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Rapid profiling of protein kinase inhibitors by quantitative proteomics.

MedChemComm

Golkowski M, Brigham JL, Perera GK, Romano GE, Maly DJ, Ong SE.
PMID: 24648882
Medchemcomm. 2014 Mar;5(3):363-369. doi: 10.1039/C3MD00315A.

The ability to determine structure-activity relationships (SAR) and identify cellular targets from cell lysates and tissues is of great utility for kinase inhibitor drug discovery. We describe a streamlined mass spectrometry-based chemoproteomics workflow to examine the SAR and target...

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Golkowski M, Brigham JL, Perera GK, et al. Rapid profiling of protein kinase inhibitors by quantitative proteomics. Medchemcomm. 2014;5(3):363-369doi: 10.1039/C3MD00315A.
Golkowski, M., Brigham, J. L., Perera, G. K., Romano, G. E., Maly, D. J., & Ong, S. E. (2014). Rapid profiling of protein kinase inhibitors by quantitative proteomics. MedChemComm, 5(3), 363-369. https://doi.org/10.1039/C3MD00315A
Golkowski, Martin, et al. "Rapid profiling of protein kinase inhibitors by quantitative proteomics." MedChemComm vol. 5,3 (2014): 363-369. doi: https://doi.org/10.1039/C3MD00315A
Golkowski M, Brigham JL, Perera GK, Romano GE, Maly DJ, Ong SE. Rapid profiling of protein kinase inhibitors by quantitative proteomics. Medchemcomm. 2014 Mar;5(3):363-369. doi: 10.1039/C3MD00315A. PMID: 24648882; PMCID: PMC3955727.
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Biphasic Mathematical Model of Cell-Drug Interaction That Separates Target-Specific and Off-Target Inhibition and Suggests Potent Targeted Drug Combinations for Multi-Driver Colorectal Cancer Cells.

Cancers

Shen J, Li L, Yang T, Cohen PS, Sun G.
PMID: 32069833
Cancers (Basel). 2020 Feb 13;12(2). doi: 10.3390/cancers12020436.

Quantifying the response of cancer cells to a drug, and understanding the mechanistic basis of the response, are the cornerstones for anti-cancer drug discovery. Classical single target-based IC

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Shen J, Li L, Yang T, et al. Biphasic Mathematical Model of Cell-Drug Interaction That Separates Target-Specific and Off-Target Inhibition and Suggests Potent Targeted Drug Combinations for Multi-Driver Colorectal Cancer Cells. Cancers (Basel). 2020;12(2)doi: 10.3390/cancers12020436.
Shen, J., Li, L., Yang, T., Cohen, P. S., & Sun, G. (2020). Biphasic Mathematical Model of Cell-Drug Interaction That Separates Target-Specific and Off-Target Inhibition and Suggests Potent Targeted Drug Combinations for Multi-Driver Colorectal Cancer Cells. Cancers, 12(2), . https://doi.org/10.3390/cancers12020436
Shen, Jinyan, et al. "Biphasic Mathematical Model of Cell-Drug Interaction That Separates Target-Specific and Off-Target Inhibition and Suggests Potent Targeted Drug Combinations for Multi-Driver Colorectal Cancer Cells." Cancers vol. 12,2 (2020). doi: https://doi.org/10.3390/cancers12020436
Shen J, Li L, Yang T, Cohen PS, Sun G. Biphasic Mathematical Model of Cell-Drug Interaction That Separates Target-Specific and Off-Target Inhibition and Suggests Potent Targeted Drug Combinations for Multi-Driver Colorectal Cancer Cells. Cancers (Basel). 2020 Feb 13;12(2). doi: 10.3390/cancers12020436. PMID: 32069833; PMCID: PMC7072552.
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Recommendations for the management of cardiovascular risk in patients with chronic myeloid leukemia on tyrosine kinase inhibitors: risk assessment, stratification, treatment and monitoring.

Hematology, transfusion and cell therapy

Seguro FS, Silva CMPDC, Moura CMB, Conchon M, Fogliatto L, Funke VAM, Abdo A, Macedo AVS, Santos MHHD, Saraiva JFK.
PMID: 32631809
Hematol Transfus Cell Ther. 2021 Apr-Jun;43(2):191-200. doi: 10.1016/j.htct.2020.04.009. Epub 2020 Jul 01.

This manuscript summarizes the results of the consensus meeting composed of hematologists and cardiologists to establish recommendations for the prevention and follow-up of cardiovascular (CV) risk in patients with chronic myeloid leukemia (CML) treated with BCR-ABL tyrosine kinase inhibitors...

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Seguro FS, Silva CMPDC, Moura CMB, et al. Recommendations for the management of cardiovascular risk in patients with chronic myeloid leukemia on tyrosine kinase inhibitors: risk assessment, stratification, treatment and monitoring. Hematol Transfus Cell Ther. 2020;43(2):191-200doi: 10.1016/j.htct.2020.04.009.
Seguro, F. S., Silva, C. M. P. D. C., Moura, C. M. B., Conchon, M., Fogliatto, L., Funke, V. A. M., Abdo, A., Macedo, A. V. S., Santos, M. H. H. D., & Saraiva, J. F. K. (2021). Recommendations for the management of cardiovascular risk in patients with chronic myeloid leukemia on tyrosine kinase inhibitors: risk assessment, stratification, treatment and monitoring. Hematology, transfusion and cell therapy, 43(2), 191-200. https://doi.org/10.1016/j.htct.2020.04.009
Seguro, Fernanda Salles, et al. "Recommendations for the management of cardiovascular risk in patients with chronic myeloid leukemia on tyrosine kinase inhibitors: risk assessment, stratification, treatment and monitoring." Hematology, transfusion and cell therapy vol. 43,2 (2021): 191-200. doi: https://doi.org/10.1016/j.htct.2020.04.009
Seguro FS, Silva CMPDC, Moura CMB, Conchon M, Fogliatto L, Funke VAM, Abdo A, Macedo AVS, Santos MHHD, Saraiva JFK. Recommendations for the management of cardiovascular risk in patients with chronic myeloid leukemia on tyrosine kinase inhibitors: risk assessment, stratification, treatment and monitoring. Hematol Transfus Cell Ther. 2021 Apr-Jun;43(2):191-200. doi: 10.1016/j.htct.2020.04.009. Epub 2020 Jul 01. PMID: 32631809; PMCID: PMC8211634.
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Skeletal muscle wasting and renewal: a pivotal role of myokine IL-6.

SpringerPlus

Belizário JE, Fontes-Oliveira CC, Borges JP, Kashiabara JA, Vannier E.
PMID: 27330885
Springerplus. 2016 May 13;5:619. doi: 10.1186/s40064-016-2197-2. eCollection 2016.

Adult skeletal tissue is composed of heterogeneous population of cells that constantly self-renew by means of a controlled process of activation and proliferation of tissue-resident stem cells named satellite cells. Many growth factors, cytokines and myokines produced by skeletal...

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Belizário JE, Fontes-Oliveira CC, Borges JP, et al. Skeletal muscle wasting and renewal: a pivotal role of myokine IL-6. Springerplus. 2016;5:619doi: 10.1186/s40064-016-2197-2.
Belizário, J. E., Fontes-Oliveira, C. C., Borges, J. P., Kashiabara, J. A., & Vannier, E. (2016). Skeletal muscle wasting and renewal: a pivotal role of myokine IL-6. SpringerPlus, 5619. https://doi.org/10.1186/s40064-016-2197-2
Belizário, José E, et al. "Skeletal muscle wasting and renewal: a pivotal role of myokine IL-6." SpringerPlus vol. 5 (2016): 619. doi: https://doi.org/10.1186/s40064-016-2197-2
Belizário JE, Fontes-Oliveira CC, Borges JP, Kashiabara JA, Vannier E. Skeletal muscle wasting and renewal: a pivotal role of myokine IL-6. Springerplus. 2016 May 13;5:619. doi: 10.1186/s40064-016-2197-2. eCollection 2016. PMID: 27330885; PMCID: PMC4870483.
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Insulin activation of NADH ferricyanide reductase in human erythrocytes is mediated by the insulin receptor tyrosine kinase: a comparative study in normal and diabetic states.

Redox report : communications in free radical research

Marques F, Crespo ME, Pantaleão O, Bicho M.
PMID: 27406671
Redox Rep. 1996 Dec;2(6):373-8. doi: 10.1080/13510002.1996.11747077.

We have previously reported that NADH ferricyanide reductase in human erythrocytes is stimulated by insulin. Hormone-stimulated activities are attenuated in the presence of glycolytic inhibitors like vanadate, indicating the involvement of glycolysis in the mechanism by which insulin stimulates...

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Marques F, Crespo ME, Pantaleão O, et al. Insulin activation of NADH ferricyanide reductase in human erythrocytes is mediated by the insulin receptor tyrosine kinase: a comparative study in normal and diabetic states. Redox Rep. 1996;2(6):373-8doi: 10.1080/13510002.1996.11747077.
Marques, F., Crespo, M. E., Pantaleão, O., & Bicho, M. (1996). Insulin activation of NADH ferricyanide reductase in human erythrocytes is mediated by the insulin receptor tyrosine kinase: a comparative study in normal and diabetic states. Redox report : communications in free radical research, 2(6), 373-8. https://doi.org/10.1080/13510002.1996.11747077
Marques, F, et al. "Insulin activation of NADH ferricyanide reductase in human erythrocytes is mediated by the insulin receptor tyrosine kinase: a comparative study in normal and diabetic states." Redox report : communications in free radical research vol. 2,6 (1996): 373-8. doi: https://doi.org/10.1080/13510002.1996.11747077
Marques F, Crespo ME, Pantaleão O, Bicho M. Insulin activation of NADH ferricyanide reductase in human erythrocytes is mediated by the insulin receptor tyrosine kinase: a comparative study in normal and diabetic states. Redox Rep. 1996 Dec;2(6):373-8. doi: 10.1080/13510002.1996.11747077. PMID: 27406671.
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Identification of inactive conformation-selective interleukin-2-inducible T-cell kinase (ITK) inhibitors based on second-harmonic generation.

FEBS open bio

Hantani Y, Iio K, Hantani R, Umetani K, Sato T, Young T, Connell K, Kintz S, Salafsky J.
PMID: 30186743
FEBS Open Bio. 2018 Jul 30;8(9):1412-1423. doi: 10.1002/2211-5463.12489. eCollection 2018 Sep.

Many clinically approved protein kinase inhibitors stabilize an inactive conformation of their kinase target. Such inhibitors are generally highly selective compared to active conformation inhibitors, and consequently, general methods to identify inhibitors that stabilize an inactive conformation are much...

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Hantani Y, Iio K, Hantani R, et al. Identification of inactive conformation-selective interleukin-2-inducible T-cell kinase (ITK) inhibitors based on second-harmonic generation. FEBS Open Bio. 2018;8(9):1412-1423doi: 10.1002/2211-5463.12489.
Hantani, Y., Iio, K., Hantani, R., Umetani, K., Sato, T., Young, T., Connell, K., Kintz, S., & Salafsky, J. (2018). Identification of inactive conformation-selective interleukin-2-inducible T-cell kinase (ITK) inhibitors based on second-harmonic generation. FEBS open bio, 8(9), 1412-1423. https://doi.org/10.1002/2211-5463.12489
Hantani, Yoshiji, et al. "Identification of inactive conformation-selective interleukin-2-inducible T-cell kinase (ITK) inhibitors based on second-harmonic generation." FEBS open bio vol. 8,9 (2018): 1412-1423. doi: https://doi.org/10.1002/2211-5463.12489
Hantani Y, Iio K, Hantani R, Umetani K, Sato T, Young T, Connell K, Kintz S, Salafsky J. Identification of inactive conformation-selective interleukin-2-inducible T-cell kinase (ITK) inhibitors based on second-harmonic generation. FEBS Open Bio. 2018 Jul 30;8(9):1412-1423. doi: 10.1002/2211-5463.12489. eCollection 2018 Sep. PMID: 30186743; PMCID: PMC6120236.
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Retraction Note: Reprogramming glioblastoma multiforme cells into neurons by protein kinase inhibitors.

Journal of experimental & clinical cancer research : CR

Yuan J, Zhang F, Hallahan D, Zhang Z, He L, Wu LG, You M, Yang Q.
PMID: 34794497
J Exp Clin Cancer Res. 2021 Nov 18;40(1):368. doi: 10.1186/s13046-021-02172-6.

No abstract available.

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Yuan J, Zhang F, Hallahan D, et al. Retraction Note: Reprogramming glioblastoma multiforme cells into neurons by protein kinase inhibitors. J Exp Clin Cancer Res. 2021;40(1):368doi: 10.1186/s13046-021-02172-6.
Yuan, J., Zhang, F., Hallahan, D., Zhang, Z., He, L., Wu, L. G., You, M., & Yang, Q. (2021). Retraction Note: Reprogramming glioblastoma multiforme cells into neurons by protein kinase inhibitors. Journal of experimental & clinical cancer research : CR, 40(1), 368. https://doi.org/10.1186/s13046-021-02172-6
Yuan, Jie, et al. "Retraction Note: Reprogramming glioblastoma multiforme cells into neurons by protein kinase inhibitors." Journal of experimental & clinical cancer research : CR vol. 40,1 (2021): 368. doi: https://doi.org/10.1186/s13046-021-02172-6
Yuan J, Zhang F, Hallahan D, Zhang Z, He L, Wu LG, You M, Yang Q. Retraction Note: Reprogramming glioblastoma multiforme cells into neurons by protein kinase inhibitors. J Exp Clin Cancer Res. 2021 Nov 18;40(1):368. doi: 10.1186/s13046-021-02172-6. PMID: 34794497; PMCID: PMC8600789.
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Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update.

Pharmacological research

Roskoski R.
PMID: 34921994
Pharmacol Res. 2022 Jan;175:106037. doi: 10.1016/j.phrs.2021.106037. Epub 2021 Dec 15.

Owing to the dysregulation of protein kinase activity in many diseases including cancer, this enzyme family has become one of the most important drug targets in the 21st century. There are 68 FDA-approved therapeutic agents that target about two...

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Roskoski R. Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update. Pharmacol Res. 2021;175:106037doi: 10.1016/j.phrs.2021.106037.
Roskoski, R. (2022). Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update. Pharmacological research, 175106037. https://doi.org/10.1016/j.phrs.2021.106037
Roskoski, Robert. "Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update." Pharmacological research vol. 175 (2022): 106037. doi: https://doi.org/10.1016/j.phrs.2021.106037
Roskoski R. Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update. Pharmacol Res. 2022 Jan;175:106037. doi: 10.1016/j.phrs.2021.106037. Epub 2021 Dec 15. PMID: 34921994; PMCID: PMC8691985.
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Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies.

Pharmacological research

Roskoski R.
PMID: 33774181
Pharmacol Res. 2021 Jun;168:105579. doi: 10.1016/j.phrs.2021.105579. Epub 2021 Mar 26.

The discovery of the phosphatidylinositol 3-kinase (PI 3-kinase) pathway was a major advance in understanding eukaryotic signal transduction. The high frequency of PI 3-kinase pathway mutations in many cancers stimulated the development of drugs targeting these oncogenic mutants. The...

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Roskoski R. Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies. Pharmacol Res. 2021;168:105579doi: 10.1016/j.phrs.2021.105579.
Roskoski, R. (2021). Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies. Pharmacological research, 168105579. https://doi.org/10.1016/j.phrs.2021.105579
Roskoski, Robert. "Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies." Pharmacological research vol. 168 (2021): 105579. doi: https://doi.org/10.1016/j.phrs.2021.105579
Roskoski R. Properties of FDA-approved small molecule phosphatidylinositol 3-kinase inhibitors prescribed for the treatment of malignancies. Pharmacol Res. 2021 Jun;168:105579. doi: 10.1016/j.phrs.2021.105579. Epub 2021 Mar 26. PMID: 33774181.
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Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update.

Pharmacological research

Roskoski R.
PMID: 34921994
Pharmacol Res. 2021 Dec 15;175:106037. doi: 10.1016/j.phrs.2021.106037. Epub 2021 Dec 15.

Owing to the dysregulation of protein kinase activity in many diseases including cancer, this enzyme family has become one of the most important drug targets in the 21st century. There are 68 FDA-approved therapeutic agents that target about two...

Cite
Roskoski R. Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update. Pharmacol Res. 2021;175:106037doi: 10.1016/j.phrs.2021.106037.
Roskoski, R. (2021). Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update. Pharmacological research, 175106037. https://doi.org/10.1016/j.phrs.2021.106037
Roskoski, Robert. "Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update." Pharmacological research vol. 175 (2021): 106037. doi: https://doi.org/10.1016/j.phrs.2021.106037
Roskoski R. Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update. Pharmacol Res. 2021 Dec 15;175:106037. doi: 10.1016/j.phrs.2021.106037. Epub 2021 Dec 15. PMID: 34921994; PMCID: PMC8691985.
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A novel graph convolutional neural network for predicting interaction sites on protein kinase inhibitors in phosphorylation.

Scientific reports

Wang F, Chen YT, Yang JM, Akutsu T.
PMID: 34997142
Sci Rep. 2022 Jan 07;12(1):229. doi: 10.1038/s41598-021-04230-7.

Protein kinase-inhibitor interactions are key to the phosphorylation of proteins involved in cell proliferation, differentiation, and apoptosis, which shows the importance of binding mechanism research and kinase inhibitor design. In this study, a novel machine learning module (i.e., the...

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Wang F, Chen YT, Yang JM, et al. A novel graph convolutional neural network for predicting interaction sites on protein kinase inhibitors in phosphorylation. Sci Rep. 2022;12(1):229doi: 10.1038/s41598-021-04230-7.
Wang, F., Chen, Y. T., Yang, J. M., & Akutsu, T. (2022). A novel graph convolutional neural network for predicting interaction sites on protein kinase inhibitors in phosphorylation. Scientific reports, 12(1), 229. https://doi.org/10.1038/s41598-021-04230-7
Wang, Feiqi, et al. "A novel graph convolutional neural network for predicting interaction sites on protein kinase inhibitors in phosphorylation." Scientific reports vol. 12,1 (2022): 229. doi: https://doi.org/10.1038/s41598-021-04230-7
Wang F, Chen YT, Yang JM, Akutsu T. A novel graph convolutional neural network for predicting interaction sites on protein kinase inhibitors in phosphorylation. Sci Rep. 2022 Jan 07;12(1):229. doi: 10.1038/s41598-021-04230-7. PMID: 34997142; PMCID: PMC8742007.
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Discovery of Cysteine-targeting Covalent Protein Kinase Inhibitors.

Journal of medicinal chemistry

Lu X, Smaill JB, Patterson AV, Ding K.
PMID: 34962782
J Med Chem. 2022 Jan 13;65(1):58-83. doi: 10.1021/acs.jmedchem.1c01719. Epub 2021 Dec 28.

Small molecule covalent kinase inhibitors (CKIs) have entered a new era in drug discovery, which have the advantage for sustained target inhibition and high selectivity. An increased understanding of binding kinetics of CKIs and discovery of additional irreversible and...

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Lu X, Smaill JB, Patterson AV, et al. Discovery of Cysteine-targeting Covalent Protein Kinase Inhibitors. J Med Chem. 2021;65(1):58-83doi: 10.1021/acs.jmedchem.1c01719.
Lu, X., Smaill, J. B., Patterson, A. V., & Ding, K. (2022). Discovery of Cysteine-targeting Covalent Protein Kinase Inhibitors. Journal of medicinal chemistry, 65(1), 58-83. https://doi.org/10.1021/acs.jmedchem.1c01719
Lu, Xiaoyun, et al. "Discovery of Cysteine-targeting Covalent Protein Kinase Inhibitors." Journal of medicinal chemistry vol. 65,1 (2022): 58-83. doi: https://doi.org/10.1021/acs.jmedchem.1c01719
Lu X, Smaill JB, Patterson AV, Ding K. Discovery of Cysteine-targeting Covalent Protein Kinase Inhibitors. J Med Chem. 2022 Jan 13;65(1):58-83. doi: 10.1021/acs.jmedchem.1c01719. Epub 2021 Dec 28. PMID: 34962782.
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Showing 13 to 24 of 210 entries