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Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems.

mBio

Culviner PH, Nocedal I, Fortune SM, Laub MT.
PMID: 34544284
mBio. 2021 Oct 26;12(5):e0201221. doi: 10.1128/mBio.02012-21. Epub 2021 Sep 21.

Toxin-antitoxin systems are widely distributed genetic modules typically featuring toxins that can inhibit bacterial growth and antitoxins that can reverse inhibition. Although Escherichia coli encodes 11 toxins with known or putative endoribonuclease activity, the targets of most of these...

Cite
Culviner PH, Nocedal I, Fortune SM, et al. Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems. mBio. 2021;12(5):e0201221doi: 10.1128/mBio.02012-21.
Culviner, P. H., Nocedal, I., Fortune, S. M., & Laub, M. T. (2021). Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems. mBio, 12(5), e0201221. https://doi.org/10.1128/mBio.02012-21
Culviner, Peter H, et al. "Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems." mBio vol. 12,5 (2021): e0201221. doi: https://doi.org/10.1128/mBio.02012-21
Culviner PH, Nocedal I, Fortune SM, Laub MT. Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems. mBio. 2021 Oct 26;12(5):e0201221. doi: 10.1128/mBio.02012-21. Epub 2021 Sep 21. PMID: 34544284; PMCID: PMC8546651.
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Clostridioides difficile - phage relationship the RNA way.

Current opinion in microbiology

Kreis V, Soutourina O.
PMID: 34922145
Curr Opin Microbiol. 2021 Dec 15;66:1-10. doi: 10.1016/j.mib.2021.11.012. Epub 2021 Dec 15.

Clostridioides difficile (formerly Clostridium difficile)-associated diarrhea is currently the most frequently occurring nosocomial diarrhea worldwide. During its infection cycle this pathogen needs to survive in phage-rich gut communities. Recent data strongly suggest that regulatory RNAs control gene expression in...

Cite
Kreis V, Soutourina O. Clostridioides difficile - phage relationship the RNA way. Curr Opin Microbiol. 2021;66:1-10doi: 10.1016/j.mib.2021.11.012.
Kreis, V., & Soutourina, O. (2021). Clostridioides difficile - phage relationship the RNA way. Current opinion in microbiology, 661-10. https://doi.org/10.1016/j.mib.2021.11.012
Kreis, Victor, and Soutourina, Olga. "Clostridioides difficile - phage relationship the RNA way." Current opinion in microbiology vol. 66 (2021): 1-10. doi: https://doi.org/10.1016/j.mib.2021.11.012
Kreis V, Soutourina O. Clostridioides difficile - phage relationship the RNA way. Curr Opin Microbiol. 2021 Dec 15;66:1-10. doi: 10.1016/j.mib.2021.11.012. Epub 2021 Dec 15. PMID: 34922145.
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A Primary Physiological Role of Toxin/Antitoxin Systems Is Phage Inhibition.

Frontiers in microbiology

Song S, Wood TK.
PMID: 32903830
Front Microbiol. 2020 Aug 13;11:1895. doi: 10.3389/fmicb.2020.01895. eCollection 2020.

Toxin/antitoxin (TA) systems are present in most prokaryote genomes. Toxins are almost exclusively proteins that reduce metabolism (but do not cause cell death), and antitoxins are either RNA or proteins that counteract the toxin or the RNA that encodes...

Cite
Song S, Wood TK. A Primary Physiological Role of Toxin/Antitoxin Systems Is Phage Inhibition. Front Microbiol. 2020;11:1895doi: 10.3389/fmicb.2020.01895.
Song, S., & Wood, T. K. (2020). A Primary Physiological Role of Toxin/Antitoxin Systems Is Phage Inhibition. Frontiers in microbiology, 111895. https://doi.org/10.3389/fmicb.2020.01895
Song, Sooyeon, and Wood, Thomas K. "A Primary Physiological Role of Toxin/Antitoxin Systems Is Phage Inhibition." Frontiers in microbiology vol. 11 (2020): 1895. doi: https://doi.org/10.3389/fmicb.2020.01895
Song S, Wood TK. A Primary Physiological Role of Toxin/Antitoxin Systems Is Phage Inhibition. Front Microbiol. 2020 Aug 13;11:1895. doi: 10.3389/fmicb.2020.01895. eCollection 2020. PMID: 32903830; PMCID: PMC7438911.
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Induced DNA bending by unique dimerization of HigA antitoxin.

IUCrJ

Park JY, Kim HJ, Pathak C, Yoon HJ, Kim DH, Park SJ, Lee BJ.
PMID: 32695421
IUCrJ. 2020 Jun 26;7:748-760. doi: 10.1107/S2052252520006466. eCollection 2020 Jul 01.

The bacterial toxin-antitoxin (TA) system regulates cell growth under various environmental stresses.

Cite
Park JY, Kim HJ, Pathak C, et al. Induced DNA bending by unique dimerization of HigA antitoxin. IUCrJ. 2020;7:748-760doi: 10.1107/S2052252520006466.
Park, J. Y., Kim, H. J., Pathak, C., Yoon, H. J., Kim, D. H., Park, S. J., & Lee, B. J. (2020). Induced DNA bending by unique dimerization of HigA antitoxin. IUCrJ, 7748-760. https://doi.org/10.1107/S2052252520006466
Park, Jin-Young, et al. "Induced DNA bending by unique dimerization of HigA antitoxin." IUCrJ vol. 7 (2020): 748-760. doi: https://doi.org/10.1107/S2052252520006466
Park JY, Kim HJ, Pathak C, Yoon HJ, Kim DH, Park SJ, Lee BJ. Induced DNA bending by unique dimerization of HigA antitoxin. IUCrJ. 2020 Jun 26;7:748-760. doi: 10.1107/S2052252520006466. eCollection 2020 Jul 01. PMID: 32695421; PMCID: PMC7340258.
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Clostridioides difficile - phage relationship the RNA way.

Current opinion in microbiology

Kreis V, Soutourina O.
PMID: 34922145
Curr Opin Microbiol. 2021 Dec 15;66:1-10. doi: 10.1016/j.mib.2021.11.012. Epub 2021 Dec 15.

Clostridioides difficile (formerly Clostridium difficile)-associated diarrhea is currently the most frequently occurring nosocomial diarrhea worldwide. During its infection cycle this pathogen needs to survive in phage-rich gut communities. Recent data strongly suggest that regulatory RNAs control gene expression in...

Cite
Kreis V, Soutourina O. Clostridioides difficile - phage relationship the RNA way. Curr Opin Microbiol. 2021;66:1-10doi: 10.1016/j.mib.2021.11.012.
Kreis, V., & Soutourina, O. (2021). Clostridioides difficile - phage relationship the RNA way. Current opinion in microbiology, 661-10. https://doi.org/10.1016/j.mib.2021.11.012
Kreis, Victor, and Soutourina, Olga. "Clostridioides difficile - phage relationship the RNA way." Current opinion in microbiology vol. 66 (2021): 1-10. doi: https://doi.org/10.1016/j.mib.2021.11.012
Kreis V, Soutourina O. Clostridioides difficile - phage relationship the RNA way. Curr Opin Microbiol. 2021 Dec 15;66:1-10. doi: 10.1016/j.mib.2021.11.012. Epub 2021 Dec 15. PMID: 34922145.
Copy Download .nbib Format: NLM
Clostridioides difficile - phage relationship the RNA way.

Current opinion in microbiology

Kreis V, Soutourina O.
PMID: 34922145
Curr Opin Microbiol. 2021 Dec 15;66:1-10. doi: 10.1016/j.mib.2021.11.012. Epub 2021 Dec 15.

Clostridioides difficile (formerly Clostridium difficile)-associated diarrhea is currently the most frequently occurring nosocomial diarrhea worldwide. During its infection cycle this pathogen needs to survive in phage-rich gut communities. Recent data strongly suggest that regulatory RNAs control gene expression in...

Cite
Kreis V, Soutourina O. Clostridioides difficile - phage relationship the RNA way. Curr Opin Microbiol. 2021;66:1-10doi: 10.1016/j.mib.2021.11.012.
Kreis, V., & Soutourina, O. (2021). Clostridioides difficile - phage relationship the RNA way. Current opinion in microbiology, 661-10. https://doi.org/10.1016/j.mib.2021.11.012
Kreis, Victor, and Soutourina, Olga. "Clostridioides difficile - phage relationship the RNA way." Current opinion in microbiology vol. 66 (2021): 1-10. doi: https://doi.org/10.1016/j.mib.2021.11.012
Kreis V, Soutourina O. Clostridioides difficile - phage relationship the RNA way. Curr Opin Microbiol. 2021 Dec 15;66:1-10. doi: 10.1016/j.mib.2021.11.012. Epub 2021 Dec 15. PMID: 34922145.
Copy Download .nbib Format: NLM
Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems.

mBio

Culviner PH, Nocedal I, Fortune SM, Laub MT.
PMID: 34544284
mBio. 2021 Oct 26;12(5):e0201221. doi: 10.1128/mBio.02012-21. Epub 2021 Sep 21.

Toxin-antitoxin systems are widely distributed genetic modules typically featuring toxins that can inhibit bacterial growth and antitoxins that can reverse inhibition. Although Escherichia coli encodes 11 toxins with known or putative endoribonuclease activity, the targets of most of these...

Cite
Culviner PH, Nocedal I, Fortune SM, et al. Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems. mBio. 2021;12(5):e0201221doi: 10.1128/mBio.02012-21.
Culviner, P. H., Nocedal, I., Fortune, S. M., & Laub, M. T. (2021). Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems. mBio, 12(5), e0201221. https://doi.org/10.1128/mBio.02012-21
Culviner, Peter H, et al. "Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems." mBio vol. 12,5 (2021): e0201221. doi: https://doi.org/10.1128/mBio.02012-21
Culviner PH, Nocedal I, Fortune SM, Laub MT. Global Analysis of the Specificities and Targets of Endoribonucleases from Escherichia coli Toxin-Antitoxin Systems. mBio. 2021 Oct 26;12(5):e0201221. doi: 10.1128/mBio.02012-21. Epub 2021 Sep 21. PMID: 34544284; PMCID: PMC8546651.
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What Is the Link between Stringent Response, Endoribonuclease Encoding Type II Toxin-Antitoxin Systems and Persistence?.

Frontiers in microbiology

Ramisetty BC, Ghosh D, Roy Chowdhury M, Santhosh RS.
PMID: 27933045
Front Microbiol. 2016 Nov 23;7:1882. doi: 10.3389/fmicb.2016.01882. eCollection 2016.

Persistence is a transient and non-inheritable tolerance to antibiotics by a small fraction of a bacterial population. One of the proposed determinants of bacterial persistence is toxin-antitoxin systems (TASs) which are also implicated in a wide range of stress-related...

Cite
Ramisetty BC, Ghosh D, Roy Chowdhury M, et al. What Is the Link between Stringent Response, Endoribonuclease Encoding Type II Toxin-Antitoxin Systems and Persistence?. Front Microbiol. 2016;7:1882doi: 10.3389/fmicb.2016.01882.
Ramisetty, B. C., Ghosh, D., Roy Chowdhury, M., & Santhosh, R. S. (2016). What Is the Link between Stringent Response, Endoribonuclease Encoding Type II Toxin-Antitoxin Systems and Persistence?. Frontiers in microbiology, 71882. https://doi.org/10.3389/fmicb.2016.01882
Ramisetty, Bhaskar C M, et al. "What Is the Link between Stringent Response, Endoribonuclease Encoding Type II Toxin-Antitoxin Systems and Persistence?." Frontiers in microbiology vol. 7 (2016): 1882. doi: https://doi.org/10.3389/fmicb.2016.01882
Ramisetty BC, Ghosh D, Roy Chowdhury M, Santhosh RS. What Is the Link between Stringent Response, Endoribonuclease Encoding Type II Toxin-Antitoxin Systems and Persistence?. Front Microbiol. 2016 Nov 23;7:1882. doi: 10.3389/fmicb.2016.01882. eCollection 2016. PMID: 27933045; PMCID: PMC5120126.
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The pharmaceuticalisation of security: Molecular biomedicine, antiviral stockpiles, and global health security.

Review of international studies

Elbe S.
PMID: 27570356
Rev Int Stud. 2014 Dec;40(5):919-938. doi: 10.1017/S0260210514000151.

Pharmaceuticals are now critical to the security of populations. Antivirals, antibiotics, next-generation vaccines, and antitoxins are just some of the new 'medical countermeasures' that governments are stockpiling in order to defend their populations against the threat of pandemics and...

Cite
Elbe S. The pharmaceuticalisation of security: Molecular biomedicine, antiviral stockpiles, and global health security. Rev Int Stud. 2014;40(5):919-938doi: 10.1017/S0260210514000151.
Elbe, S. (2014). The pharmaceuticalisation of security: Molecular biomedicine, antiviral stockpiles, and global health security. Review of international studies, 40(5), 919-938. https://doi.org/10.1017/S0260210514000151
Elbe, Stefan. "The pharmaceuticalisation of security: Molecular biomedicine, antiviral stockpiles, and global health security." Review of international studies vol. 40,5 (2014): 919-938. doi: https://doi.org/10.1017/S0260210514000151
Elbe S. The pharmaceuticalisation of security: Molecular biomedicine, antiviral stockpiles, and global health security. Rev Int Stud. 2014 Dec;40(5):919-938. doi: 10.1017/S0260210514000151. PMID: 27570356; PMCID: PMC4983762.
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Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing.

Nature chemical biology

Grabe GJ, Giorgio RT, Hall AMJ, Morgan RML, Dubois L, Sisley TA, Rycroft JA, Hare SA, Helaine S.
PMID: 34556858
Nat Chem Biol. 2021 Dec;17(12):1296-1304. doi: 10.1038/s41589-021-00862-y. Epub 2021 Sep 23.

Toxin-antitoxin (TA) systems are a large family of genes implicated in the regulation of bacterial growth and its arrest in response to attacks. These systems encode nonsecreted toxins and antitoxins that specifically pair, even when present in several paralogous...

Cite
Grabe GJ, Giorgio RT, Hall AMJ, et al. Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing. Nat Chem Biol. 2021;17(12):1296-1304doi: 10.1038/s41589-021-00862-y.
Grabe, G. J., Giorgio, R. T., Hall, A. M. J., Morgan, R. M. L., Dubois, L., Sisley, T. A., Rycroft, J. A., Hare, S. A., & Helaine, S. (2021). Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing. Nature chemical biology, 17(12), 1296-1304. https://doi.org/10.1038/s41589-021-00862-y
Grabe, Grzegorz J, et al. "Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing." Nature chemical biology vol. 17,12 (2021): 1296-1304. doi: https://doi.org/10.1038/s41589-021-00862-y
Grabe GJ, Giorgio RT, Hall AMJ, Morgan RML, Dubois L, Sisley TA, Rycroft JA, Hare SA, Helaine S. Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing. Nat Chem Biol. 2021 Dec;17(12):1296-1304. doi: 10.1038/s41589-021-00862-y. Epub 2021 Sep 23. PMID: 34556858.
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Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems.

Frontiers in molecular biosciences

Chan WT, Espinosa M, Yeo CC.
PMID: 27047942
Front Mol Biosci. 2016 Mar 22;3:9. doi: 10.3389/fmolb.2016.00009. eCollection 2016.

In their initial stages of discovery, prokaryotic toxin-antitoxin (TA) systems were confined to bacterial plasmids where they function to mediate the maintenance and stability of usually low- to medium-copy number plasmids through the post-segregational killing of any plasmid-free daughter...

Cite
Chan WT, Espinosa M, Yeo CC. Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems. Front Mol Biosci. 2016;3:9doi: 10.3389/fmolb.2016.00009.
Chan, W. T., Espinosa, M., & Yeo, C. C. (2016). Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems. Frontiers in molecular biosciences, 39. https://doi.org/10.3389/fmolb.2016.00009
Chan, Wai Ting, et al. "Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems." Frontiers in molecular biosciences vol. 3 (2016): 9. doi: https://doi.org/10.3389/fmolb.2016.00009
Chan WT, Espinosa M, Yeo CC. Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems. Front Mol Biosci. 2016 Mar 22;3:9. doi: 10.3389/fmolb.2016.00009. eCollection 2016. PMID: 27047942; PMCID: PMC4803016.
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Structure, Evolution, and Functions of Bacterial Type III Toxin-Antitoxin Systems.

Toxins

Goeders N, Chai R, Chen B, Day A, Salmond GP.
PMID: 27690100
Toxins (Basel). 2016 Sep 28;8(10). doi: 10.3390/toxins8100282.

Toxin-antitoxin (TA) systems are small genetic modules that encode a toxin (that targets an essential cellular process) and an antitoxin that neutralises or suppresses the deleterious effect of the toxin. Based on the molecular nature of the toxin and...

Cite
Goeders N, Chai R, Chen B, et al. Structure, Evolution, and Functions of Bacterial Type III Toxin-Antitoxin Systems. Toxins (Basel). 2016;8(10)doi: 10.3390/toxins8100282.
Goeders, N., Chai, R., Chen, B., Day, A., & Salmond, G. P. (2016). Structure, Evolution, and Functions of Bacterial Type III Toxin-Antitoxin Systems. Toxins, 8(10), . https://doi.org/10.3390/toxins8100282
Goeders, Nathalie, et al. "Structure, Evolution, and Functions of Bacterial Type III Toxin-Antitoxin Systems." Toxins vol. 8,10 (2016). doi: https://doi.org/10.3390/toxins8100282
Goeders N, Chai R, Chen B, Day A, Salmond GP. Structure, Evolution, and Functions of Bacterial Type III Toxin-Antitoxin Systems. Toxins (Basel). 2016 Sep 28;8(10). doi: 10.3390/toxins8100282. PMID: 27690100; PMCID: PMC5086642.
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Showing 13 to 24 of 84 entries