Ultrasensitive Characterization of Native Bacterial Biofilms via Dynamic Nuclear Polarization‐Enhanced Solid‐State NMR
Open accessAbstract
Bacterial biofilms are major contributors to persistent infections and antimicrobial resistance, posing significant challenges to treatment. However, obtaining high‐resolution structural information on native bacterial biofilms has remained elusive due to the methodological limitations associated with analyzing complex biological samples. Solid‐state NMR (ssNMR) has shown promise in this regard, but its conventional application is hindered by sensitivity constraints for unlabeled samples. In this study, we utilized high‐sensitivity Dynamic Nuclear Polarization (DNP) ssNMR to characterize native Pseudomonas fluorescens colony biofilms. The ~75‐fold sensitivity enhancement provided by DNP enabled structural characterization without isotope labeling or chemical/physical modification. We successfully collected 1D 13 C/15 N, and 2D 1 H−13 C, 1 H−15 N and 13 C−13 C ssNMR spectra within seconds, minutes or hours, facilitating the identification and quantification of biofilm extracellular matrix (ECM) components. Additionally, DNP ssNMR allowed quantitative detection of both flexible and rigid biofilm components by favorable freezing conditions. This study represents the first application of ultrasensitive DNP ssNMR to characterize a native bacterial biofilm, significantly expanding the capabilities of ssNMR for analyzing the composition and structure of a wide array of in vitro and ex vivo biofilms. The versatility of this approach will accelerate structure‐guided efforts to combat infections caused by biofilm‐forming microbes.
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AsymPolPOK and other biradicals are small, water-soluble molecules that diffuse through porous cell walls without disrupting their structure.
“AsymPolPOK and other biradicals are small (2–3 nm), water-soluble molecules that diffuse through porous cell walls without disrupting their structure, enabling widespread use in the structural analysis of plant, fungal, algal, and bacterial cell wall materials as well as intact mammalian cells84–90.”
From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [87]
The Results and Discussion (page unavailable) report that AsymPol-POK was dissolved in a predominantly water-based buffer and was uniformly distributed within a wet bacterial biofilm. They do not establish its 2–3 nm size, diffusion through porous cell walls, or preservation of cell-wall structure after incubation; the micrographs showing intact bacteria were taken before radical incubation. The paper also does not extend those properties to other biradicals or the full range of organisms named in the citing sentence. (LLM, conf=0.84)
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Cites
Flemming, H.-C., & Wingender, J. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2415 · Cited by 10,137 · see citing works
Ceri, H., Olson, M. E., Stremick, C., Read, R. R., Morck, D., & Buret, A. (1999) · Journal of Clinical Microbiology · doi:10.1128/jcm.37.6.1771-1776.1999 · Cited by 2,155 · see citing works
Lewis, K. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.4.999-1007.2001 · Cited by 1,988 · see citing works
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00227471 · Cited by 1,635 · see citing works
Biofilm Matrixome: Extracellular Components in Structured Microbial Communities
Karygianni, L., Ren, Z. F., Koo, H., & Thurnheer, T. (2020) · Trends in Microbiology · doi:10.1016/j.tim.2020.03.016 · Cited by 1,515 · see citing works
The biofilm matrix: multitasking in a shared space
Flemming, H., van Hullebusch, E. D., Neu, T. R., Nielsen, P. H., Seviour, T. W., Stoodley, P., Wingender, J., & Wuertz, S. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00791-0 · Cited by 1,025 · see citing works
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211764 · Cited by 1,012 · see citing works
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
Tuttle, M. D., Comellas, G., Nieuwkoop, A. J., Covell, D. J., Berthold, D. A., Kloepper, K. D., Courtney, J. M., Kim, J. K., Barclay, A. M., Kendall, A. K., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3194 · Cited by 951 · see citing works
Amyloid fibers provide structural integrity to Bacillus subtilis biofilms
Romero, D., Aguilar, C., Losick, R. M., & Kolter, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910560107 · Cited by 793 · see citing works
Hohwy, M., JAKOBSEN, H. J., Edén, M., Levitt, M. H., & Nielsen, N. C. (1998) · The Journal of Chemical Physics · doi:10.1063/1.475661 · Cited by 559 · see citing works
Lignin-polysaccharide interactions in plant secondary cell walls revealed by solid-state NMR
Kang, X., Kirui, A., Widanage, M. C. D., Mentink-Vigier, F., Cosgrove, D., & Wang, T. (2019) · Nature Communications · doi:10.1038/s41467-018-08252-0 · Cited by 525 · see citing works
Self-citationFrequency-switched pulse sequences: Homonuclear decoupling and dilute spin NMR in solids
Bielecki, A., Kolbert, A. C., & Levitt, M. H. (1989) · Chemical Physics Letters · doi:10.1016/0009-2614(89)87166-0 · Cited by 485 · see citing works
Molecular architecture of fungal cell walls revealed by solid-state NMR
Kang, X., Kirui, A., Muszyński, A., Widanage, M. C. D., Chen, A., Azadi, P., Wang, P., Mentink-Vigier, F., & Wang, T. (2018) · Nature Communications · doi:10.1038/s41467-018-05199-0 · Cited by 356 · see citing works
Self-citationBajaj, V. S., Mak–Jurkauskas, M. L., Belenky, M., Herzfeld, J., & Griffin, R. G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900908106 · Cited by 330 · see citing works
Carbohydrate-aromatic interface and molecular architecture of lignocellulose
Kirui, A., Zhao, W., Deligey, F., Yang, H., Kang, X., Mentink-Vigier, F., & Wang, T. (2022) · Nature Communications · doi:10.1038/s41467-022-28165-3 · Cited by 290 · see citing works
Self-citationAmyloids — a functional coat for microorganisms
Gebbink, M. F. B. G., Claessen, D., Bouma, B., Dijkhuizen, L., & Wösten, H. A. B. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1127 · Cited by 287 · see citing works
ssNake: A cross-platform open-source NMR data processing and fitting application
van Meerten, S. G. J., Franssen, W. M. J., & Kentgens, A. P. M. (2019) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2019.02.006 · Cited by 286 · see citing works
Mak–Jurkauskas, M. L., Bajaj, V. S., Hornstein, M. K., Belenky, M., Griffin, R. G., & Herzfeld, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706156105 · Cited by 216 · see citing works
Inhibiting bacterial cooperation is an evolutionarily robust anti-biofilm strategy
Dieltjens, L., Appermans, K., Lissens, M., Lories, B., Kim, W., der Eycken, E. V. V., Foster, K. R., & Steenackers, H. P. L. (2020) · Nature Communications · doi:10.1038/s41467-019-13660-x · Cited by 207 · see citing works
Self-citationIn Situ Cryo-Electron Tomography: A Post-Reductionist Approach to Structural Biology
Asano, S. M., Engel, B. D., & Baumeister, W. P. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.09.030 · Cited by 198 · see citing works
Mentink‐Vigier, F., Paul, S., Lee, D. J., Feintuch, A., Hediger, S., Vega, S., & Paëpe, G. D. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp03457d · Cited by 190 · see citing works
Self-citationGhassemi, N., Poulhazan, A., Deligey, F., Mentink‐Vigier, F., Marcotte, I., & Wang, T. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00669 · Cited by 187 · see citing works
Self-citationJennings, L. K., Dreifus, J. E., Reichhardt, C., Storek, K. M., Secor, P. R., Wozniak, D. J., Hisert, K. B., & Parsek, M. R. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108782 · Cited by 173 · see citing works
Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR
Romaniuk, J. A. H., & Cegelski, L. (2015) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2015.0024 · Cited by 171 · see citing works
Dynamic Nuclear Polarization of Deuterated Proteins
Akbey, Ü., Franks, W. T., Linden, A., Lange, S., Griffin, R. G., van Rossum, B., & Oschkinat, H. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201002044 · Cited by 171 · see citing works
Self-citationMentink-Vigier, F., Marin-Montesinos, I., Jagtap, A. P., Halbritter, T., van Tol, J., Hediger, S., Lee, D., Sigurdsson, S. T., & De Paëpe, G. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b04911 · Cited by 171 · see citing works
Self-citationCell morphology drives spatial patterning in microbial communities
Smith, W. P. J., Davit, Y., Osborne, J. M., Kim, W., Foster, K. R., & Pitt‐Francis, J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613007114 · Cited by 159 · see citing works
Self-citationImportance of positioning for microbial evolution
Kim, W., Racimo, F., Schlüter, J., Levy, S. B., & Foster, K. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323632111 · Cited by 150 · see citing works
Self-citationSensitivity-Enhanced NMR Reveals Alterations in Protein Structure by Cellular Milieus
Frederick, K. K., Michaelis, V. K., Corzilius, B., Ong, T., Jacavone, A. C., Griffin, R. G., & Lindquist, S. L. (2015) · Cell · doi:10.1016/j.cell.2015.09.024 · Cited by 149 · see citing works
Takahashi, H., Ayala, I., Bardet, M., De Paëpe, G., Simorre, J.-P., & Hediger, S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja312501d · Cited by 149 · see citing works
Structural changes of TasA in biofilm formation of Bacillus subtilis
Diehl, A., Roske, Y., Ball, L., Chowdhury, A., Hiller, M., Molière, N., Kramer, R., Friedrich, D., Worth, C. L., Schlegel, B., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718102115 · Cited by 144 · see citing works
Self-citationDNP NMR of biomolecular assemblies
Jaudzems, K., Polenova, T. E., Pintacuda, G., Oschkinat, H., & Lesage, A. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.09.011 · Cited by 96 · see citing works
Bacterial biofilms in the human body: prevalence and impacts on health and disease
Perry, E. K., & Tan, M. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1237164 · Cited by 95 · see citing works
Reichhardt, C., Ferreira, J. A. G., Joubert, L., Clemons, K. V., Stevens, D. A., & Cegelski, L. (2015) · Eukaryotic Cell · doi:10.1128/ec.00050-15 · Cited by 91 · see citing works
Influenza A surface glycosylation and vaccine design
Wu, C., Lin, C.-W., Tsai, T.-I., Lee, C.-C. D., Chuang, H.-Y., Chen, J.-B., Tsai, M.-H., Chen, B.-R., Lo, P.-W., Liu, C.-P., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617174114 · Cited by 91 · see citing works
Structural Biology outside the box — inside the cell
Plitzko, J. M., Schuler, B., & Selenko, P. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.06.007 · Cited by 90 · see citing works
Functional amyloids from bacterial biofilms – structural properties and interaction partners
Akbey, Ü., & Andreasen, M. (2022) · Chemical Science · doi:10.1039/d2sc00645f · Cited by 87 · see citing works
Self-citationChow, W. Y., De Paëpe, G., & Hediger, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01043 · Cited by 87 · see citing works
Structural analysis and architectural principles of the bacterial amyloid curli
Sleutel, M., Pradhan, B., Volkov, A. N., & Remaut, H. K. (2023) · Nature Communications · doi:10.1038/s41467-023-38204-2 · Cited by 85 · see citing works
Rapid radiation in bacteria leads to a division of labour
Kim, W., Levy, S. B., & Foster, K. R. (2016) · Nature Communications · doi:10.1038/ncomms10508 · Cited by 82 · see citing works
Self-citationElkins, M. R., Sergeyev, I. V., & Hong, M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09658 · Cited by 73 · see citing works
Highly Efficient Polarizing Agents for MAS‐DNP of Proton‐Dense Molecular Solids
Harrabi, R., Halbritter, T., Aussenac, F., Dakhlaoui, O., van Tol, J., Damodaran, K. K., Lee, D. J., Paul, S., Hediger, S., Mentink‐Vigier, F., et al. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202114103 · Cited by 72 · see citing works
Self-citationIn-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells
Ghosh, R., Xiao, Y., Kragelj, J., & Frederick, K. K. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c06680 · Cited by 66 · see citing works
CCMRD: a solid-state NMR database for complex carbohydrates
Kang, X., Zhao, W.-C., Widanage, M. C. D., Kirui, A., Ozdenvar, U., & Wang, T. (2020) · Journal of Biomolecular NMR · doi:10.1007/s10858-020-00304-2 · Cited by 64 · see citing works
Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency
Bougault, C., Ayala, I., Vollmer, W., Simorre, J., & Schanda, P. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.07.009 · Cited by 60 · see citing works
Cegelski, L., Steuber, D., Mehta, A. K., Kulp, D. W., Axelsen, P. H., & Schaefer, J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.040 · Cited by 58 · see citing works
Biofilm aggregates and the host airway-microbial interface
Hall‐Stoodley, L., & McCoy, K. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.969326 · Cited by 50 · see citing works
Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR
Lange, S., Franks, W. T., Rajagopalan, N., Döring, K., Geiger, M., Linden, A., van Rossum, B., Krämer, G., Bukau, B., & Oschkinat, H. (2016) · Science Advances · doi:10.1126/sciadv.1600379 · Cited by 47 · see citing works
Characterization of the Vibrio cholerae extracellular matrix: A top-down solid-state NMR approach
Reichhardt, C., Fong, J. C. N., Yildiz, F. H., & Cegelski, L. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.05.030 · Cited by 45 · see citing works
Comparative Genomics of the Rhodococcus Genus Shows Wide Distribution of Biodegradation Traits
Garrido‐Sanz, D., Redondo‐Nieto, M., Martín, M., & Rivilla, R. (2020) · Microorganisms · doi:10.3390/microorganisms8050774 · Cited by 45 · see citing works
Romaniuk, J. A. H., & Cegelski, L. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00495 · Cited by 45 · see citing works
Nygaard, R., Romaniuk, J. A. H., Rice, D. M., & Cegelski, L. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.01.037 · Cited by 44 · see citing works
Characterization of the Peptidoglycan of Vancomycin-Susceptible Enterococcus faecium
Patti, G. J., Kim, S. J., & Schaefer, J. (2008) · Biochemistry · doi:10.1021/bi8008032 · Cited by 41 · see citing works
Frequency-Swept Integrated and Stretched Solid Effect Dynamic Nuclear Polarization
Can, T. V., McKay, J. E., Weber, R. T., Yang, C., Dubroca, T., van Tol, J., Hill, S., & Griffin, R. G. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.8b01002 · Cited by 39 · see citing works
In-Cell Quantification of Drugs by Magic-Angle Spinning Dynamic Nuclear Polarization NMR
Bertarello, A., Berruyer, P., Artelsmair, M., Elmore, C. S., Heydarkhan‐Hagvall, S., Schade, M., Chiarparin, E., Schantz, S., & Emsley, L. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c12442 · Cited by 38 · see citing works
Singewald, K., Lawless, M. J., & Saxena, S. (2018) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2018.12.005 · Cited by 35 · see citing works
Blanco-Romero, E., Garrido‐Sanz, D., Rivilla, R., Redondo‐Nieto, M., & Martín, M. (2020) · Microorganisms · doi:10.3390/microorganisms8111740 · Cited by 35 · see citing works
When Small becomes Too Big: Expanding the Use of In‐Cell Solid‐State NMR Spectroscopy
Narasimhan, S., Folkers, G. E., & Baldus, M. (2020) · ChemPlusChem · doi:10.1002/cplu.202000167 · Cited by 32 · see citing works
Structural insight into Escherichia coli CsgA amyloid fibril assembly
Bu, F., Dee, D. R., & Liu, B. (2024) · mBio · doi:10.1128/mbio.00419-24 · Cited by 32 · see citing works
Structure of biofilm-forming functional amyloid PSMα1 from Staphylococcus aureus
Hansen, K. H., Byeon, C., Liu, Q., Drace, T., Boesen, T. P., Conway, J. F., Andreasen, M., & Akbey, Ü. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2406775121 · Cited by 31 · see citing works
Self-citationJeffries, J., Thongsomboon, W., Visser, J. A., Enriquez, K. T., Yager, D., & Cegelski, L. (2020) · Biopolymers · doi:10.1002/bip.23395 · Cited by 31 · see citing works
Fast MAS 1H–13C correlation NMR for structural investigations of plant cell walls
Phyo, P., & Hong, M. (2019) · Journal of Biomolecular NMR · doi:10.1007/s10858-019-00277-x · Cited by 26 · see citing works
Chatterjee, S., Venkatesh, A., Sigurdsson, S. T., & Mentink‐Vigier, F. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.3c03472 · Cited by 26 · see citing works
Self-citationSolid State NMR Studies of Intact Lipopolysaccharide Endotoxin
Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi, A., Molinaro, A., & Simorre, J. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00271 · Cited by 25 · see citing works
TapA acts as specific chaperone in TasA filament formation by strand complementation
Roske, Y., Lindemann, F., Diehl, A., Cremer, N., Higman, V. A., Schlegel, B., Leidert, M., Driller, K., Turgay, K., Schmieder, P., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217070120 · Cited by 24 · see citing works
Vallet, A., Ayala, I., Perrone, B., Hassan, A., Simorre, J., Bougault, C., & Schanda, P. (2024) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2024.107708 · Cited by 24 · see citing works
Reichhardt, C., Joubert, L., Clemons, K. V., Stevens, D. A., & Cegelski, L. (2018) · Medical Mycology · doi:10.1093/mmy/myy140 · Cited by 23 · see citing works
Xiao, Y., Ghosh, R., & Frederick, K. K. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.789478 · Cited by 21 · see citing works
Bastos, R., Marín-Montesinos, I., Ferreira, S. S., Mentink‐Vigier, F., Sardo, M., Mafra, L., Coimbra, M. A., & Coelho, E. (2023) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2023.121475 · Cited by 21 · see citing works
Self-citationByeon, C., Kinney, T., Saricayir, H., Srinivasa, S., Wells, M. K., Kim, W., & Akbey, Ü. (2023) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2023.107587 · Cited by 14 · see citing works
Self-citationMicrobiology catches the cryo-EM bug
Earl, L. A., Falconieri, V., & Subramaniam, S. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2018.02.012 · Cited by 12 · see citing works
Evans, A. F., Wells, M. K., Denk, J., Mazza, W., Santos, R., Delprince, A., & Kim, W. (2022) · Journal of Bacteriology · doi:10.1128/jb.00285-22 · Cited by 9 · see citing works
Self-citationKessler, C., & Kim, W. (2022) · mSystems · doi:10.1128/msystems.00737-22 · Cited by 6 · see citing works
Self-citationSensitivity-Enhanced Dnp NMR for In Situ Structural Biology
Frederick, K. K. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2018.11.1119 · Cited by 3 · see citing works
Dissecting the Bacterial Cell Wall with Solid-State NMR
Romaniuk, J. A. H., & Cegelski, L. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.885 · Cited by 2 · see citing works
Flagged first, then by citations
Research works printed but not linked: 5
- Murray C. J., 2022, Lancet
- Kang X., 2019, Nat. Commun., 10
- Byeon C.-H., 2024, bioRxiv, 2024.2005.2028.
- Kim W., 2016, Nat. Commun., 7
- Kang X., 2018, Nat. Commun., 9
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Dickwella Widanage, M. C., Singh, K., Li, J., Yarava, J. R., Scott, F. J., Xu, Y., Gow, N. A. R., Mentink-Vigier, F., Wang, P., Lamoth, F., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61678-1 · Cited by 51 · see citing works
Self-citationLiu, Y., Gao, L., & Yu, Z. (2025) · Applied Sciences · doi:10.3390/app15105246 · Cited by 21 · see citing works
Yarava, J. R., Gautam, I., Jacob, A., Fu, R., & Wang, T. (2025) · bioRxiv · doi:10.1021/jacs.5c04054 · Cited by 21 · see citing works
α-Glucan Remodeling by GH13-Domain Enzymes Shapes Fungal Cell Wall Architecture
Jacob, A., Willet, A. H., Igarashi, M. G., Nokab, M. E. H. E., Turner, L. A., Alsanad, A., Wang, T., & Gould, K. (2025) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2505509122 · Cited by 19 · see citing works
Byeon, C., Wang, Y.-H., Tunc, A., Franks, W. T., DePas, W. H., & Akbey, Ü. (2026) · Solid State Nuclear Magnetic Resonance · doi:10.1016/j.ssnmr.2026.102128 · Cited by 4 · see citing works
Self-citationGautam, I., Valdés-Muñoz, G., Karai, A., Paul-Latge, J., Pérez‐Llano, Y., Gunde‐Cimerman, N., Batista‐García, R. A., & Wang, T. (2026) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2026.125157
A Stepwise Approach to Biofilm Detection Using Nuclear Magnetic Resonance
Abirami, K. (2026) · Springer protocols handbooks/Springer protocols · doi:10.1007/978-1-0716-5535-1_19
- Authors
- Byeon, C., Kinney, T., Saricayir, H., Holst Hansen, K., Scott, F. J., Srinivasa, S., Wells, M. K., Mentink‐Vigier, F., Kim, W., & Akbey, Ü.
- Affiliations
- University of Pittsburgh (US)
- Department of Structural Biology School of Medicine University of Pittsburgh Pittsburgh PA 15261 USA
- Florida State University (US)
- Duquesne University (US)
- National High Magnetic Field Laboratory Florida State University Tallahassee FL 32310 USA
- Corresponding author
- Akbey, Ümit
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2025-01-15
- Volume
- 64
- Issue
- 12
- Pages
- e202418146-e202418146
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- PMC
- PMC11919551
- OpenAlex
- W4406143038
- Cited by
- 7
- References
- 76
- Citations by year
- 2026: 3 · 2025: 4
- FWCI
- 1.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Angewandte Chemie International Edition (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed Central (submittedVersion)
- Scopus (Elsevier) (submittedVersion, other-oa)
- Funders
- National Science Foundation (DMR-1,644,779, 1644779, 2128556)
- Florida State University (DMR-1644779)
- University of Pittsburgh
- National High Magnetic Field Laboratory (DMR - 1644779, 1644779, DMR-2128556)
- National Institutes of Health (1r15gm132856-01a1, GM122698)
- National Institute of General Medical Sciences (GM148766, R15 GM132856, P41GM122698, GM122698, 1R15GM132856, RM1GM148766)
- Division of Materials Research (DMR-2128556, 1644779, DMR- 1644779, 2128556)
- High Magnetic Field Laboratory, Chinese Academy of Sciences
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
- Physical Sciences › Physics and Astronomy › Nuclear and High Energy Physics › NMR spectroscopy and applications
- Keywords
- bacterial biofilms, dynamic nuclear polarization, solid-state NMR, Pseudomonas fluorescens, extracellular matrix, biofilm structure, 13C and 15N labeling, biofilm composition
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 ›
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