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Vertical transmission of Mycoplasma wenyonii in cattle, supported by analysis of the ribonuclease P RNA gene - Short communication.

Acta veterinaria Hungarica

Sasaoka F, Suzuki J, Hirata T, Ichijo T, Furuhama K, Harasawa R, Satoh H.
PMID: 26551417
Acta Vet Hung. 2015 Sep;63(3):271-4. doi: 10.1556/004.2015.025.

The vertical transmission of Mycoplasma (M.) wenyonii was investigated in beef cattle raised on a farm in Japan by analysing the ribonuclease P RNA (rnpB) gene sequence using PCR. Peripheral blood samples from 17 dams infected with M. wenyonii...

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Sasaoka F, Suzuki J, Hirata T, et al. Vertical transmission of Mycoplasma wenyonii in cattle, supported by analysis of the ribonuclease P RNA gene - Short communication. Acta Vet Hung. 2015;63(3):271-4doi: 10.1556/004.2015.025.
Sasaoka, F., Suzuki, J., Hirata, T., Ichijo, T., Furuhama, K., Harasawa, R., & Satoh, H. (2015). Vertical transmission of Mycoplasma wenyonii in cattle, supported by analysis of the ribonuclease P RNA gene - Short communication. Acta veterinaria Hungarica, 63(3), 271-4. https://doi.org/10.1556/004.2015.025
Sasaoka, Fumina, et al. "Vertical transmission of Mycoplasma wenyonii in cattle, supported by analysis of the ribonuclease P RNA gene - Short communication." Acta veterinaria Hungarica vol. 63,3 (2015): 271-4. doi: https://doi.org/10.1556/004.2015.025
Sasaoka F, Suzuki J, Hirata T, Ichijo T, Furuhama K, Harasawa R, Satoh H. Vertical transmission of Mycoplasma wenyonii in cattle, supported by analysis of the ribonuclease P RNA gene - Short communication. Acta Vet Hung. 2015 Sep;63(3):271-4. doi: 10.1556/004.2015.025. PMID: 26551417.
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Expression of α-amylase and other gibberellin-regulated genes in aleurone tissue of developing wheat grains.

Planta

Cornford CA, Black M, Chapman JM, Baulcombe DC.
PMID: 24232656
Planta. 1986 Nov;169(3):420-8. doi: 10.1007/BF00392140.

Aleurone tissue from freshly harvested immature wheat grains (Triticum aestivum L. cv. Sappo) which is normally unresponsive to gibberellic acid can be made responsive by subjecting the tissue to a pre-incubation treatment in a simple buffered medium prior to...

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Cornford CA, Black M, Chapman JM, et al. Expression of α-amylase and other gibberellin-regulated genes in aleurone tissue of developing wheat grains. Planta. 1986;169(3):420-8doi: 10.1007/BF00392140.
Cornford, C. A., Black, M., Chapman, J. M., & Baulcombe, D. C. (1986). Expression of α-amylase and other gibberellin-regulated genes in aleurone tissue of developing wheat grains. Planta, 169(3), 420-8. https://doi.org/10.1007/BF00392140
Cornford, C A, et al. "Expression of α-amylase and other gibberellin-regulated genes in aleurone tissue of developing wheat grains." Planta vol. 169,3 (1986): 420-8. doi: https://doi.org/10.1007/BF00392140
Cornford CA, Black M, Chapman JM, Baulcombe DC. Expression of α-amylase and other gibberellin-regulated genes in aleurone tissue of developing wheat grains. Planta. 1986 Nov;169(3):420-8. doi: 10.1007/BF00392140. PMID: 24232656.
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Separation of antigens by immunological specificity: Use of cellulose-linked antibodies as immunosorbents.

The Biochemical journal

Gallop RG, Tozer BT, Stephen J, Smith H.
PMID: 16742449
Biochem J. 1966 Dec;101(3):711-6. doi: 10.1042/bj1010711.

1. Immunosorbents were prepared by coupling activated aminocellulose with the gamma-globulin concentrates of antisera prepared against ovalbumin and human serum albumin. 2. The immunosorbents were low in solubility, but high in capacity for homologous antigens. 3. The high specificity...

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Gallop RG, Tozer BT, Stephen J, et al. Separation of antigens by immunological specificity: Use of cellulose-linked antibodies as immunosorbents. Biochem J. 1966;101(3):711-6doi: 10.1042/bj1010711.
Gallop, R. G., Tozer, B. T., Stephen, J., & Smith, H. (1966). Separation of antigens by immunological specificity: Use of cellulose-linked antibodies as immunosorbents. The Biochemical journal, 101(3), 711-6. https://doi.org/10.1042/bj1010711
Gallop, R G, et al. "Separation of antigens by immunological specificity: Use of cellulose-linked antibodies as immunosorbents." The Biochemical journal vol. 101,3 (1966): 711-6. doi: https://doi.org/10.1042/bj1010711
Gallop RG, Tozer BT, Stephen J, Smith H. Separation of antigens by immunological specificity: Use of cellulose-linked antibodies as immunosorbents. Biochem J. 1966 Dec;101(3):711-6. doi: 10.1042/bj1010711. PMID: 16742449; PMCID: PMC1270177.
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In Vitro Protein Synthesis by Plastids of Phaseolus vulgaris. I. Localization of Activity in the Chloroplasts of a Chloroplast Containing Fraction from Developing Leaves.

Plant physiology

Parenti F, Margulies MM.
PMID: 16656637
Plant Physiol. 1967 Sep;42(9):1179-86. doi: 10.1104/pp.42.9.1179.

The incorporation of uniformly labeled leucine-(14)C into protein by a chloroplast containing fraction from developing primary leaves of bean is reported. Chloroplasts, obtained from week old plants grown in darkness, and then illuminated with white light for 12 hours,...

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Parenti F, Margulies MM. In Vitro Protein Synthesis by Plastids of Phaseolus vulgaris. I. Localization of Activity in the Chloroplasts of a Chloroplast Containing Fraction from Developing Leaves. Plant Physiol. 1967;42(9):1179-86doi: 10.1104/pp.42.9.1179.
Parenti, F., & Margulies, M. M. (1967). In Vitro Protein Synthesis by Plastids of Phaseolus vulgaris. I. Localization of Activity in the Chloroplasts of a Chloroplast Containing Fraction from Developing Leaves. Plant physiology, 42(9), 1179-86. https://doi.org/10.1104/pp.42.9.1179
Parenti, F, and Margulies, M M. "In Vitro Protein Synthesis by Plastids of Phaseolus vulgaris. I. Localization of Activity in the Chloroplasts of a Chloroplast Containing Fraction from Developing Leaves." Plant physiology vol. 42,9 (1967): 1179-86. doi: https://doi.org/10.1104/pp.42.9.1179
Parenti F, Margulies MM. In Vitro Protein Synthesis by Plastids of Phaseolus vulgaris. I. Localization of Activity in the Chloroplasts of a Chloroplast Containing Fraction from Developing Leaves. Plant Physiol. 1967 Sep;42(9):1179-86. doi: 10.1104/pp.42.9.1179. PMID: 16656637; PMCID: PMC1086699.
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Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains.

Biology

Nozawa Y, Hagihara M, Rahman MS, Matsumura S, Ikawa Y.
PMID: 31480450
Biology (Basel). 2019 Aug 31;8(3). doi: 10.3390/biology8030065.

The modular structural domains of multidomain RNA enzymes can often be dissected into separate domain RNAs and their noncovalent assembly can often reconstitute active enzymes. These properties are important to understand their basic characteristics and are useful for their...

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Nozawa Y, Hagihara M, Rahman MS, et al. Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains. Biology (Basel). 2019;8(3)doi: 10.3390/biology8030065.
Nozawa, Y., Hagihara, M., Rahman, M. S., Matsumura, S., & Ikawa, Y. (2019). Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains. Biology, 8(3), . https://doi.org/10.3390/biology8030065
Nozawa, Yuri, et al. "Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains." Biology vol. 8,3 (2019). doi: https://doi.org/10.3390/biology8030065
Nozawa Y, Hagihara M, Rahman MS, Matsumura S, Ikawa Y. Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains. Biology (Basel). 2019 Aug 31;8(3). doi: 10.3390/biology8030065. PMID: 31480450; PMCID: PMC6783828.
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Identification of the .

Frontiers in microbiology

Davies-Sala C, Jani S, Zorreguieta A, Tolmasky ME.
PMID: 30349524
Front Microbiol. 2018 Oct 08;9:2408. doi: 10.3389/fmicb.2018.02408. eCollection 2018.

The bacterial ribonuclease P or RNase P holoenzyme is usually composed of a catalytic RNA subunit, M1, and a cofactor protein, C5. This enzyme was first identified for its role in maturation of tRNAs by endonucleolytic cleavage of the...

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Davies-Sala C, Jani S, Zorreguieta A, et al. Identification of the . Front Microbiol. 2018;9:2408doi: 10.3389/fmicb.2018.02408.
Davies-Sala, C., Jani, S., Zorreguieta, A., & Tolmasky, M. E. (2018). Identification of the . Frontiers in microbiology, 92408. https://doi.org/10.3389/fmicb.2018.02408
Davies-Sala, Carol, et al. "Identification of the ." Frontiers in microbiology vol. 9 (2018): 2408. doi: https://doi.org/10.3389/fmicb.2018.02408
Davies-Sala C, Jani S, Zorreguieta A, Tolmasky ME. Identification of the . Front Microbiol. 2018 Oct 08;9:2408. doi: 10.3389/fmicb.2018.02408. eCollection 2018. PMID: 30349524; PMCID: PMC6186949.
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Interplay Between Amphetamine and Activity Level in Gene Networks of the Mouse Striatum.

Bioinformatics and biology insights

Goncalves TM, Southey BR, Rodriguez-Zas SL.
PMID: 30559594
Bioinform Biol Insights. 2018 Dec 11;12:1177932218815152. doi: 10.1177/1177932218815152. eCollection 2018.

The psychostimulant amphetamine can be prescribed to ameliorate the symptoms of narcolepsy, attention-deficit hyperactivity disorder and to facilitate weight loss. This stimulant can also have negative effects including toxicity and addiction risk. The impact of amphetamine on gene networks...

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Goncalves TM, Southey BR, Rodriguez-Zas SL. Interplay Between Amphetamine and Activity Level in Gene Networks of the Mouse Striatum. Bioinform Biol Insights. 2018;12:1177932218815152doi: 10.1177/1177932218815152.
Goncalves, T. M., Southey, B. R., & Rodriguez-Zas, S. L. (2018). Interplay Between Amphetamine and Activity Level in Gene Networks of the Mouse Striatum. Bioinformatics and biology insights, 121177932218815152. https://doi.org/10.1177/1177932218815152
Goncalves, Tassia M, et al. "Interplay Between Amphetamine and Activity Level in Gene Networks of the Mouse Striatum." Bioinformatics and biology insights vol. 12 (2018): 1177932218815152. doi: https://doi.org/10.1177/1177932218815152
Goncalves TM, Southey BR, Rodriguez-Zas SL. Interplay Between Amphetamine and Activity Level in Gene Networks of the Mouse Striatum. Bioinform Biol Insights. 2018 Dec 11;12:1177932218815152. doi: 10.1177/1177932218815152. eCollection 2018. PMID: 30559594; PMCID: PMC6291885.
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CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25.

Anti-cancer drugs

Feng L, Zhao M, Wu A.
PMID: 34407047
Anticancer Drugs. 2022 Jan 01;33(1):e155-e165. doi: 10.1097/CAD.0000000000001167.

Circular RNAs have been identified as vital regulators to regulate the development of human cancers, including cervical cancer. Therefore, this study was designed to clarify the underlying mechanism of circASAP1 in cervical cancer. The real-time quantitative PCR assay was...

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Feng L, Zhao M, Wu A. CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25. Anticancer Drugs. 2022;33(1):e155-e165doi: 10.1097/CAD.0000000000001167.
Feng, L., Zhao, M., & Wu, A. (2022). CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25. Anti-cancer drugs, 33(1), e155-e165. https://doi.org/10.1097/CAD.0000000000001167
Feng, Lei, et al. "CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25." Anti-cancer drugs vol. 33,1 (2022): e155-e165. doi: https://doi.org/10.1097/CAD.0000000000001167
Feng L, Zhao M, Wu A. CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25. Anticancer Drugs. 2022 Jan 01;33(1):e155-e165. doi: 10.1097/CAD.0000000000001167. PMID: 34407047.
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The Progression of Acute Myeloid Leukemia from First Diagnosis to Chemoresistant Relapse: A Comparison of Proteomic and Phosphoproteomic Profiles.

Cancers

Aasebø E, Berven FS, Hovland R, Døskeland SO, Bruserud Ø, Selheim F, Hernandez-Valladares M.
PMID: 32512867
Cancers (Basel). 2020 Jun 04;12(6). doi: 10.3390/cancers12061466.

Acute myeloid leukemia (AML) is an aggressive hematological malignancy. Nearly 50% of the patients who receive the most intensive treatment develop chemoresistant leukemia relapse. Although the leukemogenic events leading to relapse seem to differ between patients (i.e., regrowth from...

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Aasebø E, Berven FS, Hovland R, et al. The Progression of Acute Myeloid Leukemia from First Diagnosis to Chemoresistant Relapse: A Comparison of Proteomic and Phosphoproteomic Profiles. Cancers (Basel). 2020;12(6)doi: 10.3390/cancers12061466.
Aasebø, E., Berven, F. S., Hovland, R., Døskeland, S. O., Bruserud, �. �., Selheim, F., & Hernandez-Valladares, M. (2020). The Progression of Acute Myeloid Leukemia from First Diagnosis to Chemoresistant Relapse: A Comparison of Proteomic and Phosphoproteomic Profiles. Cancers, 12(6), . https://doi.org/10.3390/cancers12061466
Aasebø, Elise, et al. "The Progression of Acute Myeloid Leukemia from First Diagnosis to Chemoresistant Relapse: A Comparison of Proteomic and Phosphoproteomic Profiles." Cancers vol. 12,6 (2020). doi: https://doi.org/10.3390/cancers12061466
Aasebø E, Berven FS, Hovland R, Døskeland SO, Bruserud Ø, Selheim F, Hernandez-Valladares M. The Progression of Acute Myeloid Leukemia from First Diagnosis to Chemoresistant Relapse: A Comparison of Proteomic and Phosphoproteomic Profiles. Cancers (Basel). 2020 Jun 04;12(6). doi: 10.3390/cancers12061466. PMID: 32512867; PMCID: PMC7352627.
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Isolation and analysis of virus-specific ribonucleoprotein of tobacco mosaic virus-infected tobacco.

Virology

Dorokhov YL, Alexandrova NM, Miroshnichenko NA, Atabekov JG.
PMID: 18644308
Virology. 1983 Jun;127(2):237-52. doi: 10.1016/0042-6822(83)90141-1.

A ribonucleoprotein fraction (vRNP) of a characteristic buoyant density greater than the buoyant density of tobacco mosaic virus (TMV) particles has been isolated from infected tissue by Cs2SO4 density gradient centrifugation. The vRNP particles appear to be TMV specific...

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Dorokhov YL, Alexandrova NM, Miroshnichenko NA, et al. Isolation and analysis of virus-specific ribonucleoprotein of tobacco mosaic virus-infected tobacco. Virology. 1983;127(2):237-52doi: 10.1016/0042-6822(83)90141-1.
Dorokhov, Y. L., Alexandrova, N. M., Miroshnichenko, N. A., & Atabekov, J. G. (1983). Isolation and analysis of virus-specific ribonucleoprotein of tobacco mosaic virus-infected tobacco. Virology, 127(2), 237-52. https://doi.org/10.1016/0042-6822(83)90141-1
Dorokhov, Y L, et al. "Isolation and analysis of virus-specific ribonucleoprotein of tobacco mosaic virus-infected tobacco." Virology vol. 127,2 (1983): 237-52. doi: https://doi.org/10.1016/0042-6822(83)90141-1
Dorokhov YL, Alexandrova NM, Miroshnichenko NA, Atabekov JG. Isolation and analysis of virus-specific ribonucleoprotein of tobacco mosaic virus-infected tobacco. Virology. 1983 Jun;127(2):237-52. doi: 10.1016/0042-6822(83)90141-1. PMID: 18644308.
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CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25.

Anti-cancer drugs

Feng L, Zhao M, Wu A.
PMID: 34407047
Anticancer Drugs. 2021 Aug 16; doi: 10.1097/CAD.0000000000001167. Epub 2021 Aug 16.

Circular RNAs have been identified as vital regulators to regulate the development of human cancers, including cervical cancer. Therefore, this study was designed to clarify the underlying mechanism of circASAP1 in cervical cancer. The real-time quantitative PCR assay was...

Cite
Feng L, Zhao M, Wu A. CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25. Anticancer Drugs. 2021;doi: 10.1097/CAD.0000000000001167.
Feng, L., Zhao, M., & Wu, A. (2021). CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25. Anti-cancer drugs, . https://doi.org/10.1097/CAD.0000000000001167
Feng, Lei, et al. "CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25." Anti-cancer drugs vol. (2021). doi: https://doi.org/10.1097/CAD.0000000000001167
Feng L, Zhao M, Wu A. CircASAP1 promotes the development of cervical cancer through sponging miR-338-3p to upregulate RPP25. Anticancer Drugs. 2021 Aug 16; doi: 10.1097/CAD.0000000000001167. Epub 2021 Aug 16. PMID: 34407047.
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Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences.

Molecular therapy. Nucleic acids

Li W, Sheng J, Xu M, Vu GP, Yang Z, Liu Y, Sun X, Trang P, Lu S, Liu F.
PMID: 29246310
Mol Ther Nucleic Acids. 2017 Dec 15;9:322-332. doi: 10.1016/j.omtn.2017.10.007. Epub 2017 Oct 16.

External guide sequence (EGS) RNAs are associated with ribonuclease P (RNase P), a tRNA processing enzyme, and represent promising agents for gene-targeting applications as they can direct RNase-P-mediated cleavage of a target mRNA. Using murine cytomegalovirus (MCMV) as a...

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Li W, Sheng J, Xu M, et al. Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences. Mol Ther Nucleic Acids. 2017;9:322-332doi: 10.1016/j.omtn.2017.10.007.
Li, W., Sheng, J., Xu, M., Vu, G. P., Yang, Z., Liu, Y., Sun, X., Trang, P., Lu, S., & Liu, F. (2017). Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences. Molecular therapy. Nucleic acids, 9322-332. https://doi.org/10.1016/j.omtn.2017.10.007
Li, Wei, et al. "Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences." Molecular therapy. Nucleic acids vol. 9 (2017): 322-332. doi: https://doi.org/10.1016/j.omtn.2017.10.007
Li W, Sheng J, Xu M, Vu GP, Yang Z, Liu Y, Sun X, Trang P, Lu S, Liu F. Inhibition of Murine Cytomegalovirus Infection in Animals by RNase P-Associated External Guide Sequences. Mol Ther Nucleic Acids. 2017 Dec 15;9:322-332. doi: 10.1016/j.omtn.2017.10.007. Epub 2017 Oct 16. PMID: 29246310; PMCID: PMC5684469.
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Showing 1 to 12 of 30 entries