The DOI matches its Crossref record; 82 of the 83 references it cites were found in a registry or an index.
MSCRAMM-MEDIATED ADHERENCE OF MICROORGANISMS TO HOST TISSUES
Abstract
Microbial adhesion to host tissue is the initial critical event in the pathogenesis of most infections and, as such, is an attractive target for the development of new antimicrobial therapeutics. Specific microbial components (adhesins) mediate adherence to host tissues by participating in amazingly sophisticated interactions with host molecules. This review focuses on a class of cell surface adhesins that specifically interact with extracellular matrix components and which we have designated MSCRAMMs (microbial surface components recognizing adhesive matrix molecules). MSCRAMMs recognizing fibronectin-, fibrinogen-, collagen-, and heparin-related polysaccharides are discussed in terms of structural organization, ligand-binding structures, importance in host tissue colonization and invasion, and role as virulence factors.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Some bacterial adhesins, for example surface proteins that interact with extracellular matrix molecules of their host (fibronectin, collagen, laminin, fibrinogen or others), have been classified as microbial surface components recognizing adhesive matrix molecules (MSCRAMMs); full reviews of MSCRAMMs have been published elsewhere [4].”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [4]
Citations
Cites
Beachey, E. H. (1981) · Journal of Infectious Diseases · doi:10.1093/infdis/143.3.325 · Cited by 1,411
Isberg, R. R., & Leong, J. M. (1990) · Cell · doi:10.1016/0092-8674(90)90099-z · Cited by 798
Fibronectin binding mediated by a novel class of surface organelles on Escherichia coll
Olsén, A., Jonsson, A., & Normark, S. J. (1989) · Nature · doi:10.1038/338652a0 · Cited by 614
Isberg, R. R., Voorhis, D. L., & Falkow, S. (1987) · Cell · doi:10.1016/0092-8674(87)90335-7 · Cited by 597
Liotta, L. A., Goldfarb, R. H., Brundage, R. A., Siegal, G. P., Terranova, V. P., & Garbisa, S. (1981) · PubMed · Cited by 597
Fibronectin binds to Staphylococcus aureus
Kuusela, P. (1978) · Nature · doi:10.1038/276718a0 · Cited by 457
Fischetti, V. A., Pancholi, V., & Schneewind, O. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb02072.x · Cited by 411
Korhonen, T. K., Valtonen, M., Parkkinen, J., Väisänen-Rhen, V., Finne, J., Ørskov, F., Ørskov, I., Svenson, S. B., & Mäkelä, P. H. (1985) · Infection and Immunity · doi:10.1128/iai.48.2.486-491.1985 · Cited by 360
Frevert, U., Sinnis, P., Cerami, C., Shreffler, W. G., Takács, B., & Nussenzweig, V. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.5.1287 · Cited by 351
Marcantonio, E. E., & Hynes, R. O. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.5.1765 · Cited by 319
Cited by
Sorted by citations
Items 101–200 of 999
Structure and function of fibronectin modules
Potts, J. R., & Campbell, I. D. (1996) · Matrix Biology · doi:10.1016/s0945-053x(96)90133-x · Cited by 207
Jenkins, A. L., Diep, B. A., Mai, T. T., Vo, N. H., Warrener, P., Suzich, J., Stover, C. K., & Sellman, B. R. (2015) · mBio · doi:10.1128/mbio.02272-14 · Cited by 202
Temporal and Stochastic Control of Staphylococcus aureus Biofilm Development
Moormeier, D. E., Bose, J. L., Horswill, A. R., & Bayles, K. W. (2014) · mBio · doi:10.1128/mbio.01341-14 · Cited by 196
Nallapareddy, S. R., Weinstock, G. M., & Murray, B. E. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03417.x · Cited by 202
Key Role for Clumping Factor B in Staphylococcus aureus Nasal Colonization of Humans
Wertheim, H. F. L., Walsh, E. J., Choudhurry, R. S. R., Melles∗, D. C., Boelens, H. A. M., Miajlović, H., Verbrugh, H. A., Foster, T. J., & van Belkum, A. (2008) · PLoS Medicine · doi:10.1371/journal.pmed.0050017 · Cited by 202
Genetic regulation of the intercellular adhesion locus in staphylococci
Cue, D. R., Lei, M. G., & Lee, C. Y. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00038 · Cited by 189
Hauck, C. R., & Ohlsen, K. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.12.002 · Cited by 193
Nishitani, K., Sutipornpalangkul, W., Bentley, K. L. D. M., Varrone, J. J., Bello‐Irizarry, S. N., Ito, H., Matsuda, S., Kates, S. L., Daiss, J. L., & Schwarz, E. M. (2015) · Journal of Orthopaedic Research® · doi:10.1002/jor.22907 · Cited by 190
Biofilm-Based Implant Infections in Orthopaedics
Arciola, C. R., Campoccia, D., Ehrlich, G. D., & Montanaro, L. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-11038-7_2 · Cited by 186
Barbosa, M. S., Báo, S. N., Andreotti, P. F., de Faria, F. P., Felipe, M. S. S., Feitosa, L. D. S., Mendes‐Giannini, M. J. S., & Soares, C. M. D. A. (2005) · Infection and Immunity · doi:10.1128/iai.74.1.382-389.2006 · Cited by 189
Streptococcus pyogenes Serotype M1 Encodes Multiple Pathways for Entry into Human Epithelial Cells
Cue, D. R., Dombek, P. E., Lam, H., & Cleary, P. P. (1998) · Infection and Immunity · doi:10.1128/iai.66.10.4593-4601.1998 · Cited by 189
Guiton, P. S., Hung, C., Hancock, L. E., Caparon, M. G., & Hultgren, S. J. (2010) · Infection and Immunity · doi:10.1128/iai.00711-10 · Cited by 184
Is Staphylococcus aureus an intracellular pathogen?
Lowy, F. D. (2000) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01803-5 · Cited by 186
Dego, O. K., van Dijk, J. E., & Nederbragt, H. (2002) · Veterinary Quarterly · doi:10.1080/01652176.2002.9695135 · Cited by 182
Vaudaux, P. E., François, P., Bisognano, C., Kelley, W. L., Lew, D. P., Schrenzel, J., Proctor, R. A., McNamara, P. J., Peters, G., & von Eiff, C. (2002) · Infection and Immunity · doi:10.1128/iai.70.10.5428-5437.2002 · Cited by 185
Staphylococcus aureus collagen adhesin contributes to the pathogenesis of osteomyelitis
Elasri, M. O., Thomas, J. R., Skinner, R. A., Blevins, J. S., Beenken, K. E., Nelson, C. L., & Smelter, M. S. (2002) · Bone · doi:10.1016/s8756-3282(01)00632-9 · Cited by 182
Gaur, N. K., & Klotz, S. A. (1997) · Infection and Immunity · doi:10.1128/iai.65.12.5289-5294.1997 · Cited by 182
Agerer, F., Lux, S., Michel, A., Rohde, M., Ohlsen, K., & Hauck, C. R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02328 · Cited by 187
Ricciardi, B. F., Muthukrishnan, G., Masters, E. A., Ninomiya, M. J., Lee, C. C., & Schwarz, E. M. (2018) · Current Reviews in Musculoskeletal Medicine · doi:10.1007/s12178-018-9501-4 · Cited by 182
Models matter: the search for an effective Staphylococcus aureus vaccine
Salgado‐Pabón, W., & Schlievert, P. M. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3308 · Cited by 179
Nilsson, I. M., Patti, J. M., Bremell, T., Höök, M., & Tarkowski, A. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1823 · Cited by 179
Self-citationStaphylococcus aureus (Including Staphylococcal Toxic Shock)
Que, Y., & Moreillon, P. (2010) · Elsevier eBooks · doi:10.1016/b978-0-443-06839-3.00195-8 · Cited by 177
Insects as alternative hosts for phytopathogenic bacteria
Nadarasah, G., & Stavrinides, J. (2011) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2011.00264.x · Cited by 174
Nina, H., Schlesier, T., Schmidt, M. A., Götz, F., Peters, G., & Heilmann, C. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01506.x · Cited by 172
Claro, T., Widaa, A., O’Seaghdha, M., Miajlović, H., Foster, T. J., O’Brien, F. J., & Kerrigan, S. W. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018748 · Cited by 178
Krahn, K. N., Bouten, C. V. C., van Tuijl, S., van Zandvoort, M. A. M. J., & Merkx, M. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.01.013 · Cited by 172
The extracellular matrix protein mindin is a pattern-recognition molecule for microbial pathogens
He, Y.-W., Li, H., Zhang, J., Hsu, C.-L., Lin, E., Zhang, N., Guo, J., Forbush, K. A., & Bevan, M. J. (2004) · Nature Immunology · doi:10.1038/ni1021 · Cited by 171
A second IgG-binding protein in Staphylococcus aureus
Zhang, L., Jacobsson, K., Vasi, J., Lindberg, M., & Frykberg, L. (1998) · Microbiology · doi:10.1099/00221287-144-4-985 · Cited by 170
Modification of the Staphylococcus aureus fibronectin binding phenotype by V8 protease
Mcgavin, M. J., Zahradka, C., Rice, K. C., & Scott, J. E. (1997) · Infection and Immunity · doi:10.1128/iai.65.7.2621-2628.1997 · Cited by 168
Self-citationImmunopathogenesis of Staphylococcus aureus pulmonary infection
Parker, D., & Prince, A. S. (2011) · Seminars in Immunopathology · doi:10.1007/s00281-011-0291-7 · Cited by 176
Environmental Influences on Biofilm Development
Goller, C., & Romeo, T. (2008) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-75418-3_3 · Cited by 178
Deivanayagam, C. C. S., Rich, R. L., Carson, M., Owens, R. T., Danthuluri, S., Bice, T., Höök, M., & Narayana, S. V. L. (2000) · Structure · doi:10.1016/s0969-2126(00)00081-2 · Cited by 165
Self-citationWidaa, A., Claro, T., Foster, T. J., O’Brien, F. J., & Kerrigan, S. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040586 · Cited by 166
Lactobacillus fermentumRC‐14 InhibitsStaphylococcus aureusInfection of Surgical Implants in Rats
Gan, B. S., Kim, J., Reid, G., Cadieux, P. A., & Howard, J. C. (2002) · The Journal of Infectious Diseases · doi:10.1086/340126 · Cited by 162
Emergence of coagulase-negative staphylococci
Becker, K., Both, A., Weißelberg, S., Heilmann, C., & Rohde, H. (2020) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2020.1730813 · Cited by 167
Kaempferol Inhibits the Primary Attachment Phase of Biofilm Formation in Staphylococcus aureus
Di, M., Wang, D., Cao, F., Xiang, H., Mu, D., Cao, J., Li, B., Zhong, L., Dong, X., Zhong, X., et al. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02263 · Cited by 161
A structural basis for complement inhibition by Staphylococcus aureus
Hammel, M., Sfyroera, G., Ricklin, D., Magotti, P., Lambris, J. D., & Geisbrecht, B. V. (2007) · Nature Immunology · doi:10.1038/ni1450 · Cited by 159
Bacterial virulence as a target for antimicrobial chemotherapy
Alksne, L. E., & Projan, S. J. (2000) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00155-5 · Cited by 156
Biofilms in Infections of the Eye
Bispo, P. J. M., Haas, W., & Gilmore, M. S. (2015) · Pathogens · doi:10.3390/pathogens4010111 · Cited by 158
RrgA is a pilus‐associated adhesin in Streptococcus pneumoniae
Nelson, A. L., Ries, J., Bagnoli, F., Dahlberg, S., Fälker, S., Rounioja, S., Tschöp, J., Morfeldt, E., Ferlenghi, I., Hilleringmann, M., et al. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05908.x · Cited by 157
van Putten, J. P. M., Duensing, T. D., & Cole, R. L. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00951.x · Cited by 157
Characterization of the Collagen-Binding S-Layer Protein CbsA of Lactobacillus crispatus
Sillanpää, J., Martı́nez, B., Antikainen, J., Toba, T., Kalkkinen, N., Tankka, S., Lounatmaa, K., Keränen, J., Höök, M., Westerlund‐Wikström, B., et al. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.22.6440-6450.2000 · Cited by 157
Self-citationKarlsson, A., Saravia‐Otten, P., Tegmark, K., Morfeldt, E., & Arvidson, S. (2001) · Infection and Immunity · doi:10.1128/iai.69.8.4742-4748.2001 · Cited by 157
Downer, R., Roche, F. M., Park, P. W., Mecham, R. P., & Foster, T. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107621200 · Cited by 156
DeJonge, M. H., Burchfield, D. J., Bloom, B. T., Dueñas, M., Walker, W., Polak, M. J., Jung, E., MILLARD, D. D., Schelonka, R. L., Eyal, F. G., et al. (2007) · The Journal of Pediatrics · doi:10.1016/j.jpeds.2007.04.060 · Cited by 155
Self-citationPeacock, S. J., Day, N., Thomas, M. G., Berendt, A. R., & Foster, T. J. (2000) · Journal of Infection · doi:10.1053/jinf.2000.0657 · Cited by 155
Wesson, C. A., Liou, L. E., Todd, K. M., Bohach, G. A., Trumble, W. R., & Bayles, K. W. (1998) · Infection and Immunity · doi:10.1128/iai.66.11.5238-5243.1998 · Cited by 155
Characterization of Biofilm Formation by Clinically Relevant Serotypes of Group A Streptococci
Lembke, C., Podbielski, A., Hidalgo‐Grass, C., Jonas, L., Hanski, E., & Kreikemeyer, B. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.4.2864-2875.2006 · Cited by 157
Surface Proteins ofStaphylococcus aureus
Foster, T. J. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.gpp3-0046-2018 · Cited by 178
Virulence Factors in Coagulase-Negative Staphylococci
França, Â., Gaio, V., Lopes, N., & Melo, L. D. R. (2021) · Pathogens · doi:10.3390/pathogens10020170 · Cited by 171
McAleese, F., Walsh, E. J., Sieprawska, M., Potempa, J., & Foster, T. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102389200 · Cited by 153
Microbial interactions in Staphylococcus epidermidis biofilms
Mack, D., Davies, A. P., Harris, L. G., Rohde, H., Horstkotte, M. A., & Knobloch, J. K. ‐. (2006) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-006-0745-2 · Cited by 151
Cafiso, V., Bertuccio, T., Santagati, M., Campanile, F., Amicosante, G., Perilli, M., Selan, L., Artini, M., Nicoletti, G., & Stefani, S. (2004) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2004.01024.x · Cited by 152
Jing, X., Xu, C., Su, W., Ding, Q., Ye, B., Su, Y., Yu, K., Zeng, L., Yang, X., Qu, Y., et al. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202201349 · Cited by 151
Immune Evasion Mechanisms of Staphylococcus epidermidis Biofilm Infection
LE, K. Y., Park, M. D., & Otto, M. J. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00359 · Cited by 153
Singh, K. V., Nallapareddy, S. R., Sillanpää, J., & Murray, B. E. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000716 · Cited by 148
Heilmann, C., Hartleib, J., Hussain, M. S., & Peters, G. (2005) · Infection and Immunity · doi:10.1128/iai.73.8.4793-4802.2005 · Cited by 149
Airborne Staphylococcus aureus in different environments—a review
Kozajda, A., Jeżak, K., & Kapsa, A. (2019) · Environmental Science and Pollution Research · doi:10.1007/s11356-019-06557-1 · Cited by 151
Kang, M., Ko, Y.-P., Liang, X., Ross, C. L., Liu, Q., Murray, B. E., & Höök, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.454462 · Cited by 146
Self-citationHall, A. E., Domanski, P. J., Patel, P. R., Vernachio, J. H., Syribeys, P. J., Gorovits, E., Johnson, M. A., Ross, J., Hutchins, J. T., & Patti, J. M. (2003) · Infection and Immunity · doi:10.1128/iai.71.12.6864-6870.2003 · Cited by 146
Self-citationSchroeder, K., Jularic, M., Horsburgh, S. M., Nina, H., Neumann, C., Bertling, A., Schulte, A., Foster, S. J., Kehrel, B. E., Peters, G., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007567 · Cited by 143
Hell, W., Meyer, H. W., & Gatermann, S. G. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00983.x · Cited by 143
Hydrolysis of Epithelial Junctional Proteins byPorphyromonas gingivalisGingipains
Katz, J., Yang, Q.-B., Zhang, P., Potempa, J., Travis, J. W., Michalek, S. M., & Balkovetz, D. F. (2002) · Infection and Immunity · doi:10.1128/iai.70.5.2512-2518.2002 · Cited by 143
Chagnot, C., Listrat, A., Astruc, T., & Desvaux, M. (2012) · Cellular Microbiology · doi:10.1111/cmi.12002 · Cited by 142
Dziewanowska, K., Carson, A. R., Patti, J. M., Deobald, C. F., Bayles, K. W., & Bohach, G. A. (2000) · Infection and Immunity · doi:10.1128/iai.68.11.6321-6328.2000 · Cited by 142
Self-citationIntramolecular isopeptide bonds: protein crosslinks built for stress?
Kang, H. J., & Baker, E. N. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.007 · Cited by 146
Kouidhi, B., Zmantar, T., Hentati, H. A. A., & Bakhrouf, A. (2010) · Microbial Pathogenesis · doi:10.1016/j.micpath.2010.03.007 · Cited by 141
Peri-Implant Infections of Oral Biofilm Etiology
Belibasakis, G. N., Charalampakis, G., Bostancı, N., & Stadlinger, B. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-11038-7_4 · Cited by 147
Resistance to Lyme disease in decorin-deficient mice
Brown, E. L., Wooten, R. M., Johnson, B. J. B., Iozzo, R. V., Smith, A. P., Dolan, M. C., Guo, B. P., Weis, J. J., & Höök, M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11692 · Cited by 140
Self-citationInhibition of Complement Activation by a Secreted Staphylococcus aureus Protein
Lee, L. Y., Höök, M., Haviland, D. L., Wetsel, R. A., Yonter, E. O., Syribeys, P. J., Vernachio, J. H., & Brown, E. L. (2004) · The Journal of Infectious Diseases · doi:10.1086/422259 · Cited by 139
Self-citationInternalization of Staphylococcus aureus by Human Keratinocytes
Kintarak, S., Whawell, S. A., Speight, P. M., Packer, S., & Nair, S. P. (2004) · Infection and Immunity · doi:10.1128/iai.72.10.5668-5675.2004 · Cited by 139
Li, N., Ren, A., Wang, X., Fan, X., Zhao, Y. X., Gao, G. F., Cleary, P. P., & Wang, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414422112 · Cited by 138
The molecular basis of Streptococcus equi infection and disease
Harrington, D. J., Sutcliffe, I. C., & Chanter, N. (2002) · Microbes and Infection · doi:10.1016/s1286-4579(02)01565-4 · Cited by 137
Castro, S. L., Nelman-Gonzalez, M. A., Nickerson, C. A., & Ott, C. M. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.00175-11 · Cited by 136
Hoke, D. E., Egan, S., Cullen, P. A., & Adler, B. (2008) · Infection and Immunity · doi:10.1128/iai.01643-07 · Cited by 136
Brouillette, É., Grondin, G., Shkreta, L., Lacasse, P., & Talbot, B. G. (2003) · Microbial Pathogenesis · doi:10.1016/s0882-4010(03)00112-8 · Cited by 135
Human Factor inStaphylococcus aureusNasal Carriage
Nouwen, J. L., Boelens, H. A. M., van Belkum, A., & Verbrugh, H. A. (2004) · Infection and Immunity · doi:10.1128/iai.72.11.6685-6688.2004 · Cited by 135
Agerer, F., Michel, A., Ohlsen, K., & Hauck, C. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302096200 · Cited by 134
Mechanism and consequences of invasion of endothelial cells by Staphylococcus aureus
Herrmann, M., & Sinha, B. N. M. (2005) · Thrombosis and Haemostasis · doi:10.1160/th05-04-0235 · Cited by 132
Pöhlmann‐Dietze, P., Ulrich, M., Kiser, K. B., Döring, G., Lee, J. C., Fournier, J.-M., Botzenhart, K., & Wolz, C. (2000) · Infection and Immunity · doi:10.1128/iai.68.9.4865-4871.2000 · Cited by 133
Lee, L. Y., Liang, X., Höök, M., & Brown, E. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408570200 · Cited by 131
Self-citationPili 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
Pike, R. N., Potempa, J., McGraw, W. T., Coetzer, T. H. T., & Travis, J. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.10.2876-2882.1996 · Cited by 131
Arciola, C. R., Campoccia, D., Gamberini, S., Baldassarri, L., & Montanaro, L. (2005) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2005.03.035 · Cited by 130
The Collagen-Binding Adhesin Is a Virulence Factor in Staphylococcus aureus Keratitis
Rhem, M. N., Lech, E. M., Patti, J. M., McDevitt, D., Höök, M., Jones, D. B., & Wilhelmus, K. R. (2000) · Infection and Immunity · doi:10.1128/iai.68.6.3776-3779.2000 · Cited by 130
Self-citationThe Fbe (SdrG) protein of Staphylococcus epidermidis HB promotes bacterial adherence to fibrinogen
Hartford, O. M., O’Brien, L., Schofield, K. M., Wells, J. M., & Foster, T. J. (2001) · Microbiology · doi:10.1099/00221287-147-9-2545 · Cited by 130
Wolz, C., Pöhlmann‐Dietze, P., Steinhuber, A., Chien, Y., Manna, A. C., van Wamel, W. J. B., & Cheung, A. L. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01853.x · Cited by 130
Protective Niche for Borrelia burgdorferi to Evade Humoral Immunity
Liang, F. T., Brown, E. L., Wang, T. Z., Iozzo, R. V., & Fikrig, E. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63359-7 · Cited by 129
Iron Acquisition and Transport in Staphylococcus aureus
Maresso, A. W., & Schneewind, O. (2006) · BioMetals · doi:10.1007/s10534-005-4863-7 · Cited by 133
Xu, Y., Rivas, J. M., Brown, E. L., Liang, X., & Höök, M. (2004) · The Journal of Infectious Diseases · doi:10.1086/420851 · Cited by 129
Self-citationO'Connell, D. P., Nanavaty, T., McDevitt, D., Gurusiddappa, S., Höök, M., & Foster, T. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6821 · Cited by 128
Self-citationInvasion of Host Cells by Microsporidia
Han, B., Takvorian, P. M., & Weiss, L. M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00172 · Cited by 127
Repeated Domains of Leptospira Immunoglobulin-like Proteins Interact with Elastin and Tropoelastin
Lin, Y., Lee, D., McDonough, S. P., Nicholson, L. K., Sharma, Y., & Chang, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.004531 · Cited by 126
Speziale, P., Pietrocola, G., Rindi, S., Provenzano, M., Provenza, G., Poto, A. D., Visai, L., & Arciola, C. R. (2009) · Future Microbiology · doi:10.2217/fmb.09.102 · Cited by 133
Nallapareddy, S. R., Singh, K. V., Duh, R.-W., Weinstock, G. M., & Murray, B. E. (2000) · Infection and Immunity · doi:10.1128/iai.68.9.5210-5217.2000 · Cited by 125
Microbial Biofilms in Ophthalmology and Infectious Disease
Behlau, I. (2008) · Archives of Ophthalmology · doi:10.1001/archopht.126.11.1572 · Cited by 125
Lee, L. Y., Miyamoto, Y., McIntyre, B. W., Höök, M., McCrea, K. W., McDevitt, D., & Brown, E. L. (2002) · Journal of Clinical Investigation · doi:10.1172/jci16318 · Cited by 124
Self-citationRoggenkamp, A., NEUBERGER, H., Flügel, A., Schmoll, T., & Heesemann, J. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.tb02343.x · Cited by 124
Molecular determinants of staphylococcal biofilm dispersal and structuring
LE, K. Y., Dastgheyb, S., Ho, T. V., & Otto, M. J. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00167 · Cited by 125
Structural biology of gram‐positive bacterial adhesins
Krishnan, V., & Narayana, S. V. L. (2011) · Protein Science · doi:10.1002/pro.613 · Cited by 122
Metadata
- Authors
- Patti, J. M., Allen, B. L., McGavin, M. J., & Höök, M.
- Affiliations
- Texas A&M University (US)
- Venue
- Annual Review of Microbiology
- Publisher
- Annual Reviews
- Published
- 1994-10
- Volume
- 48
- Issue
- 1
- Pages
- 585-617
- ISSN
- 0066-4227 (ISSN-L)
- 1545-3251
- OpenAlex
- W2176472482
- Cited by
- 1,191
- References
- 83
- Citations by year
- 2026: 11 · 2025: 18 · 2024: 32 · 2023: 20 · 2022: 19 · 2021: 29 · 2020: 40 · 2019: 32 · 2018: 23 · 2017: 36 · 2016: 36 · 2015: 40 · 2014: 64 · 2013: 51 · 2012: 56
- FWCI
- 6.02
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl047313-03)
- National Heart, Lung, and Blood Institute (HL 47313)
- National Institute of Allergy and Infectious Diseases (AI20624)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
- Keywords
- MSCRAMMs, microbial adhesion, extracellular matrix, adhesins, fibronectin, fibrinogen, collagen, heparin, ligand binding, virulence factors, host-pathogen interaction, antimicrobial agents
- MeSH terms
- Amino Acid Sequence, Bacterial Adhesion, Gram-Negative Bacteria, Gram-Positive Bacteria, Heparin, Molecular Sequence Data, Extracellular Matrix Proteins, Adhesins, Bacterial
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review