@misc{KirchnerIgnatova2015,
  author    = {Kirchner, Sebastian and Ignatova, Zoya},
  title     = {Emerging roles of tRNA in adaptive translation, signalling dynamics and disease},
  series = {Nature reviews},
  volume    = {16},
  journal   = {Nature reviews},
  number    = {2},
  publisher = {Nature Publ. Group},
  address   = {London},
  issn      = {1471-0056},
  doi       = {10.1038/nrg3861},
  pages     = {98 -- 112},
  year      = {2015},
  abstract  = {tRNAs, nexus molecules between mRNAs and proteins, have a central role in translation. Recent discoveries have revealed unprecedented complexity of tRNA biosynthesis, modification patterns, regulation and function. In this Review, we present emerging concepts regarding how tRNA abundance is dynamically regulated and how tRNAs (and their nucleolytic fragments) are centrally involved in stress signalling and adaptive translation, operating across a wide range of timescales. Mutations in tRNAs or in genes affecting tRNA biogenesis are also linked to complex human diseases with surprising heterogeneity in tissue vulnerability, and we highlight cell-specific aspects that modulate the disease penetrance of tRNA-based pathologies.},
  language  = {en}
}
@misc{ZhangIgnatova2011,
  author    = {Zhang, Gong and Ignatova, Zoya},
  title     = {Folding at the birth of the nascent chain: coordinating translation with co-translational folding},
  series = {Current opinion in structural biology : review of all advances ; evaluation of key references ; comprehensive listing of papers},
  volume    = {21},
  journal   = {Current opinion in structural biology : review of all advances ; evaluation of key references ; comprehensive listing of papers},
  number    = {1},
  publisher = {Elsevier},
  address   = {London},
  issn      = {0959-440X},
  doi       = {10.1016/j.sbi.2010.10.008},
  pages     = {25 -- 31},
  year      = {2011},
  abstract  = {In the living cells, the folding of many proteins is largely believed to begin co-translationally, during their biosynthesis at the ribosomes. In the ribosomal tunnel, the nascent peptide may establish local interactions and stabilize alpha-helical structures. Long-range contacts are more likely outside the ribosomes after release of larger segments of the nascent chain. Examples suggest that domains can attain native-like structure on the ribosome with and without population of folding intermediates. The co-translational folding is limited by the speed of the gradual extrusion of the nascent peptide which imposes conformational restraints on its folding landscape. Recent experimental and in silico modeling studies indicate that translation kinetics fine-tunes co-translational folding by providing a time delay for sequential folding of distinct portions of the nascent chain.},
  language  = {en}
}