Vladimír Sklenář - Publications#


Sklenář, V., Miyashiro, H., Zon, G., Miles, T., Bax, A. Assignment of the 31P Resonances in Oligonucleotides by Two-dimensional NMR Spectroscopy. FEBS Letters 1986, 208, 94.

(A basic method for structural characterization of DNA (391 citations))

Sklenář, V. and Bax, A. Spin-Echo Water Suppression for the Generation of Pure-Phase Two-Dimensional NMR Spectra. J.Magn.Reson. 1987, 74, 469.

(The first efficient method for the measurements of biomacromolecules in water solution using multidimensional NMR without phase distortions (410 citations))

Sklenář, V., Feigon, J. Formation of a Stable Triplex from a Single DNA Strand. Nature 1990, 345, 836.

(The very first study of an intramolecular triplex formation (161 citations))

Piotto, M., Saudek, V. and Sklenář, V. Gradient-tailored Excitation for Single-quantum NMR Spectroscopy of Aqueous Solutions. J. Biomol. NMR 1992, 2, 661.

(Essential tool for structural studies introducing a new method for water suppression now used worldwide. The paper received more than 3400 citatons)

Sklenář, V. Suppression of Radiation Damping in Multidimensional NMR Experiments Using Magnetic Field Gradients. J. Magn Reson. Ser. A. 1995, 114, 132-135.

(A very efficient approach to suppress the adverse effects of water magnetization during the NMR studies of biomacromolecules (133 citations))

Sklenář, V., Peterson, R.D., Rejante, M.R., Wang, E. and Feigon, J. Two-Dimensional Triple-Resonance HCNCH Experiment for Direct Correlation of Ribose H1' and Base H8, H6 Protons in 13C, 15N-Labeled RNA Oligonucleotides. J. Am. Chem. Soc. 1993, 115, 12181-12182.

(One of the very first studies of isotopically labeled RNA oligonucleotides using NMR)

Nováček, J., Zawadska-Kazimierczuk, A., Motáčková, V., Žídek, L., Koźmiński, W., and Sklenář, V. 5D 13C-detected NMR experiments for backbone assignment of unstructured proteins with a very low signal dispersion. J. Biomol. NMR, 2011, 50, 1–11.

(Methodology to tremendously increase sensitivity and resolution of NMR studies of intrinsically disordered proteins)

Babinský, M., Fiala, R., Kejnovská, I., Bednařová, K., Marek, R., Sagi, J., Sklenář, V., Vorlíčková, M., Loss of loop adenines alters human telomere d[AG3(TTAG3)3]] quadruplex folding. Nucl. Acids. Res. 2014, 42, 14031-14041.

Kadeřávek, P., Zapletal, V., Fiala, R., Srb, P., Padrta, P., Přecechtělová, J., Šoltésová, M., Kowalewski, J., Wildmalm, G., Chmelík, J. Jr., Sklenář, V., and Žídek, L. Spectral Density Mapping at Multiple Magnetic Fields Suitable for 13C NMR Relaxation Studies. J. Magn. Reson., 2016, 266, 23-40.

Srb P, Nováček J, Kadeřávek P, Rabatinová A, Krásný L, Žídková J, Bobálová J, Sklenář V, Žídek L. Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins. J Biomol NMR. 2017, 69(3):133-146. doi: 10.1007/s10858-017-0138-1.

Sicorello A, Kelly G, Oregioni A, Nováček J, Sklenář V, Pastore A. The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3. Biophys J. 2018,115(1):59-71. doi: 10.1016/j.bpj.2018.05.029. (The complete assignment of an intrinsically disordered 40kDa protein of high medical importance).

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