Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 130

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Surface-attached molecules control Staphylococcus aureus quorum sensing and biofilm development

Kim, Minyoung Kevin, Zhao, Aishan, Wang, Ashley, Brown, Zachary Z., Muir, Tom W., Stone, Howard A., Bassler, Bonnie L.·2017·Nature Microbiology
DOI 10.1038/nmicrobiol.2017.80
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nmicrobiol.2017.80

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 53

  1. Wang, B. & Muir, T. W. Regulation of virulence in Staphylococcus aureus: molecular mechanisms and remaining puzzles. Cell Chem. Biol. 23, 214–224 (2016). · DOI · Paper page
  2. Kong, K. F., Vuong, C. & Otto, M. Staphylococcus quorum sensing in biofilm formation and infection. Int. J. Med. Microbiol. 296, 133–139 (2006). · DOI · Paper page
  3. Drescher, K. et al. Architectural transitions in Vibrio cholerae biofilms at single-cell resolution. Proc. Natl Acad. Sci. USA 113, E2066–E2072 (2016). · DOI · Paper page
  4. Yan, J., Sharo, A. G., Stone, H. A., Wingreen, N. S. & Bassler, B. L. Vibrio cholerae biofilm growth program and architecture revealed by single-cell live imaging. Proc. Natl Acad. Sci. USA 113, E5337–E5343 (2016). · DOI · Paper page
  5. Nadell, C. D., Drescher, K. & Foster, K. R. Spatial structure, cooperation and competition in biofilms. Nat. Rev. Microbiol. 14, 589–600 (2016). · DOI · Paper page
  6. Waters, C. M. & Bassler, B. L. Quorum sensing: cell-to-cell communication in bacteria. Annu. Rev. Cell Dev. Biol. 21, 319–346 (2005). · DOI · Paper page
  7. Papenfort, K. & Bassler, B. L. Quorum sensing signal-response systems in Gram-negative bacteria. Nat. Rev. Microbiol. 14, 576–588 (2016). · DOI · Paper page
  8. Novick, R. P. & Geisinger, E. Quorum sensing in staphylococci. Annu. Rev. Genet. 42, 541–564 (2008). · DOI · Paper page
  9. Dinges, M. M., Orwin, P. M. & Schlievert, P. M. Exotoxins of Staphylococcus aureus. Clin. Microbiol. Rev. 13, 16–34 (2000). · DOI · Paper page
  10. Arvidson, S. & Tegmark, K. Regulation of virulence determinants in Staphylococcus aureus. Int. J. Med. Microbiol. 291, 159–170 (2001). · DOI · Paper page
  11. Hammer, B. K. & Bassler, B. L. Quorum sensing controls biofilm formation in Vibrio cholerae. Mol. Microbiol. 50, 101–104 (2003). · DOI · Paper page
  12. Ismail, A. S., Valastyan, J. S. & Bassler, B. L. A host-produced autoinducer-2 mimic activates bacterial quorum sensing. Cell Host Microbe 19, 470–480 (2016). · DOI · Paper page
  13. O'Loughlin, C. T. et al. A quorum-sensing inhibitor blocks Pseudomonas aeruginosa virulence and biofilm formation. Proc. Natl Acad. Sci. USA 110, 17981–17986 (2013). · DOI · Paper page
  14. Sully, E. K. et al. Selective chemical inhibition of agr quorum sensing in Staphylococcus aureus promotes host defense with minimal impact on resistance. PLoS Pathog. 10, e1004174 (2014). · DOI · Paper page
  15. Otto, M. Quorum-sensing control in Staphylococci—a target for antimicrobial drug therapy? FEMS Microbiol. Lett. 241, 135–141 (2004). · DOI · Paper page
  16. Kim, M. K., Ingremeau, F. B., Zhao, A., Bassler, B. L. & Stone, H. A. Local and global consequence of flow on bacterial quorum sensing. Nat. Microbiol. 1, 15005 (2016). · DOI · Paper page
  17. Lu, H. D. et al. Modulating Vibrio cholerae quorum-sensing-controlled communication using autoinducer-loaded nanoparticles. Nano Lett. 15, 2235–2241 (2015). · DOI
  18. Persat, A. et al. The mechanical world of bacteria. Cell 161, 988–997 (2015). · DOI · Paper page
  19. Kim, M. K., Drescher, K., Pak, O. S., Bassler, B. L. & Stone, H. A. Filaments in curved streamlines: rapid formation of Staphylococcus aureus biofilm streamers. New J. Phys. 16, 065024 (2014). · doi:10.1088/1367-2630/16/1/015024
  20. Broderick, A. H. et al. Surface coatings that promote rapid release of peptide-based AgrC inhibitors for attenuation of quorum sensing in Staphylococcus aureus. Adv. Healthc. Mater. 3, 97–105 (2014). · DOI
  21. Ho, K. K. K. et al. Quorum sensing inhibitory activities of surface immobilized antibacterial dihydropyrrolones via click chemistry. Biomaterials 35, 2336–2345 (2014). · DOI
  22. Lowy, F. D. Staphylococcus aureus infections. New Engl. J. Med. 339, 2026–2027 (1998). · DOI · Paper page
  23. Gordon, R. J. & Lowy, F. D. Pathogenesis of methicillin-resistant Staphylococcus aureus infection. Clin. Infect. Dis. 46, S350–S359 (2008). · DOI · Paper page
  24. Zhang, L. S., Gray, L., Novick, R. P. & Ji, G. Y. Transmembrane topology of AgrB, the protein involved in the post-translational modification of AgrD in Staphylococcus aureus. J. Biol. Chem. 277, 34736–34742 (2002). · DOI
  25. Wang, B. Y., Zhao, A. S., Novick, R. P. & Muir, T. W. Key driving forces in the biosynthesis of autoinducing peptides required for staphylococcal virulence. Proc. Natl Acad. Sci. USA 112, 10679–10684 (2015). · DOI
  26. Lina, G. et al. Transmembrane topology and histidine protein kinase activity of AgrC, the agr signal receptor in Staphylococcus aureus. Mol. Microbiol. 28, 655–662 (1998). · DOI · Paper page
  27. Wang, B. Y., Zhao, A. S., Novick, R. P. & Muir, T. W. Activation and inhibition of the receptor histidine kinase AgrC occurs through opposite helical transduction motions. Mol. Cell 53, 929–940 (2014). · DOI · Paper page
  28. Koenig, R. L., Ray, J. L., Maleki, S. J., Smeltzer, M. S. & Hurlburt, B. K. Staphylococcus aureus AgrA binding to the RNAIII-agr regulatory region. J. Bacteriol. 186, 7549–7555 (2004). · DOI · Paper page
  29. Fechter, P., Caldelari, I., Lioliou, E. & Romby, P. Novel aspects of RNA regulation in Staphylococcus aureus. FEBS Lett. 588, 2523–2529 (2014). · DOI
  30. Lyon, G. J., Wright, J. S., Muir, T. W. & Novick, R. P. Key determinants of receptor activation in the agr autoinducing peptides of Staphylococcus aureus. Biochemistry 41, 10095–10104 (2002). · DOI · Paper page
  31. Hong, V., Presolski, S. I., Ma, C. & Finn, M. G. Analysis and optimization of copper-catalyzed azide-alkyne cycloaddition for bioconjugation. Angew. Chem. Int. Ed. 48, 9879–9883 (2009). · DOI · Paper page
  32. Emilsson, G. et al. Strongly stretched protein resistant poly(ethylene glycol) brushes prepared by grafting-to. ACS Appl. Mater. Inter. 7, 7505–7515 (2015). · doi:10.1021/acsami.5b01590
  33. Cisar, E. A., Geisinger, E., Muir, T. W. & Novick, R. P. Symmetric signalling within asymmetric dimers of the Staphylococcus aureus receptor histidine kinase AgrC. Mol. Microbiol. 74, 44–57 (2009). · DOI
  34. Vollmer, W., Blanot, D. & de Pedro, M. A. Peptidoglycan structure and architecture. FEMS Microbiol. Rev. 32, 149–167 (2008). · DOI · Paper page
  35. Traber, K. E. et al. Agr function in clinical Staphylococcus aureus isolates. Microbiology 154, 2265–2274 (2008). · DOI · Paper page
  36. Khodaparast, S., Kim, M. K., Silpe, J. & Stone, H. A. Bubble-driven detachment of bacteria from confined microgeometries. Environ. Sci. Technol. 51, 1340–1347 (2017). · doi:10.1021/acs.est.6b04369
  37. Vasilev, K., Cook, J. & Griesser, H. J. Antibacterial surfaces for biomedical devices. Expert Rev. Med. Devices 6, 553–567 (2009). · DOI · Paper page
  38. Gallo, J., Holinka, M. & Moucha, C. S. Antibacterial surface treatment for orthopaedic implants. Int. J. Mol. Sci. 15, 13849–13880 (2014). · DOI · Paper page
  39. Lee, J. J. et al. Synthetic ligand-coated magnetic nanoparticles for microfluidic bacterial separation from blood. Nano Lett. 14, 1–5 (2014). · DOI · Paper page
  40. Boles, B. R. & Horswill, A. R. agr-mediated dispersal of Staphylococcus aureus biofilms. PLoS Pathog. 4, e1000052 (2008). · DOI · Paper page
  41. Davies, D. Understanding biofilm resistance to antibacterial agents. Nat. Rev. Drug Discov. 2, 114–122 (2003). · DOI · Paper page
  42. Painter, K. L., Krishna, A., Wigneshweraraj, S. & Edwards, A. M. What role does the quorum-sensing accessory gene regulator system play during Staphylococcus aureus bacteremia? Trends Microbiol. 22, 676–685 (2014). · DOI
  43. Huycke, M. M., Spiegel, C. A. & Gilmore, M. S. Bacteremia caused by hemolytic, high-level gentamicin-resistant Enterococcus faecalis. Antimicrob. Agents Chemother. 35, 1626–1634 (1991). · DOI · Paper page
  44. Cook, L. C. & Federle, M. J. Peptide pheromone signaling in Streptococcus and Enterococcus. FEMS Microbiol. Rev. 38, 473–492 (2014). · DOI · Paper page
  45. Nakayama, J. et al. Development of a peptide antagonist against fsr quorum sensing of Enterococcus faecalis. ACS Chem. Biol. 8, 804–811 (2013). · DOI
  46. Gray, B., Hall, P. & Gresham, H. Targeting agr- and agr-like quorum sensing systems for development of common therapeutics to treat multiple Gram-positive bacterial infections. Sensors 13, 5130–5166 (2013). · DOI · Paper page
  47. Fujii, T. et al. Two homologous agr-like quorum-sensing systems cooperatively control adherence, cell morphology, and cell viability properties in Lactobacillus plantarum WCFS1. J. Bacteriol. 190, 7655–7665 (2008). · DOI
  48. Wang, I. N., Smith, D. L. & Young, R. Holins: the protein clocks of bacteriophage infections. Annu. Rev. Microbiol. 54, 799–825 (2000). · DOI · Paper page
  49. Goedhart, J. et al. Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%. Nat. Commun. 3, 751 (2012). · DOI · Paper page
  50. Nadell, C. D., Drescher, K., Wingreen, N. S. & Bassler, B. L. Extracellular matrix structure governs invasion resistance in bacterial biofilms. ISME J. 9, 1700–1709 (2015). · DOI · Paper page
  51. Chen, J., Yoong, P., Ram, G., Torres, V. J. & Novick, R. P. Single-copy vectors for integration at the SaPI1 attachment site for Staphylococcus aureus. Plasmid 76, 1–7 (2014). · DOI
  52. Lyon, G. J., Mayville, P., Muir, T. W. & Novick, R. P. Rational design of a global inhibitor of the virulence response in Staphylococcus aureus, based in part on localization of the site of inhibition to the receptor-histidine kinase, AgrC. Proc. Natl Acad. Sci. USA 97, 13330–13335 (2000). · DOI · Paper page
  53. Charpentier, E. et al. Novel cassette-based shuttle vector system for Gram-positive bacteria. Appl. Environ. Microbiol. 70, 6076–6085 (2004). · DOI · Paper page

Cited by

See all 130

Metadata

Authors
Kim, M. K., Zhao, A., Wang, A., Brown, Z. Z., Muir, T. W., Stone, H. A., & Bassler, B. L.
Venue
Nature Microbiology
Publisher
Springer Science and Business Media LLC
Published
2017-05-22
Volume
2
Issue
8
ISSN
2058-5276
DOI
10.1038/nmicrobiol.2017.80
Cited by
130
References
2
Language
en
Licence

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

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.