Cell Wall Structure and Function in Lactic Acid Bacteria

Peptidoglycan types of bacterial cell walls and their taxonomic implications

SCHLEIFER, K. H., & Kandler, O. (1972) · Bacteriological Reviews · doi:10.1128/br.36.4.407-477.1972 · Cited by 4,203 · see citing works

Comparative genomics of the lactic acid bacteria.

Makarova, K., Slesarev, A., Wolf, Y., Sorokin, A., Mirkin, B., Koonin, E., Pavlov, A., Pavlova, N., Karamychev, V., Polouchine, N., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607117103 · Cited by 1,391 · see citing works

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391 · see citing works

The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis

Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., & Charlier, P. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2008.00105.x · Cited by 1,322 · see citing works

From the regulation of peptidoglycan synthesis to bacterial growth and morphology

Typas, A., Banzhaf, M., Gross, C. A., & Vollmer, W. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2677 · Cited by 1,258 · see citing works

Lactic acid bacteria of foods and their current taxonomy

Stiles, M. E., & Holzapfel, W. H. (1997) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(96)01233-0 · Cited by 1,100 · see citing works

Host interactions of probiotic bacterial surface molecules: comparison with commensals and pathogens

Lebeer, S., Vanderleyden, J., & De Keersmaecker, S. C. J. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2297 · Cited by 1,062 · see citing works

A Continuum of Anionic Charge: Structures and Functions of d -Alanyl-Teichoic Acids in Gram-Positive Bacteria

Neuhaus, F. C., & BADDILEY, J. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.686-723.2003 · Cited by 1,035 · see citing works

Wall Teichoic Acids of Gram-Positive Bacteria

Brown, S., Santa Maria, J. P., & Walker, S. (2013) · Annual Review of Microbiology · doi:10.1146/annurev-micro-092412-155620 · Cited by 966 · see citing works

Bacterial peptidoglycan (murein) hydrolases

Vollmer, W., Joris, B., Charlier, P., & Foster, S. J. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00099.x · Cited by 880 · see citing works

Heteropolysaccharides from lactic acid bacteria

Vuyst, L. D., & Degeest, B. (1999) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1999.tb00395.x · Cited by 840 · see citing works

Soluble Proteins Produced by Probiotic Bacteria Regulate Intestinal Epithelial Cell Survival and Growth

Yan, F., Cao, H., Cover, T. L., Whitehead, R. H., Washington, M. K., & Polk, D. B. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.11.022 · Cited by 828 · see citing works

Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions

Weidenmaier, C., & Peschel, A. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1861 · Cited by 777 · see citing works

Genetic Analysis of the Capsular Biosynthetic Locus from All 90 Pneumococcal Serotypes

Bentley, S. D., Aanensen, D. M., Mavroidi, A., Saunders, D., Rabbinowitsch, E., Collins, M. D., Donohoe, K., Harris, D. J., Murphy, L., Quail, M. A., et al. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020031 · Cited by 759 · see citing works

Comparative genomic analysis of <i>Lactobacillus rhamnosus</i> GG reveals pili containing a human- mucus binding protein

Kankainen, M., Paulin, L., Tynkkynen, S., von Ossowski, I., Reunanen, J., Partanen, P., Satokari, R., Vesterlund, S., Hendrickx, A. P. A., Lebeer, S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908876106 · Cited by 740 · see citing works

Cheese flavour formation by amino acid catabolism

Yvon, M., & Rijnen, L. (2001) · International Dairy Journal · doi:10.1016/s0958-6946(01)00049-8 · Cited by 736 · see citing works

Cytoplasmic steps of peptidoglycan biosynthesis

Barreteau, H., Kovač, A., Boniface, A., Sova, M., Gobec, S., & Blanot, D. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2008.00104.x · Cited by 727 · see citing works

Peptidoglycan Molecular Requirements Allowing Detection by Nod1 and Nod2

Girardin, S. E., Travassos, L. H., Hervé, M., Blanot, D., Boneca, I. G., Philpott, D. J., Sansonetti, P. J., & Mengin‐Lecreulx, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307198200 · Cited by 684 · see citing works

LysM, a widely distributed protein motif for binding to (peptido)glycans

Buist, G., Steen, A., Kok, J., & Kuipers, O. P. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06211.x · Cited by 628 · see citing works

S layer protein A of Lactobacillus acidophilus NCFM regulates immature dendritic cell and T cell functions

Konstantinov, S. R., Smidt, H., de Vos, W. M., Bruijns, S. C. M., Singh, S., Valence, F., Mollé, D., Lortal, S., Altermann, E., Klaenhammer, T. R., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810305105 · Cited by 568 · see citing works

Exopolysaccharides from lactic acid bacteria: perspectives and challenges

Welman, A. D., & Maddox, I. S. (2003) · Trends in biotechnology · doi:10.1016/s0167-7799(03)00107-0 · Cited by 523 · see citing works

Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O ‐acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus

Bera, A., Herbert, S., Jakob, A., Vollmer, W., & Götz, F. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04446.x · Cited by 481 · see citing works

The biosynthesis of peptidoglycan lipid-linked intermediates

Bouhss, A., Trunkfield, A. E., Bugg, T. D. H., & Mengin‐Lecreulx, D. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00089.x · Cited by 446 · see citing works

Enhanced antiinflammatory capacity of a Lactobacillus plantarum mutant synthesizing modified teichoic acids

Grangette, C., Nutten, S., Palumbo, E., Morath, S., Hermann, C., Dewulf, J., Pot, B., Härtung, T., Pascal Hols, A., & Mercenier, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504084102 · Cited by 443 · see citing works

Immunomodulatory mechanisms of lactobacilli

Wells, J. M. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-s1-s17 · Cited by 431 · see citing works

Wall Teichoic Acid Function, Biosynthesis, and Inhibition

Swoboda, J. G., Campbell, J., Meredith, T. C., & Walker, S. (2009) · ChemBioChem · doi:10.1002/cbic.200900557 · Cited by 413 · see citing works

Autolysins of Bacillus subtilis: multiple enzymes with multiple functions

Smith, T. J., Blackman, S. A., & Foster, S. J. (2000) · Microbiology · doi:10.1099/00221287-146-2-249 · Cited by 411 · see citing works

Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development

Mandlik, A., Swierczynski, A., Das, A., & Ton‐That, H. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2007.10.010 · Cited by 403 · see citing works

Cell envelope stress response in Gram-positive bacteria

Jordan, S., Hutchings, M. I., & Mascher, T. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00091.x · Cited by 387 · see citing works

Sortase‐catalysed anchoring of surface proteins to the cell wall of <i>Staphylococcus aureus</i>

Mazmanian, S. K., Ton‐That, H., & Schneewind, O. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02411.x · Cited by 387 · see citing works

Functional Analysis of Lactobacillus rhamnosus GG Pili in Relation to Adhesion and Immunomodulatory Interactions with Intestinal Epithelial Cells

Lebeer, S., Claes, I. J. J., Tytgat, H. L. P., Verhoeven, T. L. A., Marien, E., von Ossowski, I., Reunanen, J., Palva, A., de Vos, W. M., Keersmaecker, S. C. J. D., et al. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.06192-11 · Cited by 378 · see citing works

Functional genome analysis of <i>Bifidobacterium breve</i> UCC2003 reveals type IVb tight adherence (Tad) pili as an essential and conserved host-colonization factor

O'Connell Motherway, M., Zomer, A., Leahy, S. C., Reunanen, J., Bottacini, F., Claesson, M. J., O'Brien, F., Flynn, K., Casey, P. G., Moreno Munoz, J. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105380108 · Cited by 376 · see citing works

Colon-specific delivery of a probiotic-derived soluble protein ameliorates intestinal inflammation in mice through an EGFR-dependent mechanism

Yan, F., Cao, H., Cover, T. L., Washington, M. K., Shi, Y., Liu, L., Chaturvedi, R., Peek, R. M., Wilson, K. T., & Polk, D. B. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44031 · Cited by 376 · see citing works

Anti-inflammatory capacity of selected lactobacilli in experimental colitis is driven by NOD2-mediated recognition of a specific peptidoglycan-derived muropeptide

Fernandez, E. M., Valenti, V., Rockel, C., Hermann, C., Pot, B., Boneca, I. G., & Grangette, C. (2011) · Gut · doi:10.1136/gut.2010.232918 · Cited by 376 · see citing works

Structural variation in the glycan strands of bacterial peptidoglycan

Vollmer, W. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00088.x · Cited by 370 · see citing works

Regulation of intestinal homeostasis and immunity with probiotic lactobacilli

van Baarlen, P., Wells, J. M., & Kleerebezem, M. (2013) · Trends in Immunology · doi:10.1016/j.it.2013.01.005 · Cited by 369 · see citing works

The Peptidoglycan of Stationary-Phase Mycobacterium tuberculosis Predominantly Contains Cross-Links Generated by l,d -Transpeptidation

Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Véziris, N., Blanot, D., Gutmann, L., & Mainardi, J. (2008) · Journal of Bacteriology · doi:10.1128/jb.00239-08 · Cited by 349 · see citing works

New Insights into the WalK/WalR (YycG/YycF) Essential Signal Transduction Pathway Reveal a Major Role in Controlling Cell Wall Metabolism and Biofilm Formation inStaphylococcus aureus

Dubrac, S., Boneca, I. G., Poupel, O., & Msadek, T. (2007) · Journal of Bacteriology · doi:10.1128/jb.00645-07 · Cited by 347 · see citing works

Lipoteichoic Acids from Lactobacillus Strains Elicit Strong Tumor Necrosis Factor Alpha-Inducing Activities in Macrophages through Toll-Like Receptor 2

Matsuguchi, T., Takagi, A., Matsuzaki, T., Nagaoka, M., Ishikawa, K., Yokokura, T., & Yoshikai, Y. (2003) · Clinical Diagnostic Laboratory Immunology · doi:10.1128/cdli.10.2.259-266.2003 · Cited by 328 · see citing works

Identification of FtsW as a transporter of lipid‐linked cell wall precursors across the membrane

Mohammadi, T., van Dam, V., Sijbrandi, R., Vernet, T., Zapun, A., Bouhss, A., Bruin, M. D.-D., Nguyen‐Distèche, M., KRUIJFF, B. D., & Breukink, E. J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.61 · Cited by 314 · see citing works

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Oliveira, H., Melo, L. D. R., Santos, S. R. B., Nóbrega, F. L., Ferreira, E. C., Cerca, N., Azeredo, J., & Kluskens, L. (2013) · Journal of Virology · doi:10.1128/jvi.03277-12 · Cited by 288 · see citing works

Incorporation of D-Alanine into Lipoteichoic Acid and Wall Teichoic Acid in Bacillus subtilis

Perego, M., Glaser, P., Minutello, A., Strauch, M. A., Leopold, K., & Fischer, W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.26.15598 · Cited by 287 · see citing works

The biosynthesis and functionality of the cell-wall of lactic acid bacteria.

Delcour, J., Ferain, T., Deghorain, M., Palumbo, E., & Pascal Hols, A. (1999) · PubMed · Cited by 286 · see citing works

Lactobacillus surface layer proteins: Structure, function and applications

Hynönen, U., & Palva, A. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-4962-2 · Cited by 283 · see citing works

The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin

Gupta, R., Lavollay, M., Mainardi, J.-L., Arthur, M., Bishai, W. R., & Lamichhane, G. (2010) · Nature Medicine · doi:10.1038/nm.2120 · Cited by 281 · see citing works

Regulation of induced colonic inflammation by Lactobacillus acidophilus deficient in lipoteichoic acid

Mohamadzadeh, M., Pfeiler, E. A., Brown, J. B., Zadeh, M., Gramarossa, M., Managlia, E. Z., Bere, P., Sarraj, B., Khan, M. W., Pakanati, K. C., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005066107 · Cited by 279 · see citing works

A widespread family of bacterial cell wall assembly proteins

Kawai, Y., Marles‐Wright, J., Cleverley, R. M., Emmins, R., Ishikawa, S., Kuwano, M., Heinz, N., Bui, N. K., Hoyland, C. N., Ogasawara, N., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.358 · Cited by 275 · see citing works

Identification of a Gene Cluster for the Biosynthesis of a Long, Galactose-Rich Exopolysaccharide in Lactobacillus rhamnosus GG and Functional Analysis of the Priming Glycosyltransferase

Lebeer, S., Verhoeven, T. L. A., Francius, G., Schoofs, G., Lambrichts, I., Dufrêne, Y. F., Vanderleyden, J., & Keersmaecker, S. C. J. D. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.02919-08 · Cited by 271 · see citing works

The pgdA Gene Encodes for a PeptidoglycanN-Acetylglucosamine Deacetylase in Streptococcus pneumoniae

Vollmer, W., & Tomasz, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910189199 · Cited by 269 · see citing works

Teichoic acids are temporal and spatial regulators of peptidoglycan cross-linking in Staphylococcus aureus

Atilano, M. L., Pereira, P. M., Yates, J. R., Reed, P., Veiga, H., Pinho, M. G., & Filipe, S. R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004304107 · Cited by 266 · see citing works

Architects at the bacterial surface — sortases and the assembly of pili with isopeptide bonds

Hendrickx, A. P. A., Budzik, J. M., Oh, S., & Schneewind, O. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2520 · Cited by 264 · see citing works

The biosynthesis and functionality of the cell-wall of lactic acid bacteria

Delcour, J., Ferain, T., Deghorain, M., Palumbo, E., & Pascal Hols, A. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002089722581 · Cited by 262 · see citing works

Role of staphylococcal wall teichoic acid in targeting the major autolysin Atl

Schlag, M., Biswas, R., Krismer, B., Kohler, T. P., Zoll, S., Yu, W., Schwarz, H., Peschel, A., & Götz, F. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.07007.x · Cited by 260 · see citing works

Protein secretion and surface display in Gram-positive bacteria

Schneewind, O., & Missiakas, D. M. (2012) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0210 · Cited by 253 · see citing works

Protein cell surface display in Gram-positive bacteria: from single protein to macromolecular protein structure.

Desvaux, M., Dumas, É., Chafsey, I., & Hébraud, M. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00122.x · Cited by 250 · see citing works

Cell Wall Attachment of a Widely Distributed Peptidoglycan Binding Domain Is Hindered by Cell Wall Constituents

Steen, A., Buist, G., Leenhouts, K. J., Khattabi, M. E., Grijpstra, F., Zomer, A., Venema, G., Kuipers, O. P., & Kok, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211055200 · Cited by 248 · see citing works

Cell Surface-Associated Lipoteichoic Acid Acts as an Adhesion Factor for Attachment of Lactobacillus johnsonii La1 to Human Enterocyte-Like Caco-2 Cells

Granato, D., Perotti, F., Masserey‐Elmelegy, I., Rouvet, M., Golliard, M., Servin, A. L., & Brassart, D. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.3.1071-1077.1999 · Cited by 248 · see citing works

Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation

Buist, G., Kok, J., Leenhouts, K. J., Dabrowska, M., Venema, G., & Haandrikman, A. J. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.6.1554-1563.1995 · Cited by 247 · see citing works

Inactivation of the <i>srtA</i> gene in <i>Listeria monocytogenes</i> inhibits anchoring of surface proteins and affects virulence

Bierne, H., Mazmanian, S. K., Trost, M., Pucciarelli, M. G., Liu, G., Dehoux, P., the European Listeria Genome Consortium, Jänsch, L., Portillo, F. G., Schneewind, O., et al. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02798.x · Cited by 223 · see citing works

Mucosal Adhesion Properties of the Probiotic Lactobacillus rhamnosus GG SpaCBA and SpaFED Pilin Subunits

von Ossowski, I., Reunanen, J., Satokari, R. M., Vesterlund, S., Kankainen, M., Huhtinen, H., Tynkkynen, S., Salminen, S., de Vos, W. M., & Palva, A. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.01958-09 · Cited by 216 · see citing works

The Role of Autolysis of Lactic Acid Bacteria in the Ripening of Cheese

Crow, V. L., Coolbear, T., Gopal, P. K., Martley, F. G., McKay, L. L., & Riepe, H. (1995) · International Dairy Journal · doi:10.1016/0958-6946(95)00036-4 · Cited by 215 · see citing works

HtrA is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing

Poquet, I., Saint, V., Seznec, E., Simoes, N., Bolotin, A., & Gruss, A. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01757.x · Cited by 212 · see citing works

Lesions in Teichoic Acid Biosynthesis in Staphylococcus aureus Lead to a Lethal Gain of Function in the Otherwise Dispensable Pathway

D’Elia, M. A., Pereira, M. P., Chung, Y. S., Zhao, W., Chau, A. S., Kenney, T. J., Sulavik, M. C., Black, T. A., & Brown, E. D. (2006) · Journal of Bacteriology · doi:10.1128/jb.00197-06 · Cited by 196 · see citing works

Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan

van HEIJENOORT, J. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00016-07 · Cited by 194 · see citing works

Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in Gram-positive bacteria of the phylum Firmicutes

Reichmann, N. T., & Gründling, A. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02260.x · Cited by 192 · see citing works

Comparative analysis of proteins with a mucus-binding domain found exclusively in lactic acid bacteria

Boekhorst, J., Helmer, Q., Kleerebezem, M., & Siezen, R. J. (2005) · Microbiology · doi:10.1099/mic.0.28415-0 · Cited by 191 · see citing works

Distinct and essential morphogenic functions for wall‐ and lipo‐teichoic acids in Bacillus subtilis

Schirner, K., Marles‐Wright, J., Lewis, R. J., & Errington, J. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.25 · Cited by 189 · see citing works

Wall Teichoic Acid Polymers Are Dispensable for Cell Viability in Bacillus subtilis

D’Elia, M. A., Millar, K. E., Beveridge, T. J., & Brown, E. D. (2006) · Journal of Bacteriology · doi:10.1128/jb.01336-06 · Cited by 181 · see citing works

Exopolysaccharides of Lactobacillus rhamnosus GG form a protective shield against innate immune factors in the intestine

Lebeer, S., Claes, I. J. J., Verhoeven, T. L. A., Vanderleyden, J., & Keersmaecker, S. C. J. D. (2010) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2010.00199.x · Cited by 179 · see citing works

Novel Surface Display System for Proteins on Non-Genetically Modified Gram-Positive Bacteria

Bosma, T., Kanninga, R., Neef, J., Audouy, S. A. L., van Roosmalen, M. L., Steen, A., Buist, G., Kok, J., Kuipers, O. P., Robillard, G. T., et al. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.1.880-889.2006 · Cited by 178 · see citing works

Cell Surface of Lactococcus lactis Is Covered by a Protective Polysaccharide Pellicle

Chapot, M.-P., VINOGRADOV, E. V., Sadovskaya, I., André, G., Mistou, M., Trieu‐Cuot, P., Furlan, S., Bidnenko, E., Courtin, P., Péchoux, C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082958 · Cited by 176 · see citing works

A Lactobacillus rhamnosus GG-derived Soluble Protein, p40, Stimulates Ligand Release from Intestinal Epithelial Cells to Transactivate Epidermal Growth Factor Receptor

Yan, F., Liu, L., Dempsey, P. J., Tsai, Y.-H., Raines, E. W., Wilson, C. L., Cao, H., Cao, Z., Liu, L., & Polk, D. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.492397 · Cited by 171 · see citing works

Spx-RNA Polymerase Interaction and Global Transcriptional Control during Oxidative Stress

Zuber, P. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.7.1911-1918.2004 · Cited by 171 · see citing works

Bacteriophage defence systems in lactic acid bacteria

Forde, A., & Fitzgerald, G. F. (1999) · Springer eBooks · doi:10.1007/978-94-017-2027-4_4 · Cited by 171 · see citing works

Cross-Linked Peptidoglycan Mediates Lysostaphin Binding to the Cell Wall Envelope of Staphylococcus aureus

Gründling, A., & Schneewind, O. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.7.2463-2472.2006 · Cited by 166 · see citing works

Engineering lactococci and lactobacilli for human health

Bermúdez‐Humarán, L. G., Aubry, C., Motta, J., Deraison, C., Steidler, L., Vergnolle, N., Chatel, J., & Langella, P. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.06.002 · Cited by 164 · see citing works

Bacteriophage defence systems in lactic acid bacteria

Forde, A., & Fitzgerald, G. F. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002027321171 · Cited by 158 · see citing works

Role, Mechanisms and Control of Lactic Acid Bacteria Lysis in Cheese

Lortal, S., & Chapot-Chartier, M.-P. (2005) · International Dairy Journal · doi:10.1016/j.idairyj.2004.08.024 · Cited by 154 · see citing works

Lipoteichoic Acids, Phosphate-Containing Polymers in the Envelope of Gram-Positive Bacteria

Schneewind, O., & Missiakas, D. M. (2014) · Journal of Bacteriology · doi:10.1128/jb.01155-13 · Cited by 152 · see citing works

Sec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteria

Schneewind, O., & Missiakas, D. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.009 · Cited by 149 · see citing works

Perspectives on the contribution of lactic acid bacteria to cheese flavor development

Steele, J. L., Broadbent, J. R., & Kok, J. (2012) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2012.12.001 · Cited by 143 · see citing works

Imaging the nanoscale organization of peptidoglycan in living Lactococcus lactis cells

André, G., Kulakauskas, S., Chapot, M.-P., Navet, B., Deghorain, M., Bernard, E., Pascal Hols, A., & Dufrêne, Y. F. (2010) · Nature Communications · doi:10.1038/ncomms1027 · Cited by 142 · see citing works

Suppressive Effect on Activation of Macrophages by Lactobacillus casei Strain Shirota Genes Determining the Synthesis of Cell Wall-Associated Polysaccharides

Yasuda, E., Serata, M., & Sako, T. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.00412-08 · Cited by 142 · see citing works

LPxTG surface proteins of enterococci

Hendrickx, A. P. A., Willems, R. J. L., Bonten, M. J. M., & van Schaik, W. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.06.004 · Cited by 139 · see citing works

d ‐Alanyl ester depletion of teichoic acids in Lactobacillus reuteri 100‐23 results in impaired colonization of the mouse gastrointestinal tract

Walter, J., Loach, D. M., Alqumber, M. A. A., Rockel, C., Hermann, C., Pfitzenmaier, M., & Tannock, G. W. (2007) · Environmental Microbiology · doi:10.1111/j.1462-2920.2007.01292.x · Cited by 134 · see citing works

Clostridium difficile Has an Original Peptidoglycan Structure with a High Level of N-Acetylglucosamine Deacetylation and Mainly 3-3 Cross-links

Johann, P., Courtin, P., Meouche, I. E., Lemée, L., Chapot‐Chartier, M., & Pons, J.-L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.259150 · Cited by 133 · see citing works

Cell Wall-targeting Domain of Glycylglycine Endopeptidase Distinguishes among Peptidoglycan Cross-bridges

Lu, J. Z., Fujiwara, T., Komatsuzawa, H., Sugai, M., & Sakon, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509691200 · Cited by 132 · see citing works

Impact of 4 Lactobacillus plantarum Capsular Polysaccharide Clusters on Surface Glycan Composition and Host Cell Signaling

Remus, D. M., van Kranenburg, R., van Swam, I. I., Taverne, N., Bongers, R. S., Wels, M., Wells, J. M., Bron, P. A., & Kleerebezem, M. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-149 · Cited by 131 · see citing works

Pili of Gram-positive bacteria: roles in host colonization

Danne, C., & Dramsi, S. (2012) · Research in Microbiology · doi:10.1016/j.resmic.2012.10.012 · Cited by 129 · see citing works

Functional Analysis of d -Alanylation of Lipoteichoic Acid in the Probiotic StrainLactobacillus rhamnosusGG

Vélez, M. P., Verhoeven, T. L. A., Draing, C., von Aulock, S., Pfitzenmaier, M., Geyer, A., Lambrichts, I., Grangette, C., Pot, B., Vanderleyden, J., et al. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.02083-06 · Cited by 125 · see citing works

Comparative analysis of the exopolysaccharide biosynthesis gene clusters from four strains of Lactobacillus rhamnosus

Péant, B., LaPointe, G., Gilbert, C., Atlan, D., Ward, P., & Roy, D. (2005) · Microbiology · doi:10.1099/mic.0.27852-0 · Cited by 122 · see citing works

AcmA of Lactococcus lactis is an N‐acetylglucosaminidase with an optimal number of LysM domains for proper functioning

Steen, A., Buist, G., Horsburgh, G. J., Venema, G., Kuipers, O. P., Foster, S. J., & Kok, J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04706.x · Cited by 120 · see citing works

Super‐resolution microscopy reveals cell wall dynamics and peptidoglycan architecture in ovococcal bacteria

Wheeler, R., Mesnage, S., Boneca, I. G., Hobbs, J. K., & Foster, S. J. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07871.x · Cited by 120 · see citing works

OatA, a peptidoglycan O-acetyltransferase involved in Listeria monocytogenes immune escape, is critical for virulence.

Aubry, C., Goulard, C., Nahori, M., Cayet, N., Decalf, J., Sachse, M., Boneca, I., Cossart, P., & Dussurget, O. (2011) · Journal of Infectious Diseases · doi:10.1093/infdis/jir396 · Cited by 119 · see citing works

Characterization of O-Acetylation of N-Acetylglucosamine

Bernard, E., Rolain, T., Courtin, P., Guillot, A., Langella, P., Pascal Hols, A., & Chapot, M.-P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241414 · Cited by 117 · see citing works

Transcriptome Analysis Reveals Mechanisms by Which Lactococcus lactis Acquires Nisin Resistance

Kramer, N. E., van Hijum, S. A. F. T., Knol, J., Kok, J., & Kuipers, O. P. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.50.5.1753-1761.2006 · Cited by 116 · see citing works

Lipoteichoic acid is an important microbe-associated molecular pattern of Lactobacillus rhamnosus GG

Claes, I. J. J., Segers, M. E., Verhoeven, T. L. A., Dusselier, M., Sels, B. F., Keersmaecker, S. C. J. D., Vanderleyden, J., & Lebeer, S. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-161 · Cited by 116 · see citing works

Stretching polysaccharides on live cells using single molecule force spectroscopy

Francius, G., Alsteens, D., Duprès, V., Lebeer, S., Keersmaecker, S. C. J. D., Vanderleyden, J., Gruber, H. J., & Dufrêne, Y. F. (2009) · Nature Protocols · doi:10.1038/nprot.2009.65 · Cited by 114 · see citing works

Identification and in vitro Analysis of the GatD/MurT Enzyme-Complex Catalyzing Lipid II Amidation in Staphylococcus aureus

Münch, D., Roemer, T., Lee, S. H., Engeser, M., Sahl, H. G., & Schneider, T. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002509 · Cited by 114 · see citing works

Investigation of the Relationship between Lactococcal Host Cell Wall Polysaccharide Genotype and 936 Phage Receptor Binding Protein Phylogeny

Mahony, J., Kot, W., Murphy, J., Ainsworth, S., Neve, H., Hansen, L. H., Heller, K. J., S�rensen, S. J., Hammer, K., Cambillau, C., et al. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.00653-13 · Cited by 114 · see citing works

C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive Bacteria

Brinster, S., Furlan, S., & Serror, P. (2007) · Journal of Bacteriology · doi:10.1128/jb.00773-06 · Cited by 112 · see citing works

Differences in Lactococcal Cell Wall Polysaccharide Structure Are Major Determining Factors in Bacteriophage Sensitivity

Ainsworth, S., Sadovskaya, I., Vinogradov, E., Courtin, P., Guérardel, Y., Mahony, J., Grard, T., Cambillau, C., Chapot, M.-P., & van Sinderen, D. (2014) · mBio · doi:10.1128/mbio.00880-14 · Cited by 112 · see citing works

Lactobacillus plantarum gene clusters encoding putative cell-surface protein complexes for carbohydrate utilization are conserved in specific gram-positive bacteria

Siezen, R. J., Boekhorst, J., Muscariello, L., Molenaar, D., Renckens, B., & Kleerebezem, M. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-126 · Cited by 112 · see citing works

Structural Studies of the Exopolysaccharide Produced by Lactobacillus rhamnosus strain GG (ATCC 53103)

Landersjö, C., Yang, Z., Huttunen, E., & Widmalm, G. (2002) · Biomacromolecules · doi:10.1021/bm020040q · Cited by 111 · see citing works

Impact of lipoteichoic acid modification on the performance of the probiotic Lactobacillus rhamnosus GG in experimental colitis

Claes, I. J. J., Lebeer, S., Shen, C., Verhoeven, T. L. A., Dilissen, E., Hertogh, G., Bullens, D. M. A., Ceuppens, J. L., Assche, G. V., Vermeire, S., et al. (2010) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2010.04228.x · Cited by 109 · see citing works

Revised mechanism of d-alanine incorporation into cell wall polymers in Gram-positive bacteria

Reichmann, N. T., Cassona, C. P., & Gründling, A. (2013) · Microbiology · doi:10.1099/mic.0.069898-0 · Cited by 109 · see citing works

Structure, Adsorption to Host, and Infection Mechanism of Virulent Lactococcal Phage p2

Bebeacua, C., Tremblay, D. M., Farenc, C., Chapot, M.-P., Sadovskaya, I., van Heel, M., Veesler, D., Moineau, S., & Cambillau, C. (2013) · Journal of Virology · doi:10.1128/jvi.02033-13 · Cited by 105 · see citing works

Identification of Genetic Determinants and Enzymes Involved with the Amidation of Glutamic Acid Residues in the Peptidoglycan of Staphylococcus aureus

Figueiredo, T. A., Sobral, R. G., Ludovice, A. M., Almeida, J. M. G. C. F., Bui, N. K., Vollmer, W., de LENCASTRE, H., & Tomasz, A. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002508 · Cited by 103 · see citing works

Cell wall assembly in Bacillus subtilis: how spirals and spaces challenge paradigms

Bhavsar, A. P., & Brown, E. D. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05169.x · Cited by 103 · see citing works

SpxB Regulates O-Acetylation-dependent Resistance of Lactococcus lactis Peptidoglycan to Hydrolysis

Veiga, P., Bulbarela-Sampieri, C., Furlan, S., Maisons, A., Chapot, M.-P., Erkelenz, M., Mervelet, P., Noirot, P. H., Frees, D., Kuipers, O. P., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611308200 · Cited by 101 · see citing works

Cell envelope stress induced by the bacteriocin Lcn972 is sensed by the lactococcal two‐component system CesSR

Martı́nez, B., Zomer, A., Rodrı́guez, A., Kok, J., & Kuipers, O. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05668.x · Cited by 101 · see citing works

Autolysis of Lactococcus lactis Is Increased upon d -Alanine Depletion of Peptidoglycan and Lipoteichoic Acids

Steen, A., Palumbo, E., Deghorain, M., Cocconcelli, P. S., Delcour, J., Kuipers, O. P., Kok, J., Buist, G., & Pascal Hols, A. (2004) · Journal of Bacteriology · doi:10.1128/jb.187.1.114-124.2005 · Cited by 99 · see citing works

Anchoring of proteins to lactic acid bacteria

Leenhouts, K., Buist, G., & Kok, J. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002095802571 · Cited by 97 · see citing works

Aslfm, the D-Aspartate Ligase Responsible for the Addition of D-Aspartic Acid onto the Peptidoglycan Precursor of Enterococcus faecium

Bellais, S., Arthur, M., Dubost, L., Hugonnet, J., Gutmann, L., van HEIJENOORT, J., Legrand, R., Brouard, J., Rice, L. B., & Mainardi, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600114200 · Cited by 94 · see citing works

Recombinant lactic acid bacteria as mucosal biotherapeutic agents

Daniel, C., Roussel, Y., Kleerebezem, M., & Pot, B. (2011) · Trends in biotechnology · doi:10.1016/j.tibtech.2011.05.002 · Cited by 93 · see citing works

The bacteriophage kh receptor of Lactococcus lactis subsp. cremoris KH is the rhamnose of the extracellular wall polysaccharide

Valyasevi, R., Sandine, W. E., & Geller, B. L. (1990) · Applied and Environmental Microbiology · doi:10.1128/aem.56.6.1882-1889.1990 · Cited by 90 · see citing works

LAB-Secretome: a genome-scale comparative analysis of the predicted extracellular and surface-associated proteins of Lactic Acid Bacteria

Zhou, M., Theunissen, D. H. J., Wels, M., & Siezen, R. J. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-651 · Cited by 90 · see citing works

O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems

Moynihan, P. J., & Clarke, A. J. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.08.007 · Cited by 89 · see citing works

Determinants of Murein Hydrolase Targeting to Cross-wall of Staphylococcus aureus Peptidoglycan

Frankel, M. B., & Schneewind, O. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336404 · Cited by 89 · see citing works

Peptidoglycan Structure Analysis of Lactococcus lactis Reveals the Presence of an l , d -Carboxypeptidase Involved in Peptidoglycan Maturation

Courtin, P., Miranda, G., Guillot, A., Wessner, F., Mézange, C., Domakova, E., Kulakauskas, S., & Chapot, M.-P. (2006) · Journal of Bacteriology · doi:10.1128/jb.00285-06 · Cited by 89 · see citing works

Molecular organization of selected prokaryotic S-layer proteins.

Claus, H., Akca, E., Debaerdemaeker, T., Evrard, C., Declercq, J., Harris, J., Schlott, B., & König, H. (2005) · Canadian Journal of Microbiology (print) · doi:10.1139/w05-093 · Cited by 88 · see citing works

Identification of Lactococcus lactis Genes Required for Bacteriophage Adsorption

Dupont, K., Janzen, T., Vogensen, F. K., Josephsen, J., & Stuer‐Lauridsen, B. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.10.5825-5832.2004 · Cited by 86 · see citing works

The Lactococcal Phages Tuc2009 and TP901-1 Incorporate Two Alternate Forms of Their Tail Fiber into Their Virions for Infection Specialization*

Stockdale, S. R., Mahony, J., Courtin, P., Chapot, M.-P., van Pijkeren, J., Britton, R. A., Neve, H., Heller, K. J., Aideh, B., Vogensen, F. K., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.444901 · Cited by 85 · see citing works

Structures and host-adhesion mechanisms of lactococcal siphophages

Spinelli, S., Veesler, D., Bebeacua, C., & Cambillau, C. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00003 · Cited by 84 · see citing works

Virulence or Niche Factors: What's in a Name?

Hill, C. (2012) · Journal of Bacteriology · doi:10.1128/jb.00980-12 · Cited by 83 · see citing works

Genetic and Biochemical Characterization of the Cell Wall Hydrolase Activity of the Major Secreted Protein of Lactobacillus rhamnosus GG

Claes, I. J. J., Schoofs, G., Regulski, K., Courtin, P., Chapot, M.-P., Rolain, T., Pascal Hols, A., von Ossowski, I., Reunanen, J., de Vos, W. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031588 · Cited by 81 · see citing works

Cell surface-associated compounds of probiotic lactobacilli sustain the strain-specificity dogma

Bron, P. A., Tomita, S., Mercenier, A., & Kleerebezem, M. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.06.001 · Cited by 80 · see citing works

Fluorescence and Atomic Force Microscopy Imaging of Wall Teichoic Acids in Lactobacillus plantarum

André, G., Deghorain, M., Bron, P. A., van Swam, I. I., Kleerebezem, M., Pascal Hols, A., & Dufrêne, Y. F. (2011) · ACS Chemical Biology · doi:10.1021/cb1003509 · Cited by 80 · see citing works

Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis

Meyrand, M., Boughammoura, A., Courtin, P., Mézange, C., Guillot, A., & Chapot, M.-P. (2007) · Microbiology · doi:10.1099/mic.0.2007/005835-0 · Cited by 78 · see citing works

Surface Proteome Analysis of a Natural Isolate of Lactococcus lactis Reveals the Presence of Pili Able to Bind Human Intestinal Epithelial Cells

Meyrand, M., Guillot, A., Goin, M., Furlan, S., Armalytė, J., Kulakauskas, S., Cortes‐Perez, N. G., Thomas, G., Chat, S., Péchoux, C., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.029066 · Cited by 75 · see citing works

A new morphogenesis pathway in bacteria: unbalanced activity of cell wall synthesis machineries leads to coccus-to-rod transition and filamentation in ovococci

Pérez-Núñez, D., Briandet, R., David, B., Gautier, C., Renault, P., Hallet, B., Pascal Hols, A., Carballido‐López, R., & Guédon, É. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07483.x · Cited by 75 · see citing works

Bacteriophage defence systems in lactic acid bacteria.

Forde, A., & Fitzgerald, G. F. (1999) · PubMed · Cited by 74 · see citing works

Pilus Biogenesis in Lactococcus lactis: Molecular Characterization and Role in Aggregation and Biofilm Formation

Oxaran, V., Ledue-Clier, F., Dieye, Y., Herry, J.-M., Péchoux, C., Meylheuc, T., Briandet, R., Juillard, V., & Piard, J.-C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050989 · Cited by 73 · see citing works

Synthesis of the l-Alanyl-l-alanine Cross-bridge of Enterococcus faecalis Peptidoglycan

Bouhss, A., Josseaume, N., Severin, A. I., Tabei, K., Hugonnet, J., Shlaes, D. M., Mengin‐Lecreulx, D., van HEIJENOORT, J., & Arthur, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207449200 · Cited by 73 · see citing works

Characterization of Lactococcus lactis UV-sensitive mutants obtained by ISS1 transposition

Duwat, P., Cochu, A., Ehrlich, S. D., & Gruss, A. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.14.4473-4479.1997 · Cited by 73 · see citing works

The major secreted protein Msp1/p75 is O-glycosylated in Lactobacillus rhamnosus GG

Lebeer, S., Claes, I. J. J., Balog, C. I. A., Schoofs, G., Verhoeven, T. L. A., Nys, K., von Ossowski, I., de Vos, W. M., Tytgat, H. L. P., Agostinis, P., et al. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-15 · Cited by 72 · see citing works

Molecular Insights on the Recognition of a Lactococcus lactis Cell Wall Pellicle by the Phage 1358 Receptor Binding Protein

Farenc, C., Spinelli, S., VINOGRADOV, E. V., Tremblay, D. M., Blangy, S., Sadovskaya, I., Moineau, S., & Cambillau, C. (2014) · Journal of Virology · doi:10.1128/jvi.00739-14 · Cited by 70 · see citing works

Peptidoglycan hydrolases, bacterial shape, and pathogenesis

Frirdich, E., & Gaynor, E. C. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.09.005 · Cited by 68 · see citing works

Autolysis of<i>Lactococcus lactis</i>Is Influenced by Proteolysis

Buist, G., Venema, G., & Kok, J. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.22.5947-5953.1998 · Cited by 68 · see citing works

Genetic Response to Bacteriophage Infection in Lactococcus lactis Reveals a Four-Strand Approach Involving Induction of Membrane Stress Proteins, d -Alanylation of the Cell Wall, Maintenance of Proton Motive Force, and Energy Conservation

Fallico, V., Ross, R. P., Fitzgerald, G. F., & McAuliffe, O. E. (2011) · Journal of Virology · doi:10.1128/jvi.00275-11 · Cited by 67 · see citing works

Lactobacillus plantarum possesses the capability for wall teichoic acid backbone alditol switching

Bron, P. A., Tomita, S., van Swam, I. I., Remus, D. M., Meijerink, M., Wels, M., Okada, S., Wells, J. M., & Kleerebezem, M. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-123 · Cited by 67 · see citing works

Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis

Huard‐Chauveau, C., Miranda, G., Wessner, F., Bolotin, A., Hansen, J., Foster, S. J., & Chapot, M.-P. (2003) · Microbiology · doi:10.1099/mic.0.25875-0 · Cited by 66 · see citing works

d -Alanyl Ester Depletion of Teichoic Acids in Lactobacillus plantarum Results in a Major Modification of Lipoteichoic Acid Composition and Cell Wall Perforations at the Septum Mediated by the Acm2 Autolysin

Palumbo, E., Deghorain, M., Cocconcelli, P. S., Kleerebezem, M., Geyer, A., Härtung, T., Morath, S., & Pascal Hols, A. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.10.3709-3715.2006 · Cited by 64 · see citing works

Diversity of Firmicutes peptidoglycan hydrolases and specificities of those involved in daughter cell separation

Layec, S., Decaris, B., & Leblond‐Bourget, N. (2008) · Research in Microbiology · doi:10.1016/j.resmic.2008.06.008 · Cited by 64 · see citing works

Enhanced Mucosal Delivery of Antigen with Cell Wall Mutants of Lactic Acid Bacteria

Grangette, C., Müller‐Alouf, H., Pascal Hols, A., Goudercourt, D., Delcour, J., Turneer, M., & Mercenier, A. (2004) · Infection and Immunity · doi:10.1128/iai.72.5.2731-2737.2004 · Cited by 63 · see citing works

Identification of an essential gene responsible for d ‐Asp incorporation in the Lactococcus lactis peptidoglycan crossbridge

Veiga, P., Piquet, S., Maisons, A., Furlan, S., Courtin, P., Chapot, M.-P., & Kulakauskas, S. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05474.x · Cited by 62 · see citing works

Interactions of the cell-wall glycopolymers of lactic acid bacteria with their bacteriophages

Chapot, M.-P. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00236 · Cited by 60 · see citing works

Molecular Interaction between Lipoteichoic Acids and Lactobacillus delbrueckii Phages Depends on d -Alanyl and α-Glucose Substitution of Poly(Glycerophosphate) Backbones

Räisänen, L., Draing, C., Pfitzenmaier, M., Schubert, K., Jaakonsaari, T., von Aulock, S., Härtung, T., & Alatossava, T. (2007) · Journal of Bacteriology · doi:10.1128/jb.00078-07 · Cited by 59 · see citing works

Studies of the Genetics, Function, and Kinetic Mechanism of TagE, the Wall Teichoic Acid Glycosyltransferase in Bacillus subtilis 168

Allison, S. E., D’Elia, M. A., Arar, S. H., Monteiro, M. A., & Brown, E. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241265 · Cited by 59 · see citing works

Towards a nanoscale view of lactic acid bacteria

Tripathi, P., Beaussart, A., André, G., Rolain, T., Lebeer, S., Vanderleyden, J., Pascal Hols, A., & Dufrêne, Y. F. (2012) · Micron · doi:10.1016/j.micron.2012.01.001 · Cited by 57 · see citing works

Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1

Rolain, T., Bernard, E., Courtin, P., Bron, P. A., Kleerebezem, M., Chapot, M.-P., & Pascal Hols, A. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-137 · Cited by 54 · see citing works

Unraveling the Role of Surface Mucus-Binding Protein and Pili in Muco-Adhesion of Lactococcus lactis

Le, D. T. L., Tran, T.-L., Duviau, M.-P., Meyrand, M., Guérardel, Y., Castelain, M., Loubière, P., Chapot, M.-P., Dague, É., & Mercier‐Bonin, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079850 · Cited by 52 · see citing works

Identification and Characterization of a Novel Polysaccharide Deacetylase C (PdaC) from Bacillus subtilis

Kobayashi, K., Sudiarta, I. P., Kodama, T., Fukushima, T., Ara, K., Ozaki, K., & Sekiguchi, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329490 · Cited by 52 · see citing works

Analysis of the Peptidoglycan Hydrolase Complement of Lactobacillus casei and Characterization of the Major γ-D-Glutamyl-L-Lysyl-Endopeptidase

Regulski, K., Courtin, P., Meyrand, M., Claes, I. J. J., Lebeer, S., Vanderleyden, J., Pascal Hols, A., Guillot, A., & Chapot, M.-P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032301 · Cited by 52 · see citing works

Different subcellular locations of secretome components of Gram-positive bacteria

Buist, G., Ridder, A. N. J. A., Kok, J., & Kuipers, O. P. (2006) · Microbiology · doi:10.1099/mic.0.29113-0 · Cited by 51 · see citing works

Deciphering the Nanometer-Scale Organization and Assembly of Lactobacillus rhamnosus GG Pili Using Atomic Force Microscopy

Tripathi, P., Duprès, V., Beaussart, A., Lebeer, S., Claes, I. J. J., Vanderleyden, J., & Dufrêne, Y. F. (2011) · Langmuir · doi:10.1021/la203834d · Cited by 51 · see citing works

Murein and pseudomurein cell wall binding domains of bacteria and archaea—a comparative view

Visweswaran, G. R. R., Dijkstra, B. W., & Kok, J. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3637-0 · Cited by 51 · see citing works

Lectin Microarray Reveals Binding Profiles of Lactobacillus casei Strains in a Comprehensive Analysis of Bacterial Cell Wall Polysaccharides

Yasuda, E., Tateno, H., Hirabarashi, J., Iino, T., & Sako, T. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.00240-11 · Cited by 47 · see citing works

Structure of Polysaccharide-Peptidoglycan Complex from the Cell Wall of Lactobacillus casei YIT9018

Nagaoka, M., Muto, M., Nomoto, K., Matuzaki, T., Watanabe, T., & Yokokura, T. (1990) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a123243 · Cited by 47 · see citing works

The Response of Lactococcus lactis to Membrane Protein Production

Marreddy, R. K. R., Pinto, J. P. C., Wolters, J. C., Geertsma, E. R., Fusetti, F., Permentier, H. P., Kuipers, O. P., Kok, J., & Poolman, B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024060 · Cited by 46 · see citing works

AcmD, a Homolog of the Major Autolysin AcmA of Lactococcus lactis, Binds to the Cell Wall and Contributes to Cell Separation and Autolysis

Visweswaran, G. R. R., Steen, A., Leenhouts, K. J., Szeliga, M., Ruban, B., Hesseling‐Meinders, A., Dijkstra, B. W., Kuipers, O. P., Kok, J., & Buist, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072167 · Cited by 45 · see citing works

Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis : Identification of a Third N- Acetylglucosaminidase, AcmC

Huard‐Chauveau, C., Miranda, G., Redko, Y., Wessner, F., Foster, S. J., & Chapot‐Chartier, M. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.6.3493-3499.2004 · Cited by 43 · see citing works

Functionality of Sortase A in Lactococcus lactis

Dièye, Y., Oxaran, V., Ledue, F., Alkhalaf, W., Buist, G., Juillard, V., Lee, C. W., & Piard, J.-C. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00928-10 · Cited by 43 · see citing works

The Major Autolysin Acm2 from Lactobacillus plantarum Undergoes Cytoplasmic O-Glycosylation

Fredriksen, L., Mathiesen, G., Moen, A. R., Bron, P. A., Kleerebezem, M., Eijsink, V. G. H., & Egge-Jacobsen, W. M. (2011) · Journal of Bacteriology · doi:10.1128/jb.06314-11 · Cited by 42 · see citing works

Coordinate regulation of Gram-positive cell surface components

Hanson, B. R., & Neely, M. N. (2012) · Current Opinion in Microbiology · doi:10.1016/j.mib.2011.12.011 · Cited by 41 · see citing works

The extracellular phage-host interactions involved in the bacteriophage LL-H infection of Lactobacillus delbrueckii ssp. lactis ATCC 15808

Munsch-Alatossava, P., & Alatossava, T. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00408 · Cited by 39 · see citing works

Identification of the Amidotransferase AsnB1 as Being Responsible for meso -Diaminopimelic Acid Amidation in Lactobacillus plantarum Peptidoglycan

Bernard, E., Rolain, T., Courtin, P., Pascal Hols, A., & Chapot‐Chartier, M. (2011) · Journal of Bacteriology · doi:10.1128/jb.05060-11 · Cited by 39 · see citing works

Identification of the Asparagine Synthase Responsible for d -Asp Amidation in the Lactococcus lactis Peptidoglycan Interpeptide Crossbridge

Veiga, P., Erkelenz, M., Bernard, E., Courtin, P., Kulakauskas, S., & Chapot, M.-P. (2009) · Journal of Bacteriology · doi:10.1128/jb.00126-09 · Cited by 38 · see citing works

Variations in the Degree of d -Alanylation of Teichoic Acids in Lactococcus lactis Alter Resistance to Cationic Antimicrobials but Have No Effect on Bacterial Surface Hydrophobicity and Charge

Giaouris, E. D., Briandet, R., Meyrand, M., Courtin, P., & Chapot, M.-P. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.00078-08 · Cited by 37 · see citing works

O-Glycosylation as a Novel Control Mechanism of Peptidoglycan Hydrolase Activity

Rolain, T., Bernard, E., Beaussart, A., Degand, H., Courtin, P., Egge-Jacobsen, W. M., Bron, P. A., Morsomme, P., Kleerebezem, M., Chapot, M.-P., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470716 · Cited by 37 · see citing works

Selectivity for d -Lactate Incorporation into the Peptidoglycan Precursors of Lactobacillus plantarum : Role of Aad, a VanX-Like d -Alanyl- d -Alanine Dipeptidase

Deghorain, M., Goffin, P., Fontaine, L., Mainardi, J., Daniel, R. A., Errington, J., Hallet, B., & Pascal Hols, A. (2007) · Journal of Bacteriology · doi:10.1128/jb.01829-06 · Cited by 36 · see citing works

The CHAP domain of Cse functions as an endopeptidase that acts at mature septa to promote Streptococcus thermophilus cell separation

Layec, S., Gérard, J., Legué, V., Chapot, M.-P., Courtin, P., Borges, F., Decaris, B., & Leblond‐Bourget, N. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06595.x · Cited by 36 · see citing works

Assay for peptidoglycan O-acetyltransferase: A potential new antibacterial target

Moynihan, P. J., & Clarke, A. J. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.04.022 · Cited by 35 · see citing works

Structural studies of the cell wall polysaccharides from three strains of Lactobacillus helveticus with different autolytic properties: DPC4571, BROI, and LH1

VINOGRADOV, E. V., Valence, F., Maes, E., Jebavá, I., Chuat, V., Lortal, S., Grard, T., Guérardel, Y., & Sadovskaya, I. (2013) · Carbohydrate Research · doi:10.1016/j.carres.2013.05.020 · Cited by 33 · see citing works

Influence of Lipoteichoic Acid d -Alanylation on Protein Secretion in Lactococcus lactis as Revealed by Random Mutagenesis

Nouaille, S., Commissaire, J., Gratadoux, J., Ravn, P., Bolotin, A., Gruss, A., Loir, Y. L., & Langella, P. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.3.1600-1607.2004 · Cited by 33 · see citing works

Comparison of Components and Synthesis Genes of Cell Wall Teichoic Acid amongLactobacillus plantarumStrains

Tomita, S., Irisawa, T., Tanaka, N., Nukada, T., Satoh, E., Uchimura, T., & Okada, S. (2010) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.90736 · Cited by 30 · see citing works

Effects of a muramidase on a mixed bacterial community

Mercier, C., Domakova, E., Tremblay, J., & Kulakauskas, S. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb09135.x · Cited by 28 · see citing works

A Novel Type of Peptidoglycan-binding Domain Highly Specific for Amidated d-Asp Cross-bridge, Identified in Lactobacillus casei Bacteriophage Endolysins

Regulski, K., Courtin, P., Kulakauskas, S., & Chapot‐Chartier, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.446344 · Cited by 28 · see citing works

Efficient Overproduction of Membrane Proteins in Lactococcus lactis Requires the Cell Envelope Stress Sensor/Regulator Couple CesSR

Pinto, J. P. C., Kuipers, O. P., Marreddy, R. K. R., Poolman, B., & Kok, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021873 · Cited by 27 · see citing works

Dual Role for the O-Acetyltransferase OatA in Peptidoglycan Modification and Control of Cell Septation in Lactobacillus plantarum

Bernard, E., Rolain, T., David, B., André, G., Duprès, V., Dufrêne, Y. F., Hallet, B., Chapot, M.-P., & Pascal Hols, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047893 · Cited by 26 · see citing works

Impact of peptidoglycan O‐acetylation on autolytic activities of the Enterococcus faecalis N‐acetylglucosaminidase AtlA and N‐acetylmuramidase AtlB

Emirian, A., Fromentin, S., Eckert, C., Chau, F., Dubost, L., Delepierre, M., Gutmann, L., Arthur, M., & Mesnage, S. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.08.010 · Cited by 22 · see citing works

Reduced Lysis upon Growth of Lactococcus lactis on Galactose Is a Consequence of Decreased Binding of the Autolysin AcmA

Steen, A., Buist, G., Kramer, N. E., Jalving, R., Benus, G. F. J. D., Venema, G., Kuipers, O. P., & Kok, J. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.00103-08 · Cited by 21 · see citing works

Binding Mechanism of the Peptidoglycan Hydrolase Acm2: Low Affinity, Broad Specificity

Beaussart, A., Rolain, T., Duchêne, M.-C., El‐Kirat‐Chatel, S., André, G., Pascal Hols, A., & Dufrêne, Y. F. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.06.035 · Cited by 19 · see citing works

GtfA and GtfB Are Both Required for Protein O -Glycosylation in Lactobacillus plantarum

Lee, I.-C., van Swam, I. I., Tomita, S., Morsomme, P., Rolain, T., Pascal Hols, A., Kleerebezem, M., & Bron, P. A. (2014) · Journal of Bacteriology · doi:10.1128/jb.01401-13 · Cited by 19 · see citing works

Lactococcus lactis Gene yjgB Encodes a γ- d -Glutaminyl- l -Lysyl- Endopeptidase Which Hydrolyzes Peptidoglycan

Redko, Y., Courtin, P., Mézange, C., Huard‐Chauveau, C., & Chapot, M.-P. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.00705-07 · Cited by 18 · see citing works

Functional and Morphological Adaptation to Peptidoglycan Precursor Alteration in Lactococcus lactis

Deghorain, M., Fontaine, L., David, B., Mainardi, J., Courtin, P., Daniel, R. A., Errington, J., Sorokin, A., Bolotin, A., Chapot‐Chartier, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143636 · Cited by 15 · see citing works

The nine peptidoglycan hydrolases genes in Lactobacillus helveticus are ubiquitous and early transcribed

Jebavá, I., Plocková, M., Lortal, S., & Valence, F. (2011) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2011.04.015 · Cited by 12 · see citing works

The structure of an alternative wall teichoic acid produced by a Lactobacillus plantarum WCFS1 mutant contains a 1,5-linked poly(ribitol phosphate) backbone with 2-α-d-glucosyl substitutions

Tomita, S., de Waard, P., Bakx, E. J., Schols, H. A., Kleerebezem, M., & Bron, P. A. (2013) · Carbohydrate Research · doi:10.1016/j.carres.2013.01.018 · Cited by 12 · see citing works

Role of PBPs in the ovoid Lactococcus lactis cell cycle

David, B. (2013) · DIAL (Catholic University of Leuven) · Cited by 1 · see citing works

Stress Physiology of Lactic Acid Bacteria.

Papadimitriou, K., Alegría, Á., Bron, P. A., de Angelis, M., Gobbetti, M., Kleerebezem, M., Lemos, J. A., Linares, D. M., Ross, P., Stanton, C., et al. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00076-15 · Cited by 914 · see citing works

Postbiotics-Parabiotics: The New Horizons in Microbial Biotherapy and Functional Foods

Nataraj, B. H., Ali, S. A., Behare, P. V., & Yadav, H. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01426-w · Cited by 737 · see citing works

Vaginal microbiota and the potential of Lactobacillus derivatives in maintaining vaginal health

Chee, W. J. Y., Chew, S. Y., & Than, L. T. L. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01464-4 · Cited by 709 · see citing works

Microbial synthesis of zinc oxide nanoparticles and their potential application as an antimicrobial agent and a feed supplement in animal industry: a review

Yusof, H. M., Mohamad, R., Zaidan, U. H., & Rahman, N. A. A. (2019) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-019-0368-z · Cited by 647 · see citing works

Living together in biofilms: the microbial cell factory and its biotechnological implications

Berlanga, M., & Guerrero, R. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0569-5 · Cited by 323 · see citing works

Lactic acid bacteria as antifungal and anti-mycotoxigenic agents: A comprehensive review

Sadiq, F. A., Yan, B., Tian, F., Zhao, J., Zhang, H., & Chen, W. (2019) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12481 · Cited by 313 · see citing works

Green Synthesis: An Eco-friendly Route for the Synthesis of Iron Oxide Nanoparticles

Priya, Naveen, Kaur, K., & Sidhu, A. K. (2021) · Frontiers in Nanotechnology · doi:10.3389/fnano.2021.655062 · Cited by 291 · see citing works

The Evolving Facets of Bacterial Vaginosis: Implications for HIV Transmission

McKinnon, L. R., Achilles, S. L., Bradshaw, C. S., Burgener, A., Crucitti, T., Fredricks, D. N., Jaspan, H. B., Kaul, R., Kaushic, C., Klatt, N. R., et al. (2019) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2018.0304 · Cited by 273 · see citing works

Biosynthesis of zinc oxide nanoparticles by cell-biomass and supernatant of Lactobacillus plantarum TA4 and its antibacterial and biocompatibility properties

Yusof, H. M., Rahman, N. A., Mohamad, R., Zaidan, U. H., & Samsudin, A. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-76402-w · Cited by 229 · see citing works

Bacterial Glycobiology: Rhamnose-Containing Cell Wall Polysaccharides in Gram-Positive Bacteria

Mistou, M.-Y., Sutcliffe, I. C., & van Sorge, N. M. (2016) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuw006 · Cited by 215 · see citing works

Lactic Acid Bacteria Exopolysaccharides Producers: A Sustainable Tool for Functional Foods

Prete, R., Alam, M. K., Perpetuini, G., Perla, C., Pittia, P., & Corsetti, A. (2021) · Foods · doi:10.3390/foods10071653 · Cited by 194 · see citing works

The Surface-Associated Exopolysaccharide of Bifidobacterium longum 35624 Plays an Essential Role in Dampening Host Proinflammatory Responses and Repressing Local T H 17 Responses

Schiavi, E., Gleinser, M., Molloy, E. M., Groeger, D., Frei, R., Ferstl, R., Rodríguez‐Pérez, N., Ziegler, M., Grant, R., Moriarty, T. F., et al. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.02238-16 · Cited by 173 · see citing works

Biological Detoxification of Mycotoxins: Current Status and Future Advances

Liu, L., Xie, M., & Wei, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031064 · Cited by 162 · see citing works

Review on the Biological Detoxification of Mycotoxins Using Lactic Acid Bacteria to Enhance the Sustainability of Foods Supply

Muhialdin, B. J., Saari, N., & Hussin, A. S. M. (2020) · Molecules · doi:10.3390/molecules25112655 · Cited by 166 · see citing works

Bacteriocins as antimicrobial and preservative agents in food: Biosynthesis, separation and application

Verma, D. K., Thakur, M., Sıngh, S., Tripathy, S., Gupta, A. K., Baranwal, D., Patel, A. R., Shah, N., Utama, G. L., Niamah, A. K., et al. (2022) · Food Bioscience · doi:10.1016/j.fbio.2022.101594 · Cited by 150 · see citing works

The art of strain improvement of industrial lactic acid bacteria without the use of recombinant DNA technology

Derkx, P. M. F., Janzen, T., Sørensen, K. I., Christensen, J. E., Stuer‐Lauridsen, B., & Johansen, E. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-s1-s5 · Cited by 147 · see citing works

Sustainable microbial cell nanofactory for zinc oxide nanoparticles production by zinc-tolerant probiotic Lactobacillus plantarum strain TA4

Yusof, H. M., Mohamad, R., Zaidan, U. H., & Rahman, N. A. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-1279-6 · Cited by 139 · see citing works

Mussel-inspired hydrogel tissue adhesives for wound closure

Rahimnejad, M., & Zhong, W. (2017) · RSC Adv. · doi:10.1039/c7ra06743g · Cited by 135 · see citing works

Exopolysaccharides of Lactobacillus reuteri: Their Influence on Adherence of E. Coli to Epithelial Cells and Inflammatory Response

Kšonžeková, P., Bystrický, P., Vlčková, S., Pätoprstý, V., Pulzová, L., Mudroňová, D., Kubašková, T., Csank, T., & Tkáčiková, Ľ. (2016) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2015.12.037 · Cited by 122 · see citing works

Designing a novel multi-epitope vaccine to evoke a robust immune response against pathogenic multidrug-resistant Enterococcus faecium bacterium

Dey, J., Mahapatra, S. R., Raj, T. K., Kaur, T., Jain, P., Tiwari, A., Patro, S., Misra, N., & Suar, M. (2022) · Gut Pathogens · doi:10.1186/s13099-022-00495-z · Cited by 120 · see citing works

Antibacterial activities of anthraquinones: structure–activity relationships and action mechanisms

Tang, Q., Zhou, T., Hao, J., Wang, C., Zhang, K., Xu, J., Wang, X., & Zhou, W. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00116d · Cited by 119 · see citing works

Lactic acid bacteria in dairy food: Surface characterization and interactions with food matrix components

Burgain, J., Scher, J., Francius, G., Borges, F., Corgneau, M., Revol‐Junelles, A., Cailliez‐Grimal, C., & Gaïani, C. (2014) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2014.09.005 · Cited by 120 · see citing works

Molecular and Cellular Mechanisms Influenced by Postbiotics

Jastrząb, R., Graczyk, D., & Siedlecki, P. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413475 · Cited by 121 · see citing works

Microbe-mediated intestinal NOD2 stimulation improves linear growth of undernourished infant mice

Schwarzer, M., Gautam, U. K., Makki, K., Lambert, A., Brabec, T., Joly, A., Šrůtková, D., Poinsot, P., Novotná, T., Geoffroy, S., et al. (2023) · Science · doi:10.1126/science.ade9767 · Cited by 117 · see citing works

Metabolic engineering of Corynebacterium glutamicum for enhanced production of 5-aminovaleric acid

Shin, J. H., Park, S. H., Oh, Y. H., Choi, J. W., Lee, M. H., Cho, J. S., Joo, J. C., Joo, J. C., Yu, J., Park, S. J., et al. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0566-8 · Cited by 113 · see citing works

Metabolomics reveals impact of seven functional foods on metabolic pathways in a gut microbiota model

Farag, M. A., Abdelwareth, A., Sallam, I. E., Shorbagi, M., Jehmlich, N., Fritz‐Wallace, K., Schäpe, S. S., Rolle-Kampczyk, U. E., Ehrlich, A., Wessjohann, L. A., et al. (2020) · Journal of Advanced Research · doi:10.1016/j.jare.2020.01.001 · Cited by 112 · see citing works

Insight into the ecology of vaginal bacteria through integrative analyses of metagenomic and metatranscriptomic data

France, M., Fu, L., Rutt, L., Yang, H., Humphrys, M. S., Narina, S., Gajer, P., Ma, B., Forney, L. J., & Ravel, J. (2022) · Genome biology · doi:10.1186/s13059-022-02635-9 · Cited by 102 · see citing works

Aflatoxins biodetoxification strategies based on probiotic bacteria

Afshar, P., Shokrzadeh, M., Raeisi, S. N., Ghorbani‐HasanSaraei, A., & Nasiraie, L. R. (2020) · Toxicon · doi:10.1016/j.toxicon.2020.02.007 · Cited by 105 · see citing works

Cell wall homeostasis in lactic acid bacteria: threats and defences

Martı́nez, B., Rodrı́guez, A., Kulakauskas, S., & Chapot, M.-P. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa021 · Cited by 104 · see citing works

A visual review of the human pathogen Streptococcus pneumoniae

Engholm, D. H., Kilian, M., Goodsell, D. S., Andersen, E. S., & Kjærgaard, R. S. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux037 · Cited by 101 · see citing works

Microbial cells as colloidal particles: Pickering oil-in-water emulsions stabilized by bacteria and yeast

Firoozmand, H., & Rousseau, D. (2015) · Food Research International · doi:10.1016/j.foodres.2015.10.018 · Cited by 97 · see citing works

Unraveling the selective antibacterial activity and chemical composition of citrus essential oils

Ambrosio, C. M. S., Ikeda, N. Y., Miano, A. C., Saldaña, E., Moreno, A. M., Stashenko, E. E., Contreras-Castillo, C. J., & da Glória, E. M. (2019) · Scientific Reports · doi:10.1038/s41598-019-54084-3 · Cited by 94 · see citing works

Gut health benefit and application of postbiotics in animal production

Zhong, Y., Wang, S., Di, H., Deng, Z., Liu, J., & Wang, H. (2022) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-022-00688-1 · Cited by 93 · see citing works

Cutting Edge: Probiotics and Fecal Microbiota Transplantation in Immunomodulation

Zeng, W., Shen, J., Bo, T., Peng, L., Xu, H., Nasser, M. I., Zhuang, Q., & Zhao, M. (2019) · Journal of Immunology Research · doi:10.1155/2019/1603758 · Cited by 89 · see citing works

The Chemical Composition and Antibacterial and Antioxidant Activities of Five Citrus Essential Oils

Li, Y., Liu, S., Zhao, C., Zhang, Z., Nie, D., Tang, W., & Li, Y. (2022) · Molecules · doi:10.3390/molecules27207044 · Cited by 89 · see citing works

Microbial Mediated Synthesis of Silver Nanoparticles by Lactobacillus Plantarum TA4 and its Antibacterial and Antioxidant Activity

Yusof, H. M., Rahman, N. A., Mohamad, R., & Zaidan, U. H. (2020) · Applied Sciences · doi:10.3390/app10196973 · Cited by 86 · see citing works

The potential of lactic acid bacteria to colonize biotic and abiotic surfaces and the investigation of their interactions and mechanisms

Arena, M. P., Capozzi, V., Spano, G., & Fiocco, D. (2017) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-017-8182-z · Cited by 86 · see citing works

Mechanism study of intracellular zinc oxide nanocomposites formation

Król, A., Railean‐Plugaru, V., Pomastowski, P., Złoch, M., & Buszewski, B. (2018) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2018.05.069 · Cited by 85 · see citing works

Microbiology neutralization of zearalenone using Lactococcus lactis and Bifidobacterium sp.

Król, A. I., Pomastowski, P., Rafińska, K., Railean‐Plugaru, V., Walczak‐Skierska, J., & Buszewski, B. (2017) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-017-0555-8 · Cited by 83 · see citing works

Journey of the Probiotic Bacteria: Survival of the Fittest

Mendonça, A. A., Pinto-Neto, W. D. P., da Paixão, G. A., Santos, D. D. S., De Morais, M. A., & De Souza, R. B. (2022) · Microorganisms · doi:10.3390/microorganisms11010095 · Cited by 82 · see citing works

Another Brick in the Wall: a Rhamnan Polysaccharide Trapped inside Peptidoglycan of Lactococcus lactis

Sadovskaya, I., VINOGRADOV, E. V., Courtin, P., Armalytė, J., Meyrand, M., Giaouris, E. D., Palussière, S., Furlan, S., Péchoux, C., Ainsworth, S., et al. (2017) · mBio · doi:10.1128/mbio.01303-17 · Cited by 82 · see citing works

Antibacterial magnetic nanoparticles for therapeutics: a review

Allafchian, A., & Hosseini, S. S. (2019) · IET Nanobiotechnology · doi:10.1049/iet-nbt.2019.0146 · Cited by 81 · see citing works

How fermentation by lactic acid bacteria can address safety issues in legumes food products?

Licandro, H., Ho, P. H., Nguyen, T. K. C., Petchkongkaew, A., Nguyen, H. V., Chu‐Ky, S., Nguyen, T. V. A., Lorn, D., & Waché, Y. (2019) · Food Control · doi:10.1016/j.foodcont.2019.106957 · Cited by 81 · see citing works

In vitro and in vivo probiotic assessment of Leuconostoc mesenteroides P45 isolated from pulque, a Mexican traditional alcoholic beverage

Gilés-Gómez, M., García, J. G. S., Matus, V., Quintana, I. C., Bolívar, F. G., & Escalante, A. (2016) · SpringerPlus · doi:10.1186/s40064-016-2370-7 · Cited by 79 · see citing works

Adhesion Properties of Lactobacillus plantarum Dad-13 and Lactobacillus plantarum Mut-7 on Sprague Dawley Rat Intestine

Darmastuti, A., Hasan, P. N., Wikandari, R., Utami, T., Rahayu, E. S., & Suroto, D. A. (2021) · Microorganisms · doi:10.3390/microorganisms9112336 · Cited by 78 · see citing works

Co-evolution of strain design methods based on flux balance and elementary mode analysis

Machado, D., & Herrgård, M. J. (2015) · Metabolic Engineering Communications · doi:10.1016/j.meteno.2015.04.001 · Cited by 74 · see citing works

Endoplasmic reticulum-derived reactive oxygen species (ROS) is involved in toxicity of cell wall stress to Candida albicans

Yu, Q., Zhang, B., Lǐ, J., Zhang, B., Wang, H., & Li, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.014 · Cited by 74 · see citing works

Using probiotics for mitigation of acrylamide in food products: a mini review

Khorshidian, N., Yousefi, M., Shadnoush, M., Siadat, S. D., Mohammadi, M., & Mortazavian, A. M. (2020) · Current Opinion in Food Science · doi:10.1016/j.cofs.2020.01.011 · Cited by 73 · see citing works

Korean kimchi-derived lactic acid bacteria inhibit foodborne pathogenic biofilm growth on seafood and food processing surface materials

Toushik, S. H., Kim, K., Ashrafudoulla, M., Mizan, M. F. R., Roy, P. K., Nahar, S., Kim, Y., & Ha, S. (2021) · Food Control · doi:10.1016/j.foodcont.2021.108276 · Cited by 71 · see citing works

Inflammatory and antimicrobial properties differ between vaginal Lactobacillus isolates from South African women with non-optimal versus optimal microbiota

Manhanzva, M. T., Abrahams, A. G., Gamieldien, H., Froissart, R., Jaspan, H. B., Jaumdally, S. Z., Barnabas, S. L., Dabee, S., Bekker, L., Gray, G., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-62184-8 · Cited by 70 · see citing works

Cwp19 Is a Novel Lytic Transglycosylase Involved in Stationary-Phase Autolysis Resulting in Toxin Release in Clostridium difficile

Wydau-Dematteis, S., Meouche, I. E., Courtin, P., Hamiot, A., Lai–Kuen, R., Saubaméa, B., Fenaille, F., Butel, M., Pons, J.-L., Dupuy, B., et al. (2018) · mBio · doi:10.1128/mbio.00648-18 · Cited by 71 · see citing works

The Evolution of gene regulation research in Lactococcus lactis

Kok, J., van Gijtenbeek, L. A., de Jong, A., van der Meulen, S. B., Solopova, A., & Kuipers, O. P. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux028 · Cited by 69 · see citing works

Invited Review: Starter Lactic Acid Bacteria Survival in Cheese: New Perspectives on Cheese Microbiology

Wilkinson, M. G., & LaPointe, G. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-18960 · Cited by 68 · see citing works

Ultrafast physical bacterial inactivation and photocatalytic self-cleaning of ZnO nanoarrays for rapid and sustainable bactericidal applications

Xie, Y., Qu, X., Li, J., Li, D., Wei, W., Hui, D., Zhang, Q., Meng, F., Yin, H. F., Xu, X., et al. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.139714 · Cited by 67 · see citing works

Novel approach for biosynthesizing of zinc oxide nanoparticles using Lactobacillus gasseri and their influence on microbiological, chemical, sensory properties of integrated yogurt

El-Sayed, H. S., El-Sayed, S. M., & Youssef, A. M. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130513 · Cited by 66 · see citing works

Immunomodulation of dendritic cells byLactobacillus reuterisurface components and metabolites

Engevik, M. A., Ruan, W. H., Esparza, M., Fultz, R., Shi, Z., Engevik, K. A., Engevik, A. C., Ihekweazu, F. D., Visuthranukul, C., Venable, S. F., et al. (2021) · Physiological Reports · doi:10.14814/phy2.14719 · Cited by 65 · see citing works

Recent developments in applications of lactic acid bacteria against mycotoxin production and fungal contamination

Bangar, S. P., Sharma, N., Kumar, M., Özoğul, F., Purewal, S. S., & Trif, M. (2021) · Food Bioscience · doi:10.1016/j.fbio.2021.101444 · Cited by 61 · see citing works

Antimicrobial and inflammatory properties of South African clinical Lactobacillus isolates and vaginal probiotics

Chetwin, E., Manhanzva, M. T., Abrahams, A. G., Froissart, R., Gamieldien, H., Jaspan, H. B., Jaumdally, S. Z., Barnabas, S. L., Dabee, S., Happel, A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-38253-4 · Cited by 60 · see citing works

Effects of ε-Poly-l-lysine on the cell wall of Saccharomyces cerevisiae and its involved antimicrobial mechanism

Tan, Z., Bo, T., Guo, F., Cui, J., & Jia, S. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.07.094 · Cited by 59 · see citing works

Overview of the rules of the microbial engagement in the gut microbiome: a step towards microbiome therapeutics

Yadav, M., & Chauhan, N. S. (2020) · Journal of Applied Microbiology · doi:10.1111/jam.14883 · Cited by 59 · see citing works

Label-Free Quantitative Proteomics Reveals the Multitargeted Antibacterial Mechanisms of Lactobionic Acid against Methicillin-Resistant Staphylococcus aureus (MRSA) using SWATH-MS Technology

Kang, S., Kong, F., Liang, X., Li, M., Yang, N., Cao, X., Yang, M., Tao, D., Yue, X., & Zheng, Y. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b06364 · Cited by 58 · see citing works

Heavy metals remediation through lactic acid bacteria: Current status and future prospects

Ma, X. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.174455 · Cited by 57 · see citing works

Potential anti-carcinogenic effect of probiotic and lactic acid bacteria in detoxification of benzo[a]pyrene: A review

Shoukat, S. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.02.029 · Cited by 57 · see citing works

Biomolecule-corona formation confers resistance of bacteria to nanoparticle-induced killing: Implications for the design of improved nanoantibiotics

Siemer, S., Westmeier, D., Barz, M., Eckrich, J., Gül, D., Seckert, C. K., Thyssen, C., Schilling, O., Hasenberg, M., Pang, C., et al. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.11.028 · Cited by 56 · see citing works

The role of beneficial bacteria wall elasticity in regulating innate immune response

Mokrozub, V. V., Lazarenko, L. M., Sichel, L. M., Babenko, L. P., Lytvyn, P. M., Demchenko, O. M., Melnichenko, Y. O., Boyko, N., Biavati, B., Gioia, D. D., et al. (2015) · The EPMA Journal · doi:10.1186/s13167-015-0035-1 · Cited by 56 · see citing works

Purification and primary characterization of a novel bacteriocin, LiN333, from Lactobacillus casei, an isolate from a Chinese fermented food

Ullah, N., Wang, X., Wu, J. C., Guo, Y. Q., Ge, H., Li, T., Khan, S., Li, Z., & Feng, X. (2017) · LWT · doi:10.1016/j.lwt.2017.04.056 · Cited by 54 · see citing works

Lactobacillus cell envelope-coated nanoparticles for antibiotic delivery against cariogenic biofilm and dental caries

Weng, L.-T., Wu, L., Guo, R., Ye, J., Wen, L., Wu, W., Chen, L., & Yang, D. (2022) · Journal of Nanobiotechnology · doi:10.1186/s12951-022-01563-x · Cited by 52 · see citing works

Structural studies of the rhamnose-rich cell wall polysaccharide of Lactobacillus casei BL23

VINOGRADOV, E. V., Sadovskaya, I., Grard, T., & Chapot, M.-P. (2016) · Carbohydrate Research · doi:10.1016/j.carres.2016.10.002 · Cited by 52 · see citing works

Astaxanthin from Jerusalem artichoke: Production by fed-batch fermentation using Phaffia rhodozyma and application in cosmetics

Jiang, G.-L., Zhou, L., Wang, Y.-T., & Zhu, M. (2017) · Process Biochemistry · doi:10.1016/j.procbio.2017.08.013 · Cited by 49 · see citing works

An Exopolysaccharide Produced by Bifidobacterium longum 35624® Inhibits Osteoclast Formation via a TLR2-Dependent Mechanism

Wallimann, A., Hildebrand, M., Groeger, D., Stanić, B., Akdiş, C. A., Zeiter, S., Richards, R. G., Moriarty, T. F., O’Mahony, L., & Thompson, K. (2021) · Calcified Tissue International · doi:10.1007/s00223-020-00790-4 · Cited by 48 · see citing works

Recent advances in the application of biofilm in bioremediation of industrial wastewater and organic pollutants

Maurya, A., & Raj, A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819001-2.00005-x · Cited by 49 · see citing works

Potential of Prebiotic D-Tagatose for Prevention of Oral Disease

Mayumi, S., Kuboniwa, M., Sakanaka, A., Hashino, E., Ishikawa, A., Ijima, Y., & Amano, A. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.767944 · Cited by 47 · see citing works

Co-encapsulation: An effective strategy to enhance the synergistic effects of probiotics and polyphenols

Ma, M., Liu, Y., Chen, Y., Zhang, S., & Yuan, Y. (2025) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.104927 · Cited by 46 · see citing works

Host recognition by lactic acid bacterial phages

Mahony, J., Cambillau, C., & van Sinderen, D. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux019 · Cited by 46 · see citing works

Use of Lactobacillus paracasei strain for zearalenone binding and metabolization

Złoch, M., Rogowska, A., Pomastowski, P., Railean‐Plugaru, V., Walczak‐Skierska, J., Rudnicka, J., & Buszewski, B. (2020) · Toxicon · doi:10.1016/j.toxicon.2020.03.011 · Cited by 45 · see citing works

Microbial function and genital inflammation in young South African women at high risk of HIV infection

Alisoltani, A., Manhanzva, M. T., Potgieter, M. G., Balle, C., Bell, L., Ross, E. J., Iranzadeh, A., du Plessis, M., Radzey, N., McDonald, Z., et al. (2020) · Microbiome · doi:10.1186/s40168-020-00932-8 · Cited by 45 · see citing works

Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display

Desvaux, M., Candela, T., & Serror, P. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00100 · Cited by 44 · see citing works

From Waste to Taste—Efficient Production of the Butter Aroma Compound Acetoin from Low-Value Dairy Side Streams Using a Natural (Nonengineered) Lactococcus lactis Dairy Isolate

Liu, J., Chen, L., Dorau, R., Lillevang, S. K., Jensen, P. R., & Solem, C. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c00882 · Cited by 44 · see citing works

Surface Proteins of Lactococcus lactis: Bacterial Resources for Muco-adhesion in the Gastrointestinal Tract

Mercier‐Bonin, M., & Chapot, M.-P. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02247 · Cited by 43 · see citing works

Cell Wall Glycans Mediate Recognition of the Dairy Bacterium Streptococcus thermophilus by Bacteriophages

Szymczak, P., Filipe, S. R., Covas, G., Vogensen, F. K., Neves, A. R., & Janzen, T. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.01847-18 · Cited by 43 · see citing works

Cytotoxicity Analysis of Biosynthesized Selenium Nanoparticles Towards A549 Lung Cancer Cell Line

Menon, S. V., & Shanmugam, V. (2019) · Journal of Inorganic and Organometallic Polymers and Materials · doi:10.1007/s10904-019-01409-4 · Cited by 43 · see citing works

Group A, B, C, and G Streptococcus Lancefield antigen biosynthesis is initiated by a conserved α-d-GlcNAc-β-1,4-l-rhamnosyltransferase

Zorzoli, A., Meyer, B. H., Adair, E., Torgov, V. I., Veselovsky, V. V., Danilov, L. L., Uhrı́n, D., & Dorfmueller, H. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009894 · Cited by 42 · see citing works

DNA extraction method influences human milk bacterial profiles

Cheema, A. S., Stinson, L. F., Lai, C. T., Geddes, D. T., & Payne, M. (2020) · Journal of Applied Microbiology · doi:10.1111/jam.14780 · Cited by 41 · see citing works

LytR-CpsA-Psr Glycopolymer Transferases: Essential Bricks in Gram-Positive Bacterial Cell Wall Assembly

Stefanović, C., Hager‐Mair, F. F., & Schäffer, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020908 · Cited by 41 · see citing works

A systematic review to introduce the most effective postbiotics derived from probiotics for aflatoxin detoxification in vitro

Zamanpour, S., Noori, S. M. A., Yancheshmeh, B. S., Afshari, A., & Hashemi, M. B. (2023) · Italian Journal of Food Science · doi:10.15586/ijfs.v35i4.2369 · Cited by 39 · see citing works

Genetic determinants of lactococcal C2viruses for host infection and their role in phage evolution

Millen, A. M., & Romero, D. A. (2016) · Journal of General Virology · doi:10.1099/jgv.0.000499 · Cited by 38 · see citing works

A dual-chain assembly pathway generates the high structural diversity of cell-wall polysaccharides in Lactococcus lactis

Theodorou, I., Courtin, P., Palussière, S., Kulakauskas, S., Bidnenko, E., Péchoux, C., Fenaille, F., Penno, C., Mahony, J., van Sinderen, D., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009957 · Cited by 38 · see citing works

Sugarcoating it: Enterococcal polysaccharides as key modulators of host–pathogen interactions

Ramos, Y., Sansone, S., & Morales, D. K. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009822 · Cited by 35 · see citing works

Genome Editing of Food-Grade Lactobacilli To Develop Therapeutic Probiotics

van Pijkeren, J., & Barrangou, R. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.bad-0013-2016 · Cited by 37 · see citing works

Screening and Growth Characterization of Non-conventional Yeasts in a Hemicellulosic Hydrolysate

de Oliveira, P. M., Aborneva, D., Bonturi, N., & Lahtvee, P. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.659472 · Cited by 37 · see citing works

Peptidoglycan-based immunomodulation

Sun, Q., Liu, X., & Li, X. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11795-4 · Cited by 36 · see citing works

The molecular architecture of Lactobacillus S-layer: Assembly and attachment to teichoic acids

Sagmeister, T., Gubensäk, N., Buhlheller, C., Grininger, C., Eder, M., Đordić, A., Millán, C., Medina, A., Sánchez‐Murcia, P. A., Berni, F., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2401686121 · Cited by 38 · see citing works

Effect of paraprobiotic prepared from Kimchi-derived Lactobacillus plantarum K8 on skin moisturizing activity in human keratinocyte

Kim, H., Jeon, B., Kim, W. J., & Chung, D. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.104244 · Cited by 34 · see citing works

Enterococcus faecalis: implications for host health

Boeder, A. M., Spiller, F., Carlström, M., & Izídio, G. S. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-04007-w · Cited by 35 · see citing works

Plant lectins: A new antimicrobial frontier

Konozy, E. H. E., Osman, M. E. M., Dirar, A. I., & Ghartey‐Kwansah, G. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113735 · Cited by 34 · see citing works

A novel in vitro co-culture model comprised of Caco-2/RBL-2H3 cells to evaluate anti-allergic effects of food factors through the intestine

Yamashita, S., Yokoyama, Y., Hashimoto, T., & Mizuno, M. (2016) · Journal of Immunological Methods · doi:10.1016/j.jim.2016.04.011 · Cited by 32 · see citing works

Transcriptional Regulator AcrR Increases Ethanol Tolerance through Regulation of Fatty Acid Synthesis in Lactobacillus plantarum

Yang, X., Teng, K., Li, L., Su, R., Zhang, J., Ai, G., & Zhong, J. (2019) · Applied and Environmental Microbiology · doi:10.1128/aem.01690-19 · Cited by 31 · see citing works

Differential Immunostimulatory Effects of Lipoteichoic Acids Isolated from Four Strains of Lactiplantibacillus plantarum

Jung, B.-J., Kim, H., & Chung, D. (2022) · Applied Sciences · doi:10.3390/app12030954 · Cited by 31 · see citing works

Promoting acid resistance and nisin yield of Lactococcus lactis F44 by genetically increasing D-Asp amidation level inside cell wall

Hao, P., Liang, D., Cao, L., Qiao, B., Wu, H., Caiyin, Q., Zhu, H., & Qiao, J. (2017) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-017-8365-7 · Cited by 31 · see citing works

Lactobacillus plantarum postbiotics trigger AMPK‐dependent autophagy to s uppress Salmonella intracellular infection and NLRP3 inflammasome activation

Wu, Y., Hu, A., Shu, X., Huang, W., Zhang, R., Xu, Y., & Yang, C. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.31016 · Cited by 31 · see citing works

From 11th International Symposium on Lactic Acid Bacteria

Chapot‐Chartier, M., & Kulakauskas, S. (2014)

The biosynthesis and functionality of the cell-wall of lactic acid bacteria

Delcour, J., Ferain, T., Deghorain, M., Palumbo, E., & Pascal Hols, A. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002089722581 · Cited by 262 · see citing works

© 1999 Kluwer Academic Publishers. Printed in the Netherlands. 159 The biosynthesis and functionality of the cell-wall of lactic acid bacteria

Delcour, J., Ferain, T., Deghorain, M., Palumbo, E., & Pascal Hols, A. (2015)

Cell wall homeostasis in lactic acid bacteria: threats and defences

Martı́nez, B., Rodrı́guez, A., Kulakauskas, S., & Chapot, M.-P. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa021 · Cited by 104 · see citing works

The cell wall of lactic acid bacteria: Surface constituents and macromolecular conformations

Ubbink, J., & Zammaretti, P. (2003) · European Cells and Materials · Cited by 1 · see citing works