Publications

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1. Terpetschnig E., Szmacinski H., Malak H., and Lakowicz J. R. Metal-Ligand Complexes as a New Class of Long-Lived Fluorophores for Protein Hydrodynamics. Biophys. J. 68, 342-350 (1995).

2. Szmacinski H., Terpetschnig E., & Lakowicz J. R. Synthesis and evaluation of Ru-complexes as anisotropy probes for protein hydrodynamics and immunoassays of high-molecular-weight antigens. Biophysical Chem. 62(1-3), 109-120 (1996).

3. Youn H. J., Terpetschnig E., Szmacinski H., & Lakowicz J. R. Fluorescence energy transfer immunoassay based on a long-lifetime luminescent metal-ligand complex. Anal. Biochem. 232(1), 24-30 (1995).

4. Oswald B., Patsenker L., Duschl J., Szmacinski H., Wolfbeis O.S., and Terpetschnig E. Synthesis, Spectral Properties, and Detection limits of reactive squaraine dyes, a new class of diode laser compatible fluorescent protein labels. Bioconj. Chem. 10, 925-931 (1999).

5. Oswald B., Lehmann F., Simon L., Terpetschnig E., and Wolfbeis O.S. Red laser-Induced fluorescence energy transfer in an immunosystem. Anal. Biochem. 280, 272–277 (2000).

6. Patsenker L., Kolosova O., Tatarets A., Fedyunyayeva I., Povrozin Ye., Yermolenko I., Kudryavtseva Yu., Terpetschnig E. Fluorescent probes and labels for biomedical applications. 10th Conference on Methods and Applications of Fluorescence (MAF-10), Salzburg (Austria), 9–12 September 2007, P. 154. Poster PRLS-36.

7. Patsenker L., Tatarets A., Kolosova O., Obukhova O., Povrozin Y., Fedyunyayeva I., Yermolenko I., Terpetschnig E. Fluorescent probes and labels for biomedical applications. Ann. N.Y. Acad. Sci. 1130, 179–187 (2008).

8. Luchowski R., Matveeva E.G., Gryczynski I., Terpetschnig E.A., Patsenker L., Laczko G., Borejdo J., Gryczynski Z. Single molecule studies of multiple-fluorophore labeled antibodies. Effect of homo-FRET on the number of photons available before photobleaching. Curr. Pharm. Biotech. 9, 411-420 (2008).

9. Povrozin Ye.A., Markova L.I., Tatarets A.L., Sidorov V.I. Terpetschnig E.A., Patsenker L.D. Near-infrared, dual-ratiometric fluorescent label for measurement of pH. Anal. Biochem. 390, 136–140 (2009).

10. Povrozin Y.A., Kolosova O.S., Obukhova O.M., Tatarets A.L., Sidorov V.I., Terpetschnig E.A., and Patsenker L.D. Seta-633 - A NIR fluorescence lifetime label for low-molecular-weight analytes. Bioconj. Chem. 20, 1807–1812 (2009).

11. Markova L.I., Povrozin Y.A., Khabuseva S.U., Patsenker L.D., Terpetschnig E.A. Seta-647 — A brighter and more photostable replacement for Cy5. 11th Conference on Methods and Applications of Fluorescence (MAF-11), Budapest (Hungary), 6–9 September 2009, Poster 63.

12. Fedyunyayeva I.A, Klochko O.P., Sidorov V.I., Khabuseva S.U., and Patsenker L.D. Long-wavelength, pH-sensitive benzodipyrrolenine-squaraine dye with pKa in the acidic pH Range. 11th Conference on Methods and Applications of Fluorescence (MAF-11), Budapest (Hungary), 6–9 September 2009, P. 65. Poster 7.

13. Kudriavtseva Y.A., Yermolenko I.G., Klochko O.P., Povrozin Y.A., Terpetschnig E.A., and Patsenker L.D. SeTau-665 — next generation, long-wavelength label with advanced characteristics. 11th Conference on Methods and Applications of Fluorescence (MAF-11), Budapest (Hungary), 6–9 September 2009, P. 66. Poster 8.

14. Tatarets A.L., Povrozin Y.A., Markova L.I., Sidorov V.I., Vysekantzev I.P., and Patsenker L.D. Dual ratiometric, red fluorescent dye for biolabelling in pH-sensing applications. 11th Conference on Methods and Applications of Fluorescence (MAF-11), Budapest (Hungary), 6–9 September 2009, P. 118. Poster 58.

15. Obukhova O.M., Povrozin Y.A., Terpetschnig E.A., and Patsenker L.D. New long-wavelength fluorescent protein labels with advanced characteristics. 11th Conference on Methods and Applications of Fluorescence (MAF-11), Budapest (Hungary), 6–9 September 2009, P. 155. Poster 95.

16. Luchowski R., Matveeva E.G., Shtoyko T., Sarkar P., Patsenker L.D., Klochko O.P., Terpetschnig E.A., Borejdo J., Akopova I., Gryczynski Z., Gryczynski I. Single molecule immunoassay on plasmonic platforms. Curr. Pharm. Biotech. 11, 96-102 (2010).

17. Roy R, Hohng S, and Ha T. A practical guide to single molecule FRET. Nature Methods. 5, 507 - 516 (2008).

18. Ioffe V.M., Gorbenko G.P., Tatarets A.L., Patsenker L.D. and Terpetschnig E.A. Examining protein-lipid interactions in model systems with a new squarylium fluorescent dye. J. Fluoresc. 16 (4), 547-554 (2006).

19. Lopukhin Y.M., Dobretsov G.E., Gryzunov Y.A. Bulletin of Experimental Biology and Medicine. 130:1, 615-619 (2000).

20. Dobretsov G.E., Syreishchikova T.I., Gryzunov Yu.A., Smolina N.V., Komar A.A. Biophysics. 55:2, 182-187 (2010). 

21. Webster et al. Comparison of nonlinear absorption in three similar dyes: polymethine, squaraine, and tetraone. Chem. Phys 348:143–151 (2008).

22. Przhonska O.V. et al. Two-photon absorption in NIR conjugated molecules: design strategy and structure-property relations in Advance Fluorescence Reporters in Chemistry and Biology (Vol. Ed. Demchenko) Springer Series of Fluorescence 8 (Series Ed. O.S. Wolfbeis) (2010). 

23. Liu L. et al. Homogeneous immunoassay based on two-photon excitation fluorescence resonance energy transfer. Anal. Chem. 80, 7735–7741 (2008). 

24. Podgorski K. et al. Ultra-bright and -stable red and NIR squaraine fluorphores for In-vivo 2-photon imaging. PLOS ONE 7(12):e51980 (2012). 

25. Resch-Genger U., DeRose P.C. Fluorescence standards: Classification, terminology, and recommendations on their selection, use, and production (IUPAC Technical Report). Pure Appl. Chem., 82:12, 2315–2335 (2010).

26. Midde K. Studies in molecular mechanisms of skeletal muscle contraction: applications to transgenic mice with inherited cardiomyopathies. UNTHSC, 2013.

27. Midde K., Rich R., Marandos P., Fudala R., Li A., Gryczynski I., Borejdo J. Comparison of orientation androtational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain. J. Biol. Chem. 288:10, 7012–7023 (2013).

28. Berezin M. Y. et al. Long Fluorescence Lifetime Molecular Probes Based on Near Infrared Pyrrolopyrrole Cyanine Fluorophores for In Vivo Imaging. Biophysical Journal 97(9) L22–L24 (2009).

29. Duggal D. et al. No Difference in Myosin Kinetics and Spatial Distribution of the Lever Armin the Left and Right Ventricles of Human Hearts. Front. Physiol. 8:732 (2017).

30. Egorova A.V. et al. New Sm(III) complexes as electronic-excitation donors of the Seta-632 squaraine dye.
Optics and Spectroscopy, 119 (1) 59–65 (2015).

31. Shkand, T. V. et al. (2016). Assessment of alginate hydrogel degradation in biological tissue using viscosity-sensitive fluorescent dyes. Methods and Applications in Fluorescence. 4. 1-12. 10.1088/2050-6120/4/4/044002.

32. Tsunoyama, T. A. et al. Super-long single-molecule tracking reveals dynamic-anchorage-induced integrin function. Nat. Chem. Biol. 14, 497–506 (2018).

33. Mohan, J.F. et al.  Imaging the emergence and natural progression of spontaneous autoimmune diabetes. PNAS, 114(37):E7776-E7785. https://www.pnas.org/cgi/doi/10.1073/pnas.1707381114 (2017).

34. Schlegel J. et al.  Super-resolution microscopy reveals local accumulation of plasma menbrane gangliosides at Neisseria invasion sites. Front. Cell Dev. Biol. 13(7), 194, Sept. 2019.

35. Fabian U. Zwettler et al. Tracking down the molecular architecture of the synaptonemal complex by expanion microscopy. https://www.biorxiv.org/content/biorxiv/early/2019/10/29/821298.full.pdf ://dx.doi.org/10.1101/821298.

36. F. Wäldchen et al. Whole-cell imaging of plasma membrane receptors by 3D lattice light-sheet dSTORM. Nat. Commun. 11, 887 (2020). https://doi.org/10.1038/s41467-020-14731-0

37. Abdablah et al. Profiling glucose-stimulated M3 receptor-activated insulin secretion dynamics from islets of Langerhans using an extended-lifetime fluorescence dye. Anal. Chem. 2020, 92, 12, 8464 - 8471.

38. K. Ojima et al. Ligand-directed two-step labeling to quantify neuronal glutamate receptor trafficking. Nature Com. 12, 831 (2021). https://doi.org/10.1038/s41467-021-21082-x

39. Fujiwara et al. Ultrafast single-molecule imaging reveals focal adhesion nano-architecture and molecular dynamics. J. Cell Biol. 2023 (8) 222. https://doi.org/10.1083/jcb.202110162.

40. Sørensen et al. Proteolytic performance is dependent on binding efficiency, processivity and turnover: single protease insights. bioRxiv, 2024. https://doi.org/10.1101/2024.06.10.598230.

41. S.S.R.Kommidi et al. Steric protection of near-infrared fluorescent dyes for enhanced bioimaging. J. Mater. Chem. B, 34, 2024. DOI: 10.1039/d4tb01281j.

42. Erbacher et al. Interaction of human keratinocytes and nerve fiber terminals at the neuro-cutaneous unit. eLife 2024; 13:e77761. DOI: https://doi.org/10.7554/eLife.77761.

 43. Deep brain imaging utilizing novel surgical techniques: Cranical imaging window and cannula with intravital 2-P-microscopy. 2P-deep brain imaging using SeTau-647-CD31

44. C.T. Lewis et al. Remodelling of skeletal muscle myosin metabolic states in hibernating mammals.doi: https://doi.org/10.1101/2023.11.14.566992. bioRxiv Nov.2023.

45. C. Ricard et al., Brain Structure and Function, 2018, 223 (7), 3011 - 3043. 2-photon dyes review ￿