Publications

• Maiti S., Bhattacharya K., Wider D., Hany D., Panasenko O., Bernasconi L., Hulo N., Picard D. (2023), Hsf1 and the molecular chaperone Hsp90 support a "rewiring stress response" leading to an adaptive cell size increase in chronic stress, eLife, 12, RP8865
• Dohnalkova M., Krasnykov K., Mendel M., Li L., Panasenko O.O.,  Fleury-Olela F., Broberg Vågbø C., Homolka D., Pillai R.S., (2023) Essential roles of RNA cap-proximal ribose methylation in mammalian embryonic development and fertility. Cell Reports, 42, 112786
• Chen S., Allen G.E., Panasenko O.O., Collart M.A. (2023) Not4-dependent targeting of MMF1 mRNA to mitochondria limits its expression via ribosome pausing, Egd1 ubiquitination, Caf130, No-Go-Decay and autophagy. BioRxiv, Nucleic Acids Research, 51, 5022.
• Allen G.E., Weiss B., Panasenko O.O., Huch S., Villanyi Z., Albert B., Dilg D., Zagatti M., Schaughency P., Liao S.E., Corden J., Polte C., Shore D., Ignatova Z., Pelechano V., Collart M.A. (2023), Not1 and Not4 inversely determine mRNA solubility that sets the dynamics of co-translational events. Genome Biology, 24, 30
• Allen G.E., Panasenko O.O., Villanyi Z., Zagatti M., Weiss B., Pagliazzo L., Huch S., Polte C., Zahoran Z., Hughes C.S., Pelechano V., Ignatova Z., Collart M.A. (2021) Not4 and Not5 modulate translation elongation by Rps7A ubiquitination, Rli1 moonlighting, and condensates that exclude eIF5A. Cell Reports. 36, 109633
• Bezrukov F., Prados J., Renzoni A. Panasenko O.O. (2021) MazF toxin causes alterations in Staphylococcus aureus transcriptome, translatome and proteome that underlie bacterial dormancy. Nucleic Acids Research, 49, 2085
• Sierra R., Prados J., Panasenko O.O., Andrey D.O., Baldi A., Fleuchot B., Redder P., Kelley W.L., Viollier P., Renzoni A. (2020) Insights into the global effect on Staphylococcus aureus growth arrest by induction of the endoribonuclease MazF toxin. Nucleic Acids Research, 48, 8545
• Panasenko O.O., Bezrukov F., Komarynets O., Renzoni A. (2020) YjbH Solubility Controls Spx in Staphylococcus aureus: Implication for MazEF Toxin-Antitoxin System Regulation Frontiers in Microbiology, 11, 113
• Ramadori G., Ioris R.M., Villanyi Z., Firnkes R., Panasenko O.O., Allen G., Konstantinidou G, Aras E., Brenachot X., Biscotti T., Charollais A., Luchetti M., Bezrukov F., Santinelli A., Samad M., Baldi P., Collart M.A., Coppari R. (2020) FKBP10 Regulates Protein Translation to Sustain Lung Cancer Growth, Cell Reports, 30, 3851
• Allen G.E., Panasenko O.O., Villanyi Z., Zagatti M., Weiss B., Polte C., Ignatova Z., Collart M.A., (2019) Switch from translation initiation to elongation needs Not4 and Not5 collaboration. bioRxiv, 850859
• Roch M., Lelong-Alborini E., Panasenko O.O., Sierra R., Renzoni A., Kelley W.L. (2019) PBP2A: a temperature sensitive enzyme requiring extracellular folding factors, PrsA and HtrA1, for β-lactam resistance in Staphylococcus aureus MRSA, Communications Biology, 2, 417
• Panasenko O.O., Somasekharan S.P., Villanyi Z., Zagatti M., Bezrukov F., Rashpa R., Cornut J, Iqbal J., Longis M., Carl S.H., Peña C., Panse V.G., Collart M.A. (2019) Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes, Nature Structural & Molecular Biology, 26, 110
• Collart M.A., Panasenko O.O. (2017) The Ccr4-Not complex: Architecture and structural insights, Subcellular Biochemistry, chapter in a book “Macromolecular Protein Complexes”, 83, 349
• Gupta I., Villanyi Z., Kassem S., Hughes C., Panasenko O.O., Steinmetz L., Collart M.A. (2016), Translational capacity of a cell is determined during transcription elongation via the Ccr4-Not complex, Cell Reports, 15, 1782
• Villanyi Z., Ribaud V., Kassem S., Panasenko O.O., Pahi Z., Boros I., Collart M.A. (2014), Not5 subunit of the Ccr4-Not complex connects transcription and translation, PLoS Genet., 10, e1004569
• Panasenko O.O. (2014) The role of E3 ligase, Not4, in cotranslational quality control, Front.Genet, 5, 141
• Panasenko O.O. (2014) Identification of ubiquitinated proteins, Material and Methods, 4, 827.
• Halter D., Collart M.A., Panasenko O.O. (2014) The Not4 E3 ligase and Caf1/Ccr4 deadenylase play distinct roles in protein quality control, PLoS ONE, 9, e86218.
• Collart M.A., Panasenko O.O., Nikolaev S. (2013) The Not3/5 subunit of the Ccr4-Not complex: a central regulator of gene expression that integrates signals between the cytoplasm and the nucleus in eukaryotic cells, Cellular Signaling, 25, 743.
• Panasenko O.O. (2012) Co-immunoprecipitation in Yeast, Bio-protocol, 2 (16), e250.
• Collart M.A., Panasenko O.O. (2012) The Ccr4-Not4 complex, Gene, 492, 42.
• Panasenko O.O., Collart M.A. (2012) Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase, Mol. Microbiol.,83, 640.
• Panasenko O.O. (2012) Ribosome Fractionation in Yeast, Bio-protocol, 2 (16), e251.
• Panasenko O.O., Collart M.A. (2011) Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29, Mol Cell Biol, 31, 1610.
• Azzouz N., Panasenko O.O., Colau G., Collart M.A. (2009) The CCR4-NOT complex physically and functionally connects TRAMP and the nuclear exosome, PLoS ONE, 4, e6760.
• Panasenko O.O., Fabrice P.A.D., Collart M.A. (2009) Ribosome association and stability of the nascent polypeptide associated complex is dependent upon its own ubiquitination, Genetics, 181, 447.
• Azzouz N., Panasenko O.O., Deluen, C., Hsieh, J., Theiler, G., Collart M.A. (2009) Specific roles for the CCR4-NOT complex subunits in expression of the genome, RNA, 15, 377.
• Panasenko O., Landrieux E., Feuermann M., Finka A., Paquet N., Collart M.A. (2006) The yeast CCR4-NOT complex controls ubiquitination of the nascent associated polypeptide complex (NAC), J Biol Chem., 281, 31389.
• Chernik I.S., Panasenko O.O., Li Y., Marston S.B., Gusev N.B. (2004) pH-induced changes of the structure of small heat shock protein with molecular mass 25/27 kDa (HspB1), BBRC, 324, 1199.
• Panasenko O.O., Kim, M.V., Marston S.B., Gusev N.B. (2003) Interaction of the small heat shock protein with molecular weight 25 kDa (HSP25) with actin, Eur. J. Biochem., 270, 892.
• Panasenko O.O., Seit-Nebi A., Bukach O.V., Marston S.B., Gusev N.B. (2002) Structure and properties of avian small heat shock protein (sHSP) with apparent molecular weight 25 kDa, Biochim Biophys Acta - Proteins and Proteomics, 1601, 64.
• Panasenko O.O., Gusev N.B. (2001) Mutual effects of alpha-actinin, calponin and filamin on actin binding, Biochim Biophys Acta - Protein Structure and Molecular Enzymology, 1544, 393.
• Panasenko O.O., Gusev N.B. (2000) Simultaneous interaction of actin with alpha-actinin and calponin, IUBMB Life, 49, 277.