Miklós Kellermayer - Selected Publications#
1. Pertici I, Bongini L, Melli L, Bianchi G, Salvi L, Falorsi G, Squarci C, Bozó T, Cojoc D, Kellermayer MSZ, Lombardi V, Bianco P. A myosin II nanomachine mimicking the striated muscle. Nat Commun. 2018 Aug 30;9(1):3532.
2. Kellermayer MSZ, Vörös Z, Csík G, Herényi L. Forced phage uncorking: viral DNA ejection triggered by a mechanically sensitive switch. Nanoscale. 2018 Jan 25;10(4):1898-1904.
3. Zsuzsanna Vörös, Gabriella Csík, Levente Herényi and Miklós S. Z. Kellermayer. Stepwise reversible nanomechanical buckling in a viral capsid. Nanoscale 9, 1136-1143, 2017.
4. Csaba I. Pongor, Pasquale Bianco, György Ferenczy, Richárd Kellermayer and Miklós Kellermayer Optical trapping nanometry of hypermethylated CpG-island DNA. Biophys. J. 112, 512–522, 2017.
5. Zsolt Mártonfalvi, Pasquale Bianco, Katalin Naftz, György G. Ferenczy, Miklós Kellermayer. Force generation by titin folding. Prot. Sci. 2017 Jul;26(7):1380-1390.
6. Mártonfalvi Z, Bianco P, Linari M, Caremani M, Nagy A, Lombardi V, Kellermayer M. Low-force transitions in single titin molecules reflect a memory of contractile history. J Cell Sci. 127, 858-870, 2014.
7. Ricardo H. Pires, Árpád Karsai, Maria J. Saraiva, Ana M. Damas, Miklós S. Z. Kellermayer. Distinct Annular Oligomers Captured Along the Assembly and Disassembly Pathways of Transthyretin Amyloid Protofibrils. PLoS One 7(9), e44992, 2012.
8. Miklós S.Z. Kellermayer, Árpád Karsai, Margit Benke, Katalin Soós, and Botond Penke. Stepwise dynamics of epitaxially growing single amyloid fibrils. Proc Natl. Acad. Sci. USA. 105(1):141-4, 2008.
9. Kellermayer, M.S.Z., Grama, L., Karsai, Á., Nagy, A., Kahn, A., Datki, Z. and Penke, B. Reversible unzipping of amyloid ß-fibrils. J. Biol. Chem. 280(9), 8464-8470, 2005.
10. Kellermayer, M.S.Z., Smith, S.B., Granzier, H.L. and Bustamante, C. Folding-unfolding transitions in single titin molecules characterized with force-measuring laser tweezers. Science 276, 1112-1116, 1997.
Total Impact Factor: 410
Total citations (Google Scholar): 4100
h-index (Google Scholar): 30
