Results 211 to 220 of about 4,312 (239)
Some of the next articles are maybe not open access.

Related searches:

RNA Editing by Mammalian ADARs

2011
The main type of RNA editing in mammals is the conversion of adenosine to inosine which is translated as if it were guanosine. The enzymes that catalyze this reaction are ADARs (adenosine deaminases that act on RNA), of which there are four in mammals, two of which are catalytically inactive. ADARs edit transcripts that encode proteins expressed mainly
Marion, Hogg   +3 more
openaire   +2 more sources

ADAR Proteins: Structure and Catalytic Mechanism

2011
Since the discovery of the adenosine deaminase (ADA) acting on RNA (ADAR) family of proteins in 1988 (Bass and Weintraub, Cell 55:1089-1098, 1988) (Wagner et al. Proc Natl Acad Sci U S A 86:2647-2651, 1989), we have learned much about their structure and catalytic mechanism.
Rena A, Goodman   +2 more
openaire   +2 more sources

ADAR and Immune Silencing in Cancer

Trends in Cancer, 2019
The regulation of immune responses by tumors is central to their survival. By diminishing the production of interferon (IFN) and other inflammatory mediators, tumors enhance immune evasion. Responses initiated by nucleic acid sensors and triggered by dysregulated RNA transcription and cytoplasmic DNA undergo down-modulation in tumors.
openaire   +2 more sources

Editing specificity of ADAR isoforms

Adenosine to inosine deaminases acting on RNA (ADARs) enzymes are found in all metazoa. Their sequence and protein organization is conserved but also shows distinct differences. Moreover, the number of ADAR genes differs between organisms, ranging from one in flies to three in mammals.
Cornelia, Vesely, Michael F, Jantsch
openaire   +2 more sources

Purification and Assay of ADAR Activity

2007
ADAR editing enzymes are found in all multicellular animals and are conserved in sequence and protein organization. The number of ADAR genes differs between animals, ranging from three in mammals to one in Drosophila. ADAR is also alternatively spliced to generate isoforms that can differ significantly in enzymatic activity.
Liam P, Keegan   +3 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy