Chloroplastic Protein NRIP1 Mediates Innate Immune Receptor Recognition of a Viral Effector
Cell, ISSN: 0092-8674, Vol: 132, Issue: 3, Page: 449-462
2008
- 312Citations
- 342Captures
- 2Mentions
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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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
- Citations312
- Citation Indexes312
- 312
- CrossRef266
- Captures342
- Readers342
- 342
- Mentions2
- References2
- Wikipedia2
Article Description
Plant innate immunity relies on the recognition of pathogen effector molecules by nucleotide-binding-leucine-rich repeat (NB-LRR) immune receptor families. Previously we have shown the N immune receptor, a member of TIR-NB-LRR family, indirectly recognizes the 50 kDa helicase (p50) domain of Tobacco mosaic virus (TMV) through its TIR domain. We have identified an N receptor-interacting protein, NRIP1, that directly interacts with both N's TIR domain and p50. NRIP1 is a functional rhodanese sulfurtransferase and is required for N to provide complete resistance to TMV. Interestingly, NRIP1 that normally localizes to the chloroplasts is recruited to the cytoplasm and nucleus by the p50 effector. As a consequence, NRIP1 interacts with N only in the presence of the p50 effector. Our findings show that a chloroplastic protein is intimately involved in pathogen recognition. We propose that N's activation requires a prerecognition complex containing the p50 effector and NRIP1.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0092867408000524; http://dx.doi.org/10.1016/j.cell.2007.12.031; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=38849106202&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/18267075; https://linkinghub.elsevier.com/retrieve/pii/S0092867408000524
Elsevier BV
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