Abstract

Protein analysis is the foundation to understanding the mechanisms of complex biological processes. As one of the most widely used techniques to determine protein species and contents, protein dot blot aids biology research but needs corresponding antibodies for marking. A label-free detection method based on terahertz time-domain spectroscopy (THz-TDS) is proposed and demonstrated to improve this traditional technology. A membrane loaded with protein samples is directly scanned using a transmission THz-TDS system for spectral imaging. Different kinds of proteins can be distinguished by the refractive index extracted from the THz transmission spectrum. The intensity or shade imaged with the THz transmission spectrum can help detect the protein quantitatively. The feasibility of this new protein assay is demonstrated by the results of systematic testing with actual samples prepared with the dot-blot protocol.

© 2018 Optical Society of America under the terms of the OSA Open Access Publishing Agreement

Full Article  |  PDF Article

Corrections

7 February 2018: A typographical correction was made to the author listing.


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References

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    [Crossref]

2017 (2)

M.-M. Hu and H.-B. Shu, “Multifaceted roles of TRIM38 in innate immune and inflammatory responses,” Cell. Mol. Immunol. 14(4), 331–338 (2017).
[Crossref] [PubMed]

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

2016 (2)

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

2015 (1)

L. Xie, W. Gao, J. Shu, Y. Ying, and J. Kono, “Extraordinary sensitivity enhancement by metasurfaces in terahertz detection of antibiotics,” Sci. Rep. 5(1), 8671 (2015).
[Crossref] [PubMed]

2014 (3)

Z. P. Zheng, W. H. Fan, H. Li, and J. Tang, “Terahertz spectral investigation of anhydrous and monohydrated glucose using terahertz spectroscopy and solid-state theory,” J. Mol. Spectrosc. 296, 9–13 (2014).
[Crossref]

S. Funkner, G. Niehues, D. A. Schmidt, and E. Brundermann, “Terahertz Absorption of Chemicals in Water: Ideal and Real Solutions and Mixtures,” J Infrared Millim Te 35(1), 38–52 (2014).
[Crossref]

C. P. Moritz, S. X. Marz, R. Reiss, T. Schulenborg, and E. Friauf, “Epicocconone staining: A powerful loading control for Western blots,” Proteomics 14(2-3), 162–168 (2014).
[Crossref] [PubMed]

2013 (5)

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

J. E. Gilda and A. V. Gomes, “Stain-Free total protein staining is a superior loading control to β-actin for Western blots,” Anal. Biochem. 440(2), 186–188 (2013).
[Crossref] [PubMed]

Y. H. Ma, Q. Wang, and L. Y. Li, “PLS model investigation of thiabendazole based on THz spectrum,” J Quant Spectrosc Ra 117(3), 7–14 (2013).
[Crossref]

Q. Wang and Y. H. Ma, “Qualitative and quantitative identification of nitrofen in terahertz region,” Chemometr Intell Lab 127, 43–48 (2013).
[Crossref]

2012 (2)

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

2011 (2)

P. U. Jepsen, D. G. Cooke, and M. Koch, “Terahertz spectroscopy and imaging - Modern techniques and applications,” Laser Photonics Rev. 5(1), 124–166 (2011).
[Crossref]

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

2010 (1)

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

2009 (1)

B. Born, H. Weingärtner, E. Bründermann, and M. Havenith, “Solvation Dynamics of Model Peptides Probed by Terahertz Spectroscopy. Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[Crossref] [PubMed]

2007 (1)

D. F. Plusquellic, K. Siegrist, E. J. Heilweil, and O. Esenturk, “Applications of terahertz spectroscopy in biosystems,” ChemPhysChem 8(17), 2412–2431 (2007).
[Crossref] [PubMed]

2003 (1)

A. Fernández and R. Scott, “Dehydron: A structurally encoded signal for protein interaction,” Biophys. J. 85(3), 1914–1928 (2003).
[Crossref] [PubMed]

2002 (1)

B. M. Fischer, M. Walther, and P. Uhd Jepsen, “Far-infrared vibrational modes of DNA components studied by terahertz time-domain spectroscopy,” Phys. Med. Biol. 47(21), 3807–3814 (2002).
[Crossref] [PubMed]

2001 (1)

P. A. Fields, “Review: Protein function at thermal extremes: balancing stability and flexibility,” Comp. Biochem. Physiol. A Mol. Integr. Physiol. 129(2-3), 417–431 (2001).
[Crossref] [PubMed]

1999 (1)

L. Vera-Cabrera, A. Rendon, M. Diaz-Rodriguez, V. Handzel, and A. Laszlo, “Dot Blot Assay for Detection of Antidiacyltrehalose Antibodies in Tuberculous Patients,” Clin. Diagn. Lab. Immunol. 6(5), 686–689 (1999).
[PubMed]

1998 (1)

R. Folitse, D. A. Halvorson, and V. Sivanandan, “A Dot Immunoblotting Assay (Dot Blot ELISA) for Early Detection of Newcastle Disease Antibodies in Chickens,” Avian Dis. 42(1), 14–19 (1998).
[Crossref] [PubMed]

1997 (1)

T. H. Duong and K. Zakrzewska, “Calculation and analysis of low frequency normal modes for DNA,” J. Comput. Chem. 18(6), 796–811 (1997).
[Crossref]

1996 (2)

T. Zor and Z. Selinger, “Linearization of the bradford protein assay increases its sensitivity: Theoretical and experimental studies,” Anal. Biochem. 236(2), 302–308 (1996).
[Crossref] [PubMed]

L. Duvillaret, F. Garet, and J. L. Coutaz, “A reliable method for extraction of material parameters in terahertz timedomain spectroscopy,” IEEE J Sel Top Quant 2(3), 739–746 (1996).
[Crossref]

1995 (1)

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

1993 (1)

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

1883 (1)

K. Johan, “New method for the determination of nitrogen in organic substances,” Z. Anal. Chem. 22(1), 366–383 (1883).

1847 (1)

W. George, “New decomposition product of urea,” J. Prakt. Chem. 42(3–4), 255–256 (1847).

Abbey, Y. A.

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

Amemiya, C. T.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Balci, S.

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

Baughman, W. E.

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

Biller, S. A.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Born, B.

B. Born, H. Weingärtner, E. Bründermann, and M. Havenith, “Solvation Dynamics of Model Peptides Probed by Terahertz Spectroscopy. Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[Crossref] [PubMed]

Brundermann, E.

S. Funkner, G. Niehues, D. A. Schmidt, and E. Brundermann, “Terahertz Absorption of Chemicals in Water: Ideal and Real Solutions and Mixtures,” J Infrared Millim Te 35(1), 38–52 (2014).
[Crossref]

Bründermann, E.

B. Born, H. Weingärtner, E. Bründermann, and M. Havenith, “Solvation Dynamics of Model Peptides Probed by Terahertz Spectroscopy. Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[Crossref] [PubMed]

Bryant, Q. M.

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

Cerna, C. Z.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Chang, A.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Chang, T.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Chen, J.

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Chertihin, O.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Chu, C. H.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Cooke, D. G.

P. U. Jepsen, D. G. Cooke, and M. Koch, “Terahertz spectroscopy and imaging - Modern techniques and applications,” Laser Photonics Rev. 5(1), 124–166 (2011).
[Crossref]

Coutaz, J. L.

L. Duvillaret, F. Garet, and J. L. Coutaz, “A reliable method for extraction of material parameters in terahertz timedomain spectroscopy,” IEEE J Sel Top Quant 2(3), 739–746 (1996).
[Crossref]

Cui, H. L.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

Cui, H.-L.

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Diaz-Rodriguez, M.

L. Vera-Cabrera, A. Rendon, M. Diaz-Rodriguez, V. Handzel, and A. Laszlo, “Dot Blot Assay for Detection of Antidiacyltrehalose Antibodies in Tuberculous Patients,” Clin. Diagn. Lab. Immunol. 6(5), 686–689 (1999).
[PubMed]

Dickson, J. K.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Dorofeeva, T.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Du, C.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
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Duong, T. H.

T. H. Duong and K. Zakrzewska, “Calculation and analysis of low frequency normal modes for DNA,” J. Comput. Chem. 18(6), 796–811 (1997).
[Crossref]

Duvillaret, L.

L. Duvillaret, F. Garet, and J. L. Coutaz, “A reliable method for extraction of material parameters in terahertz timedomain spectroscopy,” IEEE J Sel Top Quant 2(3), 739–746 (1996).
[Crossref]

Esenturk, O.

D. F. Plusquellic, K. Siegrist, E. J. Heilweil, and O. Esenturk, “Applications of terahertz spectroscopy in biosystems,” ChemPhysChem 8(17), 2412–2431 (2007).
[Crossref] [PubMed]

Everette, J. D.

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

Fan, W. H.

Z. P. Zheng, W. H. Fan, H. Li, and J. Tang, “Terahertz spectral investigation of anhydrous and monohydrated glucose using terahertz spectroscopy and solid-state theory,” J. Mol. Spectrosc. 296, 9–13 (2014).
[Crossref]

Fernández, A.

A. Fernández and R. Scott, “Dehydron: A structurally encoded signal for protein interaction,” Biophys. J. 85(3), 1914–1928 (2003).
[Crossref] [PubMed]

Fields, P. A.

P. A. Fields, “Review: Protein function at thermal extremes: balancing stability and flexibility,” Comp. Biochem. Physiol. A Mol. Integr. Physiol. 129(2-3), 417–431 (2001).
[Crossref] [PubMed]

Fischer, B. M.

B. M. Fischer, M. Walther, and P. Uhd Jepsen, “Far-infrared vibrational modes of DNA components studied by terahertz time-domain spectroscopy,” Phys. Med. Biol. 47(21), 3807–3814 (2002).
[Crossref] [PubMed]

Folitse, R.

R. Folitse, D. A. Halvorson, and V. Sivanandan, “A Dot Immunoblotting Assay (Dot Blot ELISA) for Early Detection of Newcastle Disease Antibodies in Chickens,” Avian Dis. 42(1), 14–19 (1998).
[Crossref] [PubMed]

Friauf, E.

C. P. Moritz, S. X. Marz, R. Reiss, T. Schulenborg, and E. Friauf, “Epicocconone staining: A powerful loading control for Western blots,” Proteomics 14(2-3), 162–168 (2014).
[Crossref] [PubMed]

Fu, W.

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

Funkner, S.

S. Funkner, G. Niehues, D. A. Schmidt, and E. Brundermann, “Terahertz Absorption of Chemicals in Water: Ideal and Real Solutions and Mixtures,” J Infrared Millim Te 35(1), 38–52 (2014).
[Crossref]

Gao, W.

L. Xie, W. Gao, J. Shu, Y. Ying, and J. Kono, “Extraordinary sensitivity enhancement by metasurfaces in terahertz detection of antibiotics,” Sci. Rep. 5(1), 8671 (2015).
[Crossref] [PubMed]

Garet, F.

L. Duvillaret, F. Garet, and J. L. Coutaz, “A reliable method for extraction of material parameters in terahertz timedomain spectroscopy,” IEEE J Sel Top Quant 2(3), 739–746 (1996).
[Crossref]

Gelmont, B.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
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W. George, “New decomposition product of urea,” J. Prakt. Chem. 42(3–4), 255–256 (1847).

Gilda, J. E.

J. E. Gilda and A. V. Gomes, “Stain-Free total protein staining is a superior loading control to β-actin for Western blots,” Anal. Biochem. 440(2), 186–188 (2013).
[Crossref] [PubMed]

Globus, T.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Gomes, A. V.

J. E. Gilda and A. V. Gomes, “Stain-Free total protein staining is a superior loading control to β-actin for Western blots,” Anal. Biochem. 440(2), 186–188 (2013).
[Crossref] [PubMed]

Green, A. M.

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

Gregg, R. E.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Grote, A.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Grundt, J. E.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Haire, R. N.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Halvorson, D. A.

R. Folitse, D. A. Halvorson, and V. Sivanandan, “A Dot Immunoblotting Assay (Dot Blot ELISA) for Early Detection of Newcastle Disease Antibodies in Chickens,” Avian Dis. 42(1), 14–19 (1998).
[Crossref] [PubMed]

Han, X.

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Handzel, V.

L. Vera-Cabrera, A. Rendon, M. Diaz-Rodriguez, V. Handzel, and A. Laszlo, “Dot Blot Assay for Detection of Antidiacyltrehalose Antibodies in Tuberculous Patients,” Clin. Diagn. Lab. Immunol. 6(5), 686–689 (1999).
[PubMed]

Havenith, M.

B. Born, H. Weingärtner, E. Bründermann, and M. Havenith, “Solvation Dynamics of Model Peptides Probed by Terahertz Spectroscopy. Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[Crossref] [PubMed]

Heilweil, E. J.

D. F. Plusquellic, K. Siegrist, E. J. Heilweil, and O. Esenturk, “Applications of terahertz spectroscopy in biosystems,” ChemPhysChem 8(17), 2412–2431 (2007).
[Crossref] [PubMed]

Hinds-Frey, K. R.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Hu, M.-M.

M.-M. Hu and H.-B. Shu, “Multifaceted roles of TRIM38 in innate immune and inflammatory responses,” Cell. Mol. Immunol. 14(4), 331–338 (2017).
[Crossref] [PubMed]

Hulst, M.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Ibey, B. L.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Jamil, H.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Jepsen, P. U.

P. U. Jepsen, D. G. Cooke, and M. Koch, “Terahertz spectroscopy and imaging - Modern techniques and applications,” Laser Photonics Rev. 5(1), 124–166 (2011).
[Crossref]

Johan, K.

K. Johan, “New method for the determination of nitrogen in organic substances,” Z. Anal. Chem. 22(1), 366–383 (1883).

Khromova, T.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Kim, S. M.

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

Koch, M.

P. U. Jepsen, D. G. Cooke, and M. Koch, “Terahertz spectroscopy and imaging - Modern techniques and applications,” Laser Photonics Rev. 5(1), 124–166 (2011).
[Crossref]

Kono, J.

L. Xie, W. Gao, J. Shu, Y. Ying, and J. Kono, “Extraordinary sensitivity enhancement by metasurfaces in terahertz detection of antibiotics,” Sci. Rep. 5(1), 8671 (2015).
[Crossref] [PubMed]

Koryakina, Y.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Kung, P.

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

Lago, M. W.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Laman, N.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Lang, M.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Laszlo, A.

L. Vera-Cabrera, A. Rendon, M. Diaz-Rodriguez, V. Handzel, and A. Laszlo, “Dot Blot Assay for Detection of Antidiacyltrehalose Antibodies in Tuberculous Patients,” Clin. Diagn. Lab. Immunol. 6(5), 686–689 (1999).
[PubMed]

Li, H.

Z. P. Zheng, W. H. Fan, H. Li, and J. Tang, “Terahertz spectral investigation of anhydrous and monohydrated glucose using terahertz spectroscopy and solid-state theory,” J. Mol. Spectrosc. 296, 9–13 (2014).
[Crossref]

Li, L. Y.

Y. H. Ma, Q. Wang, and L. Y. Li, “PLS model investigation of thiabendazole based on THz spectrum,” J Quant Spectrosc Ra 117(3), 7–14 (2013).
[Crossref]

Li, W.

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Litman, G. W.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Litman, R. T.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Liu, Y.

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

Luo, Y.

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

Lvovska, M.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Ma, Y.

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Ma, Y. H.

Y. H. Ma, Q. Wang, and L. Y. Li, “PLS model investigation of thiabendazole based on THz spectrum,” J Quant Spectrosc Ra 117(3), 7–14 (2013).
[Crossref]

Q. Wang and Y. H. Ma, “Qualitative and quantitative identification of nitrofen in terahertz region,” Chemometr Intell Lab 127, 43–48 (2013).
[Crossref]

Marz, S. X.

C. P. Moritz, S. X. Marz, R. Reiss, T. Schulenborg, and E. Friauf, “Epicocconone staining: A powerful loading control for Western blots,” Proteomics 14(2-3), 162–168 (2014).
[Crossref] [PubMed]

Moritz, C. P.

C. P. Moritz, S. X. Marz, R. Reiss, T. Schulenborg, and E. Friauf, “Epicocconone staining: A powerful loading control for Western blots,” Proteomics 14(2-3), 162–168 (2014).
[Crossref] [PubMed]

Munaretto, C.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Niehues, G.

S. Funkner, G. Niehues, D. A. Schmidt, and E. Brundermann, “Terahertz Absorption of Chemicals in Water: Ideal and Real Solutions and Mixtures,” J Infrared Millim Te 35(1), 38–52 (2014).
[Crossref]

Peralta, X. G.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Placzek, S.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Plusquellic, D. F.

D. F. Plusquellic, K. Siegrist, E. J. Heilweil, and O. Esenturk, “Applications of terahertz spectroscopy in biosystems,” ChemPhysChem 8(17), 2412–2431 (2007).
[Crossref] [PubMed]

Rast, J. P.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Reiss, R.

C. P. Moritz, S. X. Marz, R. Reiss, T. Schulenborg, and E. Friauf, “Epicocconone staining: A powerful loading control for Western blots,” Proteomics 14(2-3), 162–168 (2014).
[Crossref] [PubMed]

Rendon, A.

L. Vera-Cabrera, A. Rendon, M. Diaz-Rodriguez, V. Handzel, and A. Laszlo, “Dot Blot Assay for Detection of Antidiacyltrehalose Antibodies in Tuberculous Patients,” Clin. Diagn. Lab. Immunol. 6(5), 686–689 (1999).
[PubMed]

Rinehart, J. K.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Rivest, B. D.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Roach, W. P.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Roess, W.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Roth, C. C.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Rother, M.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Scheer, M.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Schmidt, D. A.

S. Funkner, G. Niehues, D. A. Schmidt, and E. Brundermann, “Terahertz Absorption of Chemicals in Water: Ideal and Real Solutions and Mixtures,” J Infrared Millim Te 35(1), 38–52 (2014).
[Crossref]

Schomburg, D.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Schomburg, I.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Schulenborg, T.

C. P. Moritz, S. X. Marz, R. Reiss, T. Schulenborg, and E. Friauf, “Epicocconone staining: A powerful loading control for Western blots,” Proteomics 14(2-3), 162–168 (2014).
[Crossref] [PubMed]

Schulkin, B.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Scott, R.

A. Fernández and R. Scott, “Dehydron: A structurally encoded signal for protein interaction,” Biophys. J. 85(3), 1914–1928 (2003).
[Crossref] [PubMed]

Selinger, Z.

T. Zor and Z. Selinger, “Linearization of the bradford protein assay increases its sensitivity: Theoretical and experimental studies,” Anal. Biochem. 236(2), 302–308 (1996).
[Crossref] [PubMed]

Shamblott, M. J.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Shi, C.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Shu, H.-B.

M.-M. Hu and H.-B. Shu, “Multifaceted roles of TRIM38 in innate immune and inflammatory responses,” Cell. Mol. Immunol. 14(4), 331–338 (2017).
[Crossref] [PubMed]

Shu, J.

L. Xie, W. Gao, J. Shu, Y. Ying, and J. Kono, “Extraordinary sensitivity enhancement by metasurfaces in terahertz detection of antibiotics,” Sci. Rep. 5(1), 8671 (2015).
[Crossref] [PubMed]

Siegrist, K.

D. F. Plusquellic, K. Siegrist, E. J. Heilweil, and O. Esenturk, “Applications of terahertz spectroscopy in biosystems,” ChemPhysChem 8(17), 2412–2431 (2007).
[Crossref] [PubMed]

Sivanandan, V.

R. Folitse, D. A. Halvorson, and V. Sivanandan, “A Dot Immunoblotting Assay (Dot Blot ELISA) for Early Detection of Newcastle Disease Antibodies in Chickens,” Avian Dis. 42(1), 14–19 (1998).
[Crossref] [PubMed]

Sizov, I.

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Söhngen, C.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Stelzer, M.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Tang, J.

Z. P. Zheng, W. H. Fan, H. Li, and J. Tang, “Terahertz spectral investigation of anhydrous and monohydrated glucose using terahertz spectroscopy and solid-state theory,” J. Mol. Spectrosc. 296, 9–13 (2014).
[Crossref]

Tongue, T.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Uhd Jepsen, P.

B. M. Fischer, M. Walther, and P. Uhd Jepsen, “Far-infrared vibrational modes of DNA components studied by terahertz time-domain spectroscopy,” Phys. Med. Biol. 47(21), 3807–3814 (2002).
[Crossref] [PubMed]

Ulas, S.

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Vera-Cabrera, L.

L. Vera-Cabrera, A. Rendon, M. Diaz-Rodriguez, V. Handzel, and A. Laszlo, “Dot Blot Assay for Detection of Antidiacyltrehalose Antibodies in Tuberculous Patients,” Clin. Diagn. Lab. Immunol. 6(5), 686–689 (1999).
[PubMed]

Walker, R. B.

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

Walther, M.

B. M. Fischer, M. Walther, and P. Uhd Jepsen, “Far-infrared vibrational modes of DNA components studied by terahertz time-domain spectroscopy,” Phys. Med. Biol. 47(21), 3807–3814 (2002).
[Crossref] [PubMed]

Wang, Q.

Y. H. Ma, Q. Wang, and L. Y. Li, “PLS model investigation of thiabendazole based on THz spectrum,” J Quant Spectrosc Ra 117(3), 7–14 (2013).
[Crossref]

Q. Wang and Y. H. Ma, “Qualitative and quantitative identification of nitrofen in terahertz region,” Chemometr Intell Lab 127, 43–48 (2013).
[Crossref]

Wangila, G. W.

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

Wei, D.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Weingärtner, H.

B. Born, H. Weingärtner, E. Bründermann, and M. Havenith, “Solvation Dynamics of Model Peptides Probed by Terahertz Spectroscopy. Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[Crossref] [PubMed]

Wetterau, J. R.

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

Wilbert, D. S.

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

Wilmink, G. J.

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

Xie, L.

L. Xie, W. Gao, J. Shu, Y. Ying, and J. Kono, “Extraordinary sensitivity enhancement by metasurfaces in terahertz detection of antibiotics,” Sci. Rep. 5(1), 8671 (2015).
[Crossref] [PubMed]

Xing, L.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

Yang, K.

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

Yang, X.

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

Ying, Y.

L. Xie, W. Gao, J. Shu, Y. Ying, and J. Kono, “Extraordinary sensitivity enhancement by metasurfaces in terahertz detection of antibiotics,” Sci. Rep. 5(1), 8671 (2015).
[Crossref] [PubMed]

Yokus, H.

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

Zakrzewska, K.

T. H. Duong and K. Zakrzewska, “Calculation and analysis of low frequency normal modes for DNA,” J. Comput. Chem. 18(6), 796–811 (1997).
[Crossref]

Zhang, J.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Zhang, S.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

Zhang, Y.

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Zhang, Z.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

Zhao, X.

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

Zheng, Z. P.

Z. P. Zheng, W. H. Fan, H. Li, and J. Tang, “Terahertz spectral investigation of anhydrous and monohydrated glucose using terahertz spectroscopy and solid-state theory,” J. Mol. Spectrosc. 296, 9–13 (2014).
[Crossref]

Zhou, Y.

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Zhou, Z.

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

Zilch, A.

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Zor, T.

T. Zor and Z. Selinger, “Linearization of the bradford protein assay increases its sensitivity: Theoretical and experimental studies,” Anal. Biochem. 236(2), 302–308 (1996).
[Crossref] [PubMed]

American Journal of Biomedical Engineering (2)

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz vibrational spectroscopy of bacterial cells and molecular components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

T. Globus, T. Dorofeeva, I. Sizov, B. Gelmont, M. Lvovska, T. Khromova, O. Chertihin, and Y. Koryakina, “Sub-THz Vibrational Spectroscopy of Bacterial Cells and Molecular Components,” American Journal of Biomedical Engineering 2(4), 143–154 (2012).
[Crossref]

Anal. Biochem. (2)

T. Zor and Z. Selinger, “Linearization of the bradford protein assay increases its sensitivity: Theoretical and experimental studies,” Anal. Biochem. 236(2), 302–308 (1996).
[Crossref] [PubMed]

J. E. Gilda and A. V. Gomes, “Stain-Free total protein staining is a superior loading control to β-actin for Western blots,” Anal. Biochem. 440(2), 186–188 (2013).
[Crossref] [PubMed]

Avian Dis. (1)

R. Folitse, D. A. Halvorson, and V. Sivanandan, “A Dot Immunoblotting Assay (Dot Blot ELISA) for Early Detection of Newcastle Disease Antibodies in Chickens,” Avian Dis. 42(1), 14–19 (1998).
[Crossref] [PubMed]

Biophys. J. (1)

A. Fernández and R. Scott, “Dehydron: A structurally encoded signal for protein interaction,” Biophys. J. 85(3), 1914–1928 (2003).
[Crossref] [PubMed]

Cell. Mol. Immunol. (1)

M.-M. Hu and H.-B. Shu, “Multifaceted roles of TRIM38 in innate immune and inflammatory responses,” Cell. Mol. Immunol. 14(4), 331–338 (2017).
[Crossref] [PubMed]

Chemometr Intell Lab (1)

Q. Wang and Y. H. Ma, “Qualitative and quantitative identification of nitrofen in terahertz region,” Chemometr Intell Lab 127, 43–48 (2013).
[Crossref]

ChemPhysChem (1)

D. F. Plusquellic, K. Siegrist, E. J. Heilweil, and O. Esenturk, “Applications of terahertz spectroscopy in biosystems,” ChemPhysChem 8(17), 2412–2431 (2007).
[Crossref] [PubMed]

Clin. Diagn. Lab. Immunol. (1)

L. Vera-Cabrera, A. Rendon, M. Diaz-Rodriguez, V. Handzel, and A. Laszlo, “Dot Blot Assay for Detection of Antidiacyltrehalose Antibodies in Tuberculous Patients,” Clin. Diagn. Lab. Immunol. 6(5), 686–689 (1999).
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P. A. Fields, “Review: Protein function at thermal extremes: balancing stability and flexibility,” Comp. Biochem. Physiol. A Mol. Integr. Physiol. 129(2-3), 417–431 (2001).
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IEEE J Sel Top Quant (1)

L. Duvillaret, F. Garet, and J. L. Coutaz, “A reliable method for extraction of material parameters in terahertz timedomain spectroscopy,” IEEE J Sel Top Quant 2(3), 739–746 (1996).
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IEEE J. Biomed. Health Inform. (1)

W. E. Baughman, H. Yokus, S. Balci, D. S. Wilbert, P. Kung, and S. M. Kim, “Observation of Hydrofluoric Acid Burns on Osseous Tissues by Means of Terahertz Spectroscopic Imaging,” IEEE J. Biomed. Health Inform. 17(4), 798–805 (2013).
[Crossref] [PubMed]

J Infrared Millim Te (1)

S. Funkner, G. Niehues, D. A. Schmidt, and E. Brundermann, “Terahertz Absorption of Chemicals in Water: Ideal and Real Solutions and Mixtures,” J Infrared Millim Te 35(1), 38–52 (2014).
[Crossref]

J Quant Spectrosc Ra (1)

Y. H. Ma, Q. Wang, and L. Y. Li, “PLS model investigation of thiabendazole based on THz spectrum,” J Quant Spectrosc Ra 117(3), 7–14 (2013).
[Crossref]

J. Agric. Food Chem. (1)

J. D. Everette, Q. M. Bryant, A. M. Green, Y. A. Abbey, G. W. Wangila, and R. B. Walker, “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent,” J. Agric. Food Chem. 58(14), 8139–8144 (2010).
[Crossref] [PubMed]

J. Am. Chem. Soc. (1)

B. Born, H. Weingärtner, E. Bründermann, and M. Havenith, “Solvation Dynamics of Model Peptides Probed by Terahertz Spectroscopy. Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[Crossref] [PubMed]

J. Biol. Chem. (1)

H. Jamil, J. K. Dickson, C. H. Chu, M. W. Lago, J. K. Rinehart, S. A. Biller, R. E. Gregg, and J. R. Wetterau, “Microsomal triglyceride transfer protein. Specificity of lipid binding and transport,” J. Biol. Chem. 270(12), 6549–6554 (1995).
[Crossref] [PubMed]

J. Biomed. Opt. (1)

G. J. Wilmink, B. L. Ibey, T. Tongue, B. Schulkin, N. Laman, X. G. Peralta, C. C. Roth, C. Z. Cerna, B. D. Rivest, J. E. Grundt, and W. P. Roach, “Development of a compact terahertz time-domain spectrometer for the measurement of the optical properties of biological tissues,” J. Biomed. Opt. 16(4), 047006 (2011).
[Crossref] [PubMed]

J. Comput. Chem. (1)

T. H. Duong and K. Zakrzewska, “Calculation and analysis of low frequency normal modes for DNA,” J. Comput. Chem. 18(6), 796–811 (1997).
[Crossref]

J. Mol. Spectrosc. (1)

Z. P. Zheng, W. H. Fan, H. Li, and J. Tang, “Terahertz spectral investigation of anhydrous and monohydrated glucose using terahertz spectroscopy and solid-state theory,” J. Mol. Spectrosc. 296, 9–13 (2014).
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P. U. Jepsen, D. G. Cooke, and M. Koch, “Terahertz spectroscopy and imaging - Modern techniques and applications,” Laser Photonics Rev. 5(1), 124–166 (2011).
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Mol. Biol. Evol. (1)

G. W. Litman, J. P. Rast, M. J. Shamblott, R. N. Haire, M. Hulst, W. Roess, R. T. Litman, K. R. Hinds-Frey, A. Zilch, and C. T. Amemiya, “Phylogenetic diversification of immunoglobulin genes and the antibody repertoire,” Mol. Biol. Evol. 10(1), 60–72 (1993).
[PubMed]

Nucleic Acids Res. (1)

I. Schomburg, A. Chang, S. Placzek, C. Söhngen, M. Rother, M. Lang, C. Munaretto, S. Ulas, M. Stelzer, A. Grote, M. Scheer, and D. Schomburg, “BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA,” Nucleic Acids Res. 41, D764–D772 (2013).
[PubMed]

Phys. Med. Biol. (1)

B. M. Fischer, M. Walther, and P. Uhd Jepsen, “Far-infrared vibrational modes of DNA components studied by terahertz time-domain spectroscopy,” Phys. Med. Biol. 47(21), 3807–3814 (2002).
[Crossref] [PubMed]

Polym. Test. (1)

L. Xing, H. L. Cui, C. Shi, Z. Zhang, J. Zhang, T. Chang, D. Wei, C. Du, S. Zhang, and Z. Zhou, “Nondestructive examination of polymethacrylimide composite structures with terahertz time-domain spectroscopy,” Polym. Test. 57, 141–148 (2017).
[Crossref]

Proteomics (1)

C. P. Moritz, S. X. Marz, R. Reiss, T. Schulenborg, and E. Friauf, “Epicocconone staining: A powerful loading control for Western blots,” Proteomics 14(2-3), 162–168 (2014).
[Crossref] [PubMed]

Sci. Rep. (1)

L. Xie, W. Gao, J. Shu, Y. Ying, and J. Kono, “Extraordinary sensitivity enhancement by metasurfaces in terahertz detection of antibiotics,” Sci. Rep. 5(1), 8671 (2015).
[Crossref] [PubMed]

Sensors (Basel) (1)

J. Zhang, W. Li, H.-L. Cui, C. Shi, X. Han, Y. Ma, J. Chen, T. Chang, D. Wei, Y. Zhang, and Y. Zhou, “Nondestructive evaluation of carbon fiber reinforced polymer composites using reflective terahertz imaging,” Sensors (Basel) 16(6), 875 (2016).
[Crossref] [PubMed]

Trends Biotechnol. (1)

X. Yang, X. Zhao, K. Yang, Y. Liu, Y. Liu, W. Fu, and Y. Luo, “Biomedical applications of terahertz spectroscopy and imaging,” Trends Biotechnol. 34(10), 810–824 (2016).
[Crossref] [PubMed]

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K. Johan, “New method for the determination of nitrogen in organic substances,” Z. Anal. Chem. 22(1), 366–383 (1883).

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[Crossref]

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Figures (6)

Fig. 1
Fig. 1 Schematic diagram of the THz-TDS system in the through-transmission imaging modes (M1–M5: mirrors; HDPE: high-density polyethylene; PCA: photoconductive antenna; TX: transmitter; RX: receiver).
Fig. 2
Fig. 2 Optical image of Membrane 1 after dripping protein samples in. Scale bar = 10 mm.
Fig. 3
Fig. 3 Optical image of Membrane 2 after dripping protein samples in. Scale bar = 10 mm.
Fig. 4
Fig. 4 Refractive index of the six kinds of protein rn21, rn22, rn28, n42, n43 and n53 in Membrane 2.
Fig. 5
Fig. 5 The imaging of the membrane: (a) the dot blot result, (b) the pseudo-color image of gray image formatted by the relative THz energy integration of transmission spectrum pixel by pixel.
Fig. 6
Fig. 6 The lines graphs: (a)-(f) are respectively the line graphs of Protein rn21, Protein rn22, Protein rn28, Protein n42, Protein n43 and Protein n53. Four curves in each graph are: standardized value of identified protein area by dot blot, standardized value of average integrated relative energy, and the fitting curves of the two values.

Tables (4)

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Table 1 Molecular mass of protein samples.

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Table 2 The average grayscale of the six kinds of proteins with the same quantity.

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Table 3 Information of fitting curves for the average integrated relative energy.

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Table 4 Information of fitting curves for the identified protein area.

Equations (3)

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n s ( ω ) = φ ( ω ) c ω d + 1
P re = ln ( E s ( ω ) E r ( ω ) ) 2
P c = f 2 f 1 P r e ( f )

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