@misc{bhardwaj_gadhave_kapuganti_kumar_brotzakis_saumya_nayak_kumar_garg_vendruscolo_et al._2021, 
  title={Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes}, 
  DOI={10.1101/2021.05.29.446267}, 
  abstractNote={<jats:p>The phenomenon of protein aggregation is widespread and associated with a wide range of human diseases. Our knowledge on the aggregation behaviour of viral proteins, however, is still rather limited. Here, we investigated the distribution of aggregation-prone regions in the the SARS-CoV and SARS-CoV-2 proteomes. An initial analysis using a panel of sequence-based predictors suggested the presence of multiple aggregation-prone regions in these proteomes, and revealed an enhanced aggregation propensity in some SARS-CoV-2 proteins. We then studied the in vitro aggregation of predicted aggregation-prone regions in the of SARS-CoV-2 proteome, including the signal sequence peptide and fusion peptide 1 of the spike protein, a peptide from the NSP6 protein (NSP6-p), the ORF10 protein, and the NSP11 protein. Our re-sults show that these peptides and proteins form aggregates via a nucleation-dependent mecha-nism. Moreover, we demonstrated that the aggregates of NSP11 are toxic to mammalian cell cultures. These findings provide evidence about the aggregation of proteins in the SARS-CoV-2 proteome.</jats:p>}, 
  publisher={Cold Spring Harbor Laboratory}, 
  author={Bhardwaj, Taniya and Gadhave, Kundlik and Kapuganti, Shivani Krishna and Kumar, Prateek and Brotzakis, Zacharias Faidon and Saumya, Kumar Udit and Nayak, Namyashree and Kumar, Ankur and Garg, Neha and Vendruscolo, Michele and et al.}, 
  year={2021}, 
  month={May}
  }