Sentences with phrase «cytidine deaminase»

(2017) Phosphorylation promotes activation - induced cytidine deaminase activity at the Myc oncogene.
CRISPR base editing technologies enable the direct conversion of DNA bases (C to T / A / G) without inducing double - strand breaks of DNA by the fusion of cytidine deaminase with deactivated Cas9 (dCas9) or Cas9 nickase.
They do this by producing a «long form» of an enzyme called cytidine deaminase.
(11) This finding supports the idea that DYW domains carry cytidine deaminase activity.
Bacteria that produce the enzyme cytidine deaminase converted the drug to an inactive form.
The first base editors developed in 2016 use cytidine deaminase to change C - G base pairs to T - A pairs (top).
This domain has been hypothesized to provide the enzymatic activity needed to convert C to U because it carries motifs characteristic of cytidine deaminases.
The researchers were able to find the bacterial gene responsible for this, a gene called cytidine deaminase (CDD).
In the process of antibody production, B cells turn on the gene known as activation - induced cytidine deaminase (AID), which acts as a sort of molecular scissors that cut the chromosomes within the B - cell.
As these cells rapidly proliferate, they also express high levels of an enzyme known as activation - induced cytidine deaminase (AID), which induces mutations in their DNA.
Liu and coworkers developed last year's base editor by combining three proteins: a cytidine deaminase, a natural enzyme that converts C to uridine (U); a mutated Cas9 CRISPR enzyme that doesn't cut DNA but uses an associated guide RNA to target specific DNA sequences; and a protein that prevents reversion of U back to C.
After the cytidine deaminase changes C to U, the base editor nicks the strand opposite the modification to induce cellular machinery to replace G with A and change U to T.
Dr. Honjo is well known for his discovery of activation - induced cytidine deaminase that is essential for class switch recombination and somatic hypermutation.
Crystal structure of an ADP - ribosylated protein with a cytidine deaminase - like fold, but unknown function (TM1506), from Thermotoga maritima at 2.70 A resolution.
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