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Xylanases of Cellulomonas flavigena: expression, biochemical characterization, and biotechnological potential.

AMB Express

Lisov AV, Belova OV, Lisova ZA, Vinokurova NG, Nagel AS, Andreeva-Kovalevskaya ZI, Budarina ZI, Nagornykh MO, Zakharova MV, Shadrin AM, Solonin AS, Leontievsky AA.
PMID: 28050845
AMB Express. 2017 Dec;7(1):5. doi: 10.1186/s13568-016-0308-7. Epub 2017 Jan 03.

Four xylanases of Cellulomonas flavigena were cloned, expressed in Escherichia coli and purified. Three enzymes (CFXyl1, CFXyl2, and CFXyl4) were from the GH10 family, while CFXyl3 was from the GH11 family. The enzymes possessed moderate temperature stability and a...

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Lisov AV, Belova OV, Lisova ZA, et al. Xylanases of Cellulomonas flavigena: expression, biochemical characterization, and biotechnological potential. AMB Express. 2017;7(1):5doi: 10.1186/s13568-016-0308-7.
Lisov, A. V., Belova, O. V., Lisova, Z. A., Vinokurova, N. G., Nagel, A. S., Andreeva-Kovalevskaya, Z. I., Budarina, Z. I., Nagornykh, M. O., Zakharova, M. V., Shadrin, A. M., Solonin, A. S., & Leontievsky, A. A. (2017). Xylanases of Cellulomonas flavigena: expression, biochemical characterization, and biotechnological potential. AMB Express, 7(1), 5. https://doi.org/10.1186/s13568-016-0308-7
Lisov, Alexander V, et al. "Xylanases of Cellulomonas flavigena: expression, biochemical characterization, and biotechnological potential." AMB Express vol. 7,1 (2017): 5. doi: https://doi.org/10.1186/s13568-016-0308-7
Lisov AV, Belova OV, Lisova ZA, Vinokurova NG, Nagel AS, Andreeva-Kovalevskaya ZI, Budarina ZI, Nagornykh MO, Zakharova MV, Shadrin AM, Solonin AS, Leontievsky AA. Xylanases of Cellulomonas flavigena: expression, biochemical characterization, and biotechnological potential. AMB Express. 2017 Dec;7(1):5. doi: 10.1186/s13568-016-0308-7. Epub 2017 Jan 03. PMID: 28050845; PMCID: PMC5209306.
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Expression of thermophilic two-domain laccase from .

PeerJ

Trubitsina LI, Abdullatypov AV, Larionova AP, Trubitsin IV, Alferov SV, Ponamoreva ON, Leontievsky AA.
PMID: 34221729
PeerJ. 2021 Jun 24;9:e11646. doi: 10.7717/peerj.11646. eCollection 2021.

BACKGROUND: Two-domain laccases are copper-containing oxidases found in bacteria in the beginning of 2000ths. Two-domain laccases are known for their thermal stability, wide substrate specificity and, the most important of all, their resistance to so-called «strong inhibitors» of classical...

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Trubitsina LI, Abdullatypov AV, Larionova AP, et al. Expression of thermophilic two-domain laccase from . PeerJ. 2021;9:e11646doi: 10.7717/peerj.11646.
Trubitsina, L. I., Abdullatypov, A. V., Larionova, A. P., Trubitsin, I. V., Alferov, S. V., Ponamoreva, O. N., & Leontievsky, A. A. (2021). Expression of thermophilic two-domain laccase from . PeerJ, 9e11646. https://doi.org/10.7717/peerj.11646
Trubitsina, Liubov Igorevna, et al. "Expression of thermophilic two-domain laccase from ." PeerJ vol. 9 (2021): e11646. doi: https://doi.org/10.7717/peerj.11646
Trubitsina LI, Abdullatypov AV, Larionova AP, Trubitsin IV, Alferov SV, Ponamoreva ON, Leontievsky AA. Expression of thermophilic two-domain laccase from . PeerJ. 2021 Jun 24;9:e11646. doi: 10.7717/peerj.11646. eCollection 2021. PMID: 34221729; PMCID: PMC8236229.
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Extracellular oxidases from solid-state culture of the ligninolytic fungus panus tigrinus 8/18 .

Biochemistry. Biokhimiia

Pozdnyakova NN, Leontievsky AA, Golovleva LA.
PMID: 10231599
Biochemistry (Mosc). 1999 Apr;64(4):442-7.

Three extracellular oxidases were purified and characterized from a solid-state culture of the ligninolytic fungus Panus tigrinus 8/18. Oxidases 1 and 2 have physicochemical properties and substrate specificity typical for laccases but have no "blue" maximum in the absorption...

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Pozdnyakova NN, Leontievsky AA, Golovleva LA. Extracellular oxidases from solid-state culture of the ligninolytic fungus panus tigrinus 8/18 . Biochemistry (Mosc). 1999;64(4):442-7
Pozdnyakova, N. N., Leontievsky, A. A., & Golovleva, L. A. (1999). Extracellular oxidases from solid-state culture of the ligninolytic fungus panus tigrinus 8/18 . Biochemistry. Biokhimiia, 64(4), 442-7.
Pozdnyakova, et al. "Extracellular oxidases from solid-state culture of the ligninolytic fungus panus tigrinus 8/18 ." Biochemistry. Biokhimiia vol. 64,4 (1999): 442-7.
Pozdnyakova NN, Leontievsky AA, Golovleva LA. Extracellular oxidases from solid-state culture of the ligninolytic fungus panus tigrinus 8/18 . Biochemistry (Mosc). 1999 Apr;64(4):442-7. PMID: 10231599.
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A 2,5-Dihydroxybenzoic Acid-Gelatin Conjugate Inhibits the Basal and Hsp90-Stimulated Migration and Invasion of Tumor Cells.

Journal of functional biomaterials

Snigireva AV, Morenkov OS, Skarga YY, Lisov AV, Lisova ZA, Leontievsky AA, Zhmurina MA, Petrenko VS, Vrublevskaya VV.
PMID: 32503118
J Funct Biomater. 2020 Jun 03;11(2). doi: 10.3390/jfb11020039.

The extracellular cell surface-associated and soluble heat shock protein 90 (Hsp90) is known to participate in the migration and invasion of tumor cells. Earlier, we demonstrated that plasma membrane-associated heparan sulfate proteoglycans (HSPGs) bind the extracellular Hsp90 and thereby...

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Snigireva AV, Morenkov OS, Skarga YY, et al. A 2,5-Dihydroxybenzoic Acid-Gelatin Conjugate Inhibits the Basal and Hsp90-Stimulated Migration and Invasion of Tumor Cells. J Funct Biomater. 2020;11(2)doi: 10.3390/jfb11020039.
Snigireva, A. V., Morenkov, O. S., Skarga, Y. Y., Lisov, A. V., Lisova, Z. A., Leontievsky, A. A., Zhmurina, M. A., Petrenko, V. S., & Vrublevskaya, V. V. (2020). A 2,5-Dihydroxybenzoic Acid-Gelatin Conjugate Inhibits the Basal and Hsp90-Stimulated Migration and Invasion of Tumor Cells. Journal of functional biomaterials, 11(2), . https://doi.org/10.3390/jfb11020039
Snigireva, Anastasiya V, et al. "A 2,5-Dihydroxybenzoic Acid-Gelatin Conjugate Inhibits the Basal and Hsp90-Stimulated Migration and Invasion of Tumor Cells." Journal of functional biomaterials vol. 11,2 (2020). doi: https://doi.org/10.3390/jfb11020039
Snigireva AV, Morenkov OS, Skarga YY, Lisov AV, Lisova ZA, Leontievsky AA, Zhmurina MA, Petrenko VS, Vrublevskaya VV. A 2,5-Dihydroxybenzoic Acid-Gelatin Conjugate Inhibits the Basal and Hsp90-Stimulated Migration and Invasion of Tumor Cells. J Funct Biomater. 2020 Jun 03;11(2). doi: 10.3390/jfb11020039. PMID: 32503118; PMCID: PMC7353502.
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Draft Genome Sequence of Glyphosate-Degrading Achromobacter insolitus Strain Kg 19 (VKM B-3295), Isolated from Agricultural Soil.

Microbiology resource announcements

Tarlachkov SV, Epiktetov DO, Sviridov AV, Shushkova TV, Ermakova IT, Leontievsky AA.
PMID: 32327510
Microbiol Resour Announc. 2020 Apr 23;9(17). doi: 10.1128/MRA.00284-20.

The genome of an

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Tarlachkov SV, Epiktetov DO, Sviridov AV, et al. Draft Genome Sequence of Glyphosate-Degrading Achromobacter insolitus Strain Kg 19 (VKM B-3295), Isolated from Agricultural Soil. Microbiol Resour Announc. 2020;9(17)doi: 10.1128/MRA.00284-20.
Tarlachkov, S. V., Epiktetov, D. O., Sviridov, A. V., Shushkova, T. V., Ermakova, I. T., & Leontievsky, A. A. (2020). Draft Genome Sequence of Glyphosate-Degrading Achromobacter insolitus Strain Kg 19 (VKM B-3295), Isolated from Agricultural Soil. Microbiology resource announcements, 9(17), . https://doi.org/10.1128/MRA.00284-20
Tarlachkov, Sergey V, et al. "Draft Genome Sequence of Glyphosate-Degrading Achromobacter insolitus Strain Kg 19 (VKM B-3295), Isolated from Agricultural Soil." Microbiology resource announcements vol. 9,17 (2020). doi: https://doi.org/10.1128/MRA.00284-20
Tarlachkov SV, Epiktetov DO, Sviridov AV, Shushkova TV, Ermakova IT, Leontievsky AA. Draft Genome Sequence of Glyphosate-Degrading Achromobacter insolitus Strain Kg 19 (VKM B-3295), Isolated from Agricultural Soil. Microbiol Resour Announc. 2020 Apr 23;9(17). doi: 10.1128/MRA.00284-20. PMID: 32327510; PMCID: PMC7180283.
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Metagenomes of Lichens Solorina crocea and Peltigera canina.

Microbiology resource announcements

Vecherskii MV, Khayrullin DR, Shadrin AM, Lisov AV, Zavarzina AG, Zavarzin AA, Leontievsky AA.
PMID: 34989610
Microbiol Resour Announc. 2022 Jan 06;e0100021. doi: 10.1128/MRA.01000-21. Epub 2022 Jan 06.

Lichen genomes are usually considered genomes of separately cultured mycobiont and photobiont. Analysis of lichen metagenomes can give important information on specific lichen-associated microorganisms that can affect lichen metabolism. Here, we report a metagenome of peltigeralean lichens, containing cyanobacterial...

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Vecherskii MV, Khayrullin DR, Shadrin AM, et al. Metagenomes of Lichens Solorina crocea and Peltigera canina. Microbiol Resour Announc. 2022;e0100021doi: 10.1128/MRA.01000-21.
Vecherskii, M. V., Khayrullin, D. R., Shadrin, A. M., Lisov, A. V., Zavarzina, A. G., Zavarzin, A. A., & Leontievsky, A. A. (2022). Metagenomes of Lichens Solorina crocea and Peltigera canina. Microbiology resource announcements, e0100021. https://doi.org/10.1128/MRA.01000-21
Vecherskii, Maxim V, et al. "Metagenomes of Lichens Solorina crocea and Peltigera canina." Microbiology resource announcements vol. (2022): e0100021. doi: https://doi.org/10.1128/MRA.01000-21
Vecherskii MV, Khayrullin DR, Shadrin AM, Lisov AV, Zavarzina AG, Zavarzin AA, Leontievsky AA. Metagenomes of Lichens Solorina crocea and Peltigera canina. Microbiol Resour Announc. 2022 Jan 06;e0100021. doi: 10.1128/MRA.01000-21. Epub 2022 Jan 06. PMID: 34989610.
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Showing 1 to 6 of 6 entries