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Recent Bremsstrahlung-based assays of .

Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine

Keillor ME, Aalseth CE, Arnquist IJ, Eggemeyer TA, Fuller ES, Glasgow BD, Hoppe EW, Morley SM, Myers AW, Orrell JL, Overman CT, Seifert A, Shaff SM, Thommasson KS.
PMID: 28318931
Appl Radiat Isot. 2017 Aug;126:185-187. doi: 10.1016/j.apradiso.2017.03.001. Epub 2017 Mar 03.

Low-background lead for radiation measurement shielding is often assayed for

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Keillor ME, Aalseth CE, Arnquist IJ, et al. Recent Bremsstrahlung-based assays of . Appl Radiat Isot. 2017;126:185-187doi: 10.1016/j.apradiso.2017.03.001.
Keillor, M. E., Aalseth, C. E., Arnquist, I. J., Eggemeyer, T. A., Fuller, E. S., Glasgow, B. D., Hoppe, E. W., Morley, S. M., Myers, A. W., Orrell, J. L., Overman, C. T., Seifert, A., Shaff, S. M., & Thommasson, K. S. (2017). Recent Bremsstrahlung-based assays of . Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine, 126185-187. https://doi.org/10.1016/j.apradiso.2017.03.001
Keillor, Martin E, et al. "Recent Bremsstrahlung-based assays of ." Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine vol. 126 (2017): 185-187. doi: https://doi.org/10.1016/j.apradiso.2017.03.001
Keillor ME, Aalseth CE, Arnquist IJ, Eggemeyer TA, Fuller ES, Glasgow BD, Hoppe EW, Morley SM, Myers AW, Orrell JL, Overman CT, Seifert A, Shaff SM, Thommasson KS. Recent Bremsstrahlung-based assays of . Appl Radiat Isot. 2017 Aug;126:185-187. doi: 10.1016/j.apradiso.2017.03.001. Epub 2017 Mar 03. PMID: 28318931.
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Development of a low-level .

Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine

Williams RM, Aalseth CE, Brandenberger JM, Day AR, Finn E, Fuller ES, Hoppe EW, Humble PH, Keillor ME, Mace EK, Myers AW, Overman CT, Panisko ME, Seifert A, White SK.
PMID: 28236555
Appl Radiat Isot. 2017 Aug;126:243-248. doi: 10.1016/j.apradiso.2017.02.018. Epub 2017 Feb 17.

This paper describes the generation of

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Williams RM, Aalseth CE, Brandenberger JM, et al. Development of a low-level . Appl Radiat Isot. 2017;126:243-248doi: 10.1016/j.apradiso.2017.02.018.
Williams, R. M., Aalseth, C. E., Brandenberger, J. M., Day, A. R., Finn, E., Fuller, E. S., Hoppe, E. W., Humble, P. H., Keillor, M. E., Mace, E. K., Myers, A. W., Overman, C. T., Panisko, M. E., Seifert, A., & White, S. K. (2017). Development of a low-level . Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine, 126243-248. https://doi.org/10.1016/j.apradiso.2017.02.018
Williams, R M, et al. "Development of a low-level ." Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine vol. 126 (2017): 243-248. doi: https://doi.org/10.1016/j.apradiso.2017.02.018
Williams RM, Aalseth CE, Brandenberger JM, Day AR, Finn E, Fuller ES, Hoppe EW, Humble PH, Keillor ME, Mace EK, Myers AW, Overman CT, Panisko ME, Seifert A, White SK. Development of a low-level . Appl Radiat Isot. 2017 Aug;126:243-248. doi: 10.1016/j.apradiso.2017.02.018. Epub 2017 Feb 17. PMID: 28236555.
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Ring Substituent Effects on the Thiol Addition and Hydrolysis Reactions of N-Arylmaleimides.

The Journal of organic chemistry

Chen Y, Tsao K, De Francesco É, Keillor JW.
PMID: 26595216
J Org Chem. 2015 Dec 18;80(24):12182-92. doi: 10.1021/acs.joc.5b02036. Epub 2015 Dec 03.

Maleimide groups are used extensively in bioconjugation reactions, but limited kinetic information is available regarding their thiol addition and hydrolysis reactions. We prepared a series of fluorogenic coumarin maleimide derivatives that differ by the substituent on their maleimide C═C...

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Chen Y, Tsao K, De Francesco É, et al. Ring Substituent Effects on the Thiol Addition and Hydrolysis Reactions of N-Arylmaleimides. J Org Chem. 2015;80(24):12182-92doi: 10.1021/acs.joc.5b02036.
Chen, Y., Tsao, K., De Francesco, �. �., & Keillor, J. W. (2015). Ring Substituent Effects on the Thiol Addition and Hydrolysis Reactions of N-Arylmaleimides. The Journal of organic chemistry, 80(24), 12182-92. https://doi.org/10.1021/acs.joc.5b02036
Chen, Yingche, et al. "Ring Substituent Effects on the Thiol Addition and Hydrolysis Reactions of N-Arylmaleimides." The Journal of organic chemistry vol. 80,24 (2015): 12182-92. doi: https://doi.org/10.1021/acs.joc.5b02036
Chen Y, Tsao K, De Francesco É, Keillor JW. Ring Substituent Effects on the Thiol Addition and Hydrolysis Reactions of N-Arylmaleimides. J Org Chem. 2015 Dec 18;80(24):12182-92. doi: 10.1021/acs.joc.5b02036. Epub 2015 Dec 03. PMID: 26595216.
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Benefits of Combined All-Trans Retinoic Acid and Arsenic Trioxide Treatment of Acute Promyelocytic Leukemia Cells and Further Enhancement by Inhibition of Atypically Expressed Transglutaminase 2.

Cancers

Jambrovics K, Uray IP, Keillor JW, Fésüs L, Balajthy Z.
PMID: 32168763
Cancers (Basel). 2020 Mar 11;12(3). doi: 10.3390/cancers12030648.

Randomized trials in acute promyelocytic leukemia patients have shown that treatment with a combination of all-trans retinoic acid (ATRA) and arsenic trioxide (ATO) is superior in efficacy to monotherapy, with significantly decreased mortality. So far, there are little data...

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Jambrovics K, Uray IP, Keillor JW, et al. Benefits of Combined All-Trans Retinoic Acid and Arsenic Trioxide Treatment of Acute Promyelocytic Leukemia Cells and Further Enhancement by Inhibition of Atypically Expressed Transglutaminase 2. Cancers (Basel). 2020;12(3)doi: 10.3390/cancers12030648.
Jambrovics, K., Uray, I. P., Keillor, J. W., Fésüs, L., & Balajthy, Z. (2020). Benefits of Combined All-Trans Retinoic Acid and Arsenic Trioxide Treatment of Acute Promyelocytic Leukemia Cells and Further Enhancement by Inhibition of Atypically Expressed Transglutaminase 2. Cancers, 12(3), . https://doi.org/10.3390/cancers12030648
Jambrovics, Károly, et al. "Benefits of Combined All-Trans Retinoic Acid and Arsenic Trioxide Treatment of Acute Promyelocytic Leukemia Cells and Further Enhancement by Inhibition of Atypically Expressed Transglutaminase 2." Cancers vol. 12,3 (2020). doi: https://doi.org/10.3390/cancers12030648
Jambrovics K, Uray IP, Keillor JW, Fésüs L, Balajthy Z. Benefits of Combined All-Trans Retinoic Acid and Arsenic Trioxide Treatment of Acute Promyelocytic Leukemia Cells and Further Enhancement by Inhibition of Atypically Expressed Transglutaminase 2. Cancers (Basel). 2020 Mar 11;12(3). doi: 10.3390/cancers12030648. PMID: 32168763; PMCID: PMC7139906.
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Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity.

Molecular carcinogenesis

Rorke EA, Adhikary G, Szmacinski H, Lakowicz JR, Weber DJ, Godoy-Ruiz R, Puranik P, Keillor JW, Gates EWJ, Eckert RL.
PMID: 34610184
Mol Carcinog. 2022 Jan;61(1):19-32. doi: 10.1002/mc.23356. Epub 2021 Oct 05.

Type 2 transglutaminase (TG2) functions as an important cancer cell survival protein in a range of cancers including epidermal squamous cell carcinoma. TG2 exists in open and closed conformations each of which has a distinct and mutually exclusive activity....

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Rorke EA, Adhikary G, Szmacinski H, et al. Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Mol Carcinog. 2021;61(1):19-32doi: 10.1002/mc.23356.
Rorke, E. A., Adhikary, G., Szmacinski, H., Lakowicz, J. R., Weber, D. J., Godoy-Ruiz, R., Puranik, P., Keillor, J. W., Gates, E. W. J., & Eckert, R. L. (2022). Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Molecular carcinogenesis, 61(1), 19-32. https://doi.org/10.1002/mc.23356
Rorke, Ellen A, et al. "Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity." Molecular carcinogenesis vol. 61,1 (2022): 19-32. doi: https://doi.org/10.1002/mc.23356
Rorke EA, Adhikary G, Szmacinski H, Lakowicz JR, Weber DJ, Godoy-Ruiz R, Puranik P, Keillor JW, Gates EWJ, Eckert RL. Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Mol Carcinog. 2022 Jan;61(1):19-32. doi: 10.1002/mc.23356. Epub 2021 Oct 05. PMID: 34610184; PMCID: PMC8665039.
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Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity.

Molecular carcinogenesis

Rorke EA, Adhikary G, Szmacinski H, Lakowicz JR, Weber DJ, Godoy-Ruiz R, Puranik P, Keillor JW, Gates EWJ, Eckert RL.
PMID: 34610184
Mol Carcinog. 2022 Jan;61(1):19-32. doi: 10.1002/mc.23356. Epub 2021 Oct 05.

Type 2 transglutaminase (TG2) functions as an important cancer cell survival protein in a range of cancers including epidermal squamous cell carcinoma. TG2 exists in open and closed conformations each of which has a distinct and mutually exclusive activity....

Cite
Rorke EA, Adhikary G, Szmacinski H, et al. Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Mol Carcinog. 2021;61(1):19-32doi: 10.1002/mc.23356.
Rorke, E. A., Adhikary, G., Szmacinski, H., Lakowicz, J. R., Weber, D. J., Godoy-Ruiz, R., Puranik, P., Keillor, J. W., Gates, E. W. J., & Eckert, R. L. (2022). Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Molecular carcinogenesis, 61(1), 19-32. https://doi.org/10.1002/mc.23356
Rorke, Ellen A, et al. "Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity." Molecular carcinogenesis vol. 61,1 (2022): 19-32. doi: https://doi.org/10.1002/mc.23356
Rorke EA, Adhikary G, Szmacinski H, Lakowicz JR, Weber DJ, Godoy-Ruiz R, Puranik P, Keillor JW, Gates EWJ, Eckert RL. Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Mol Carcinog. 2022 Jan;61(1):19-32. doi: 10.1002/mc.23356. Epub 2021 Oct 05. PMID: 34610184; PMCID: PMC8665039.
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Correction to: Transamidase site-targeted agents alter the conformation of the transglutaminase cancer stem cell survival protein to reduce GTP binding activity and cancer stem cell survival.

Oncogene

Kerr C, Szmacinski H, Fisher ML, Nance B, Lakowicz JR, Akbar A, Keillor JW, Wong TL, Godoy-Ruiz R, Toth EA, Weber DJ, Eckert RL.
PMID: 33658629
Oncogene. 2021 Apr;40(13):2479-2481. doi: 10.1038/s41388-021-01709-5.

No abstract available.

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Kerr C, Szmacinski H, Fisher ML, et al. Correction to: Transamidase site-targeted agents alter the conformation of the transglutaminase cancer stem cell survival protein to reduce GTP binding activity and cancer stem cell survival. Oncogene. 2021;40(13):2479-2481doi: 10.1038/s41388-021-01709-5.
Kerr, C., Szmacinski, H., Fisher, M. L., Nance, B., Lakowicz, J. R., Akbar, A., Keillor, J. W., Wong, T. L., Godoy-Ruiz, R., Toth, E. A., Weber, D. J., & Eckert, R. L. (2021). Correction to: Transamidase site-targeted agents alter the conformation of the transglutaminase cancer stem cell survival protein to reduce GTP binding activity and cancer stem cell survival. Oncogene, 40(13), 2479-2481. https://doi.org/10.1038/s41388-021-01709-5
Kerr, C, et al. "Correction to: Transamidase site-targeted agents alter the conformation of the transglutaminase cancer stem cell survival protein to reduce GTP binding activity and cancer stem cell survival." Oncogene vol. 40,13 (2021): 2479-2481. doi: https://doi.org/10.1038/s41388-021-01709-5
Kerr C, Szmacinski H, Fisher ML, Nance B, Lakowicz JR, Akbar A, Keillor JW, Wong TL, Godoy-Ruiz R, Toth EA, Weber DJ, Eckert RL. Correction to: Transamidase site-targeted agents alter the conformation of the transglutaminase cancer stem cell survival protein to reduce GTP binding activity and cancer stem cell survival. Oncogene. 2021 Apr;40(13):2479-2481. doi: 10.1038/s41388-021-01709-5. PMID: 33658629.
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Dysregulation of Transglutaminase type 2 through GATA3 defines aggressiveness and Doxorubicin sensitivity in breast cancer.

International journal of biological sciences

Aguiari G, Crudele F, Taccioli C, Minotti L, Corrà F, Keillor JW, Grassilli S, Cervellati C, Volinia S, Bergamini CM, Bianchi N.
PMID: 34975314
Int J Biol Sci. 2022 Jan 01;18(1):1-14. doi: 10.7150/ijbs.64167. eCollection 2022.

The role of transglutaminase type 2 in cell physiology is related to protein transamidation and signal transduction (affecting extracellular, intracellular and nuclear processes) aided by the expression of truncated isoforms and of two lncRNAs with regulatory functions. In breast...

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Aguiari G, Crudele F, Taccioli C, et al. Dysregulation of Transglutaminase type 2 through GATA3 defines aggressiveness and Doxorubicin sensitivity in breast cancer. Int J Biol Sci. 2022;18(1):1-14doi: 10.7150/ijbs.64167.
Aguiari, G., Crudele, F., Taccioli, C., Minotti, L., Corrà, F., Keillor, J. W., Grassilli, S., Cervellati, C., Volinia, S., Bergamini, C. M., & Bianchi, N. (2022). Dysregulation of Transglutaminase type 2 through GATA3 defines aggressiveness and Doxorubicin sensitivity in breast cancer. International journal of biological sciences, 18(1), 1-14. https://doi.org/10.7150/ijbs.64167
Aguiari, Gianluca, et al. "Dysregulation of Transglutaminase type 2 through GATA3 defines aggressiveness and Doxorubicin sensitivity in breast cancer." International journal of biological sciences vol. 18,1 (2022): 1-14. doi: https://doi.org/10.7150/ijbs.64167
Aguiari G, Crudele F, Taccioli C, Minotti L, Corrà F, Keillor JW, Grassilli S, Cervellati C, Volinia S, Bergamini CM, Bianchi N. Dysregulation of Transglutaminase type 2 through GATA3 defines aggressiveness and Doxorubicin sensitivity in breast cancer. Int J Biol Sci. 2022 Jan 01;18(1):1-14. doi: 10.7150/ijbs.64167. eCollection 2022. PMID: 34975314; PMCID: PMC8692156.
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Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity.

Molecular carcinogenesis

Rorke EA, Adhikary G, Szmacinski H, Lakowicz JR, Weber DJ, Godoy-Ruiz R, Puranik P, Keillor JW, Gates EWJ, Eckert RL.
PMID: 34610184
Mol Carcinog. 2022 Jan;61(1):19-32. doi: 10.1002/mc.23356. Epub 2021 Oct 05.

Type 2 transglutaminase (TG2) functions as an important cancer cell survival protein in a range of cancers including epidermal squamous cell carcinoma. TG2 exists in open and closed conformations each of which has a distinct and mutually exclusive activity....

Cite
Rorke EA, Adhikary G, Szmacinski H, et al. Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Mol Carcinog. 2021;61(1):19-32doi: 10.1002/mc.23356.
Rorke, E. A., Adhikary, G., Szmacinski, H., Lakowicz, J. R., Weber, D. J., Godoy-Ruiz, R., Puranik, P., Keillor, J. W., Gates, E. W. J., & Eckert, R. L. (2022). Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Molecular carcinogenesis, 61(1), 19-32. https://doi.org/10.1002/mc.23356
Rorke, Ellen A, et al. "Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity." Molecular carcinogenesis vol. 61,1 (2022): 19-32. doi: https://doi.org/10.1002/mc.23356
Rorke EA, Adhikary G, Szmacinski H, Lakowicz JR, Weber DJ, Godoy-Ruiz R, Puranik P, Keillor JW, Gates EWJ, Eckert RL. Sulforaphane covalently interacts with the transglutaminase 2 cancer maintenance protein to alter its structure and suppress its activity. Mol Carcinog. 2022 Jan;61(1):19-32. doi: 10.1002/mc.23356. Epub 2021 Oct 05. PMID: 34610184; PMCID: PMC8665039.
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Methods for using argon-39 to age-date groundwater using ultra-low-background proportional counting.

Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine

Mace E, Aalseth C, Brandenberger J, Day A, Hoppe E, Humble P, Keillor M, Kulongoski J, Overman C, Panisko M, Seifert A, White S, Wilcox Freeburg E, Williams R.
PMID: 28017500
Appl Radiat Isot. 2017 Aug;126:9-12. doi: 10.1016/j.apradiso.2016.12.037. Epub 2016 Dec 21.

Argon-39 can be used as a tracer for age-dating glaciers, oceans, and more recently, groundwater. With a half-life of 269 years,

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Mace E, Aalseth C, Brandenberger J, et al. Methods for using argon-39 to age-date groundwater using ultra-low-background proportional counting. Appl Radiat Isot. 2016;126:9-12doi: 10.1016/j.apradiso.2016.12.037.
Mace, E., Aalseth, C., Brandenberger, J., Day, A., Hoppe, E., Humble, P., Keillor, M., Kulongoski, J., Overman, C., Panisko, M., Seifert, A., White, S., Wilcox Freeburg, E., & Williams, R. (2017). Methods for using argon-39 to age-date groundwater using ultra-low-background proportional counting. Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine, 1269-12. https://doi.org/10.1016/j.apradiso.2016.12.037
Mace, Emily, et al. "Methods for using argon-39 to age-date groundwater using ultra-low-background proportional counting." Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine vol. 126 (2017): 9-12. doi: https://doi.org/10.1016/j.apradiso.2016.12.037
Mace E, Aalseth C, Brandenberger J, Day A, Hoppe E, Humble P, Keillor M, Kulongoski J, Overman C, Panisko M, Seifert A, White S, Wilcox Freeburg E, Williams R. Methods for using argon-39 to age-date groundwater using ultra-low-background proportional counting. Appl Radiat Isot. 2017 Aug;126:9-12. doi: 10.1016/j.apradiso.2016.12.037. Epub 2016 Dec 21. PMID: 28017500.
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The Motility and Mesenchymal Features of Breast Cancer Cells Correlate with the Levels and Intracellular Localization of Transglutaminase Type 2.

Cells

Bianchi N, Brugnoli F, Grassilli S, Bourgeois K, Keillor JW, Bergamini CM, Aguiari G, Volinia S, Bertagnolo V.
PMID: 34831282
Cells. 2021 Nov 06;10(11). doi: 10.3390/cells10113059.

We have investigated motility in breast cancer cell lines in association with the expression of Transglutaminase type 2 (TG2) as well as upon the administration of Doxorubicin (Dox), an active cytotoxic agent that is employed in chemotherapy. The exposure...

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Bianchi N, Brugnoli F, Grassilli S, et al. The Motility and Mesenchymal Features of Breast Cancer Cells Correlate with the Levels and Intracellular Localization of Transglutaminase Type 2. Cells. 2021;10(11)doi: 10.3390/cells10113059.
Bianchi, N., Brugnoli, F., Grassilli, S., Bourgeois, K., Keillor, J. W., Bergamini, C. M., Aguiari, G., Volinia, S., & Bertagnolo, V. (2021). The Motility and Mesenchymal Features of Breast Cancer Cells Correlate with the Levels and Intracellular Localization of Transglutaminase Type 2. Cells, 10(11), . https://doi.org/10.3390/cells10113059
Bianchi, Nicoletta, et al. "The Motility and Mesenchymal Features of Breast Cancer Cells Correlate with the Levels and Intracellular Localization of Transglutaminase Type 2." Cells vol. 10,11 (2021). doi: https://doi.org/10.3390/cells10113059
Bianchi N, Brugnoli F, Grassilli S, Bourgeois K, Keillor JW, Bergamini CM, Aguiari G, Volinia S, Bertagnolo V. The Motility and Mesenchymal Features of Breast Cancer Cells Correlate with the Levels and Intracellular Localization of Transglutaminase Type 2. Cells. 2021 Nov 06;10(11). doi: 10.3390/cells10113059. PMID: 34831282; PMCID: PMC8616519.
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Development of new scaffolds as reversible tissue transglutaminase inhibitors, with improved potency or resistance to glutathione addition.

MedChemComm

Apperley KYP, Roy I, Saucier V, Brunet-Filion N, Piscopo SP, Pardin C, De Francesco É, Hao C, Keillor JW.
PMID: 30108749
Medchemcomm. 2016 Dec 05;8(2):338-345. doi: 10.1039/c6md00565a. eCollection 2017 Feb 01.

Previous studies within our group have yielded a class of cinnamoyl-based competitive reversible inhibitors for tissue transglutaminase (TG2), with

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Apperley KYP, Roy I, Saucier V, et al. Development of new scaffolds as reversible tissue transglutaminase inhibitors, with improved potency or resistance to glutathione addition. Medchemcomm. 2016;8(2):338-345doi: 10.1039/c6md00565a.
Apperley, K. Y. P., Roy, I., Saucier, V., Brunet-Filion, N., Piscopo, S. P., Pardin, C., De Francesco, �. �., Hao, C., & Keillor, J. W. (2017). Development of new scaffolds as reversible tissue transglutaminase inhibitors, with improved potency or resistance to glutathione addition. MedChemComm, 8(2), 338-345. https://doi.org/10.1039/c6md00565a
Apperley, Kim Y P, et al. "Development of new scaffolds as reversible tissue transglutaminase inhibitors, with improved potency or resistance to glutathione addition." MedChemComm vol. 8,2 (2017): 338-345. doi: https://doi.org/10.1039/c6md00565a
Apperley KYP, Roy I, Saucier V, Brunet-Filion N, Piscopo SP, Pardin C, De Francesco É, Hao C, Keillor JW. Development of new scaffolds as reversible tissue transglutaminase inhibitors, with improved potency or resistance to glutathione addition. Medchemcomm. 2016 Dec 05;8(2):338-345. doi: 10.1039/c6md00565a. eCollection 2017 Feb 01. PMID: 30108749; PMCID: PMC6072418.
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