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Codon-stop
Publications associées (39)
New Cu (I) complexes as catalyst for "click" reaction: An experimental and computational study
In this work, two novel well-defined Cu (I) complexes of a Schiff base ligand are described. For this purpose, N, N '-bis (trans-cinnamaldehyde) ethylenediimine [C20H20N2] (L) and Cu (I) complex of the type [CuC20H20N2)PPh3Cl] (C1) and [Cu(C20H20N2)PPh3Br] ...
WILEY2023A mitochondria-specific mutational signature of aging: increased rate of A > G substitutions on the heavy strand
Jacques Fellay, Konstantin Popadin, Dmitrii Iliushchenko, Stepan Denisov
The mutational spectrum of the mitochondrial DNA (mtDNA) does not resemble any of the known mutational signatures of the nuclear genome and variation in mtDNA mutational spectra between different organisms is still incomprehensible. Since mitochondria are ...
OXFORD UNIV PRESS2022The fitness landscape of the codon space across environments
Jeffrey David Jensen, Claudia Bank, Sebastian Matuszewski
Fitness landscapes map the relationship between genotypes and fitness. However, most fitness landscape studies ignore the genetic architecture imposed by the codon table and thereby neglect the potential role of synonymous mutations. To quantify the fitnes ...
NATURE PUBLISHING GROUP2018Distribution of the ribosome associated endonuclease Rae1 and the potential role of conserved amino acids in codon recognition
We recently identified a novel ribonuclease in Bacillus subtilis called Rae1 that cleaves mRNAs in a translation-dependent manner. Rae1 is a member of the NYN/PIN family of ribonucleases and is highly conserved in the Firmicutes, the Cyanobacteria and the ...
TAYLOR & FRANCIS INC2018Rae1/YacP, a new endoribonuclease involved in ribosome-dependent mRNA decay in Bacillus subtilis
The PIN domain plays a central role in cellular RNA biology and is involved in processes as diverse as rRNA maturation, mRNA decay and telomerase function. Here, we solve the crystal structure of the Rae1 (YacP) protein of Bacillus subtilis, a founding mem ...
Wiley2017Role of APOBEC3F Gene Variation in HIV-1 Disease Progression and Pneumocystis Pneumonia
Jacques Fellay, Christian Axel Wandall Thorball, Istvan Bartha
Human APOBEC3 cytidine deaminases are intrinsic resistance factors to HIV-1. However, HIV-1 encodes a viral infectivity factor (Vif) that degrades APOBEC3 proteins. In vitro APO-BEC3F (A3F) anti-HIV-1 activity is weaker than A3G but is partially resistant ...
Public Library of Science2016