Disassembly and reconstitution of signal recognition particle
Cell, ISSN: 0092-8674, Vol: 34, Issue: 2, Page: 525-533
1983
- 184Citations
- 71Captures
- 1Mentions
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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
- Citations184
- Citation Indexes184
- 184
- CrossRef147
- Captures71
- Readers71
- 71
- Mentions1
- References1
- 1
Article Description
Signal recognition particle (SRP) is a ribonucleoprotein consisting of six distinct polypeptides and one molecule of small cytoplasmic 7SL-RNA. The particle was previously shown to function in protein translocation across, and protein integration into, the endoplasmic reticulum membrane. A rapid procedure was developed to disassemble SRP into native protein and RNA components. The method utilizes unfolding of SRP with EDTA and dissociation on polycationic matrixes. SRP proteins prepared this way sediment below 7S and are inactive in activity assays. When recombined with 7SL-RNA in the presence of magnesium, the proteins are shown to reassociate stoichiometrically with 7SL-RNA to form fully active 11S SRP.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0092867483903859; http://dx.doi.org/10.1016/0092-8674(83)90385-9; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0020825185&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/6413076; https://linkinghub.elsevier.com/retrieve/pii/0092867483903859; http://dx.doi.org/10.1016/0092-8674%2883%2990385-9; https://dx.doi.org/10.1016/0092-8674%2883%2990385-9
Elsevier BV
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