Results 171 to 180 of about 205,532 (202)
Expanding the Genetic Code of an Animal with Two Non-Canonical Amino Acids
Vazquez Rodriguez JJ, Greiss S.
europepmc +1 more source
A new group of tyrosine recombinase-encoding retrotransposons. [PDF]
A wide variety of novel tyrosine recombinase (YR)-encoding retrotransposons were identified using data emerging from the various eukaryotic genome sequencing projects. Although many of these elements are clearly members of the previously described DIRS group of YR retrotransposons, a substantial number, including elements from a variety of fungi and ...
Russell Poulter
exaly +3 more sources
Tyrosine Recombinase Retrotransposons and Transposons.
ABSTRACT Retrotransposons carrying tyrosine recombinases (YR) are widespread in eukaryotes. The first described tyrosine recombinase mobile element, DIRS1, is a retroelement from the slime mold Dictyostelium discoideum . The YR elements are bordered by terminal repeats related to their replication via free
Russell Poulter, Margi Butler
exaly +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Cre Recombinase and Other Tyrosine Recombinases
Chemical Reviews, 2016Tyrosine-type site-specific recombinases (T-SSRs) have opened new avenues for the predictable modification of genomes as they enable precise genome editing in heterologous hosts. These enzymes are ubiquitous in eubacteria, prevalent in archaea and temperate phages, present in certain yeast strains, but barely found in higher eukaryotes.
Joachim Hauber +2 more
exaly +3 more sources
Dual Recombinase-Mediated Cassette Exchange by Tyrosine Site-Specific Recombinases
Methods in Molecular Biology, 2017Recombinase-mediated cassette exchange, or RMCE, is a genome engineering tool that can be used to swap DNA fragments of interest between two DNA molecules. In a variation of RMCE, called dual RMCE, the exchange of DNA fragments is mediated by two recombinases in contrast to one recombinase in the classic RMCE reaction.
Rachelle P Anderson
exaly +3 more sources
Molecular and Biochemical Parasitology, 2006
VIPER was initially characterized as a 2326bp LTR-like retroelement associated to SIRE, a short interspersed repetitive element specific of Trypanosoma cruzi. It carried a single ORF that coded for a putative reverse transcriptase-RNAse H protein, suggesting that it could be a truncated copy of a longer retroelement. Herein we report the identification
GermÁn A Robledo +2 more
exaly +3 more sources
VIPER was initially characterized as a 2326bp LTR-like retroelement associated to SIRE, a short interspersed repetitive element specific of Trypanosoma cruzi. It carried a single ORF that coded for a putative reverse transcriptase-RNAse H protein, suggesting that it could be a truncated copy of a longer retroelement. Herein we report the identification
GermÁn A Robledo +2 more
exaly +3 more sources
Tyrosine phosphorylation stimulates activity of human RAD51 recombinase through altered nucleoprotein filament dynamics [PDF]
Significance Homologous recombination provides the most accurate means to repair genotoxic DNA lesions. It depends on the assembly of the RAD51 DNA strand exchange protein into a dynamic nucleoprotein filament. The c-Abl tyrosine kinase and its oncogenic counterpart BCR-ABL control RAD51 by phosphorylating tyrosine residues 54 and 315.
Shyamal Subramanyam, Maria Spies
exaly +3 more sources
DIRS-1 and the other tyrosine recombinase retrotransposons
Cytogenetic and Genome Research, 2005DIRS-1 is a retroelement from the slime mold <i>Dictyostelium discoideum</i>. Until recently only two related retrotransposons had been described: PAT from the nematode <i>Panagrellus redivivus</i> and <i>Prt1</i> from the zygomycete fungus <i>Phycomyces blakesleeanus</i>.
R T M, Poulter, T J D, Goodwin
openaire +2 more sources
Strand Selection by the Tyrosine Recombinases
2005Publisher Summary This chapter focuses on four tyrosine recombinases for which there is a wealth of biochemical and structural data. This chapter reviews the biochemical and structural findings for each of these enzymes. This chapter also examines the factors that influence strand selection and consider the possible function of strand selection in ...
Linda, Lee, Paul D, Sadowski
openaire +2 more sources

