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 901–999 of 999
Bacterial binding to extracellular matrix proteins — in vitro adhesion
Schou, C., Bøg-Hansen, T. C., & Fiehn, N. (1999) · Apmis · doi:10.1111/j.1699-0463.1999.tb01585.x · Cited by 6
Hall, A. E., Patel, P. R., Domanski, P. J., Prater, B. D., Gorovits, E., Syribeys, P. J., Vernachio, J. H., Patti, J. M., & Hutchins, J. T. (2007) · Hybridoma · doi:10.1089/hyb.2006.039 · Cited by 6
Self-citationShinji, H., Kamada, M., Seki, K., Tajima, A., Iwase, T., & Masuda, S. (2007) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2007.tb03891.x · Cited by 6
Mendoza-Barberà, E., Merino, S., & Tomás, J. M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00125-8 · Cited by 5
Guo, M., Li, Y., Tang, J., Wáng, Q., Wang, Q., Zhou, H., Lin, H., Ma, Z., & Fan, H. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012513 · Cited by 5
The Biofilm Blueprint: Exopolysaccharide Form and Function in Bacterial Biofilms
Cole, S. L., & Jennings, L. K. (2024) · Springer series on biofilms · doi:10.1007/978-3-031-70476-5_1 · Cited by 5
Mashaly, G. E.-S., & Badr, D. (2022) · The Egyptian Journal of Medical Microbiology · doi:10.21608/ejmm.2022.254103 · Cited by 5
Segura-Alba, M. L., Durán-Rodríguez, A. T., Salazar, L. M., Escobar-Pérez, J. A., GUTIÉRREZ, S. A., Jeannette Navarrete, O., Pinilla, G., & Molina, L. C. M. (2022) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765202220210848 · Cited by 5
Wisal, A., Ullah, A., Anwar, W., Morel, C. M., & Hassan, S. S. (2023) · Genomics & Informatics · doi:10.5808/gi.23024 · Cited by 5
Barberán, J., Martínez, M. A. M., & Navarro, M. C. D. V. (2010) · Medicine - Programa de Formación Médica Continuada Acreditado · doi:10.1016/s0304-5412(10)70041-x · Cited by 5
Khan, M. A. A., Hunter, J. M., Tan, C., Seleem, M., & Stride, P. (2012) · Case Reports in Medicine · doi:10.1155/2012/357502 · Cited by 5
Faghri, J., Shahbazzadeh, D., Bagheri, K. P., Moghim, S., Safaei, H. G., Esfahani, B. N., Fazeli, H., Yazdani, R., & Hamid, M. (2012) · Europe PMC (PubMed Central) · Cited by 5
Specificity and affinity of the N-terminal residues in staphylocoagulase in binding to prothrombin
Maddur, A. A., Kroh, H. K., Aschenbrenner, M. E., Gibson, B. H. Y., Panizzi, P. R., Sheehan, J. H., Meiler, J., BOCK, P. E., & Verhamme, I. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012588 · Cited by 5
Surface Proteins ofStaphylococcus aureus
Foster, T. J. (2019) · ASM Press eBooks · doi:10.1128/9781683670131.ch38 · Cited by 6
Bacterial Growth on Mucosal Surfaces and Biofilms in the Large Bowel
Macfarlane, S., & Macfarlane, G. T. (2003) · Cambridge University Press eBooks · doi:10.1017/cbo9780511546297.013 · Cited by 5
Williams, R. J., Ward, J. M., Henderson, B. E., Wilson, M., & Nair, S. P. (2000) · Molecular Biotechnology · doi:10.1385/mb:15:1:11 · Cited by 5
Bloom, B. T. (2006) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.15.6.703 · Cited by 5
Kang, J., Lee, M. S., & Gorenstein, D. G. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.01.038 · Cited by 5
Hull, J. R., Shannon, J. J., Tamura, G. S., & Castner, D. G. (2007) · Biointerphases · doi:10.1116/1.2738854 · Cited by 5
A Review on Next-Generation Nano-Antimicrobials in Orthopedics: Prospects and Concerns
Gupta, A., Dev, A., Nigam, V. K., Padmanabhan, P., & Singh, S. (2020) · Nanotechnology in the life sciences · doi:10.1007/978-3-030-40337-9_2 · Cited by 5
Sillanpää, J. (2001) · Työväentutkimus Vuosikirja · Cited by 5
Characterization of Staphylococcal Adhesins for Adherence to Host Tissues
Smeltzer, M. S. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-224-1_27 · Cited by 5
Pompilio, A., Lupetti, V., Puca, V., & Bonaventura, G. D. (2025) · Antibiotics · doi:10.3390/antibiotics14040402 · Cited by 4
Jiang, W., & You, C. (2026) · Microbial Pathogenesis · doi:10.1016/j.micpath.2026.108467 · Cited by 4
Haemophilus parasuis modulates cellular invasion via TGF-β1 signaling
Li, Y., Zhang, Y., Xia, Y., Shen, Y., & Zhang, J. (2016) · Veterinary Microbiology · doi:10.1016/j.vetmic.2016.10.012 · Cited by 4
Current Microbiological, Clinical and Therapeutic Aspects of Impetigo
Lior, Z., Charach, L., & Gideon, C. (2018) · Clinical Medical Reviews and Case Reports · doi:10.23937/2378-3656/1410205 · Cited by 4
Leal, A. L. A. B., da Silva, M. C., Silva, A. K. F. E., Mesquita, A. B. D. S., Bezerra, C. F., Dotto, A. R. F., do Amaral, W., Abi-chacra, É. D. A., da Silva, L. E., Barreto, H. M., et al. (2023) · 3 Biotech · doi:10.1007/s13205-023-03681-1 · Cited by 4
Recent Advances in Infective Endocarditis
Kerrigan, S. W. (2013) · InTech eBooks · doi:10.5772/46221 · Cited by 4
Borisov, B. K., & Linkova, S. P. (2020) · Indian Journal of Surgery · doi:10.1007/s12262-020-02095-0 · Cited by 4
Does Endodontic Treatment Influence Human Endocarditis? Systematic Review
Pereira, J. S., Leutz, A. C. N., Gomes, B. P. F. D. A., Pelepenko, L. E., & Marciano, M. A. (2024) · Hearts · doi:10.3390/hearts5030023 · Cited by 4
Yadav, A. K., Bindal, V., Jangra, V. K., Khan, Z., Ahangar, S., Sharanappa, V., Khetan, M., John, S. J., Kalhan, S., & Bhatia, P. (2016) · Surgical Science · doi:10.4236/ss.2016.710061 · Cited by 4
Cook, P., & Siraj, D. S. (2016) · Elsevier eBooks · doi:10.1016/b978-0-323-31696-5.00109-1 · Cited by 4
Sortases, Surface Proteins, and Their Roles inStaphylococcus aureusDisease and Vaccine Development
Schneewind, O., & Missiakas, D. M. (2019) · ASM Press eBooks · doi:10.1128/9781683670285.ch15 · Cited by 4
Staphylococcus aureus Infection in the Respiratory Tract
Prince, A. S. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5326-0_10 · Cited by 4
Hammel, M., Ramyar, K. X., Spencer, C. T., & Geisbrecht, B. V. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309106005926 · Cited by 4
Role of Biofilms in Fungal Keratitis- An Overview
Sharma, S. (2017) · Journal of Bacteriology & Mycology Open Access · doi:10.15406/jbmoa.2017.05.00157 · Cited by 4
Staphylococcus-aureus-Infektionen
Becker, K., & von Eiff, C. (2008) · Elsevier eBooks · doi:10.1016/b978-343721741-8.50030-1 · Cited by 4
Bashore, T. M. (2014) · Elsevier eBooks · doi:10.1016/b978-1-4557-4860-0.00025-6 · Cited by 4
Bovine mastitis caused by coagulase-negative staphylococci: host response and bacterial factors
Simojoki, H. (2011) · Työväentutkimus Vuosikirja · Cited by 4
(2011) · SpringerReference · doi:10.1007/springerreference_3859 · Cited by 4
Klueh, U., Bryers, J. D., & Kreutzer, D. L. (2003) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.10602 · Cited by 4
Rodrigues, R. G., Yan, S., Walsh, T. J., & Roberts, D. D. (1998) · The Journal of Infectious Diseases · doi:10.1086/515639 · Cited by 4
Immunotherapeutics for nosocomial infections
Patti, J. M. (2004) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.13.6.673 · Cited by 4
Self-citationSynthetic Lectin Mimics Artificial Carbohydrate Receptors
Yang, X., Cheng, Y., & Wang, B. (2011) · doi:10.1002/9781118017586.ch12 · Cited by 4
Staphylococcus epidermidis: Adhesion and Biofilm Formation onto Biomaterials
Sousa, C. (2011) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · Cited by 4
Characterization of Afb, a novel bifunctional protein in Streptococcus agalactiae.
Dehbashi, S., Pourmand, M. R., & Mashhadi, R. (2016) · Europe PMC (PubMed Central) · Cited by 3
Caimano, M. J. (2006) · Springer eBooks · doi:10.1007/0-387-30747-8_9 · Cited by 3
Flores-Suárez, B., Bonilla‐Lemus, P., Rojas-Hernández, S., Terrazas-Valdés, L. L., & Carrasco‐Yépez, M. M. (2024) · Journal of Parasitology · doi:10.1645/22-86 · Cited by 3
Crossman, L. C., Sims, L. P., Dean, R., Felgate, H., Calvo, T. D., Hill, C., McNamara, I., Webber, M. A., & Wain, J. R. (2024) · BMC Genomics · doi:10.1186/s12864-024-10719-y · Cited by 3
Recognizing scientific excellence in the biology of cell adhesion
Wary, K. K. (2005) · Cell Communication and Signaling · doi:10.1186/1478-811x-3-7 · Cited by 3
Role of SraP in Adherence of Staphylococcus aureus to the Bovine Mammary Epithelia
Takamatsu, D., Hata, E., Osaki, M., Aso, H., Kobayashi, S., & Sekizaki, T. (2008) · Journal of Veterinary Medical Science · doi:10.1292/jvms.70.735 · Cited by 3
Hemalatha, G., Rao, D. S., & Guruprasad, L. (2007) · Comparative and Functional Genomics · doi:10.1155/2007/47161 · Cited by 3
Effects of Biofilm Formation on The Antimicrobial Susceptibility of Staphylococcus aureus
Cho, K. J., Jin, S., Cui, J., Yoon, T. R., & Ryu, P. Y. (2008) · Journal of Bacteriology and Virology · doi:10.4167/jbv.2008.38.4.197 · Cited by 3
Hussain, S. F., Khatoon, A., Shahid, S. M., Ismail, M. O., & Azhar, A. (2013) · African Journal of Microbiology Research · doi:10.5897/ajmr12.1713 · Cited by 3
Offner, F. A., & Klosterhalfen, B. (2003) · CRC Press eBooks · doi:10.3109/9780203913208-5 · Cited by 3
Diagnosis and Management of Laparoscopic Inguinal Hernioplasty Infections
Kavic, M. S., & Thomas, J. (2003) · CRC Press eBooks · doi:10.3109/9780203913208-10 · Cited by 3
Palraj, R., Knoll, B. M., Baddour, L. M., & Wilson, W. R. (2015) · Elsevier eBooks · doi:10.1016/b978-1-4557-4801-3.00083-7 · Cited by 4
Pathogenesis of Biomaterial-Associated Infection
Tsang, S. J., & Simpson, H. (2020) · Springer eBooks · doi:10.1007/978-3-030-34475-7_6 · Cited by 3
Studies on isolation and characterization of oral biofilm forming bacteria
Jain, K. (2011) · Cited by 3
Levón, J. (2017) · Työväentutkimus Vuosikirja · Cited by 3
Elsherif, H. M., Helal, Z. H., El‐Ansary, M. R., Fahmy, Z. A., Eltayeb, W. N., Radwan, S., & Aboshanab, K. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.03.932921 · Cited by 3
Functional and metagenomic analysis of the human tongue dorsum using phage display
Easton, S. (2009) · UCL Discovery (University College London) · Cited by 3
In Vivo Models for Studying Staphylococcal Adhesion to Biomaterials
Vaudaux, P. E. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-224-1_26 · Cited by 3
Zhang, C., Li, D., Cheng, M., Wang, L., Wang, B., & Wang, L. (2025) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2025.107609 · Cited by 2
Faghri, J., Kamran, P. B., Shahbazzadeh, D., Yazdani, R., Hamid, M., & Moghim, S. (2009) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.22038/ijbms.2009.5129 · Cited by 1
Fatores de virulência de Staphylococcus aureus
Abad, A. C. A., da Costa, M. M., Pinheiro, J. W., & Mota, R. A. (2018) · Medicina Veterinária (UFRPE) · doi:10.26605/medvet-n4-1955 · Cited by 3
Cruzado-Bravo, M. L. M., Silva, N. C. C., Rodrigues, M. X., Saldaña, E., Contreras-Castillo, C. J., & Sturion, G. L. (2018) · Scientia Agropecuaria · doi:10.17268/sci.agropecu.2018.04.03 · Cited by 2
Intramolecular Covalent Bonds in Gram‐Positive Bacterial Surface Proteins
Ma, Q., Lei, H., & Cao, Y. (2022) · ChemBioChem · doi:10.1002/cbic.202200316 · Cited by 2
Endocarditis in critically ill patients: a review
Nedel, W. L., Boniatti, M. M., & Lisboa, T. C. (2023) · Current Opinion in Critical Care · doi:10.1097/mcc.0000000000001071 · Cited by 2
Aydın, A., Golian, M., Klein, A., Redpath, C. J., Davis, D. R., Ramirez, F. D., Nair, G. M., Green, M. S., Sadek, M. M., Nery, P. B., et al. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e22229 · Cited by 2
Khatibzadeh, S. M., Dahlgren, L. A., Caswell, C. C., Ducker, W. A., Werre, S. R., & Bogers, S. H. (2024) · PLoS ONE · doi:10.1371/journal.pone.0312917 · Cited by 2
Almaadhidy, R. A. K. J., & Meani, S. A. L. A. (2024) · The Open Microbiology Journal · doi:10.2174/0118742858349916241111100231 · Cited by 2
Deysine, M. (2010) · Springer eBooks · doi:10.1007/978-3-642-11541-7_18 · Cited by 2
An Overview on the Role of Microbial Agents in Psoriasis
Sarvtin, M. T., Hedayati, M. T., Mousavi, S. A. A., & Afsarian, M. H. (2013) · Majallah-i dānishgāh-i ̒ulūm-i pizishkī-i Māzandarān/Journal of Mazandaran University of Medical Sciences · Cited by 2
Barberán, J., Varona, J. F., & Tejeda, M. I. (2014) · Medicine - Programa de Formación Médica Continuada Acreditado · doi:10.1016/s0304-5412(14)70803-0 · Cited by 2
Glycine prevents the phenotypic expression of streptococcal glucan-binding lectin
Luengpailin, J., & Doyle, R. J. (2000) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(00)00010-6 · Cited by 2
Löhr, M., Molčányi, M., Stenzel, W., Seifert, H., Tzouras, G., Röhn, G., Mohseni, D., & Hampl, J. A. (2011) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2011.09.016 · Cited by 2
Surface Protein Anchoring and Display in Staphylococci
Ton‐That, H., Mazmanian, S. K., Liu, G., & Schneewind, O. (2001) · Infectious agents and pathogenesis · doi:10.1007/0-306-46848-4_9 · Cited by 2
Ponnuvel, S., Bandaru, D., Ragunathan, P. T., & Ponnuraj, K. (2016) · RSC Advances · doi:10.1039/c6ra18275e · Cited by 2
Zhang, Y., Su, J., & Wu, D. (2017) · InTech eBooks · doi:10.5772/intechopen.70488 · Cited by 2
Pathogenic Mechanisms in Streptococcal Diseases
Caparon, M. G. (2001) · Elsevier eBooks · doi:10.1016/b978-012304220-0/50016-9 · Cited by 2
PJI with Sepsis, a Complex Emergency Situation with Prodromal Stage
Haustedt, N., González-Chapa, J. A., & Hentschke, M. (2020) · Open Journal of Orthopedics · doi:10.4236/ojo.2020.109023 · Cited by 2
Lahiri, D., Nag, M., Mukherjee, D., Garai, S., Banerjee, R., Dey, A., & Ray, R. R. (2021) · Springer eBooks · doi:10.1007/978-981-16-0745-5_7 · Cited by 2
The Regulation of Virulence in the Staphylococci
Dunman, P. M., & Projan, S. J. (2001) · Infectious agents and pathogenesis · doi:10.1007/0-306-46848-4_1 · Cited by 2
Extracellular Matrix Interactions with Gram-Positive Pathogens
Chhatwal, G. S., & Preissner, K. T. (2014) · ASM Press eBooks · doi:10.1128/9781555816513.ch8 · Cited by 2
Binding of the extracellular matrix laminin-1 to Clostridioides difficile strains
Santos, M. G. D. C., Trindade, C. N. D. R., Vommaro, R. C., Domingues, R. M. C. P., & Ferreira, E. D. O. (2022) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/0074-02760220035 · Cited by 2
Faillace, W. J., & Tan, P. (2000) · Journal of Pharmacy Technology · doi:10.1177/875512250001600411 · Cited by 2
Manne, K., Narayana, S. V. L., & Chattopadhyay, D. (2019) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x19012160 · Cited by 2
Aktaş, E., & Özgentürk, N. Ö. (2022) · Bioinformatics and Biology Insights · doi:10.1177/11779322221116320 · Cited by 2
Staphylococcus aureus-Eukaryotic Cell Interactions
Arrecubieta, C., & Lowy, F. D. (2014) · ASM Press eBooks · doi:10.1128/9781555816513.ch42 · Cited by 2
Onteniente, L. (2004) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 2
Donofrio, F. C. (2007) · Americanae (AECID Library) · Cited by 2
Facteur d'attachement au fibrinogène: perspectives
François, P., Vaudaux, P. E., Foster, T. J., & Lew, D. P. (1997) · Médecine et Maladies Infectieuses · doi:10.1016/s0399-077x(97)80013-3 · Cited by 2
Donati, L. (2001) · Journal of Chemotherapy · doi:10.1179/joc.2001.13.supplement-2.129 · Cited by 2
Secreted virulence factors in lethal illness due to Staphylococcus aureus
Spaulding, A. R. (2013) · doi:10.17077/etd.dx8depdd · Cited by 1
Mécanismes physiopathologiques des arthrites septiques
Zerkak, D., Ziza, J.-M., & Desplaces, N. (2006) · Revue du Rhumatisme · doi:10.1016/j.rhum.2005.12.006 · Cited by 2
Incidence and Epidemiology of Infection After External Abdominal Wall Herniorrhaphy
Montes, I. S., & Sanchez-Montes, J. C. (2003) · CRC Press eBooks · doi:10.3109/9780203913208-3 · Cited by 2
Gatermann, S. G., & Crossley, K. (2009) · Wiley eBooks · doi:10.1002/9781444308464.ch24 · Cited by 2
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