T2 Family ribonucleases: ancient enzymes with diverse roles
Trends in Biochemical Sciences, ISSN: 0968-0004, Vol: 35, Issue: 5, Page: 253-259
2010
- 192Citations
- 233Captures
- 4Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations192
- Citation Indexes192
- 192
- CrossRef106
- Captures233
- Readers233
- 233
- Mentions4
- References4
- Wikipedia4
Review Description
Ribonucleases of the T2 family are found in the genomes of protozoans, plants, bacteria, animals and viruses. A broad range of biological roles for these ribonucleases have been suggested, including scavenging of nucleic acids, degradation of self-RNA, serving as extra- or intracellular cytotoxins, and modulating host immune responses. Recently, RNaseT2 family members have been implicated in human pathologies such as cancer and parasitic diseases. Interestingly, certain functions of RNaseT2 family members are independent of their nuclease activity, suggesting that these proteins have additional functions. Moreover, humans lacking RNASET2 manifest a defect in neurological development, perhaps due to aberrant control of the immune system. We review the basic structure and function of RNaseT2 family members and their biological roles.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S096800041000023X; http://dx.doi.org/10.1016/j.tibs.2010.02.002; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=77952585622&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/20189811; https://linkinghub.elsevier.com/retrieve/pii/S096800041000023X; http://www.cell.com/trends/biochemical-sciences/abstract/S0968-0004(10)00023-X?_returnURL=http%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS096800041000023X%3Fshowall%3Dtrue
Elsevier BV
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