Publications by authors named "P Penev"

RiboVision2 is a web server designed to visualize phylogenetic, structural, and evolutionary properties of ribosomal RNAs simultaneously at the levels of primary, secondary, and three-dimensional structure and in the context of full ribosomal complexes. RiboVision2 instantly computes and displays a broad variety of data; it has no login requirements, is open-source, free for all users, and available at https://ribovision2.chemistry.

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Article Synopsis
  • - Methanoperedens, a type of archaea, helps reduce methane emissions and hosts unique extrachromosomal genetic elements (ECEs) called Borgs, which influence their activity; however, the diversity of these ECEs has not been thoroughly explored.
  • - New research identifies small linear ECEs, circular viruses, and other unclassified ECEs associated with Methanoperedens, with linear ECEs sharing characteristics with Borgs, prompting the term "mini-Borgs."
  • - Mini-Borgs show significant genetic diversity across at least five groups and are linked to various Methanoperedens viruses, suggesting a complex network of genetic exchange that may affect the functioning and evolution of their host
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All organisms living on Earth descended from a single, common ancestral population of cells, known as LUCA-the last universal common ancestor. Since its emergence, the diversity and complexity of life have increased dramatically. This chapter focuses on four key biological innovations throughout Earth's history that had a significant impact on the expansion of phylogenetic diversity, organismal complexity, and ecospace habitation.

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The Astrobiology Primer 3.0 (ABP3.0) is a concise introduction to the field of astrobiology for students and others who are new to the field of astrobiology.

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The ribosome serves as the universally conserved translator of the genetic code into proteins and supports life across diverse temperatures ranging from below freezing to above 120°C. Ribosomes are capable of functioning across this wide range of temperatures even though the catalytic site for peptide bond formation, the peptidyl transferase center, is nearly universally conserved. Here we find that Thermoproteota, a phylum of thermophilic Archaea, substitute cytidine for uridine at large subunit rRNA positions 2554 and 2555 (Escherichia coli numbering) in the A loop, immediately adjacent to the binding site for the 3'-end of A-site tRNA.

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