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Predicted Cellular Interactors of the Endogenous Retrovirus-K Integrase Enzyme.

Microorganisms

Benoit I, Brownell S, Douville RN.
PMID: 34361946
Microorganisms. 2021 Jul 14;9(7). doi: 10.3390/microorganisms9071509.

Integrase (IN) enzymes are found in all retroviruses and are crucial in the retroviral integration process. Many studies have revealed how exogenous IN enzymes, such as the human immunodeficiency virus (HIV) IN, contribute to altered cellular function. However, the...

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Benoit I, Brownell S, Douville RN. Predicted Cellular Interactors of the Endogenous Retrovirus-K Integrase Enzyme. Microorganisms. 2021;9(7)doi: 10.3390/microorganisms9071509.
Benoit, I., Brownell, S., & Douville, R. N. (2021). Predicted Cellular Interactors of the Endogenous Retrovirus-K Integrase Enzyme. Microorganisms, 9(7), . https://doi.org/10.3390/microorganisms9071509
Benoit, Ilena, et al. "Predicted Cellular Interactors of the Endogenous Retrovirus-K Integrase Enzyme." Microorganisms vol. 9,7 (2021). doi: https://doi.org/10.3390/microorganisms9071509
Benoit I, Brownell S, Douville RN. Predicted Cellular Interactors of the Endogenous Retrovirus-K Integrase Enzyme. Microorganisms. 2021 Jul 14;9(7). doi: 10.3390/microorganisms9071509. PMID: 34361946; PMCID: PMC8303831.
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Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments.

Environmental pollution (Barking, Essex : 1987)

Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G.
PMID: 34974089
Environ Pollut. 2021 Dec 30;297:118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30.

Wastewater treatment plants (WWTPs) are among the main hotspots of antibiotic resistance genes (ARGs) in the environment. Previously, we demonstrated that, by increasing anthropogenic pollution, the antibiotic resistome persisted in the microbial community of rivers and lakes, independently by...

Cite
Di Cesare A, Sabatino R, Yang Y, et al. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021;297:118774doi: 10.1016/j.envpol.2021.118774.
Di Cesare, A., Sabatino, R., Yang, Y., Brambilla, D., Li, P., Fontaneto, D., Eckert, E. M., & Corno, G. (2021). Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environmental pollution (Barking, Essex : 1987), 297118774. https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare, Andrea, et al. "Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments." Environmental pollution (Barking, Essex : 1987) vol. 297 (2021): 118774. doi: https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021 Dec 30;297:118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30. PMID: 34974089.
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Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments.

Environmental pollution (Barking, Essex : 1987)

Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G.
PMID: 34974089
Environ Pollut. 2021 Dec 30;297:118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30.

Wastewater treatment plants (WWTPs) are among the main hotspots of antibiotic resistance genes (ARGs) in the environment. Previously, we demonstrated that, by increasing anthropogenic pollution, the antibiotic resistome persisted in the microbial community of rivers and lakes, independently by...

Cite
Di Cesare A, Sabatino R, Yang Y, et al. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021;297:118774doi: 10.1016/j.envpol.2021.118774.
Di Cesare, A., Sabatino, R., Yang, Y., Brambilla, D., Li, P., Fontaneto, D., Eckert, E. M., & Corno, G. (2021). Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environmental pollution (Barking, Essex : 1987), 297118774. https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare, Andrea, et al. "Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments." Environmental pollution (Barking, Essex : 1987) vol. 297 (2021): 118774. doi: https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021 Dec 30;297:118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30. PMID: 34974089.
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Use of orthogonal serine integrases to multiplex plasmid conjugation and integration from .

Access microbiology

Gao H, Smith MCM.
PMID: 35024553
Access Microbiol. 2021 Dec 08;3(12):000291. doi: 10.1099/acmi.0.000291. eCollection 2021.

Some major producers of useful bioactive natural products belong to the genus

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Gao H, Smith MCM. Use of orthogonal serine integrases to multiplex plasmid conjugation and integration from . Access Microbiol. 2021;3(12):000291doi: 10.1099/acmi.0.000291.
Gao, H., & Smith, M. C. M. (2021). Use of orthogonal serine integrases to multiplex plasmid conjugation and integration from . Access microbiology, 3(12), 000291. https://doi.org/10.1099/acmi.0.000291
Gao, Hong, and Smith, Margaret C M. "Use of orthogonal serine integrases to multiplex plasmid conjugation and integration from ." Access microbiology vol. 3,12 (2021): 000291. doi: https://doi.org/10.1099/acmi.0.000291
Gao H, Smith MCM. Use of orthogonal serine integrases to multiplex plasmid conjugation and integration from . Access Microbiol. 2021 Dec 08;3(12):000291. doi: 10.1099/acmi.0.000291. eCollection 2021. PMID: 35024553; PMCID: PMC8749152.
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Metagenomic strategies identify diverse integron-integrase and antibiotic resistance genes in the Antarctic environment.

MicrobiologyOpen

Antelo V, Giménez M, Azziz G, Valdespino-Castillo P, Falcón LI, Ruberto LAM, Mac Cormack WP, Mazel D, Batista S.
PMID: 34713606
Microbiologyopen. 2021 Oct;10(5):e1219. doi: 10.1002/mbo3.1219.

The objective of this study is to identify and analyze integrons and antibiotic resistance genes (ARGs) in samples collected from diverse sites in terrestrial Antarctica. Integrons were studied using two independent methods. One involved the construction and analysis of...

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Antelo V, Giménez M, Azziz G, et al. Metagenomic strategies identify diverse integron-integrase and antibiotic resistance genes in the Antarctic environment. Microbiologyopen. 2021;10(5):e1219doi: 10.1002/mbo3.1219.
Antelo, V., Giménez, M., Azziz, G., Valdespino-Castillo, P., Falcón, L. I., Ruberto, L. A. M., Mac Cormack, W. P., Mazel, D., & Batista, S. (2021). Metagenomic strategies identify diverse integron-integrase and antibiotic resistance genes in the Antarctic environment. MicrobiologyOpen, 10(5), e1219. https://doi.org/10.1002/mbo3.1219
Antelo, Verónica, et al. "Metagenomic strategies identify diverse integron-integrase and antibiotic resistance genes in the Antarctic environment." MicrobiologyOpen vol. 10,5 (2021): e1219. doi: https://doi.org/10.1002/mbo3.1219
Antelo V, Giménez M, Azziz G, Valdespino-Castillo P, Falcón LI, Ruberto LAM, Mac Cormack WP, Mazel D, Batista S. Metagenomic strategies identify diverse integron-integrase and antibiotic resistance genes in the Antarctic environment. Microbiologyopen. 2021 Oct;10(5):e1219. doi: 10.1002/mbo3.1219. PMID: 34713606; PMCID: PMC8435808.
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Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments.

Environmental pollution (Barking, Essex : 1987)

Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G.
PMID: 34974089
Environ Pollut. 2021 Dec 30;118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30.

Wastewater treatment plants (WWTPs) are among the main hotspots of antibiotic resistance genes (ARGs) in the environment. Previously, we demonstrated that by increasing anthropogenic pollution the antibiotic resistome persisted in the microbial community of rivers and lakes, independently by...

Cite
Di Cesare A, Sabatino R, Yang Y, et al. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021;118774doi: 10.1016/j.envpol.2021.118774.
Di Cesare, A., Sabatino, R., Yang, Y., Brambilla, D., Li, P., Fontaneto, D., Eckert, E. M., & Corno, G. (2021). Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environmental pollution (Barking, Essex : 1987), 118774. https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare, Andrea, et al. "Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments." Environmental pollution (Barking, Essex : 1987) vol. (2021): 118774. doi: https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021 Dec 30;118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30. PMID: 34974089.
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Prototype Foamy Virus Integrase Displays Unique Biochemical Activities among Retroviral Integrases.

Biomolecules

Rabe AJ, Tan YY, Larue RC, Yoder KE.
PMID: 34944553
Biomolecules. 2021 Dec 20;11(12). doi: 10.3390/biom11121910.

Integrases of different retroviruses assemble as functional complexes with varying multimers of the protein. Retroviral integrases require a divalent metal cation to perform one-step transesterification catalysis. Tetrameric prototype foamy virus (PFV) intasomes assembled from purified integrase and viral DNA...

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Rabe AJ, Tan YY, Larue RC, et al. Prototype Foamy Virus Integrase Displays Unique Biochemical Activities among Retroviral Integrases. Biomolecules. 2021;11(12)doi: 10.3390/biom11121910.
Rabe, A. J., Tan, Y. Y., Larue, R. C., & Yoder, K. E. (2021). Prototype Foamy Virus Integrase Displays Unique Biochemical Activities among Retroviral Integrases. Biomolecules, 11(12), . https://doi.org/10.3390/biom11121910
Rabe, Anthony J, et al. "Prototype Foamy Virus Integrase Displays Unique Biochemical Activities among Retroviral Integrases." Biomolecules vol. 11,12 (2021). doi: https://doi.org/10.3390/biom11121910
Rabe AJ, Tan YY, Larue RC, Yoder KE. Prototype Foamy Virus Integrase Displays Unique Biochemical Activities among Retroviral Integrases. Biomolecules. 2021 Dec 20;11(12). doi: 10.3390/biom11121910. PMID: 34944553.
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Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments.

Environmental pollution (Barking, Essex : 1987)

Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G.
PMID: 34974089
Environ Pollut. 2021 Dec 30;297:118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30.

Wastewater treatment plants (WWTPs) are among the main hotspots of antibiotic resistance genes (ARGs) in the environment. Previously, we demonstrated that, by increasing anthropogenic pollution, the antibiotic resistome persisted in the microbial community of rivers and lakes, independently by...

Cite
Di Cesare A, Sabatino R, Yang Y, et al. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021;297:118774doi: 10.1016/j.envpol.2021.118774.
Di Cesare, A., Sabatino, R., Yang, Y., Brambilla, D., Li, P., Fontaneto, D., Eckert, E. M., & Corno, G. (2021). Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environmental pollution (Barking, Essex : 1987), 297118774. https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare, Andrea, et al. "Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments." Environmental pollution (Barking, Essex : 1987) vol. 297 (2021): 118774. doi: https://doi.org/10.1016/j.envpol.2021.118774
Di Cesare A, Sabatino R, Yang Y, Brambilla D, Li P, Fontaneto D, Eckert EM, Corno G. Contribution of plasmidome, metal resistome and integrases to the persistence of the antibiotic resistome in aquatic environments. Environ Pollut. 2021 Dec 30;297:118774. doi: 10.1016/j.envpol.2021.118774. Epub 2021 Dec 30. PMID: 34974089.
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Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant.

Molecular therapy. Nucleic acids

Qamar Saeed M, Dufour N, Bartholmae C, Sieranska U, Knopf M, Thierry E, Thierry S, Delelis O, Grandchamp N, Pilet H, Ravassard P, Massonneau J, Pflumio F, von Kalle C, Lachapelle F, Bemelmans AP, Schmidt M, Serguera C.
PMID: 25462529
Mol Ther Nucleic Acids. 2014 Dec 02;3:e213. doi: 10.1038/mtna.2014.65.

HIV-1 derived vectors are among the most efficient for gene transduction in mammalian tissues. As the parent virus, they carry out vector genome insertion into the host cell chromatin. Consequently, their preferential integration in transcribed genes raises several conceptual...

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Qamar Saeed M, Dufour N, Bartholmae C, et al. Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant. Mol Ther Nucleic Acids. 2014;3:e213doi: 10.1038/mtna.2014.65.
Qamar Saeed, M., Dufour, N., Bartholmae, C., Sieranska, U., Knopf, M., Thierry, E., Thierry, S., Delelis, O., Grandchamp, N., Pilet, H., Ravassard, P., Massonneau, J., Pflumio, F., von Kalle, C., Lachapelle, F., Bemelmans, A. P., Schmidt, M., & Serguera, C. (2014). Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant. Molecular therapy. Nucleic acids, 3e213. https://doi.org/10.1038/mtna.2014.65
Qamar Saeed, Muhammad, et al. "Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant." Molecular therapy. Nucleic acids vol. 3 (2014): e213. doi: https://doi.org/10.1038/mtna.2014.65
Qamar Saeed M, Dufour N, Bartholmae C, Sieranska U, Knopf M, Thierry E, Thierry S, Delelis O, Grandchamp N, Pilet H, Ravassard P, Massonneau J, Pflumio F, von Kalle C, Lachapelle F, Bemelmans AP, Schmidt M, Serguera C. Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant. Mol Ther Nucleic Acids. 2014 Dec 02;3:e213. doi: 10.1038/mtna.2014.65. PMID: 25462529; PMCID: PMC4272407.
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On the transposon origins of mammalian SCAND3 and KRBA2, two zinc-finger genes carrying an integrase/transposase domain.

Mobile genetic elements

Llorens C, Bernet GP, Ramasamy S, Feschotte C, Moya A.
PMID: 23550032
Mob Genet Elements. 2012 Sep 01;2(5):205-210. doi: 10.4161/mge.22914.

SCAND3 and KRBA2 are two mammalian proteins originally described as "cellular-integrases" due to sharing of a similar DDE-type integrase domain whose origin and relationship with other recombinases remain unclear. Here we perform phylogenetic analyses of 341 integrase/transposase sequences to...

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Llorens C, Bernet GP, Ramasamy S, et al. On the transposon origins of mammalian SCAND3 and KRBA2, two zinc-finger genes carrying an integrase/transposase domain. Mob Genet Elements. 2012;2(5):205-210doi: 10.4161/mge.22914.
Llorens, C., Bernet, G. P., Ramasamy, S., Feschotte, C., & Moya, A. (2012). On the transposon origins of mammalian SCAND3 and KRBA2, two zinc-finger genes carrying an integrase/transposase domain. Mobile genetic elements, 2(5), 205-210. https://doi.org/10.4161/mge.22914
Llorens, Carlos, et al. "On the transposon origins of mammalian SCAND3 and KRBA2, two zinc-finger genes carrying an integrase/transposase domain." Mobile genetic elements vol. 2,5 (2012): 205-210. doi: https://doi.org/10.4161/mge.22914
Llorens C, Bernet GP, Ramasamy S, Feschotte C, Moya A. On the transposon origins of mammalian SCAND3 and KRBA2, two zinc-finger genes carrying an integrase/transposase domain. Mob Genet Elements. 2012 Sep 01;2(5):205-210. doi: 10.4161/mge.22914. PMID: 23550032; PMCID: PMC3575427.
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Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study.

Acta naturae

Shadrina OA, Zatsepin TS, Agapkina YY, Isaguliants MG, Gottikh MB.
PMID: 25927004
Acta Naturae. 2015 Jan-Mar;7(1):78-86.

Integration of human immunodeficiency virus (HIV-1) DNA into the genome of an infected cell is one of the key steps in the viral replication cycle. The viral enzyme integrase (IN), which catalyzes the integration, is an attractive target for...

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Shadrina OA, Zatsepin TS, Agapkina YY, et al. Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study. Acta Naturae. 2015;7(1):78-86
Shadrina, O. A., Zatsepin, T. S., Agapkina, Y. Y., Isaguliants, M. G., & Gottikh, M. B. (2015). Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study. Acta naturae, 7(1), 78-86.
Shadrina, O A, et al. "Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study." Acta naturae vol. 7,1 (2015): 78-86.
Shadrina OA, Zatsepin TS, Agapkina YY, Isaguliants MG, Gottikh MB. Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study. Acta Naturae. 2015 Jan-Mar;7(1):78-86. PMID: 25927004; PMCID: PMC4410398.
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DNA-based memory devices for recording cellular events.

Nature reviews. Genetics

Sheth RU, Wang HH.
PMID: 30237447
Nat Rev Genet. 2018 Nov;19(11):718-732. doi: 10.1038/s41576-018-0052-8.

Measuring biological data across time and space is critical for understanding complex biological processes and for various biosurveillance applications. However, such data are often inaccessible or difficult to directly obtain. Less invasive, more robust and higher-throughput biological recording tools...

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Sheth RU, Wang HH. DNA-based memory devices for recording cellular events. Nat Rev Genet. 2018;19(11):718-732doi: 10.1038/s41576-018-0052-8.
Sheth, R. U., & Wang, H. H. (2018). DNA-based memory devices for recording cellular events. Nature reviews. Genetics, 19(11), 718-732. https://doi.org/10.1038/s41576-018-0052-8
Sheth, Ravi U, and Wang, Harris H. "DNA-based memory devices for recording cellular events." Nature reviews. Genetics vol. 19,11 (2018): 718-732. doi: https://doi.org/10.1038/s41576-018-0052-8
Sheth RU, Wang HH. DNA-based memory devices for recording cellular events. Nat Rev Genet. 2018 Nov;19(11):718-732. doi: 10.1038/s41576-018-0052-8. PMID: 30237447; PMCID: PMC6492567.
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Showing 25 to 36 of 60 entries