Year |
Citation |
Score |
2019 |
Litvín R, Bína D, Herbstová M, Pazderník M, Kotabová E, Gardian Z, Trtílek M, Prášil O, Vácha F. Red-shifted light-harvesting system of freshwater eukaryotic alga Trachydiscus minutus (Eustigmatophyta, Stramenopila). Photosynthesis Research. PMID 31375979 DOI: 10.1007/S11120-019-00662-5 |
0.806 |
|
2019 |
Bína D, Durchan M, Kuznetsova V, Vácha F, Litvín R, Polívka T. Energy transfer dynamics in a red-shifted violaxanthin-chlorophyll a light-harvesting complex. Biochimica Et Biophysica Acta. Bioenergetics. 1860: 111-120. PMID 30414929 DOI: 10.1016/J.Bbabio.2018.11.006 |
0.816 |
|
2017 |
Herbstová M, Bína D, Kaňa R, Vácha F, Litvín R. Red-light phenotype in a marine diatom involves a specialized oligomeric red-shifted antenna and altered cell morphology. Scientific Reports. 7: 11976. PMID 28931902 DOI: 10.1038/S41598-017-12247-0 |
0.804 |
|
2016 |
Bína D, Herbstová M, Gardian Z, Vácha F, Litvín R. Novel structural aspect of the diatom thylakoid membrane: lateral segregation of photosystem I under red-enhanced illumination. Scientific Reports. 6: 25583. PMID 27149693 DOI: 10.1038/Srep25583 |
0.785 |
|
2016 |
Bína D, Gardian Z, Vácha F, Litvín R. Native FMO-reaction center supercomplex in green sulfur bacteria: an electron microscopy study. Photosynthesis Research. 128: 93-102. PMID 26589322 DOI: 10.1007/S11120-015-0205-Y |
0.786 |
|
2015 |
Herbstová M, Bína D, Koník P, Gardian Z, Vácha F, Litvín R. Molecular basis of chromatic adaptation in pennate diatom Phaeodactylum tricornutum. Biochimica Et Biophysica Acta. 1847: 534-43. PMID 25748970 DOI: 10.1016/J.Bbabio.2015.02.016 |
0.799 |
|
2014 |
Durchan M, Keşan G, Slouf V, Fuciman M, Staleva H, Tichý J, Litvín R, Bína D, Vácha F, Polívka T. Highly efficient energy transfer from a carbonyl carotenoid to chlorophyll a in the main light harvesting complex of Chromera velia. Biochimica Et Biophysica Acta. 1837: 1748-55. PMID 24928296 DOI: 10.1016/J.Bbabio.2014.06.001 |
0.775 |
|
2014 |
Bína D, Gardian Z, Vácha F, Litvín R. Supramolecular organization of photosynthetic membrane proteins in the chlorosome-containing bacterium Chloroflexus aurantiacus. Photosynthesis Research. 122: 13-21. PMID 24760483 DOI: 10.1007/S11120-014-0006-8 |
0.788 |
|
2014 |
Gardian Z, Litvín R, Bína D, Vácha F. Supramolecular organization of fucoxanthin-chlorophyll proteins in centric and pennate diatoms. Photosynthesis Research. 121: 79-86. PMID 24715699 DOI: 10.1007/S11120-014-9998-3 |
0.797 |
|
2014 |
Furumaki S, Vacha F, Hirata S, Vacha M. Bacteriochlorophyll aggregates self-assembled on functionalized gold nanorod cores as mimics of photosynthetic chlorosomal antennae: a single molecule study. Acs Nano. 8: 2176-82. PMID 24559170 DOI: 10.1021/Nn500224V |
0.407 |
|
2014 |
Bína D, Gardian Z, Herbstová M, Kotabová E, Koník P, Litvín R, Prášil O, Tichý J, Vácha F. Novel type of red-shifted chlorophyll a antenna complex from Chromera velia: II. Biochemistry and spectroscopy. Biochimica Et Biophysica Acta. 1837: 802-10. PMID 24486443 DOI: 10.1016/J.Bbabio.2014.01.011 |
0.805 |
|
2013 |
Tichy J, Gardian Z, Bina D, Konik P, Litvin R, Herbstova M, Pain A, Vacha F. Light harvesting complexes of Chromera velia, photosynthetic relative of apicomplexan parasites. Biochimica Et Biophysica Acta. 1827: 723-9. PMID 23428396 DOI: 10.1016/J.Bbabio.2013.02.002 |
0.808 |
|
2012 |
Durchan M, Tichý J, Litvín R, Šlouf V, Gardian Z, Hříbek P, Vácha F, Polívka T. Role of carotenoids in light-harvesting processes in an antenna protein from the chromophyte Xanthonema debile. The Journal of Physical Chemistry. B. 116: 8880-9. PMID 22764831 DOI: 10.1021/Jp3042796 |
0.715 |
|
2012 |
Dostál J, Mančal T, Augulis R, Vácha F, Pšenčík J, Zigmantas D. Two-dimensional electronic spectroscopy reveals ultrafast energy diffusion in chlorosomes. Journal of the American Chemical Society. 134: 11611-7. PMID 22690836 DOI: 10.1021/Ja3025627 |
0.312 |
|
2012 |
Fessl T, Adamec F, Polívka T, Foldynová-Trantírková S, Vácha F, Trantírek L. Towards characterization of DNA structure under physiological conditions in vivo at the single-molecule level using single-pair FRET. Nucleic Acids Research. 40: e121. PMID 22544706 DOI: 10.1093/Nar/Gks333 |
0.736 |
|
2012 |
Alster J, Polívka T, Arellano JB, Hříbek P, Vácha F, Hála J, Pšenčík J. Self-assembly and energy transfer in artificial light-harvesting complexes of bacteriochlorophyll c with astaxanthin. Photosynthesis Research. 111: 193-204. PMID 21833799 DOI: 10.1007/S11120-011-9670-0 |
0.458 |
|
2011 |
Furumaki S, Vacha F, Habuchi S, Tsukatani Y, Bryant DA, Vacha M. Absorption linear dichroism measured directly on a single light-harvesting system: the role of disorder in chlorosomes of green photosynthetic bacteria. Journal of the American Chemical Society. 133: 6703-10. PMID 21476570 DOI: 10.1021/Ja111475Z |
0.393 |
|
2011 |
Gardian Z, Tichý J, Vácha F. Structure of PSI, PSII and antennae complexes from yellow-green alga Xanthonema debile. Photosynthesis Research. 108: 25-32. PMID 21455629 DOI: 10.1007/S11120-011-9647-Z |
0.482 |
|
2010 |
Durchan M, Herbstová M, Fuciman M, Gardian Z, Vácha F, Polívka T. Carotenoids in energy transfer and quenching processes in Pcb and Pcb-PS I complexes from Prochlorothrix hollandica. The Journal of Physical Chemistry. B. 114: 9275-82. PMID 20583762 DOI: 10.1021/Jp1026724 |
0.435 |
|
2010 |
Bína D, Litvín R, Vácha F. Absorbance changes accompanying the fast fluorescence induction in the purple bacterium Rhodobacter sphaeroides. Photosynthesis Research. 105: 115-21. PMID 20574750 DOI: 10.1007/S11120-010-9569-1 |
0.762 |
|
2010 |
Herbstová M, Litvín R, Gardian Z, Komenda J, Vácha F. Localization of Pcb antenna complexes in the photosynthetic prokaryote Prochlorothrix hollandica. Biochimica Et Biophysica Acta. 1797: 89-97. PMID 19761753 DOI: 10.1016/J.Bbabio.2009.09.002 |
0.756 |
|
2009 |
Bina D, Litvin R, Vacha F. Kinetics of in vivo bacteriochlorophyll fluorescence yield and the state of photosynthetic apparatus of purple bacteria. Photosynthesis Research. 99: 115-25. PMID 19199074 DOI: 10.1007/S11120-009-9408-4 |
0.784 |
|
2008 |
Litvin R, Bina D, Vacha F. Room temperature photooxidation of beta-carotene and peripheral chlorophyll in photosystem II reaction centre. Photosynthesis Research. 98: 179-87. PMID 18770011 DOI: 10.1007/S11120-008-9339-5 |
0.761 |
|
2008 |
Zupcanova A, Arellano JB, Bina D, Kopecky J, Psencik J, Vacha F. The length of esterifying alcohol affects the aggregation properties of chlorosomal bacteriochlorophylls. Photochemistry and Photobiology. 84: 1187-94. PMID 18331396 DOI: 10.1111/J.1751-1097.2008.00312.X |
0.586 |
|
2007 |
Gardian Z, Bumba L, Schrofel A, Herbstova M, Nebesarova J, Vacha F. Organisation of Photosystem I and Photosystem II in red alga Cyanidium caldarium: encounter of cyanobacterial and higher plant concepts. Biochimica Et Biophysica Acta. 1767: 725-31. PMID 17346666 DOI: 10.1016/j.bbabio.2007.01.021 |
0.4 |
|
2006 |
Promnares K, Komenda J, Bumba L, Nebesarova J, Vacha F, Tichy M. Cyanobacterial small chlorophyll-binding protein ScpD (HliB) is located on the periphery of photosystem II in the vicinity of PsbH and CP47 subunits. The Journal of Biological Chemistry. 281: 32705-13. PMID 16923804 DOI: 10.1074/jbc.M606360200 |
0.301 |
|
2006 |
Bína D, Litvín R, Vácha F, Siffel P. New multichannel kinetic spectrophotometer-fluorimeter with pulsed measuring beam for photosynthesis research. Photosynthesis Research. 88: 351-6. PMID 16763876 DOI: 10.1007/S11120-006-9071-Y |
0.741 |
|
2005 |
Litvín R, Bína D, Siffel P, Vácha F. Conformational changes and their role in non-radiative energy dissipation in photosystem II reaction centres. Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society For Photobiology. 4: 999-1002. PMID 16307113 DOI: 10.1039/B506166K |
0.751 |
|
2004 |
Bumba L, Havelková-Dousová H, Husák M, Vácha F. Structural characterization of photosystem II complex from red alga Porphyridium cruentum retaining extrinsic subunits of the oxygen-evolving complex. European Journal of Biochemistry. 271: 2967-75. PMID 15233792 DOI: 10.1111/j.1432-1033.2004.04226.x |
0.332 |
|
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