamy, M. H. (1993) · Infection and Immunity · doi:10.1128/iai.61.10.4415-4426.1993 · Cited by 71 · see citing works

Microbial sialidases: does bigger always mean better?

Vimr, E. R. (1994) · Trends in Microbiology · doi:10.1016/0966-842x(94)90003-5 · Cited by 71 · see citing works

Cloning and expression of the Vibrio cholerae neuraminidase gene nanH in Escherichia coli

Vimr, E. R., Lawrisuk, L., Galen, J. E., & Kaper, J. B. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.4.1495-1504.1988 · Cited by 70 · see citing works

Mechanisms of Association of Bacteria with Mucosal Surfaces

Freter, R. R. (2008) · Novartis Foundation symposium · doi:10.1002/9780470720639.ch4 · Cited by 69 · see citing works

Function and Expression of an N -Acetylneuraminic Acid-Inducible Outer Membrane Channel in Escherichia coli

Condemine, G., Berrier, C., PLUMBRIDGE, J. A., & Ghazi, A. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.6.1959-1965.2005 · Cited by 69 · see citing works

Sialic Acid Transport Contributes to Pneumococcal Colonization

Marion, C., Burnaugh, A. M., Woodiga, S. A., & King, S. J. (2010) · Infection and Immunity · doi:10.1128/iai.00832-10 · Cited by 69 · see citing works

Capnocytophaga canimorsus: A Human Pathogen Feeding at the Surface of Epithelial Cells and Phagocytes

Mally, M., Shin, H., Paroz, C., Landmann, R. M., & Cornelis, G. R. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000164 · Cited by 69 · see citing works

The Capability of Catabolic Utilization of N -Acetylneuraminic Acid, a Sialic Acid, Is Essential for Vibrio vulnificus Pathogenesis

Jeong, H. G., Oh, M. H., Kim, B. S., Lee, M. Y., Han, H. J., & Choi, S. H. (2009) · Infection and Immunity · doi:10.1128/iai.00109-09 · Cited by 68 · see citing works

Biosynthesis of the polysialic acid capsule inEscherichia coli K1

Vimr, E. R., Steenbergen, S. M., & Cieslewicz, M. J. (1995) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/bf01569991 · Cited by 66 · see citing works

Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively

Bigi, A., Morosi, L., Pozzi, C., Forcella, M. E., Tettamanti, G., Venerando, B., Monti, E., & Fusi, P. A. (2009) · Glycobiology · doi:10.1093/glycob/cwp156 · Cited by 66 · see citing works

A Novel Sialic Acid Utilization and Uptake System in the Periodontal Pathogen Tannerella forsythia

Roy, S., Douglas, C. W. I., & Stafford, G. P. (2010) · Journal of Bacteriology · doi:10.1128/jb.00079-10 · Cited by 65 · see citing works

Regulation of sialic acid transport and catabolism in <i>Haemophilus influenzae</i>

Johnston, J. W., Zaleski, A., Allen, S., Mootz, J. M., Armbruster, D., Gibson, B. W., Apicella, M. A., & Munson, R. S. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05890.x · Cited by 64 · see citing works

Cloning and Characterization of Sialidases with 2-6′ and 2-3′ Sialyl Lactose Specificity from Pasteurella multocida

Mizan, S., Henk, A. D., Stallings, A. P., Maier, M., & Lee, M. D. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.24.6874-6883.2000 · Cited by 63 · see citing works

Leukocyte Inflammatory Responses Provoked by Pneumococcal Sialidase

Chang, Y., Uchiyama, S., Varki, A. P., & Nizet, V. (2012) · mBio · doi:10.1128/mbio.00220-11 · Cited by 62 · see citing works

Commensal ocular bacteria degrade mucins

Berry, M. (2002) · British Journal of Ophthalmology · doi:10.1136/bjo.86.12.1412 · Cited by 62 · see citing works

Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O -Acetyl Esterase in Escherichia coli K1

Steenbergen, S. M., Lee, Y., Vann, W. F., Vionnet, J. A., Wright, L. F., & Vimr, E. R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00466-06 · Cited by 60 · see citing works

Sialic Acid Mutarotation Is Catalyzed by the Escherichia coli β-Propeller Protein YjhT

Severi, E., Müller, A., Potts, J. R., Leech, A., Williamson, D. C., Wilson, K. S., & Thomas, G. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707822200 · Cited by 59 · see citing works

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

Davies, L. R. L., Pearce, O. M. T., Tessier, M. B., Assar, S., Smutova, V., Pajunen, M. I., Sumida, M., Sato, C., Kitajima, K., Finne, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365056 · Cited by 58 · see citing works

Oligopeptidase-deficient mutants of Salmonella typhimurium

Vimr, E. R., Green, L., & Miller, C. G. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.3.1259-1265.1983 · Cited by 52 · see citing works

NanC Crystal Structure, a Model for Outer-Membrane Channels of the Acidic Sugar-Specific KdgM Porin Family

Wirth, C., Condemine, G., Boiteux, C., Bernèche, S., Schirmer, T., & Peneff, C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.054 · Cited by 51 · see citing works

YjhS (NanS) Is Required for Escherichia coli To Grow on 9-O-Acetylated N -Acetylneuraminic Acid

Steenbergen, S. M., Jirik, J. L., & Vimr, E. R. (2009) · Journal of Bacteriology · doi:10.1128/jb.01000-09 · Cited by 50 · see citing works

Characterization of a novel sialic acid transporter of the sodium solute symporter (SSS) family and in vivo comparison with known bacterial sialic acid transporters

Severi, E., Hosie, A. H. F., Hawkhead, J. A., & Thomas, G. H. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01881.x · Cited by 48 · see citing works

Genotype and Phenotypes of an Intestine-Adapted Escherichia coli K-12 Mutant Selected by Animal Passage for Superior Colonization

Fabich, A. J., Leatham, M. P., Grissom, J. E., Wiley, G. B., Lai, H., Najar, F. Z., Roe, B. A., Cohen, P. S., & Conway, T. (2011) · Infection and Immunity · doi:10.1128/iai.01199-10 · Cited by 48 · see citing works

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

Bergfeld, A. K., Pearce, O. M. T., Diaz, S. L., Lawrence, R., Vocadlo, D. J., Choudhury, B., Esko, J. D., & Varki, A. P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.363499 · Cited by 43 · see citing works

Cooperative regulation of the Vibrio vulnificus nan gene cluster by NanR protein, cAMP receptor protein, and N-Acetylmannosamine 6-Phosphate

Kim, B. S., Hwang, J., Kim, M. H., & Choi, S. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.300988 · Cited by 43 · see citing works

Identification, structure, and characterization of an exopolysaccharide produced by Histophilus somniduring biofilm formation

Sandal, I., Inzana, T. J., Molinaro, A., Castro, C. D., Shao, J. Q., Apicella, M. A., Cox, A. D., Michael, F. S., & Berg, G. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-186 · Cited by 42 · see citing works

The first committed step in the biosynthesis of sialic acid by Escherichia coli K1 does not involve a phosphorylated N‐acetylmannosamine intermediate

Ringenberg, M. A., Steenbergen, S. M., & Vimr, E. R. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03741.x · Cited by 41 · see citing works

Haemophilus influenzae biofilms: hypothesis or fact?

Moxon, E. R., Sweetman, W. A., Deadman, M. E., Ferguson, D. J. P., & Hood, D. W. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2007.12.005 · Cited by 40 · see citing works

Sialic acid mediated transcriptional modulation of a highly conserved sialometabolism gene cluster in Haemophilus influenzae and its effect on virulence

Jenkins, G. A., Figueira, M. A., Kumar, G. A., Sweetman, W. A., Makepeace, K., Pelton, S. I., Moxon, R. E., & Hood, D. W. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-48 · Cited by 40 · see citing works

Structural and enzymatic characterization of NanS (YjhS), a 9‐O‐Acetyl N‐acetylneuraminic acid esterase from Escherichia coli O157:H7

Rangarajan, E. S., Ruane, K. M., Proteau, A., Schrag, J. D., Valladares, R. B., González, C. F., Gilbert, M., Yakunin, A. F., & Cygler, M. (2011) · Protein Science · doi:10.1002/pro.649 · Cited by 36 · see citing works

Localisation and distribution of O-acetylated N-acetylneuraminic acids, the endogenous substrates of the hemagglutinin-esterases of murine coronaviruses, in mouse tissue

Rinninger, A., Richet, C., Pons, A., Kohla, G., Schauer, R., Bauer, H., Zanetta, J., & Vlasak, R. (2006) · Glycoconjugate Journal · doi:10.1007/s10719-006-5439-7 · Cited by 35 · see citing works

Sialic acid uptake is necessary for virulence of Pasteurella multocida in turkeys

Tatum, F. M., Tabatabai, L. B., & Briggs, R. E. (2009) · Microbial Pathogenesis · doi:10.1016/j.micpath.2009.04.003 · Cited by 34 · see citing works

Sialidase Specificity Determined by Chemoselective Modification of Complex Sialylated Glycans

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To sugarcoat bacteria

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