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Showing 1 to 12 of 22 entries
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Chromogenic detection of aminoglycoside phosphotransferases.

Methods in molecular medicine

Amoroso AM, Gutkind GO.
PMID: 21374411
Methods Mol Med. 2001;48:113-7. doi: 10.1385/1-59259-077-2:113.

Acquired resistance to aminoglycosides is most frequently due to the presence of the so-called aminoglycoside modifying enzymes (AGME) (1) able to catalyze one or more of three general reactions: N-acetylation, O-nucleotidylation and O-phosphorylation (2). Although resistance phenotype (to different...

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Amoroso AM, Gutkind GO. Chromogenic detection of aminoglycoside phosphotransferases. Methods Mol Med. 2001;48:113-7doi: 10.1385/1-59259-077-2:113.
Amoroso, A. M., & Gutkind, G. O. (2001). Chromogenic detection of aminoglycoside phosphotransferases. Methods in molecular medicine, 48113-7. https://doi.org/10.1385/1-59259-077-2:113
Amoroso, A M, and Gutkind, G O. "Chromogenic detection of aminoglycoside phosphotransferases." Methods in molecular medicine vol. 48 (2001): 113-7. doi: https://doi.org/10.1385/1-59259-077-2:113
Amoroso AM, Gutkind GO. Chromogenic detection of aminoglycoside phosphotransferases. Methods Mol Med. 2001;48:113-7. doi: 10.1385/1-59259-077-2:113. PMID: 21374411.
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Acid phosphatase/phosphotransferases from enteric bacteria.

Journal of bioscience and bioengineering

Mihara Y, Utagawa T, Yamada H, Asano Y.
PMID: 16233057
J Biosci Bioeng. 2001;92(1):50-4. doi: 10.1263/jbb.92.50.

We have investigated the enzymatic phosphorylation of nucleosides and found that Morganella morganii phoC acid phosphatase exhibits regioselective pyrophosphate (PP(i))-nucleoside phosphotransferase activity. In this study, we isolated genes encoding an acid phosphatase with regioselective phosphotransferase activity (AP/PTase) from Providencia...

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Mihara Y, Utagawa T, Yamada H, et al. Acid phosphatase/phosphotransferases from enteric bacteria. J Biosci Bioeng. 2001;92(1):50-4doi: 10.1263/jbb.92.50.
Mihara, Y., Utagawa, T., Yamada, H., & Asano, Y. (2001). Acid phosphatase/phosphotransferases from enteric bacteria. Journal of bioscience and bioengineering, 92(1), 50-4. https://doi.org/10.1263/jbb.92.50
Mihara, Y, et al. "Acid phosphatase/phosphotransferases from enteric bacteria." Journal of bioscience and bioengineering vol. 92,1 (2001): 50-4. doi: https://doi.org/10.1263/jbb.92.50
Mihara Y, Utagawa T, Yamada H, Asano Y. Acid phosphatase/phosphotransferases from enteric bacteria. J Biosci Bioeng. 2001;92(1):50-4. doi: 10.1263/jbb.92.50. PMID: 16233057.
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Merestinib monotherapy or in combination for japanese patients with advanced and/or metastatic cancer: A phase 1 study.

Cancer medicine

Doi T, Yamamoto N, Naito Y, Kuboki Y, Koyama T, Piao Y, Tsujimoto N, Asou H, Inoue K, Kondo S.
PMID: 34499416
Cancer Med. 2021 Oct;10(19):6579-6589. doi: 10.1002/cam4.4110. Epub 2021 Sep 09.

This phase 1, multi-center, nonrandomized, open-label, dose-escalation study consisted of Part A wherein merestinib 80 or 120 mg (40-mg tablets) was administered orally QD during a 28-day cycle to patients diagnosed with solid tumors and Part B wherein merestinib...

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Doi T, Yamamoto N, Naito Y, et al. Merestinib monotherapy or in combination for japanese patients with advanced and/or metastatic cancer: A phase 1 study. Cancer Med. 2021;10(19):6579-6589doi: 10.1002/cam4.4110.
Doi, T., Yamamoto, N., Naito, Y., Kuboki, Y., Koyama, T., Piao, Y., Tsujimoto, N., Asou, H., Inoue, K., & Kondo, S. (2021). Merestinib monotherapy or in combination for japanese patients with advanced and/or metastatic cancer: A phase 1 study. Cancer medicine, 10(19), 6579-6589. https://doi.org/10.1002/cam4.4110
Doi, Toshihiko, et al. "Merestinib monotherapy or in combination for japanese patients with advanced and/or metastatic cancer: A phase 1 study." Cancer medicine vol. 10,19 (2021): 6579-6589. doi: https://doi.org/10.1002/cam4.4110
Doi T, Yamamoto N, Naito Y, Kuboki Y, Koyama T, Piao Y, Tsujimoto N, Asou H, Inoue K, Kondo S. Merestinib monotherapy or in combination for japanese patients with advanced and/or metastatic cancer: A phase 1 study. Cancer Med. 2021 Oct;10(19):6579-6589. doi: 10.1002/cam4.4110. Epub 2021 Sep 09. PMID: 34499416; PMCID: PMC8495281.
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Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis.

Research in microbiology

Zhang A, Pompeo F, Galinier A.
PMID: 34500011
Res Microbiol. 2021 Nov-Dec;172(7):103871. doi: 10.1016/j.resmic.2021.103871. Epub 2021 Sep 06.

Protein phosphorylation is a post-translational modification that affects protein activity through the addition of a phosphate moiety by protein kinases or phosphotransferases. It occurs in all life forms. In addition to Hanks kinases found also in eukaryotes, bacteria encode...

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Zhang A, Pompeo F, Galinier A. Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis. Res Microbiol. 2021;172(7):103871doi: 10.1016/j.resmic.2021.103871.
Zhang, A., Pompeo, F., & Galinier, A. (2021). Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis. Research in microbiology, 172(7), 103871. https://doi.org/10.1016/j.resmic.2021.103871
Zhang, Ao, et al. "Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis." Research in microbiology vol. 172,7 (2021): 103871. doi: https://doi.org/10.1016/j.resmic.2021.103871
Zhang A, Pompeo F, Galinier A. Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis. Res Microbiol. 2021 Nov-Dec;172(7):103871. doi: 10.1016/j.resmic.2021.103871. Epub 2021 Sep 06. PMID: 34500011.
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Differential contributions of choline phosphotransferases CPT1 and CEPT1 to the biosynthesis of choline phospholipids.

Journal of lipid research

Horibata Y, Sugimoto H.
PMID: 34331935
J Lipid Res. 2021;62:100100. doi: 10.1016/j.jlr.2021.100100. Epub 2021 Jul 29.

Choline phospholipids (PLs) such as phosphatidylcholine (PC) and 1-alkyl-2-acyl-sn-glycerophosphocholine are important components for cell membranes and also serve as a source of several lipid mediators. These lipids are biosynthesized in mammals in the final step of the CDP-choline pathway...

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Horibata Y, Sugimoto H. Differential contributions of choline phosphotransferases CPT1 and CEPT1 to the biosynthesis of choline phospholipids. J Lipid Res. 2021;62:100100doi: 10.1016/j.jlr.2021.100100.
Horibata, Y., & Sugimoto, H. (2021). Differential contributions of choline phosphotransferases CPT1 and CEPT1 to the biosynthesis of choline phospholipids. Journal of lipid research, 62100100. https://doi.org/10.1016/j.jlr.2021.100100
Horibata, Yasuhiro, and Sugimoto, Hiroyuki. "Differential contributions of choline phosphotransferases CPT1 and CEPT1 to the biosynthesis of choline phospholipids." Journal of lipid research vol. 62 (2021): 100100. doi: https://doi.org/10.1016/j.jlr.2021.100100
Horibata Y, Sugimoto H. Differential contributions of choline phosphotransferases CPT1 and CEPT1 to the biosynthesis of choline phospholipids. J Lipid Res. 2021;62:100100. doi: 10.1016/j.jlr.2021.100100. Epub 2021 Jul 29. PMID: 34331935; PMCID: PMC8387743.
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Comparison of the Activities and Some Properties of Pyrophosphate and ATP Dependent Fructose-6-Phosphate 1-Phosphotransferases of Phaseolus vulgaris Seeds.

Plant physiology

Botha FC, Small JG.
PMID: 16665337
Plant Physiol. 1987 Apr;83(4):772-7. doi: 10.1104/pp.83.4.772.

THE DISTRIBUTION OF PYROPHOSPHATE: fructose 6-phosphate phosphotransferase (PFP) and ATP: fructose-6-phosphate 1-phosphotransferase (PFK) was studied in germinating bean (Phaseolus vulgaris cv Top Crop) seeds. In the cotyledons the PFP activity was comparable with that of PFK. However, in the...

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Botha FC, Small JG. Comparison of the Activities and Some Properties of Pyrophosphate and ATP Dependent Fructose-6-Phosphate 1-Phosphotransferases of Phaseolus vulgaris Seeds. Plant Physiol. 1987;83(4):772-7doi: 10.1104/pp.83.4.772.
Botha, F. C., & Small, J. G. (1987). Comparison of the Activities and Some Properties of Pyrophosphate and ATP Dependent Fructose-6-Phosphate 1-Phosphotransferases of Phaseolus vulgaris Seeds. Plant physiology, 83(4), 772-7. https://doi.org/10.1104/pp.83.4.772
Botha, F C, and Small, J G. "Comparison of the Activities and Some Properties of Pyrophosphate and ATP Dependent Fructose-6-Phosphate 1-Phosphotransferases of Phaseolus vulgaris Seeds." Plant physiology vol. 83,4 (1987): 772-7. doi: https://doi.org/10.1104/pp.83.4.772
Botha FC, Small JG. Comparison of the Activities and Some Properties of Pyrophosphate and ATP Dependent Fructose-6-Phosphate 1-Phosphotransferases of Phaseolus vulgaris Seeds. Plant Physiol. 1987 Apr;83(4):772-7. doi: 10.1104/pp.83.4.772. PMID: 16665337; PMCID: PMC1056448.
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Singular features of trypanosomatids' phosphotransferases involved in cell energy management.

Enzyme research

Pereira CA, Bouvier LA, Cámara Mde L, Miranda MR.
PMID: 21603267
Enzyme Res. 2011;2011:576483. doi: 10.4061/2011/576483. Epub 2011 Apr 04.

Trypanosomatids are responsible for economically important veterinary affections and severe human diseases. In Africa, Trypanosoma brucei causes sleeping sickness or African trypanosomiasis, while in America, Trypanosoma cruzi is the etiological agent of Chagas disease. These parasites have complex life...

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Pereira CA, Bouvier LA, Cámara Mde L, et al. Singular features of trypanosomatids' phosphotransferases involved in cell energy management. Enzyme Res. 2011;2011:576483doi: 10.4061/2011/576483.
Pereira, C. A., Bouvier, L. A., Cámara, M. d. e. . L., & Miranda, M. R. (2011). Singular features of trypanosomatids' phosphotransferases involved in cell energy management. Enzyme research, 2011576483. https://doi.org/10.4061/2011/576483
Pereira, Claudio A, et al. "Singular features of trypanosomatids' phosphotransferases involved in cell energy management." Enzyme research vol. 2011 (2011): 576483. doi: https://doi.org/10.4061/2011/576483
Pereira CA, Bouvier LA, Cámara Mde L, Miranda MR. Singular features of trypanosomatids' phosphotransferases involved in cell energy management. Enzyme Res. 2011;2011:576483. doi: 10.4061/2011/576483. Epub 2011 Apr 04. PMID: 21603267; PMCID: PMC3092577.
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Retraction. Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases.

Journal of bacteriology

[No authors listed]
PMID: 22582386
J Bacteriol. 2012 Jun;194(11):3033. doi: 10.1128/JB.00549-12.

No abstract available.

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Retraction. Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases. J Bacteriol. 2012;194(11):3033doi: 10.1128/JB.00549-12.
(2012). Retraction. Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases. Journal of bacteriology, 194(11), 3033. https://doi.org/10.1128/JB.00549-12
"Retraction. Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases." Journal of bacteriology vol. 194,11 (2012): 3033. doi: https://doi.org/10.1128/JB.00549-12
Retraction. Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases. J Bacteriol. 2012 Jun;194(11):3033. doi: 10.1128/JB.00549-12. PMID: 22582386; PMCID: PMC3370641.
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Modifying enzymes related aminoglycoside: analyses of resistant Acinetobacter isolates.

International journal of clinical and experimental medicine

Atasoy AR, Ciftci IH, Petek M.
PMID: 25932248
Int J Clin Exp Med. 2015 Feb 15;8(2):2874-80. eCollection 2015.

Enzymatic modification of aminoglycosides by nucleotidyltransferases, acetyltransferases and/or phosphotransferases accounts for the majority of aminoglycoside-resistant Acinetobacter isolates. In this study, we investigated the relationship between aminoglycoside resistance and the presence of aminoglycoside-modifying enzymes in Acinetobacter baumannii clinical isolate groups...

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Atasoy AR, Ciftci IH, Petek M. Modifying enzymes related aminoglycoside: analyses of resistant Acinetobacter isolates. Int J Clin Exp Med. 2015;8(2):2874-80
Atasoy, A. R., Ciftci, I. H., & Petek, M. (2015). Modifying enzymes related aminoglycoside: analyses of resistant Acinetobacter isolates. International journal of clinical and experimental medicine, 8(2), 2874-80.
Atasoy, Ali Riza, et al. "Modifying enzymes related aminoglycoside: analyses of resistant Acinetobacter isolates." International journal of clinical and experimental medicine vol. 8,2 (2015): 2874-80.
Atasoy AR, Ciftci IH, Petek M. Modifying enzymes related aminoglycoside: analyses of resistant Acinetobacter isolates. Int J Clin Exp Med. 2015 Feb 15;8(2):2874-80. eCollection 2015. PMID: 25932248; PMCID: PMC4402895.
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Look and Outlook on Enzyme-Mediated Macrolide Resistance.

Frontiers in microbiology

Golkar T, Zieliński M, Berghuis AM.
PMID: 30177927
Front Microbiol. 2018 Aug 20;9:1942. doi: 10.3389/fmicb.2018.01942. eCollection 2018.

Since their discovery in the early 1950s, macrolide antibiotics have been used in both agriculture and medicine. Specifically, macrolides such as erythromycin and azithromycin have found use as substitutes for β-lactam antibiotics in patients with penicillin allergies. Given the...

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Golkar T, Zieliński M, Berghuis AM. Look and Outlook on Enzyme-Mediated Macrolide Resistance. Front Microbiol. 2018;9:1942doi: 10.3389/fmicb.2018.01942.
Golkar, T., Zieliński, M., & Berghuis, A. M. (2018). Look and Outlook on Enzyme-Mediated Macrolide Resistance. Frontiers in microbiology, 91942. https://doi.org/10.3389/fmicb.2018.01942
Golkar, Tolou, et al. "Look and Outlook on Enzyme-Mediated Macrolide Resistance." Frontiers in microbiology vol. 9 (2018): 1942. doi: https://doi.org/10.3389/fmicb.2018.01942
Golkar T, Zieliński M, Berghuis AM. Look and Outlook on Enzyme-Mediated Macrolide Resistance. Front Microbiol. 2018 Aug 20;9:1942. doi: 10.3389/fmicb.2018.01942. eCollection 2018. PMID: 30177927; PMCID: PMC6109786.
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TETX: a novel nuclear selection marker for Chlamydomonas reinhardtii transformation.

Plant methods

Garcia-Echauri SA, Cardineau GA.
PMID: 25908936
Plant Methods. 2015 Apr 15;11:27. doi: 10.1186/s13007-015-0064-8. eCollection 2015.

BACKGROUND: Transformation of microalgae to obtain recombinant proteins, lipids or metabolites of economic value is of growing interest due to low costs associated with culture growth and scaling up. At present there are only three stable nuclear selection markers...

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Garcia-Echauri SA, Cardineau GA. TETX: a novel nuclear selection marker for Chlamydomonas reinhardtii transformation. Plant Methods. 2015;11:27doi: 10.1186/s13007-015-0064-8.
Garcia-Echauri, S. A., & Cardineau, G. A. (2015). TETX: a novel nuclear selection marker for Chlamydomonas reinhardtii transformation. Plant methods, 1127. https://doi.org/10.1186/s13007-015-0064-8
Garcia-Echauri, Sergio A, and Cardineau, Guy A. "TETX: a novel nuclear selection marker for Chlamydomonas reinhardtii transformation." Plant methods vol. 11 (2015): 27. doi: https://doi.org/10.1186/s13007-015-0064-8
Garcia-Echauri SA, Cardineau GA. TETX: a novel nuclear selection marker for Chlamydomonas reinhardtii transformation. Plant Methods. 2015 Apr 15;11:27. doi: 10.1186/s13007-015-0064-8. eCollection 2015. PMID: 25908936; PMCID: PMC4407551.
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Functional Repertoire of Antibiotic Resistance Genes in Antibiotic Manufacturing Effluents and Receiving Freshwater Sediments.

Frontiers in microbiology

González-Plaza JJ, Šimatović A, Milaković M, Bielen A, Wichmann F, Udiković-Kolić N.
PMID: 29387045
Front Microbiol. 2018 Jan 17;8:2675. doi: 10.3389/fmicb.2017.02675. eCollection 2017.

Environments polluted by direct discharges of effluents from antibiotic manufacturing are important reservoirs for antibiotic resistance genes (ARGs), which could potentially be transferred to human pathogens. However, our knowledge about the identity and diversity of ARGs in such polluted...

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González-Plaza JJ, Šimatović A, Milaković M, et al. Functional Repertoire of Antibiotic Resistance Genes in Antibiotic Manufacturing Effluents and Receiving Freshwater Sediments. Front Microbiol. 2018;8:2675doi: 10.3389/fmicb.2017.02675.
González-Plaza, J. J., Šimatović, A., Milaković, M., Bielen, A., Wichmann, F., & Udiković-Kolić, N. (2017). Functional Repertoire of Antibiotic Resistance Genes in Antibiotic Manufacturing Effluents and Receiving Freshwater Sediments. Frontiers in microbiology, 82675. https://doi.org/10.3389/fmicb.2017.02675
González-Plaza, Juan J, et al. "Functional Repertoire of Antibiotic Resistance Genes in Antibiotic Manufacturing Effluents and Receiving Freshwater Sediments." Frontiers in microbiology vol. 8 (2017): 2675. doi: https://doi.org/10.3389/fmicb.2017.02675
González-Plaza JJ, Šimatović A, Milaković M, Bielen A, Wichmann F, Udiković-Kolić N. Functional Repertoire of Antibiotic Resistance Genes in Antibiotic Manufacturing Effluents and Receiving Freshwater Sediments. Front Microbiol. 2018 Jan 17;8:2675. doi: 10.3389/fmicb.2017.02675. eCollection 2017. PMID: 29387045; PMCID: PMC5776109.
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